|
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 ... |
38-142 |
8.90e-75 |
|
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: 244.23 E-value: 8.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 38 DRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 117
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1389908282 118 RNDDIADGNPKLTLGLIWTIILHFQ 142
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
35-153 |
3.33e-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: 3.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 35 DERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 114
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908282 115 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 153
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
32-151 |
3.34e-70 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 232.18 E-value: 3.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 32 KNQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQ 111
Cdd:cd21236 9 RYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQ 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1389908282 112 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 151
Cdd:cd21236 89 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
155-260 |
4.08e-67 |
|
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: 222.59 E-value: 4.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 155 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 234
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1389908282 235 PEDVDVPHPDEKSIITYVSSLYDVMP 260
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
156-260 |
5.80e-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: 216.49 E-value: 5.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 235
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1389908282 236 EDVDVPHPDEKSIITYVSSLYDVMP 260
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
35-152 |
1.59e-61 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 207.19 E-value: 1.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 35 DERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 114
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1389908282 115 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 152
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
156-260 |
1.68e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.82 E-value: 1.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAEReLGVTKLLDP 235
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1389908282 236 EDVDVPHPDEKSIITYVSSLYDVMP 260
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
154-260 |
5.54e-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: 176.39 E-value: 5.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 154 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAEReLGVTKLL 233
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1389908282 234 DPEDVDVPHPDEKSIITYVSSLYDVMP 260
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
40-143 |
1.61e-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: 175.26 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 40 VQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 118
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1389908282 119 NDDIADGNPKLTLGLIWTIILHFQI 143
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 ... |
29-139 |
1.04e-49 |
|
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: 173.32 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 29 RVRKNQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21246 5 RIKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFL 84
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 139
Cdd:cd21246 85 KEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
156-256 |
3.53e-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: 162.58 E-value: 3.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 235
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1389908282 236 EDVDVPHPDEKSIITYVSSLY 256
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
29-139 |
4.40e-46 |
|
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: 162.85 E-value: 4.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 29 RVRKNQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21193 5 RIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL 84
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 108 kHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 139
Cdd:cd21193 85 -KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
156-256 |
1.57e-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: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 235
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1389908282 236 EDVDVPHPDEKSIITYVSSLY 256
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
36-143 |
1.75e-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: 158.31 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 36 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 111
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 112 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 143
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
33-256 |
9.68e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 168.58 E-value: 9.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 33 NQDERDRVQKKTFTKWVNKHLVKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKH 109
Cdd:COG5069 2 EAKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 110 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGK 188
Cdd:COG5069 82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 189 LFSAIIHKHRPALIDMNQVYRQSNQE--NLEQAFSVAERELGVTKLLDPEDV-DVPHPDEKSIITYVSSLY 256
Cdd:COG5069 159 AFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
29-139 |
1.11e-42 |
|
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: 154.03 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 29 RVRKNQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21318 27 RIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFL 106
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 139
Cdd:cd21318 107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
29-139 |
1.96e-42 |
|
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: 152.90 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 29 RVRKNQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21317 20 RIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFL 99
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 139
Cdd:cd21317 100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
36-143 |
3.34e-41 |
|
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: 148.87 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 36 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 111
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 112 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 143
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
903-979 |
1.02e-39 |
|
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: 143.13 E-value: 1.02e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 903 SWQYLMRDIHIIKTWNISMFKTLRVEEYRLALRNLEQHYQDFLRDSQDSQMFGAEDRMQVESNYNKANQHYNTMVTS 979
Cdd:pfam18373 2 SWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
143-256 |
1.32e-39 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 144.43 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 143 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 222
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908282 223 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 256
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
155-260 |
3.54e-39 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 142.84 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 155 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 234
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1389908282 235 PEDVDVPHPDEKSIITYVSSLYDVMP 260
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
156-256 |
6.20e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 142.45 E-value: 6.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 235
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1389908282 236 EDVDVPHPDEKSIITYVSSLY 256
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
40-141 |
2.32e-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: 140.23 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 40 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 117
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1389908282 118 RNDDIADGNPKLTLGLIWTIILHF 141
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
36-143 |
3.23e-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: 139.97 E-value: 3.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 36 ERDRVQKKTFTKWVNKHLVKAQ--RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 113
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1389908282 114 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 143
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
38-139 |
6.89e-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: 139.06 E-value: 6.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 38 DRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 116
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1389908282 117 IRNDDIADGNPKLTLGLIWTIIL 139
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
152-256 |
1.05e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.04 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 152 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTK 231
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1389908282 232 LLDPEDVDVPHPDEKSIITYVSSLY 256
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
155-256 |
2.42e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 137.69 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 155 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 234
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1389908282 235 PEDVDVPHPDEKSIITYVSSLY 256
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
159-260 |
1.12e-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: 135.63 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 159 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 237
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1389908282 238 VDVPHPDEKSIITYVSSLYDVMP 260
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1332-2145 |
3.08e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 152.99 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1332 VNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKE-EERRKMAEIQAELDKQKQMAEAHAKSVAKAEqealelkm 1410
Cdd:PTZ00121 1060 AEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKaEEAKKTETGKAEEARKAEEAKKKAEDARKAE-------- 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1411 kmkeEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAEL 1490
Cdd:PTZ00121 1132 ----EARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1491 QELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQA 1570
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1571 EEEKIRQIRVVEEVAQksaATQLQTKAmsfsEQTTKLEESLKKEQgnvlKLQEEADKLKKQQKEANTAREEAEQELEiwr 1650
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKK---ADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAKKAAEAAKAEAE--- 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1651 QKANEALRLRLQAEEEAQKKSHAQEEAEkqklEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEC 1730
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1731 IRlKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLE-----DELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLE 1805
Cdd:PTZ00121 1430 KK-KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAK----KKADEAKK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1806 SEALKMKqlADEAARmrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLA-AINEATRLKT-----EAEMALKAKEAENE 1879
Cdd:PTZ00121 1505 AAEAKKK--ADEAKK----AEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKaeekkKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1880 RLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDS-----ELGRQKNIVEETLKQKKVVEEEIHiiKINFHKASK 1954
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaeELKKAEEEKKKVEQLKKKEAEEKK--KAEELKKAE 1656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1955 EKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEE----VERLK 2030
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAK 1736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2031 KKAEDANKQKEKAEKEAEKqvvlaKEAAQKCTAAEQKAQDVLSKNKEDVLAQE--------------KLRDEFENAKKL- 2095
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEIRKEKEAVIEEEldeedekrrmevdkKIKDIFDNFANIi 1811
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 2096 -------------AQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2145
Cdd:PTZ00121 1812 eggkegnlvindsKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
35-143 |
1.78e-35 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 132.35 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 35 DERDRVQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 113
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1389908282 114 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 143
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
140-256 |
2.59e-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: 132.49 E-value: 2.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 140 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQA 219
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908282 220 FSVAERELGVTKLLDPEDVDVPHPDEKSIITYVSSLY 256
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1499-2415 |
3.38e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.52 E-value: 3.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1499 EAEKLRKAAQDEAERLRKQVAEETQRKKNAEDElkrksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEekirqI 1578
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADE------ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED-----A 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1579 RVVEEVAQksaatqlqtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQ--KEANTAR--EEAEQELEIwrQKAN 1654
Cdd:PTZ00121 1128 RKAEEARK--------------AEDARKAEEARKAEDAKRVEIARKAEDARKAEeaRKAEDAKkaEAARKAEEV--RKAE 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1655 EalrlrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEaaLKQKENAEKELDKQRKfaeqiAQQKLSAEQECIRLK 1734
Cdd:PTZ00121 1192 E-----LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA--VKKAEEAKKDAEEAKK-----AEEERNNEEIRKFEE 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1735 ADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQleDELNKVRsEMDSLLQMKINAEKASMVNTEKSKqlleseALKMKQL 1814
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKA--DEAKKAE-EKKKADEAKKKAEEAKKADEAKKK------AEEAKKK 1330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1815 ADEAARMrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEN--ERLKRQAEEEAYQR 1892
Cdd:PTZ00121 1331 ADAAKKK---AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKA 1407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1893 KLLEDQAAQHKQDIEEKITQLQTSSDSELgrqkniveetlkqKKVVEEeihiikinfhkasKEKADlesELKKLKGIADE 1972
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEA-------------KKKAEE-------------AKKAD---EAKKKAEEAKK 1458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1973 TQKSKLKAEE--EAEKLKKlaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQ 2050
Cdd:PTZ00121 1459 AEEAKKKAEEakKADEAKK----------------------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2051 VVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENE 2130
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2131 AAKQAkaqnDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQkvl 2210
Cdd:PTZ00121 1597 VMKLY----EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK--- 1669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2211 lDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLaeEAEKMKSLAEEAGRLS 2290
Cdd:PTZ00121 1670 -AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI--KAEEAKKEAEEDKKKA 1746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2291 VEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKlkaeaEKLQKQKDQAQETAKRLQEDKQQIQqrldketegf 2370
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-----EEDEKRRMEVDKKIKDIFDNFANII---------- 1811
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1389908282 2371 qkslEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ 2415
Cdd:PTZ00121 1812 ----EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKH 1852
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1546-2530 |
7.64e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 148.37 E-value: 7.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1546 KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTkamsFSEQTTKLEESLKKEQGNVlklqEEA 1625
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA----TEEAFGKAEEAKKTETGKA----EEA 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1626 DKLKKQQKEANTAR--EEAEQELEIwrQKANEALRlrlqaEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKE 1703
Cdd:PTZ00121 1115 RKAEEAKKKAEDARkaEEARKAEDA--RKAEEARK-----AEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1704 NAEKELDKqrkfAEQIAQQKLSAEQECIRLKADFEHAEQQRGLldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL 1783
Cdd:PTZ00121 1188 RKAEELRK----AEDARKAEAARKAEEERKAEEARKAEDAKKA---EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1784 QMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSV--AEEAKKQrqiAEEeaARQRSEAEKILKEklaAINEAT 1861
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkkADEAKKK---AEE--AKKADEAKKKAEE---AKKKAD 1332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1862 RLKTEAEMALKAKEAenerlkRQAEEEAYQRKLledQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEE 1941
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEA------AKAEAEAAADEA---EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1942 ihiikinfhkasKEKADlesELKKLKGIADETQKSKLKAEE--EAEKLKKlaaeeerrrkeaeekvkritAAEEeaarqc 2019
Cdd:PTZ00121 1404 ------------KKKAD---ELKKAAAAKKKADEAKKKAEEkkKADEAKK--------------------KAEE------ 1442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2020 kaaQEEVERLKKKAEDANKqkekaekeaekqvvlAKEAAQKctAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEa 2099
Cdd:PTZ00121 1443 ---AKKADEAKKKAEEAKK---------------AEEAKKK--AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE- 1501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2100 ekakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKE 2179
Cdd:PTZ00121 1502 -------------AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2180 AEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRR 2259
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2260 LMQKDKDSTQKLLAEEAEKMKslAEEAGRLSVE---AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAE 2336
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKK--AEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2337 KlqkQKDQAQETAKRLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASAEAEKLKLRV--KELSLAQTKAEDEAKKFKK 2414
Cdd:PTZ00121 1727 E---NKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIK 1801
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2415 QADEVKAQLQRTEKHTTEIVVQKLETQrLQSTREADDLKSAIADleeerkklkkeaeelQRKSKEMANAQQEQIEQQKAE 2494
Cdd:PTZ00121 1802 DIFDNFANIIEGGKEGNLVINDSKEME-DSAIKEVADSKNMQLE---------------EADAFEKHKFNKNNENGEDGN 1865
|
970 980 990
....*....|....*....|....*....|....*.
gi 1389908282 2495 LQQSFLTEKGLLLKREKEVEgEKKRFEKQLEDEMKK 2530
Cdd:PTZ00121 1866 KEADFNKEKDLKEDDEEEIE-EADEIEKIDKDDIER 1900
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1755-2619 |
1.80e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 147.21 E-value: 1.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1755 KNEVNSTEKQR---KQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQllESEALKMKQLADEAARMRSV------- 1824
Cdd:PTZ00121 1063 KAHVGQDEGLKpsyKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKAEEArkaedar 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1825 -AEEAKKQRQIAEEEAARQRSEAEKI---LKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 1900
Cdd:PTZ00121 1141 kAEEARKAEDAKRVEIARKAEDARKAeeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1901 QHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKlkgiADETQKS-KLK 1979
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK----AEEKKKAdEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1980 AEEEAEKLKKLAAEEERRRKEAEEKVKritaaEEEAARQCKAAQEEVERLKKKAEdANKQKEKAEKEAEKQVVLAKEAAQ 2059
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKK-----AEEAKKKADAAKKKAEEAKKAAE-AAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2060 KCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAAlLRQKAEE---AEKQKKAAEnEAAKQAK 2136
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEkkkADEAKKKAE-EAKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2137 AQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKEltvvklqldetdkqkvlldQELQ 2216
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-------------------AEAK 1509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2217 RVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKmkslAEEAGRLSVEAEET 2296
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----AEEDKNMALRKAEE 1585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2297 ARQRQiaesnlaeqralaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfqkslea 2376
Cdd:PTZ00121 1586 AKKAE-------------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-------- 1644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2377 ERKRQLEASAEAEKLKLRVKELSlaqTKAEDEakkfKKQADEVKAQlQRTEKHTTEIVVQKLETQrlqstREADDLKSAI 2456
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEA---KKAEED----KKKAEEAKKA-EEDEKKAAEALKKEAEEA-----KKAEELKKKE 1711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2457 ADLEeerkklkkeaeelqRKSKEMANAqqEQIEQQKAElqqsfltekglLLKREKEVEGEKKRFEKQLEDEMKKAKALKD 2536
Cdd:PTZ00121 1712 AEEK--------------KKAEELKKA--EEENKIKAE-----------EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2537 EQErqrKLMEEERKKLQAIMDEAVrKQKEAEEEMKNKQREMDVLDKKRLEQEKQlAEENKKLREQLQTFEISSKTVSQTK 2616
Cdd:PTZ00121 1765 EEE---KKAEEIRKEKEAVIEEEL-DEEDEKRRMEVDKKIKDIFDNFANIIEGG-KEGNLVINDSKEMEDSAIKEVADSK 1839
|
...
gi 1389908282 2617 ESQ 2619
Cdd:PTZ00121 1840 NMQ 1842
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
156-256 |
1.91e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 129.45 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 235
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1389908282 236 EDVDVPHPDEKSIITYVSSLY 256
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
29-139 |
3.42e-34 |
|
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: 130.55 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 29 RVRKNQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21316 42 RIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFL 121
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 139
Cdd:cd21316 122 KEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
155-253 |
1.14e-33 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 127.15 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 155 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 234
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1389908282 235 PEDVDVPHPDEKSIITYVS 253
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1755-2654 |
2.29e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 143.74 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1755 KNEVNSTEKQRKQL--EDELNKVRSEMDSLLQMKINAEKASmvnTEKSKQLLESEALKMKQLADEAARMRSV---AEEAK 1829
Cdd:PTZ00121 1052 IDGNHEGKAEAKAHvgQDEGLKPSYKDFDFDAKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDAR 1128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1830 KQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEeayQRKLLEDQAAQHKQDIE-- 1907
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaa 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1908 ---EKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEihiikinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEA 1984
Cdd:PTZ00121 1206 rkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA--------KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1985 EKLKKLAAeeerrrkeaeekvkritAAEEEAARQCKAAQE--EVERLKKKAEDANKQKEKAEKeaekqvvlAKEAAQKCT 2062
Cdd:PTZ00121 1278 RKADELKK-----------------AEEKKKADEAKKAEEkkKADEAKKKAEEAKKADEAKKK--------AEEAKKKAD 1332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2063 AAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEE---AEKQKKAAENEAAKQAKAQN 2139
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKK 1412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2140 DTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKeltvvklqldetdkqkvlldQELQRVK 2219
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--------------------AEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2220 GEVNDAFKQKSQVEvelarvriqmeelvKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKmkslAEEAgRLSVEAEETARQ 2299
Cdd:PTZ00121 1473 DEAKKKAEEAKKAD--------------EAKKKAEEAKKKADEAKKAAEAKKKADEAKK----AEEA-KKADEAKKAEEA 1533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2300 RQIAESNLAEQRALAEKILKekmqaiQEATKlKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERK 2379
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKK------AEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2380 RQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEV-KAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIAD 2458
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2459 LEEERKklkkeaeelQRKSKEMANAQQEQIEQQKAELQQsflteKGLLLKREKEVEGEK-KRFEKQLEDEMKKAKALKDE 2537
Cdd:PTZ00121 1687 EKKAAE---------ALKKEAEEAKKAEELKKKEAEEKK-----KAEELKKAEEENKIKaEEAKKEAEEDKKKAEEAKKD 1752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2538 QERQRKLmeEERKKLQAIMDEAVRKQKEAEEEmknkqREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKE 2617
Cdd:PTZ00121 1753 EEEKKKI--AHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK 1825
|
890 900 910
....*....|....*....|....*....|....*..
gi 1389908282 2618 SQTVSVEKLVAVttvgTSKGVLNGSTEVDGVKKEGDS 2654
Cdd:PTZ00121 1826 EMEDSAIKEVAD----SKNMQLEEADAFEKHKFNKNN 1858
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
155-253 |
8.05e-33 |
|
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: 124.56 E-value: 8.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 155 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 234
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1389908282 235 PEDVDVPHPDEKSIITYVS 253
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
143-256 |
1.32e-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: 124.18 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 143 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 222
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908282 223 AERELGVTKLLDPEDV-DVPHPDEKSIITYVSSLY 256
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
39-144 |
2.12e-32 |
|
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: 124.10 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 39 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 115
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHFQIS 144
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1354-2606 |
4.52e-32 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 138.81 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1354 DAQRRLEDDEKASEKLKEEERRKMAEIQAELdkqkqmaeaHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNI 1433
Cdd:NF041483 91 DAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1434 QQELQHLKSLSDQEIksknqqlEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAaEAEKLRKAAQDEAer 1513
Cdd:NF041483 162 ESQARRLLDESRAEA-------EQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARK-DAERLLNAASTQA-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1514 lrkqvaeetQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKirqirVVEEvAQKSAATQL 1593
Cdd:NF041483 232 ---------QEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEK-----VVAE-AKEAAAKQL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1594 QTkAMSFSEQTTKleesLKKEQgnVLKLQEEAdklkkqQKEANTAREEAEQ-------ELEIWRQKANEALRlRLQAEEE 1666
Cdd:NF041483 297 AS-AESANEQRTR----TAKEE--IARLVGEA------TKEAEALKAEAEQaladaraEAEKLVAEAAEKAR-TVAAEDT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1667 AQKKSHAQEEAEKQKLEAERDAKK--RGKAEEAALKQKEnAEKELDKQRKFAEQIAQQKLSA---------------EQE 1729
Cdd:NF041483 363 AAQLAKAARTAEEVLTKASEDAKAttRAAAEEAERIRRE-AEAEADRLRGEAADQAEQLKGAakddtkeyraktvelQEE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1730 CIRLKADfehAEQQRGLLDNELQRLKNE-----VNSTEKQRKQLEDELNKVRSEMDSLLQ-MKINAEKASMVNTEKSKQL 1803
Cdd:NF041483 442 ARRLRGE---AEQLRAEAVAEGERIRGEarreaVQQIEEAARTAEELLTKAKADADELRStATAESERVRTEAIERATTL 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1804 LESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILKEKLA-AINEATRLKTEAEMALKAKE------ 1875
Cdd:NF041483 519 RRQAEETLERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERLTAAEealada 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1876 -AENERLKRQAEEEAYQrklLEDQAAqhkqdieEKITQLQTSSDSElgrqknivEETLKQKKVVEeeihiikinfhkASK 1954
Cdd:NF041483 599 rAEAERIRREAAEETER---LRTEAA-------ERIRTLQAQAEQE--------AERLRTEAAAD------------ASA 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1955 EKADLESELKKLKG-IADETQKSKLKAEEEAEKLKklAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQE--------- 2024
Cdd:NF041483 649 ARAEGENVAVRLRSeAAAEAERLKSEAQESADRVR--AEAAAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraea 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2025 --EVERLKKKAEDANKQKEKAEKEAEKQVV-LAKEAAQKCT----AAEQKAQDVlsknkedvlaqeklRDEFENAKKLAQ 2097
Cdd:NF041483 727 dqERERAREQSEELLASARKRVEEAQAEAQrLVEEADRRATelvsAAEQTAQQV--------------RDSVAGLQEQAE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2098 EAEKAkekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRkeaeeeaarrAAAEAAALKQKQQADAemskhk 2177
Cdd:NF041483 793 EEIAG----------LRSAAEHAAERTRTEAQEEADRVRSDAYAERER----------ASEDANRLRREAQEET------ 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2178 kEAEQALQQKSqvekeltvVKLQLDETDKQKVLLDQELQRVKGEVNDAFkqkSQVEVELARVRIQM-EELVKLKLKIEEE 2256
Cdd:NF041483 847 -EAAKALAERT--------VSEAIAEAERLRSDASEYAQRVRTEASDTL---ASAEQDAARTRADArEDANRIRSDAAAQ 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2257 NRRLMQKDKDSTQKLLAE---EAEKMKSLA-EEAGRLSVEAEETARQRQIAESNLAEQ-RALAEKILKekmQAIQEATKL 2331
Cdd:NF041483 915 ADRLIGEATSEAERLTAEaraEAERLRDEArAEAERVRADAAAQAEQLIAEATGEAERlRAEAAETVG---SAQQHAERI 991
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2332 KAEAEKLqkqKDQAQETAKRLQEDKQQIQQRLDKETEgfqkslEAERKRQLEASAEAEKLKLRV-----KELSLAQTKAE 2406
Cdd:NF041483 992 RTEAERV---KAEAAAEAERLRTEAREEADRTLDEAR------KDANKRRSEAAEQADTLITEAaaeadQLTAKAQEEAL 1062
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2407 DEAKKFKKQADE-VKAQLQRTEKHTTEIVVQKlETQRLQSTREADDL-------KSAIADLEEERKKLKKEA-----EEL 2473
Cdd:NF041483 1063 RTTTEAEAQADTmVGAARKEAERIVAEATVEG-NSLVEKARTDADELlvgarrdATAIRERAEELRDRITGEieelhERA 1141
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2474 QRKSKEMANAQQEQIEQ--QKAELQQSFLTEKGLLLKREKEVEGEKKRFekqleDEMKKAKALKDEQERQRKLMEEERKK 2551
Cdd:NF041483 1142 RRESAEQMKSAGERCDAlvKAAEEQLAEAEAKAKELVSDANSEASKVRI-----AAVKKAEGLLKEAEQKKAELVREAEK 1216
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 2552 LQAimdEAVRkqkEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLrEQLQTFE 2606
Cdd:NF041483 1217 IKA---EAEA---EAKRTVEEGKRELDVLVRRREDINAEISRVQDVL-EALESFE 1264
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
161-256 |
8.28e-32 |
|
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: 121.69 E-value: 8.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 161 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED-VD 239
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1389908282 240 VPHPDEKSIITYVSSLY 256
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
40-143 |
1.48e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 120.86 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 40 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 117
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1389908282 118 RNDDIADGNPKLTLGLIWTIILHFQI 143
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
159-261 |
2.16e-31 |
|
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: 120.80 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 159 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ-ENLEQAFSVAERELGVTKLLDPE 236
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1389908282 237 DVDVPHPDEKSIITYVSSLYDVMPR 261
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
40-143 |
2.70e-31 |
|
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: 120.11 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 40 VQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 118
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1389908282 119 NDDIADGNPKLTLGLIWTIILHFQI 143
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
36-145 |
8.12e-31 |
|
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: 119.22 E-value: 8.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 36 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 111
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1389908282 112 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 145
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
159-260 |
1.58e-30 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 117.75 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 159 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 237
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1389908282 238 VDVPHPDEKSIITYVSSLYDVMP 260
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1358-1989 |
2.56e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 132.75 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1358 RLED--DEKAS--EKLKEEER--RKMAEIQAELDKQKQMAEAHAKSVAKAEQEALElkmkmkEEASKRQDVAADAEKQKQ 1431
Cdd:COG1196 190 RLEDilGELERqlEPLERQAEkaERYRELKEELKELEAELLLLKLRELEAELEELE------AELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1432 NIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIeeeihiiriqlekttahkaksEAELQELRDRAAEAEKLRKAAQDEA 1511
Cdd:COG1196 264 ELEAELEELR----LELEELELELEEAQAEEYEL---------------------LAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1512 ERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQkykmQAEEAERRMKQAEEEKIRQIRvveevAQKSAAT 1591
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELE-----ELAEELL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1592 QLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwRQKANEALRLRLQAEEEAQKKS 1671
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1672 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNEL 1751
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1752 QRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQ 1831
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA----ALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1832 RQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 1911
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1912 QLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfhkASKEKADLESELKKLKGIADETQksklkAEEEAEKLKK 1989
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEEL---LEEEELLEEEALEELPEPPDLEE-----LERELERLER 774
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
39-141 |
1.15e-29 |
|
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: 115.66 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 39 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHF 141
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1329-1908 |
1.18e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.44 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1329 QEYVNLRTRYSEL-MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALE 1407
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1408 LKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSE 1487
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1488 AELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRM 1567
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1568 KQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQEEADKLKKQQKEANTAREEAEQELE 1647
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-EADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1648 IWRQKANEALRLRLQAEEEAQkksHAQEEAEKQKLEAERDAKKRGKAEEAALkqkeNAEKELDKQRKFAEQIAQQKLSAE 1727
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNI---VVEDDEVAAAAIEYLKAAKAGRATFLPL----DKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1728 QECIRLKADFEHAEQQRGLLDNELQRLKNEvnSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKAsmvnTEKSKQLLESE 1807
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLE--AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----RRELLAALLEA 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1808 ALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEE 1887
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
570 580
....*....|....*....|.
gi 1389908282 1888 EAYQRKLLEDQAAQHKQDIEE 1908
Cdd:COG1196 758 EPPDLEELERELERLEREIEA 778
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
159-258 |
3.35e-29 |
|
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: 114.30 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 159 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED- 237
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1389908282 238 VDVPHPDEKSIITYVSSLYDV 258
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
29-143 |
5.66e-29 |
|
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: 114.47 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 29 RVRKNQDERDRVQKKTFTKWVNKHLVKAQRHV--TDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALD 105
Cdd:cd21247 9 HIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAIT 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908282 106 FLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 143
Cdd:cd21247 89 FLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1116-1982 |
7.14e-28 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 125.25 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1116 AEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSE-----AEADQVMFDRLQDDLRKAttvhDKMTRIHSERDADLE 1190
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkaEEARKAEDAKRVEIARKA----EDARKAEEARKAEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1191 HYRQLVNGLLERWQAvfaqielRLRELDLLGRHMNSYRDSYEwlIRWLTEARQRQEKIQAVPISDSRALREQLTDEKKll 1270
Cdd:PTZ00121 1176 KKAEAARKAEEVRKA-------EELRKAEDARKAEAARKAEE--ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK-- 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1271 GEIEKNKDKIDDCHKNAKAYidsvkdYEFQILTYKALQDPIASPLKKPKMECASDDIiqeyvnlrtRYSELMTLTNQYIK 1350
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAH------FARRQAAIKAEEARKADELKKAEEKKKADEA---------KKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1351 FIIDAQRRLEDDEKASE-KLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRqdvaADAEKQ 1429
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEaKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK----ADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1430 KQNIQQELQHLKSLSdQEIKSKNQQLEDALVSRRKieeeihiiRIQLEKTTAHKAKSEaELQELRDRAAEAEKLRKAAQD 1509
Cdd:PTZ00121 1386 KAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKK--------ADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEE 1455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1510 --EAERLRKQvAEETQR----KKNAEDelKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEE 1583
Cdd:PTZ00121 1456 akKAEEAKKK-AEEAKKadeaKKKAEE--AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1584 VAQKSAATQlqtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLrlqA 1663
Cdd:PTZ00121 1533 AKKADEAKK--------AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL---Y 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1664 EEEAQKKSHAQEEAEKQKLEAERDAK-KRGKAEEAALKQKENAEKELDKQRKFAEQiaQQKLSAEQECIRLKADFEHAEQ 1742
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKaEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1743 QRGllDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMR 1822
Cdd:PTZ00121 1680 AKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1823 SVAEEAKKQRQIAEEeaarQRSEAEKILKEKLAAINEATRLKTE---------AEMALKAKEAENERLKRQAEEEAYQRK 1893
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDkkikdifdnFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1894 LLEDQAAQHKQDIEEkITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESEL--KKLKGIAD 1971
Cdd:PTZ00121 1834 EVADSKNMQLEEADA-FEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIpnNNMAGKNN 1912
|
890
....*....|.
gi 1389908282 1972 ETQKSKLKAEE 1982
Cdd:PTZ00121 1913 DIIDDKLDKDE 1923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1516-2422 |
1.86e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 123.63 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1516 KQVAEETQRK-KNAEDELKRKSDAEKEAAKQkqralddLQKYKMQAEEAERRMKQAEEEKIRQIRV----VEEVAQKSAA 1590
Cdd:TIGR02168 171 KERRKETERKlERTRENLDRLEDILNELERQ-------LKSLERQAEKAERYKELKAELRELELALlvlrLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1591 TQLQTKAM-----SFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEE 1665
Cdd:TIGR02168 244 LQEELKEAeeeleELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1666 EaqkkshaQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRG 1745
Cdd:TIGR02168 324 Q-------LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1746 LLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSL----LQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARM 1821
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1822 RSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENerlKRQAEEEAYQRKLLEDQAAQ 1901
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE---GYEAAIEAALGGRLQAVVVE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1902 HKQDIEEKITQLqtsSDSELGRQKNIVEETLKQKKVVEEEIHIIKiNFHKASKEKADLESELKKLKG----------IAD 1971
Cdd:TIGR02168 554 NLNAAKKAIAFL---KQNELGRVTFLPLDSIKGTEIQGNDREILK-NIEGFLGVAKDLVKFDPKLRKalsyllggvlVVD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1972 ETQksklkaeeEAEKLKKLAAEEERRRKEAEEKVKR---ITAAEEEAARQCKAAQEEVERLKKKAEdankqkekaekeae 2048
Cdd:TIGR02168 630 DLD--------NALELAKKLRPGYRIVTLDGDLVRPggvITGGSAKTNSSILERRREIEELEEKIE-------------- 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2049 kqvvlakEAAQKCTAAEQKAQDVLSKnkedvlaQEKLRDEFENAKKLAQEaekakekaekeaalLRQKAEEAEKQKKAAE 2128
Cdd:TIGR02168 688 -------ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEE--------------LSRQISALRKDLARLE 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2129 NEAAKQAKAQNDTEKQRKEAEeeaarraaaeaaalKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQK 2208
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELE--------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2209 VLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEEnrrlmqkdkdstqklLAEEAEKMKSLAEEAGR 2288
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED---------------IESLAAEIEELEELIEE 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2289 LSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQEtakRLQEDKQQIQQRLDKETE 2368
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSE 947
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 2369 GFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTK-------AEDEAKKFKKQADEVKAQ 2422
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQ 1008
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1116-1913 |
3.29e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.33 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1116 AEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSEaEADQVMFDRLQDDLRKATTVH--DKMTRIHSERDADLEHYR 1193
Cdd:PTZ00121 1136 AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELRkaEDARKAEAARKAEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1194 QLVNGLLERWQAVFAQIELRLRELDLLGRHMNSYRDSYEwlIRWLTEAR-----QRQEKIQAVPISDSRALRE------- 1261
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE--IRKFEEARmahfaRRQAAIKAEEARKADELKKaeekkka 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1262 ---QLTDEKKLLGEIEKN----------KDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASPLKKPKMECASDDII 1328
Cdd:PTZ00121 1293 deaKKAEEKKKADEAKKKaeeakkadeaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1329 QEYVNlrtRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLK--EEERRKMAEIQAELDKQKQMAEAHAKsvAKAEQEAL 1406
Cdd:PTZ00121 1373 KEEAK---KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKK--AEEAKKAD 1447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1407 ELKmKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKS 1486
Cdd:PTZ00121 1448 EAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1487 EAELQELR--DRAAEAEKLRKAAQ-DEAERLRK--QVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAE 1561
Cdd:PTZ00121 1527 AKKAEEAKkaDEAKKAEEKKKADElKKAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1562 EAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAmsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1641
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE---AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1642 AEQEleiwrQKANEALRlrlQAEEEAQKkshaQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1721
Cdd:PTZ00121 1684 EEDE-----KKAAEALK---KEAEEAKK----AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1722 QklsaEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKsk 1801
Cdd:PTZ00121 1752 D----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK-- 1825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1802 qllESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQ-----RSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 1876
Cdd:PTZ00121 1826 ---EMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDgnkeaDFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
810 820 830
....*....|....*....|....*....|....*..
gi 1389908282 1877 ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQL 1913
Cdd:PTZ00121 1903 PNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKI 1939
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
39-141 |
4.52e-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: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 39 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHF 141
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1555-2223 |
8.48e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.20 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERRMKQAEE--EKIRQIRvvEEVAQksaatQLqtkamsfseqttkleESLKKEQGNVLK---LQEEADKLK 1629
Cdd:COG1196 169 KYKERKEEAERKLEATEEnlERLEDIL--GELER-----QL---------------EPLERQAEKAERyreLKEELKELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1630 KQQKEAntAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKEL 1709
Cdd:COG1196 227 AELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1710 DKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINA 1789
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1790 EKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAtrlkTEAEM 1869
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL----EEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1870 ALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIhiikinf 1949
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1950 hKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKlaaeeerrrkeaeekvKRITAAEEEAARQCKAAQEEVERL 2029
Cdd:COG1196 533 -EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA----------------GRATFLPLDKIRARAALAAALARG 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2030 KKKAEDANKQKEKAEKEAEKQVVLAKEAaqkctAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKE 2109
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLL-----GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2110 AALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQ 2189
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
650 660 670
....*....|....*....|....*....|....
gi 1389908282 2190 VEKELTVVKLQLDETDKQKVLLDQELQRvKGEVN 2223
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEREIEA-LGPVN 783
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1499-2598 |
1.58e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 120.70 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1499 EAEKLRKAAQDEAERLRkqvaeetqrkKNAEDELkrksdaeKEAAKQKQRALDDL--QKYKMQAE---EAERRMKQAEEE 1573
Cdd:NF041483 73 QAEQLLRNAQIQADQLR----------ADAEREL-------RDARAQTQRILQEHaeHQARLQAElhtEAVQRRQQLDQE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1574 KIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQ-----QKEANTAREEAEQeleI 1648
Cdd:NF041483 136 LAERRQTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAERLAEEarqrlGSEAESARAEAEA---I 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1649 WRQKANEALRLRLQAEEEAQK-KSHAQ----------EEAEKQKLEAERDAKKRGKAEEAALKQkenAEKELDKQRKFAE 1717
Cdd:NF041483 213 LRRARKDAERLLNAASTQAQEaTDHAEqlrsstaaesDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKVVAEAK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1718 QIAQQKLSAEQECirlkadfehAEQQRGLLDNELQRLKNE-VNSTEKQRKQLEDELNKVRSEMDSLLQMKinAEKASMVN 1796
Cdd:NF041483 290 EAAAKQLASAESA---------NEQRTRTAKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEA--AEKARTVA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1797 TEKSKQLL-----ESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKE-KLAAIN------------ 1858
Cdd:NF041483 359 AEDTAAQLakaarTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDdtkeyraktvel 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1859 --EATRLKTEAEMALKAKEAENERLKRQAEEEAYQR-----KLLEDQAAQHKQDIEEkiTQLQTSSDSELGRQKNI---- 1927
Cdd:NF041483 439 qeEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADE--LRSTATAESERVRTEAIerat 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1928 -----VEETLKQKKvVEEEIHIIKINfHKASKEKADLESELKKLKgiaDETQKS-KLKAEEEAEKLKKLAAEEErrrkea 2001
Cdd:NF041483 517 tlrrqAEETLERTR-AEAERLRAEAE-EQAEEVRAAAERAARELR---EETERAiAARQAEAAEELTRLHTEAE------ 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2002 eekvKRITAAEE-------EAARQCKAAQEEVERLkkKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSK 2074
Cdd:NF041483 586 ----ERLTAAEEaladaraEAERIRREAAEETERL--RTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVR 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2075 NKEDVLAQ-EKLRDEfenAKKLAQeaekakekaekeaallRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKeaeeeaa 2153
Cdd:NF041483 660 LRSEAAAEaERLKSE---AQESAD----------------RVRAEAAAAAERVGTEAAEALAAAQEEAARRRR------- 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2154 rraaaeaaalkqkqQADAEMSKHKKEAEQALQQ-KSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQ- 2231
Cdd:NF041483 714 --------------EAEETLGSARAEADQERERaREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQq 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2232 VEVELARVRIQM-EELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEA-EETARQRQIAESNLAE 2309
Cdd:NF041483 780 VRDSVAGLQEQAeEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAqEETEAAKALAERTVSE 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2310 QRALAEKILKEK---------------MQAIQEATKLKAEA-EKLQKQKDQAQETAKRL------QEDKQQIQQRLDKET 2367
Cdd:NF041483 860 AIAEAERLRSDAseyaqrvrteasdtlASAEQDAARTRADArEDANRIRSDAAAQADRLigeatsEAERLTAEARAEAER 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2368 EGFQKSLEAERKR----------QLEASAEAEKLKLRVKE-LSLAQTKAE---DEAKKFKKQADEVKAQLQRTEKHTTEI 2433
Cdd:NF041483 940 LRDEARAEAERVRadaaaqaeqlIAEATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEAERLRTEAREEADR 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2434 VVQklETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIE------QQKAELQQSFLTEKGLLL 2507
Cdd:NF041483 1020 TLD--EARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADtmvgaaRKEAERIVAEATVEGNSL 1097
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2508 krekeVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAimdeavRKQKEAEEEMKNKQREMDVLDKKRLEQ 2587
Cdd:NF041483 1098 -----VEKARTDADELLVGARRDATAIRERAEELRDRITGEIEELHE------RARRESAEQMKSAGERCDALVKAAEEQ 1166
|
1210
....*....|.
gi 1389908282 2588 EKQLAEENKKL 2598
Cdd:NF041483 1167 LAEAEAKAKEL 1177
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
39-144 |
1.95e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.04 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 39 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHFQIS 144
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1555-2418 |
2.72e-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: 119.78 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERRMKQAEEEKIRQIRVVEEvaqksaatqlqtkamsfseqttkLEESLKKeqgnvLKLQ-EEADKLKKQQK 1633
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNE-----------------------LERQLKS-----LERQaEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1634 EantaREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEeaALKQKENAEKELdkqr 1713
Cdd:TIGR02168 221 E----LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKEL---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1714 kfaeqiaqQKLSAEQEciRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmkinaekas 1793
Cdd:TIGR02168 291 --------YALANEIS--RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE--------- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1794 mvntekskqllesealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAlka 1873
Cdd:TIGR02168 352 ----------------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL--- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1874 kEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLqtssdselgrqknivEETLKQKKVVEEEIHIIKINFHKAS 1953
Cdd:TIGR02168 413 -EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEEL---------------EELQEELERLEEALEELREELEEAE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1954 KEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEE-------------------- 2013
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaalggrlqavvven 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2014 -EAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA 2092
Cdd:TIGR02168 555 lNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNA 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2093 KKLAQEAEKAKEKAEKEAALL--------------------RQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEA 2152
Cdd:TIGR02168 635 LELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2153 ARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNdafKQKSQV 2232
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE---ELEAQI 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2233 EVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2310
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2311 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKsLEAERKRQLEASAEAEK 2390
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYS 950
|
890 900 910
....*....|....*....|....*....|...
gi 1389908282 2391 LKL-----RVKELSLAQTKAEDEAKKFKKQADE 2418
Cdd:TIGR02168 951 LTLeeaeaLENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2011-2663 |
3.67e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.86 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2011 AEEEAARQCKAAQEE--VERLKKKAEDANKQKEKAEKEAEKQVVLAKEA-----------------AQKCTAAEQKAQDV 2071
Cdd:PTZ00121 1100 AEEAKKTETGKAEEArkAEEAKKKAEDARKAEEARKAEDARKAEEARKAedakrveiarkaedarkAEEARKAEDAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2072 LSKNKEDVLAQEKLR--------------DEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQ--- 2134
Cdd:PTZ00121 1180 AARKAEEVRKAEELRkaedarkaeaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfee 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2135 --------AKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHK----KEAEQALQQKSQVEKELTVVKLQLD 2202
Cdd:PTZ00121 1260 armahfarRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaeeaKKADEAKKKAEEAKKKADAAKKKAE 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2203 ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVK----------LKLKIEEENRRLMQKDKDSTQKLL 2272
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeekkkadeAKKKAEEDKKKADELKKAAAAKKK 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2273 AEEAEKMKSLAEEAGRLSVEAEETARQRQIAESnlAEQRALAEKILK--EKMQAIQEATKLKAEAEKLQKQKDQAQETAK 2350
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKK 1497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2351 RLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHT 2430
Cdd:PTZ00121 1498 KADEAKKAAEAK--KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2431 TEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKRE 2510
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2511 KEVEGEKKRFE-KQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQ-REMDVLDKKRLEQE 2588
Cdd:PTZ00121 1656 EEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElKKAEEENKIKAEEA 1735
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2589 KQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL----VAVTTVGTSKGVLNGSTEVDgvKKEGDSPLSFEGIRE 2663
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrkekEAVIEEELDEEDEKRRMEVD--KKIKDIFDNFANIIE 1812
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
141-256 |
4.55e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 105.94 E-value: 4.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 141 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAF 220
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908282 221 SVAERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 256
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
161-256 |
1.38e-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: 103.77 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 161 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED-VD 239
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1389908282 240 VPHPDEKSIITYVSSLY 256
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1695-2622 |
1.52e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 117.38 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1695 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNK 1774
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1775 VRSEMDSLLQmKINAEKASMvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKL 1854
Cdd:pfam02463 249 EQEEIESSKQ-EIEKEEEKL---AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1855 AAINEATRLKTEAEMALKAKEaENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ 1934
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1935 KKVVEEEIHIIKINFHKASKEKadlESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEE 2014
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2015 AARQCKaaQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLaqeKLRDEFENAKK 2094
Cdd:pfam02463 481 KLQEQL--ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA---ISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2095 LAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMS 2174
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2175 KHKKEAeqalqqKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIE 2254
Cdd:pfam02463 636 KLKESA------KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2255 EENRRLMQKDKDSTQKLLAEEAEKmkslaeeagrlsvEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAE 2334
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDK-------------INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2335 AEKLQKQKDQAQETAKRLQEdkqqiqqrldketegfqKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2414
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKL-----------------KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2415 QaDEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2494
Cdd:pfam02463 840 L-ELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2495 LQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQER-QRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNK 2573
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRlLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1389908282 2574 QREMDVLDKKRLEQEkqlaEENKKLREQLQTFEISSKTVSQTKESQTVS 2622
Cdd:pfam02463 999 RLEEEKKKLIRAIIE----ETCQRLKEFLELFVSINKGWNKVFFYLELG 1043
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
143-256 |
1.86e-25 |
|
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: 104.40 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 143 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 222
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908282 223 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 256
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1357-2119 |
2.12e-25 |
|
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: 116.69 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1357 RRLEDDEKASEKL-----KEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEeaskrqdvaadAEKQKQ 1431
Cdd:TIGR02168 216 KELKAELRELELAllvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1432 NIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEA 1511
Cdd:TIGR02168 285 ELQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1512 ERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRAlddlqkyKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT 1591
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1592 QLQTKAMSFSEqttkLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKs 1671
Cdd:TIGR02168 434 ELKELQAELEE----LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1672 hAQEEAEKQKLEAERD--------AKKRGKAEEAALK--------------------QKENAEK-----ELDKQRKFAEQ 1718
Cdd:TIGR02168 509 -KALLKNQSGLSGILGvlselisvDEGYEAAIEAALGgrlqavvvenlnaakkaiafLKQNELGrvtflPLDSIKGTEIQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1719 IAQQKLSAEQECIRLKAD--FEHAEQQRGLLDNELQRLK--NEVNSTEKQRKQLEDELNKVRSEMDSLLQ---MKINAEK 1791
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKdlVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPggvITGGSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1792 ASMVNTEKSKQLLESEAlKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAL 1871
Cdd:TIGR02168 668 TNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1872 KAKEAENERLKRQAEEEAYQRKLLEdQAAQHKQDIEEKITQLQtssdSELGRQKNIVEETLKQKKVVEEEIHIIKINFHK 1951
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELE----AQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1952 ASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKK 2031
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2032 KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKnkedvlAQEKLRDEFENAKKLAQEAEKAKEKAEKEAA 2111
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
....*...
gi 1389908282 2112 LLRQKAEE 2119
Cdd:TIGR02168 976 RLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1329-2029 |
3.10e-25 |
|
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: 116.31 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1329 QEYVNLRTRYSEL-MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELD-KQKQMAEAHAKsVAKAEQEAL 1406
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEeLRLEVSELEEE-IEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1407 ELKMKmkeeaskrqdvAADAEKQKQNIQQELQHLkslsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKS 1486
Cdd:TIGR02168 292 ALANE-----------ISRLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1487 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDEL----KRKSDAEKEAAKQKQRALD--------DLQ 1554
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleARLERLEDRRERLQQEIEEllkkleeaELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERRMKQAEEEKIRQIRVVEEV-AQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQK 1633
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1634 EANTAREEAEQELEI---WRQKANEALRLRLQA-----EEEAQKKSHAQEEAEKQK-----LEAERDAKKRGKAEEAaLK 1700
Cdd:TIGR02168 517 GLSGILGVLSELISVdegYEAAIEAALGGRLQAvvvenLNAAKKAIAFLKQNELGRvtflpLDSIKGTEIQGNDREI-LK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1701 QKENAEKELDKQRKFAEQ---------------------IAQQKLSAEQECI------RLKAD----FEHAEQQRGLL-- 1747
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnaLELAKKLRPGYRIvtldgdLVRPGgvitGGSAKTNSSILer 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1748 DNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM-------------KINAEKASMVNTEKSKQLLESE------- 1807
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleelsrQISALRKDLARLEAEVEQLEERiaqlske 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1808 ----ALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEA---EMALKAKEAENER 1880
Cdd:TIGR02168 756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1881 LKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSelgrqkniVEETLKQKKVVEEEIHIIKINFHKASKEKADLE 1960
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--------LEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1961 SELKKLKGIADETQKSKLKAEEEAEKLK--------KLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERL 2029
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
157-256 |
4.96e-25 |
|
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: 102.25 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 157 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPE 236
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1389908282 237 D-VDVPHPDEKSIITYVSSLY 256
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
156-256 |
6.93e-25 |
|
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: 101.73 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 235
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1389908282 236 EDV---DVphPDEKSIITYVSSLY 256
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
143-256 |
8.29e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 102.50 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 143 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 222
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908282 223 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 256
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1623-2461 |
8.61e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.77 E-value: 8.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1623 EEA---DKLKKQQKEANTAREEAEQEL--------EIWRQKAnealRLRLQAE--EEAQKKSHAQEEAEKQKLEAERDAK 1689
Cdd:TIGR02168 162 EEAagiSKYKERRKETERKLERTRENLdrledilnELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1690 KRgKAEEAALKQKENAEKELDKQRKFAEqiAQQKLSaEQECIRLKADFEHAEQQRGLLD--NELQRLKNEVNSTEKQRKQ 1767
Cdd:TIGR02168 238 RE-ELEELQEELKEAEEELEELTAELQE--LEEKLE-ELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1768 LEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAE 1847
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKE----ELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1848 KILKEKLAAINEATRLKTEAEMAlkakEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLqtssdselgrqkni 1927
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERL----EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEEL-------------- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1928 vEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKR 2007
Cdd:TIGR02168 450 -EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2008 ITAAEE---------------------EAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQ 2066
Cdd:TIGR02168 529 ISVDEGyeaaieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2067 KAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALL--------------------RQKAEEAEKQKKA 2126
Cdd:TIGR02168 609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2127 AENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDK 2206
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2207 QKVLLDQELQRVKGEVNdafKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLAE 2284
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIE---ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2285 EAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD 2364
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2365 KETEGFQKsLEAERKRQLEASAEAEKLklrvkELSLAQTKAEDEAKKFKKQADEVKaQLQRTEKHTTEIVVQKLETQRLQ 2444
Cdd:TIGR02168 926 QLELRLEG-LEVRIDNLQERLSEEYSL-----TLEEAEALENKIEDDEEEARRRLK-RLENKIKELGPVNLAAIEEYEEL 998
|
890
....*....|....*..
gi 1389908282 2445 STREaDDLKSAIADLEE 2461
Cdd:TIGR02168 999 KERY-DFLTAQKEDLTE 1014
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
43-140 |
1.54e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 100.85 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 43 KTFTKWVNKHLVKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 118
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1389908282 119 NDDIADGnPKLTLGLIWTIILH 140
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
156-260 |
2.52e-24 |
|
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: 100.25 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 235
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1389908282 236 EDVDVPHPDEKSIITYVSSLYDVMP 260
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
155-261 |
2.56e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.44 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 155 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ--ENLEQAFSVAERELGVTK 231
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDklENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1389908282 232 -LLDPEDVDvpHPDEKSIITYVSSLYDVMPR 261
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1759-2558 |
6.48e-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: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1759 NSTEKQRKQLEDELNKVRSEMDSLlqmKINAEKAsmvntEKSKQLleSEALKMKQLADEAARMRSvAEEAKKQRQIAEEE 1838
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSL---ERQAEKA-----ERYKEL--KAELRELELALLVLRLEE-LREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1839 AARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssd 1918
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1919 sELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIAD---ETQKSKLKAEEEAE-----KLKKL 1990
Cdd:TIGR02168 327 -ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqlETLRSKVAQLELQIaslnnEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1991 AAEEERRRKEAEEKVKRITAAEEEAAR-QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQ 2069
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2070 DVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEkeaaLLRQKAEEAEKQKKAAE--------------NEAAKQA 2135
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG----VLSELISVDEGYEAAIEaalggrlqavvvenLNAAKKA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2136 KA---QNDTEKQ-----RKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAE-----------------QALQQKSQV 2190
Cdd:TIGR02168 562 IAflkQNELGRVtflplDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddldNALELAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2191 EKELTVVKLQLD-------------ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEEL----VKLKLKI 2253
Cdd:TIGR02168 642 RPGYRIVTLDGDlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELeeelEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2254 EEENRRLmqkdkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKA 2333
Cdd:TIGR02168 722 EELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2334 EAEKLQKQKDQAQETAKRLQEDKQQIQQRLD---KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAK 2410
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLEsleRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2411 KFKKQADEVKAQLQ--RTEKHTTEIVVQKLETQRLQSTREADDLKSAIADleeerkklkkeaeelqrkskemANAQQEQI 2488
Cdd:TIGR02168 877 ALLNERASLEEALAllRSELEELSEELRELESKRSELRRELEELREKLAQ----------------------LELRLEGL 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2489 EQQKAELQQSFLTEKGLLL-----------KREKEVEGEKKRFEKQLE----------DEMKKAKALKDEQERQRKLMEE 2547
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLeeaealenkieDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERYDFLTAQKEDLTE 1014
|
890
....*....|.
gi 1389908282 2548 ERKKLQAIMDE 2558
Cdd:TIGR02168 1015 AKETLEEAIEE 1025
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
40-143 |
6.95e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 99.28 E-value: 6.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 40 VQKKTFTKWVNKHLVKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 115
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHFQI 143
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
143-256 |
2.64e-23 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 98.22 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 143 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 222
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908282 223 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 256
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1329-2195 |
7.77e-23 |
|
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: 108.52 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1329 QEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALEL 1408
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1409 -KMKMKEEASKRQDVAADAEKQKQN---------IQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK 1478
Cdd:pfam02463 246 lRDEQEEIESSKQEIEKEEEKLAQVlkenkeeekEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1479 TTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQ----RALDDLQ 1554
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEeeleLKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1634
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1635 ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1714
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1715 FAEQIAQQKLSAEQECIRLKADFE----HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAE 1790
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLplksIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1791 KASMVNTEKSKQLLESEALKMKQLADeaaRMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEma 1870
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSEL---TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE-- 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1871 lkakEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGR---QKNIVEETLKQKKVVEEEIHIIKI 1947
Cdd:pfam02463 721 ----ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELslkEKELAEEREKTEKLKVEEEKEEKL 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1948 NFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVE 2027
Cdd:pfam02463 797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2028 RLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQ----KAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAK 2103
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKeneiEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2104 EKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADA---EMSKHKKEA 2180
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLElfvSINKGWNKV 1036
|
890
....*....|....*
gi 1389908282 2181 EQALQQKSQVEKELT 2195
Cdd:pfam02463 1037 FFYLELGGSAELRLE 1051
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
159-259 |
1.13e-22 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 95.61 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 159 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPEDV 238
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1389908282 239 DVPHPDEKSIITYVSSLYDVM 259
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1862-2428 |
1.42e-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: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1862 RLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdsELGRQKNIVEETLKQKKvveEE 1941
Cdd:COG1196 204 PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE-----ELEAELAELEAELEELR---LE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1942 IHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKlaaeeerRRKEAEEKVKRITAAEEEAARQCKA 2021
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2022 AQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEK 2101
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2102 AKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQ---KQQADAEMSKHKK 2178
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2179 EAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVR------IQMEELVKLKLK 2252
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratfLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2253 IEEENRRLMQKDKDSTQKLLAEEAEKMKSL-------------AEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILK 2319
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLgdtllgrtlvaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2320 EKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELS 2399
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580
....*....|....*....|....*....
gi 1389908282 2400 LAQTKAEDEAkkfKKQADEVKAQLQRTEK 2428
Cdd:COG1196 749 EEEALEELPE---PPDLEELERELERLER 774
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1487-2355 |
2.18e-22 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 106.98 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1487 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSdAEKEAAKQKQRALDDLQKYKMQAE----- 1561
Cdd:pfam02463 197 LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL-RDEQEEIESSKQEIEKEEEKLAQVlkenk 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1562 EAERRMKQAEEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1641
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAK--EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1642 AEQELEiwrqkanealrlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQrkfaEQIAQ 1721
Cdd:pfam02463 354 EEEEEE--------------ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL----LELAR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1722 QKLSAEQECIRLKADFEHAEQQRGLLDnelQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSK 1801
Cdd:pfam02463 416 QLEDLLKEEKKEELEILEEEEESIELK---QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1802 QLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEaaRQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERL 1881
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG--RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1882 KRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLqtssDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLES 1961
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPI----LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1962 ELKKLKGIA-DETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQK 2040
Cdd:pfam02463 647 GLRKGVSLEeGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2041 ekaekeaekqvvlaKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEA 2120
Cdd:pfam02463 727 --------------VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2121 EKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKqqadAEMSKHKKEAEQALQQKSQVEKELTVVKLQ 2200
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL----ALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2201 LDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMK 2280
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 2281 SLAEEAgRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED 2355
Cdd:pfam02463 949 EKEENN-KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1959-2558 |
3.60e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1959 LESELKKLKGIADETQKSK-LKAEE---EAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAE 2034
Cdd:COG1196 198 LERQLEPLERQAEKAERYReLKEELkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2035 DANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLR 2114
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2115 QKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKEL 2194
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2195 TVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDST-QKLLA 2273
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2274 EEAEKMKSLAEEAGRLSVE--AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLkaEAEKLQKQKDQAQETAKR 2351
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2352 LQEDKQQIQQRLDKETEGFQKSLEA-------ERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQ 2424
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDtllgrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2425 RTEKHTTEIVVQKL-ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEK 2503
Cdd:COG1196 676 EAEAELEELAERLAeEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 2504 GLLLKREKEVEGEKKRFEKQLE----------DEMKKAKALKDEQERQRKLMEEERKKLQAIMDE 2558
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIEE 820
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
160-258 |
4.28e-22 |
|
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: 93.95 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 160 KLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD-PEDV 238
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1389908282 239 DVPHPDEKSIITYVSSLYDV 258
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
39-144 |
5.03e-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: 94.76 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 39 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHFQIS 144
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1424-2365 |
5.28e-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: 5.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1424 ADAEKQKQNIQQELQHL-KSLSDQEIKSKNQQLEDALVSRRKIEEeihiiriQLEKTTAHKAKSEAELQELRDRAAEAEK 1502
Cdd:TIGR02168 209 AEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEE-------ELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1503 LRKAAQDEAERLRKQVAEETQRKKnaedelkrksdaekEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvve 1582
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQ--------------ILRERLANLERQLEELEAQLEELESKLDELAEE--------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1583 evaqksaATQLQTKAMSFSEQTTKLEESLKKEQGnvlKLQEEADKLKKQQKEANTAREEAEQELEiwRQKANEALRLRLQ 1662
Cdd:TIGR02168 339 -------LAELEEKLEELKEELESLEAELEELEA---ELEELESRLEELEEQLETLRSKVAQLEL--QIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1663 AEEEAQKKSHAQEEAEKQKLEaerdakkrgkaEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQ 1742
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELL-----------KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1743 QRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMK-INAEKASMVNTEKSKQLLESEALkmkqladeAARM 1821
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgILGVLSELISVDEGYEAAIEAAL--------GGRL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1822 RSV----AEEAKKQRQ-IAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnerlkrQAEEEAyqRKLLE 1896
Cdd:TIGR02168 548 QAVvvenLNAAKKAIAfLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKL--RKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1897 DQAAQHK--QDIEEKITQLqtssdSELGRQKNIVeeTLKQKKV---------VEEEIHII---KINFHKASKEKADLESE 1962
Cdd:TIGR02168 620 YLLGGVLvvDDLDNALELA-----KKLRPGYRIV--TLDGDLVrpggvitggSAKTNSSIlerRREIEELEEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1963 LKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEK 2042
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2043 AEKeaekqvvLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEK 2122
Cdd:TIGR02168 773 AEE-------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2123 QKKAAENEAAKQAKAQNDTEKQRkeaeeeaARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLD 2202
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2203 ETDKQKVLLDQELQRVKGEVNDAFKQKSqvevelARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLlaeeaekmksl 2282
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI----------- 981
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2283 aEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKlkaeaeklqkqkdqaqETAKRLQEDKQQIQQR 2362
Cdd:TIGR02168 982 -KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR----------------EARERFKDTFDQVNEN 1044
|
...
gi 1389908282 2363 LDK 2365
Cdd:TIGR02168 1045 FQR 1047
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
39-144 |
7.45e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.00 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 39 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHFQIS 144
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
156-254 |
1.47e-21 |
|
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: 92.30 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGKLFSAIIHKHRPALIDMN-QVYRQSNQENLEQAFSVAERELGVTKLLD 234
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNeSLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1389908282 235 PEDVDVPHPDEKSIITYVSS 254
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1518-2424 |
1.54e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 104.28 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1518 VAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvvEEVAQKSAATQLQTka 1597
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL--------ELEEEYLLYLDYLK-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1598 msfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEA 1677
Cdd:pfam02463 234 ----LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1678 EKQKLEAERDAKKRGKAEEAALKQKENAEkELDKQRKFAEQIAQQKLSAEQECIRLKadfEHAEQQRGLLDNELQRLKNE 1757
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIE-ELEKELKELEIKREAEEEEEEELEKLQ---EKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1758 VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMvNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE 1837
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK-EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1838 EAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE-AENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTS 1916
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1917 SDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK-----GIADETQKSKLKAEEEAEKLKKLA 1991
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleidPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1992 AEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDV 2071
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2072 LSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEE 2151
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2152 AARRAAAEAAALKQKQQADAEMSKHKKEAEQALQqksQVEKELTVVKLQLDETDKQKVLLDQELQrvKGEVNDAFKQKSQ 2231
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELKEEQ--KLEKLAEEELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2232 VEVELARVRIQMEELVKLKLKIEEENRRLMQK-DKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2310
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKeEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2311 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfqKSLEAERKRQLEASAEaEK 2390
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK---ERLEEEKKKLIRAIIE-ET 1015
|
890 900 910
....*....|....*....|....*....|....
gi 1389908282 2391 LKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQ 2424
Cdd:pfam02463 1016 CQRLKEFLELFVSINKGWNKVFFYLELGGSAELR 1049
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
156-255 |
4.44e-21 |
|
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: 91.00 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 235
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1389908282 236 ED-VDVPHPDEKSIITYVSSL 255
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2112-2602 |
6.10e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 6.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2112 LLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVE 2191
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2192 KELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRL------MQKDK 2265
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELaeelleALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2266 DSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQA 2345
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2346 QETAKRLQEDKQQIQQRLD------KETEGFQKSLEAERK---------------------RQLEASAEAEKLKLRVKEL 2398
Cdd:COG1196 476 EAALAELLEELAEAAARLLllleaeADYEGFLEGVKAALLlaglrglagavavligveaayEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2399 SLAQTKAEDEAKKFKK------QADEVKAQLQRTEKHTT------------EIVVQKLETQRLQSTREADDLKSAIADLE 2460
Cdd:COG1196 556 DEVAAAAIEYLKAAKAgratflPLDKIRARAALAAALARgaigaavdlvasDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2461 EERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALK--DEQ 2538
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAeaEEE 715
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 2539 ERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2602
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
801-867 |
7.26e-21 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 88.86 E-value: 7.26e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 801 QLKPRNptTPLKGKMPIQAVCDFKQMEITVHRGDECALLNNSNPFKWQVLNDTGSEASVPSICFLVP 867
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
152-259 |
8.19e-21 |
|
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: 90.39 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 152 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTK 231
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1389908282 232 LLDPEDV-DVPHPDEKSIITYVSSLYDVM 259
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
156-256 |
1.91e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 89.32 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 235
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1389908282 236 EDVDV--PHPDEKSIITYVSSLY 256
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1768-2388 |
2.43e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1768 LEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAK-------KQRQIAEEEAA 1840
Cdd:COG1196 191 LEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEaeleeleAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1841 RQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdsE 1920
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-----E 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1921 LGRQKNIVEETLKQKKVVEEEIhiikinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKE 2000
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEAL-------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2001 AEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDvlSKNKEDVL 2080
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE--AAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2081 AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAE--------NEAAKQAKAQNDTEKQRKEAEEEA 2152
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqnivVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2153 ARRAAAEAAALKQKQQADAEMSKH-------KKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGE---V 2222
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAvdlvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2223 NDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQI 2302
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2303 AESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQ-------AQETAKRLQEDKQQIQQRLD------KETEG 2369
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREdleearETLEE 816
|
650
....*....|....*....
gi 1389908282 2370 FQKSLEAERKRQLEASAEA 2388
Cdd:COG1196 817 AIEEIDRETRERFLETFDA 835
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1368-2069 |
6.11e-20 |
|
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: 98.89 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1368 KLKEEERRKMAEIQAELDKQKQMA--------EAHAKSVAKAEQEALE--LKMKMKEEASKRQDVAADAEKQKQNIQQEL 1437
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLAlmefakkkSLHGKAELLTLRSQLLtlCTPCMPDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1438 QHLKSLSDQEIKSKNQQLedalvsrrKIEEEIHIIRIQLEKTTAHKAKSEaELQELRDRAAEAEKLrKAAQDEAERLRKQ 1517
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQL--------KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPL-AAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1518 VAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQirvveevAQKSAATQLQTKA 1597
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR-------EISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1598 MSFSEQTTKLEESLKKEQGNVLKLQEEAdklkkQQKEANTAREEAEQEleiwrQKANEALRLRLQAEEEAQKKSHAQEEA 1677
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQ-----ATIDTRTSAFRDLQG-----QLAHAKKQQELQQRYAELCAAAITCTA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1678 EKQKLE--AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqkLSAEQECIrLKADFEHAEQQRGLLDN------ 1749
Cdd:TIGR00618 452 QCEKLEkiHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL--ELQEEPCP-LCGSCIHPNPARQDIDNpgpltr 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1750 --------------ELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEaLKMKQLA 1815
Cdd:TIGR00618 529 rmqrgeqtyaqletSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ-CDNRSKEDIPNLQNITVRLQDL-TEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1816 DEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAineatrLKTEAEMALKAKEAENERLKRQAEEEAYQRKLL 1895
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA------LHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1896 EDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQkkvveeeIHIIKINFHKASKEKADLESELKKLKGIADETQK 1975
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE-------FNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1976 SKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRitaaeeEAARQCKAAQEEVERLK-KKAEDANKQKEKAEKEAEKQVVLA 2054
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAA------EIQFFNRLREEDTHLLKtLEAEIGQEIPSDEDILNLQCETLV 827
|
730
....*....|....*
gi 1389908282 2055 KEAAQKCTAAEQKAQ 2069
Cdd:TIGR00618 828 QEEEQFLSRLEEKSA 842
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
159-255 |
8.73e-20 |
|
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: 86.99 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 159 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ----ENLEQAFSVAERELGVTKLLD 234
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1389908282 235 PEDVDVPHPDEKSIITYVSSL 255
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
156-255 |
1.90e-19 |
|
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: 86.44 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 235
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1389908282 236 ED-VDVPHPDEKSIITYVSSL 255
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2273-2594 |
4.54e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.77 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2273 AEEAEKMKSLAEEAGRLsvEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2352
Cdd:COG1196 209 AEKAERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2353 QEDKQQIQQRLDKEtegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTE 2432
Cdd:COG1196 287 QAEEYELLAELARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2433 IVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQ-QEQIEQQKAELQQSFLTEKGLLLKREK 2511
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2512 EVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQL 2591
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
...
gi 1389908282 2592 AEE 2594
Cdd:COG1196 523 AGA 525
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
41-141 |
5.91e-19 |
|
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: 84.94 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 41 QKKTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 116
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1389908282 117 IRNDDIADGNPKLTLGLIWTIILHF 141
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1354-2451 |
7.18e-19 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 95.24 E-value: 7.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1354 DAQRRLEDDEKASEKLkEEERRKMAEIQAELDKQKQMAEAhAKSVAKAEQEALELKMK-MKEEASKRQDVAADAEKQKQN 1432
Cdd:pfam01576 79 ELESRLEEEEERSQQL-QNEKKKMQQHIQDLEEQLDEEEA-ARQKLQLEKVTTEAKIKkLEEDILLLEDQNSKLSKERKL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1433 IQQELQHLKS-LSDQEIKSKNqqledalvsrrkieeeihiiriqlekTTAHKAKSEAELQELRDRAAEAEKLRkaaqdea 1511
Cdd:pfam01576 157 LEERISEFTSnLAEEEEKAKS--------------------------LSKLKNKHEAMISDLEERLKKEEKGR------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1512 ERLRKqvaeetqrkknaedeLKRKSDAEkeaAKQKQRALDDLQkykMQAEEAERRMKQAEEE-KIRQIRVVEEVAQKSAA 1590
Cdd:pfam01576 204 QELEK---------------AKRKLEGE---STDLQEQIAELQ---AQIAELRAQLAKKEEElQAALARLEEETAQKNNA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1591 tqlqtkamsfseqttklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRlRLQAEEEAQKK 1670
Cdd:pfam01576 263 -----------------LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLD-TTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1671 SHAQEEAEKQKLEAErdaKKRGKAEEAALKQKENA-----EKELDKQRKFAEQIAQQKLSAEQECIRLKADFE------- 1738
Cdd:pfam01576 325 REQEVTELKKALEEE---TRSHEAQLQEMRQKHTQaleelTEQLEQAKRNKANLEKAKQALESENAELQAELRtlqqakq 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1739 HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASmVNTEKSKQLLESEALKMKQLADEA 1818
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKN-IKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1819 ARMRsvAEEAKKQRQIAEEEAArqrseaekiLKEKLAAINEATRlktEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQ 1898
Cdd:pfam01576 481 TRQK--LNLSTRLRQLEDERNS---------LQEQLEEEEEAKR---NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1899 AAQHKQDIEEKITQLQTSSDSelgrqkniVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKL 1978
Cdd:pfam01576 547 KKRLQRELEALTQQLEEKAAA--------YDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1979 KAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLkkkaedankqkekaekeaekqvVLAKEAA 2058
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL----------------------VSSKDDV 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2059 QKCTAAEQKAQDVLSKNKEDVLAQ-EKLRDEF---ENAKklaqeaekakekaekeaalLRQkaeEAEKQKKAAENEAAKQ 2134
Cdd:pfam01576 677 GKNVHELERSKRALEQQVEEMKTQlEELEDELqatEDAK-------------------LRL---EVNMQALKAQFERDLQ 734
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2135 AKAQNDTEKQRkeaeeeaarraaaeaAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQE 2214
Cdd:pfam01576 735 ARDEQGEEKRR---------------QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ 799
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2215 LQRVKGEVNDAfkQKSQVEVELARVRI------------QME-ELVKLK--LKIEEENRRLMQKDKDSTQKLLAEEAEKM 2279
Cdd:pfam01576 800 LKKLQAQMKDL--QRELEEARASRDEIlaqskesekklkNLEaELLQLQedLAASERARRQAQQERDELADEIASGASGK 877
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2280 KSLAEEAGRLSveaeetARQRQIAESNLAEQ---RALAEKILKEKMQAIQEATKLKAEAEKLQKQKD-------QAQETA 2349
Cdd:pfam01576 878 SALQDEKRRLE------ARIAQLEEELEEEQsntELLNDRLRKSTLQVEQLTTELAAERSTSQKSESarqqlerQNKELK 951
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2350 KRLQEDKQQIQQR-------LDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQAD----- 2417
Cdd:pfam01576 952 AKLQEMEGTVKSKfkssiaaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEkgnsr 1031
|
1130 1140 1150
....*....|....*....|....*....|....*..
gi 1389908282 2418 --EVKAQLQRTEKHTTEIVVQKLETQR-LQSTREADD 2451
Cdd:pfam01576 1032 mkQLKRQLEEAEEEASRANAARRKLQReLDDATESNE 1068
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1608-2569 |
1.78e-18 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 94.12 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1608 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALR------------LRLQAEeeaQKKSHAQE 1675
Cdd:NF041483 7 QESHRADDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAE---QLLRNAQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1676 EAEKQKLEAERdakkrgkaeeaalkqkenaekELDKQRKFAEQIAQqklsaeqecirlkadfEHAEQQrglldnelQRLK 1755
Cdd:NF041483 84 QADQLRADAER---------------------ELRDARAQTQRILQ----------------EHAEHQ--------ARLQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1756 NEVNSTEKQRKQ-LEDELNKVRSEMDSLLQMKIN-AEKASMVNTEKSKQLL-ESEALKMKQLADEAARMRSVAEEAKkQR 1832
Cdd:NF041483 119 AELHTEAVQRRQqLDQELAERRQTVESHVNENVAwAEQLRARTESQARRLLdESRAEAEQALAAARAEAERLAEEAR-QR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1833 QIAEEEAARqrSEAEKILK------EKL--AAINEATRLKTEAEMALKAKEAENERLKRQAEEeayqrklLEDQAAQHKQ 1904
Cdd:NF041483 198 LGSEAESAR--AEAEAILRrarkdaERLlnAASTQAQEATDHAEQLRSSTAAESDQARRQAAE-------LSRAAEQRMQ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1905 DIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEihiikiNFHKASKEKADLESE-LKKLKGIADETQKSKLKAEEE 1983
Cdd:NF041483 269 EAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQ------RTRTAKEEIARLVGEaTKEAEALKAEAEQALADARAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1984 AEKLkklaaeeerrrKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAekeaekqvvlAKEAAQKCTA 2063
Cdd:NF041483 343 AEKL-----------VAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAA----------AEEAERIRRE 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2064 AEQKAqDVLSKNKEDVLAQEK---LRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQND 2140
Cdd:NF041483 402 AEAEA-DRLRGEAADQAEQLKgaaKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAAR 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2141 TEKQrkeaeeeaarraaaeaaaLKQKQQADAEMSKHKKEAEQALQQKSQVEKElTVVKLQLDETdkqkvlldqeLQRVKG 2220
Cdd:NF041483 481 TAEE------------------LLTKAKADADELRSTATAESERVRTEAIERA-TTLRRQAEET----------LERTRA 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2221 EvndAFKQKSQVEVELARVRIQMEELVKlklKIEEENRRLMQkdkdstqkllAEEAEKmkslAEEAGRLSVEAEEtarQR 2300
Cdd:NF041483 532 E---AERLRAEAEEQAEEVRAAAERAAR---ELREETERAIA----------ARQAEA----AEELTRLHTEAEE---RL 588
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2301 QIAESNLAEQRALAEKILKEkmqAIQEATKLKAEA-EKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFqksleAERK 2379
Cdd:NF041483 589 TAAEEALADARAEAERIRRE---AAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASAARAEGENV-----AVRL 660
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2380 RQlEASAEAEKLKLRVKEL-----SLAQTKAE---DEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADD 2451
Cdd:NF041483 661 RS-EAAAEAERLKSEAQESadrvrAEAAAAAErvgTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEE 739
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2452 -LKSAIADLEEERKKLKKEAEELQRKSKEMANAqQEQIEQQKAElqqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKK 2530
Cdd:NF041483 740 lLASARKRVEEAQAEAQRLVEEADRRATELVSA-AEQTAQQVRD------SVAGLQEQAEEEIAGLRSAAEHAAERTRTE 812
|
970 980 990
....*....|....*....|....*....|....*....
gi 1389908282 2531 AkalKDEQERQRKLMEEERKKLQaimDEAVRKQKEAEEE 2569
Cdd:NF041483 813 A---QEEADRVRSDAYAERERAS---EDANRLRREAQEE 845
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1640-2449 |
4.16e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.82 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1640 EEAEQELEIWRQKANEalrLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQI 1719
Cdd:TIGR02169 180 EEVEENIERLDLIIDE---KRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1720 AQQKLSAEQECIRLKADFEHAEQQ-RGLLDNELQRLKNEVNSTEKQRKQLEdelnkvRSEMDSLLQMKINAEKASMVNTE 1798
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLE------RSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1799 KSKQLLESEALKmKQLADEAARMRSVAEEAKKqrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMaLKAKEAEN 1878
Cdd:TIGR02169 331 IDKLLAEIEELE-REIEEERKRRDKLTEEYAE----LKEELEDLRAELEEVDKEFAETRDELKDYREKLEK-LKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1879 ERLKRQAEEEAYQrklLEDQAAQHKQDI---EEKITQLQTSSDS---ELGRQKNIVEETLKQKKVVEEEIHIIKINFHKA 1952
Cdd:TIGR02169 405 KRELDRLQEELQR---LSEELADLNAAIagiEAKINELEEEKEDkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1953 SKEKADLESELKKLkgiadETQKSKLKAEEE----AEKLKKLAAEEERRRKEAEEKVKR--ITAAEEEAARQCKA----- 2021
Cdd:TIGR02169 482 EKELSKLQRELAEA-----EAQARASEERVRggraVEEVLKASIQGVHGTVAQLGSVGEryATAIEVAAGNRLNNvvved 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2022 ---AQEEVERLK-KKAEDA-----NKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKnkedVLAQEKLRDEFENA 2092
Cdd:TIGR02169 557 davAKEAIELLKrRKAGRAtflplNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKY----VFGDTLVVEDIEAA 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2093 KKLAQEA-------------------EKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAA 2153
Cdd:TIGR02169 633 RRLMGKYrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2154 RRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDafkqksqVE 2233
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND-------LE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2234 VELARVRIQmeELVKLKLKIEEENRRLMQKDKDSTQKL----LAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESN--L 2307
Cdd:TIGR02169 786 ARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLnrltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2308 AEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQ------KSLEAERKRQ 2381
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleeelSEIEDPKGED 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2382 LEASAE---AEKLKLRVKELSLA-------QTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV--VQKLETQRLQSTREA 2449
Cdd:TIGR02169 944 EEIPEEelsLEDVQAELQRVEEEiralepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILerIEEYEKKKREVFMEA 1023
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1341-1990 |
5.55e-18 |
|
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: 92.55 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1341 LMTLTNQYIKFIIDAQRRLEDDEKAS---EKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEAS 1417
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRqelEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1418 KRqdvaadAEKQKQNiqQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahkaKSEAELQELRD-R 1496
Cdd:pfam01576 258 QK------NNALKKI--RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSkR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1497 AAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaeKEAAKQKQRALDDLQKYKmQAEEAERRMKQAEEEKIR 1576
Cdd:pfam01576 326 EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------TEQLEQAKRNKANLEKAK-QALESENAELQAELRTLQ 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1577 QIRVVEEVAQKSAATQLQTKAMSFSE---QTTKLEESLKKEQG---NVLKLQEEAD-KLKKQQKEANTAREEAE--QEL- 1646
Cdd:pfam01576 398 QAKQDSEHKRKKLEGQLQELQARLSEserQRAELAEKLSKLQSeleSVSSLLNEAEgKNIKLSKDVSSLESQLQdtQELl 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1647 -EIWRQKANEALRLRlQAEEEAQKKSHAQEEAEKQKLEAERdakkrgkaeeaalkQKENAEKELDKQRKFAEQIAQQKLS 1725
Cdd:pfam01576 478 qEETRQKLNLSTRLR-QLEDERNSLQEQLEEEEEAKRNVER--------------QLSTLQAQLSDMKKKLEEDAGTLEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1726 AEQECIRLKADFEHAEQQrglldneLQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKasmvNTEKSKQLLE 1805
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQ-------LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK----KQKKFDQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1806 SEALKMKQLADEAARMRSVAEEaKKQRQI----AEEEAARQRSEAEKILKEKLAAINEATRLKT-------EAEMALKAK 1874
Cdd:pfam01576 612 EEKAISARYAEERDRAEAEARE-KETRALslarALEEALEAKEELERTNKQLRAEMEDLVSSKDdvgknvhELERSKRAL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1875 EAENERLKRQAEEeayqrklLED--QAAQH-KQDIEEKITQLQTSSDSELGRQKNIVEET----LKQKKVVEEEIHIIKI 1947
Cdd:pfam01576 691 EQQVEEMKTQLEE-------LEDelQATEDaKLRLEVNMQALKAQFERDLQARDEQGEEKrrqlVKQVRELEAELEDERK 763
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1389908282 1948 NFHKASKEKADLESELKKLKGIADETQKSKlkaEEEAEKLKKL 1990
Cdd:pfam01576 764 QRAQAVAAKKKLELDLKELEAQIDAANKGR---EEAVKQLKKL 803
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
158-256 |
8.34e-18 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 81.96 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 158 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 237
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1389908282 238 -VDVPHPDEKSIITYVSSLY 256
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
160-258 |
9.73e-18 |
|
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: 81.85 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 160 KLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD-PEDV 238
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1389908282 239 DVPHPDEKSIITYVSSLYDV 258
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1282-1969 |
1.13e-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: 91.18 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1282 DCHKNAKAYIDSVKDyEFQILTYKALQDPIASPLKKPKMEcasddiiQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLED 1361
Cdd:TIGR00618 187 AKKKSLHGKAELLTL-RSQLLTLCTPCMPDTYHERKQVLE-------KELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1362 DEKASEKLKEEER-----RKMAEIQAELDKQKQMAE--AHAKSVAKAEQEAL----ELKMKMKEEASKRQDVAAdAEKQK 1430
Cdd:TIGR00618 259 QQLLKQLRARIEElraqeAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQrihtELQSKMRSRAKLLMKRAA-HVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1431 QNIQQELQHLKSLSDQEIKSKNQQLEDALV----SRRKIEEEIHIIRIQ---------------LEKTTAHKAKSEAELQ 1491
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIreisCQQHTLTQHIHTLQQqkttltqklqslckeLDILQREQATIDTRTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1492 ELRD---RAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAE---DELKRKSDAEKEAAKQKQRALddLQKYKMQAEEAER 1565
Cdd:TIGR00618 418 AFRDlqgQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKihlQESAQSLKEREQQLQTKEQIH--LQETRKKAVVLAR 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1566 RMKQAEEEKI--RQIRVVEEVAQKSAATQLQTKAMSFSEQT-TKLEESLKKEQGNVLKLQEEADKLKKQQKEAntarEEA 1642
Cdd:TIGR00618 496 LLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQRGEQTyAQLETSEEDVYHQLTSERKQRASLKEQMQEI----QQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1643 EQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERdAKKRGKAEEAALKQK----ENAEKELdKQRKFAEQ 1718
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH-ALLRKLQPEQDLQDVrlhlQQCSQEL-ALKLTALH 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1719 IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMV-NT 1797
Cdd:TIGR00618 650 ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAsSS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1798 EKSKQLLESEAL-----KMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRL--KTEAEMA 1870
Cdd:TIGR00618 730 LGSDLAAREDALnqslkELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLlkTLEAEIG 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1871 LKAKEAENERLKRQaeeeayqrKLLEDQAAQHKQDIEEKITQLqtssdSELGRQKNIVEETLKQkkvveeeihiikinFH 1950
Cdd:TIGR00618 810 QEIPSDEDILNLQC--------ETLVQEEEQFLSRLEEKSATL-----GEITHQLLKYEECSKQ--------------LA 862
|
730
....*....|....*....
gi 1389908282 1951 KASKEKADLESELKKLKGI 1969
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKLNGI 881
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
42-139 |
1.49e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.85 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 42 KKTFTKWVNKHL-VKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 117
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1389908282 118 RNDDI-ADGNPKLTLGLIWTIIL 139
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
158-257 |
4.52e-17 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 79.62 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 158 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 237
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1389908282 238 VDV--PHPDEKSIITYVSSLYD 257
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
158-261 |
5.82e-17 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 79.32 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 158 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 237
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1389908282 238 VDV--PHPDEKSIITYVSSLYDVMPR 261
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
161-256 |
9.93e-17 |
|
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: 78.94 E-value: 9.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 161 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDPED-VD 239
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1389908282 240 VPHPDEKSIITYVSSLY 256
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1114-1989 |
2.11e-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: 87.42 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1114 ADAEETLKNYEARLRDVSKVPSeQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLRKATTVHDKMTRIHSERDADLEHYR 1193
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALL-VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1194 QLVNGLLERWQAVFAQIELRLREldllgrhMNSYRDSYEWLIRWLTEARQRQEKiqavpisdsraLREQLTDEKKLLGEI 1273
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESKLDE-----------LAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1274 EKNKDKIDDCHKNAKAyidsvkdyefqiltykalqdpiasplKKPKMECASDDIIQEYVNLRTRYSELMTLTNQYIKFII 1353
Cdd:TIGR02168 350 KEELESLEAELEELEA--------------------------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1354 DAQRRLEDDEKASEKLKEE--------ERRKMAEIQAELDKQKQMAEAHAKSVAKAEqEALELKMKMKEEASKRQDvaaD 1425
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEieellkklEEAELKELQAELEELEEELEELQEELERLE-EALEELREELEEAEQALD---A 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1426 AEKQKQNIQQELQHLKSLsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTA--HKAKSEA---ELQELRDRAAEA 1500
Cdd:TIGR02168 480 AERELAQLQARLDSLERL--QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyEAAIEAAlggRLQAVVVENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1501 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAkqkQRALDDLQKYKMQAEEAERRMKQaeeekirQIRV 1580
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF---LGVAKDLVKFDPKLRKALSYLLG-------GVLV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1581 VEEVAQksaATQLQtKAMSFSEQTTKLEESLKKEQGNVLklqeeadklkKQQKEANTAREEAEQELEIWRQKANEalrlr 1660
Cdd:TIGR02168 628 VDDLDN---ALELA-KKLRPGYRIVTLDGDLVRPGGVIT----------GGSAKTNSSILERRREIEELEEKIEE----- 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1661 lqAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHA 1740
Cdd:TIGR02168 689 --LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1741 EQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEalkmkqlADEAAR 1820
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRERLESLERR-------IAATER 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1821 MRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 1900
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1901 QHKQDIEEKITQLQTssdSELGRQKNIveETLKQKKVVEEEIHIIKINFHKASKEKAdlESELKKLKGIADETQKSKLKA 1980
Cdd:TIGR02168 919 ELREKLAQLELRLEG---LEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEA--RRRLKRLENKIKELGPVNLAA 991
|
....*....
gi 1389908282 1981 EEEAEKLKK 1989
Cdd:TIGR02168 992 IEEYEELKE 1000
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
158-256 |
3.80e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 77.43 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 158 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 237
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1389908282 238 -VDVPHPDEKSIITYVSSLY 256
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2168-2582 |
3.82e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.28 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2168 QADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLD--ETDKQKVLLDQELQRVKGEV---------NDAFKQKSQVEVEL 2236
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYegyellkekEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2237 ARVRiqmEELVKLKLKIEEENRRLMQKdkdstQKLLAEEAEKMKSLAEEagrlsveaeetarqrqiaesnlaEQRALAEK 2316
Cdd:TIGR02169 247 ASLE---EELEKLTEEISELEKRLEEI-----EQLLEELNKKIKDLGEE-----------------------EQLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2317 ILKekmqaiqeatkLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDK---ETEGFQKSLEAERKRQLEASAEAEKLKl 2393
Cdd:TIGR02169 296 IGE-----------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKllaEIEELEREIEEERKRRDKLTEEYAELK- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2394 rvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQStrEADDLKSAIADleeerkklkkeaeel 2473
Cdd:TIGR02169 364 --EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE--ELQRLSEELAD--------------- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2474 qrkskemANAQQEQIEQQKAELQqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERqrklMEEERKKLQ 2553
Cdd:TIGR02169 425 -------LNAAIAGIEAKINELE----EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQ 489
|
410 420
....*....|....*....|....*....
gi 1389908282 2554 AIMDEAVRKQKEAEEEMKNKQREMDVLDK 2582
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1568-2596 |
5.97e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 85.61 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1568 KQAEE--EKIRQIRVVEEVAQKSAA--TQLQTKAMSFSEQTTKLEESLKKEQgnvlKLQEEADKL------KKQQKEANT 1637
Cdd:pfam01576 2 RQEEEmqAKEEELQKVKERQQKAESelKELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMrarlaaRKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1638 AREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAER-DAKKRGKAEEAALKQKENAEKELDKQRKFA 1716
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvTTEAKIKKLEEDILLLEDQNSKLSKERKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1717 EQ-IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNS---TEKQRKQLEDELNKVRSEMdslLQMKINAEKA 1792
Cdd:pfam01576 158 EErISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGESTDLQEQI---AELQAQIAEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1793 SMVNTEKSKQLLESEALKMKQLADEAARMRSVAEeakKQRQIAE--EEAARQRSEAEKILKEKLAAINEATRLKTEAEMA 1870
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALKKIRE---LEAQISElqEDLESERAARNKAEKQRRDLGEELEALKTELEDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1871 LKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEkITQLQTSSDSELGRQkniVEETLKQKKVVEEEIHIIKinfh 1950
Cdd:pfam01576 312 LDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQE-MRQKHTQALEELTEQ---LEQAKRNKANLEKAKQALE---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1951 kasKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRItaaeeeaarqckaaQEEVERLK 2030
Cdd:pfam01576 384 ---SENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL--------------QSELESVS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2031 KKAEDANKQKEKaekeaekqvvLAKEAAQkctaAEQKAQDVLSknkedvLAQEKLRDEFENAKKLAQEAEKAKEkaekea 2110
Cdd:pfam01576 447 SLLNEAEGKNIK----------LSKDVSS----LESQLQDTQE------LLQEETRQKLNLSTRLRQLEDERNS------ 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2111 alLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQV 2190
Cdd:pfam01576 501 --LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2191 EKELTVVKLQLDET-------DKQKVLLDQELQRVKGEVNDAFKQKSQVEVElARVRiqmeELVKLKLKIEEENRRLMQK 2263
Cdd:pfam01576 579 QQELDDLLVDLDHQrqlvsnlEKKQKKFDQMLAEEKAISARYAEERDRAEAE-AREK----ETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2264 DKDSTQKLLAEEAEKMKSLAEEAGRlsvEAEETARQRQIAESNLAEQRALAEKiLKEKMQAIQEAtKLKAEAeKLQKQKD 2343
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGK---NVHELERSKRALEQQVEEMKTQLEE-LEDELQATEDA-KLRLEV-NMQALKA 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2344 QAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSL---AQTKAEDEA----KKFKKQA 2416
Cdd:pfam01576 728 QFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAqidAANKGREEAvkqlKKLQAQM 807
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2417 DEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLksaiadleeerkklkkeaeelqRKSKEMANA--QQEQIEQQKAE 2494
Cdd:pfam01576 808 KDLQRELEEARASRDEILAQSKESEKKLKNLEAELL----------------------QLQEDLAASerARRQAQQERDE 865
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2495 LQQ---SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEE-------ERKKLQAimDEAVRKQK 2564
Cdd:pfam01576 866 LADeiaSGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelaaERSTSQK--SESARQQL 943
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 1389908282 2565 EAE-EEMKNKQREMD------------VLDKKRLEQEKQLAEENK 2596
Cdd:pfam01576 944 ERQnKELKAKLQEMEgtvkskfkssiaALEAKIAQLEEQLEQESR 988
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1364-2029 |
6.73e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1364 KASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQdvaadaekqkQNIQQELQHLKS- 1442
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ----------LRVKEKIGELEAe 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1443 --LSDQEIKSKNQQLEDALVSRRKieeeihiIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAE 1520
Cdd:TIGR02169 303 iaSLERSIAEKERELEDAEERLAK-------LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1521 ETQRKKNAEDELK---RKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVaqksaatqLQTKA 1597
Cdd:TIGR02169 376 VDKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE--------KEDKA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1598 MSFSEQTTKLE---ESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL------------- 1661
Cdd:TIGR02169 448 LEIKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgtv 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1662 ----QAEEEAQKkshAQEEAEKQKLEA-----ERDAK------KRGKAEEAA---LKQKENAEKELDKQRK--------- 1714
Cdd:TIGR02169 528 aqlgSVGERYAT---AIEVAAGNRLNNvvvedDAVAKeaiellKRRKAGRATflpLNKMRDERRDLSILSEdgvigfavd 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1715 ---FAEQIAqqklSAEQECIRLKADFEHAEQQRGLLDN------------------------------------ELQRLK 1755
Cdd:TIGR02169 605 lveFDPKYE----PAFKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfeksgamtggsraprggilfsrsepaELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1756 NEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAK------ 1829
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvkse 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1830 ----------KQRQIAEEEAAR---QRSEAEKILKEKLAAIN--EATRLKTEA-----EMALKAKEAENERLKRQAEEEA 1889
Cdd:TIGR02169 760 lkelearieeLEEDLHKLEEALndlEARLSHSRIPEIQAELSklEEEVSRIEArlreiEQKLNRLTLEKEYLEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1890 YQRKLLEDQAAQHKQDIEEKITQLQtSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGI 1969
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1970 ADETqksKLKAEEEAEKLKKLAAEEERRRKEAEEkvkriTAAEEEAARQCKAAQEEVERL 2029
Cdd:TIGR02169 919 LSEL---KAKLEALEEELSEIEDPKGEDEEIPEE-----ELSLEDVQAELQRVEEEIRAL 970
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
38-137 |
1.05e-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: 76.03 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 38 DRVQKKTFTKWVNKHLVKAQ-RHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 112
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1389908282 113 KLVNIRNDDIADGNPKLTLGLIWTI 137
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
156-253 |
1.54e-15 |
|
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: 75.11 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLD 234
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1389908282 235 PEDVDVPHPDEKSIITYVS 253
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1498-2194 |
1.73e-15 |
|
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: 84.25 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1498 AEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAA------KQKQRALDDLQKYKMQAEEAERRMKQAE 1571
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQqshaylTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1572 ---------EEKIRQIRVVEEVAQKSAAT-----QLQTKAMSFSEQTTKLEESLKKEQGNV---LKLQEEADKLKKQQKE 1634
Cdd:TIGR00618 274 aqeavleetQERINRARKAAPLAAHIKAVtqieqQAQRIHTELQSKMRSRAKLLMKRAAHVkqqSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1635 ANTAREEAEQELeIWRQKANEALRLRLQAEEEAQKKSHA------------QEEAEKQKLEAERDAKKRGKAEEAALKQK 1702
Cdd:TIGR00618 354 EIHIRDAHEVAT-SIREISCQQHTLTQHIHTLQQQKTTLtqklqslckeldILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1703 ENAEKE-LDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKnEVNSTEKQRKQLEDELNKVRSEMDS 1781
Cdd:TIGR00618 433 QELQQRyAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1782 LLQMKINAEKASMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAT 1861
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQ----TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1862 RLKTEAEMALKAKEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQkkvvEEE 1941
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQ--HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE----RVR 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1942 IHIIKINFHKASK------EKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEA 2015
Cdd:TIGR00618 662 EHALSIRVLPKELlasrqlALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2016 ARQCKAAQEEverlkkkaedankqkekaekeaekqvvlAKEAAQKCTAAEQkaqdvlsKNKEDVLAQEKLRDEFENakkL 2095
Cdd:TIGR00618 742 NQSLKELMHQ----------------------------ARTVLKARTEAHF-------NNNEEVTAALQTGAELSH---L 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2096 AQEAEKAKEKAEKEAALLRQKaeEAEKQKKAAENEAAKQakAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSK 2175
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTL--EAEIGQEIPSDEDILN--LQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK 859
|
730
....*....|....*....
gi 1389908282 2176 HKKEAEQALQQKSQVEKEL 2194
Cdd:TIGR00618 860 QLAQLTQEQAKIIQLSDKL 878
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1538-2557 |
2.10e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.94 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1538 AEKEAAKQKQRALDDLQKYkMQAEEAERRMKQAEEEKIRqirvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGN 1617
Cdd:TIGR00606 166 SEGKALKQKFDEIFSATRY-IKALETLRQVRQTQGQKVQ-----EHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1618 VLKLQEEADKLKKQQKEANTARE---EAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEaEKQKLEAERDAKKRGKA 1694
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSkimKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE-QLNDLYHNHQRTVREKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1695 EEAALKQKE----NAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEV-------NSTEK 1763
Cdd:TIGR00606 319 RELVDCQREleklNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPfserqikNFHTL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1764 QRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKK----QRQIAEEEA 1839
Cdd:TIGR00606 399 VIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1840 ARQRSEAEKILKEKlaaiNEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhkqdiEEKITQLQTSSDS 1919
Cdd:TIGR00606 479 ELRKAERELSKAEK----NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ-----MEMLTKDKMDKDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1920 ELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKlaaeeerrrk 1999
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE---------- 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2000 eaeekvkRITAAEEEAARQCKAAQEEV--ERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTA----------AEQK 2067
Cdd:TIGR00606 620 -------QLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2068 AQDVLSK-NKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRK 2146
Cdd:TIGR00606 693 LQEFISDlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2147 EAEEEAARRAaaeaaaLKQKQQADAEMskhkkeAEQALQQKSQVEKELTVVKLQLDETDkqkvlLDQELQRVKGEVNDaf 2226
Cdd:TIGR00606 773 LLGTIMPEEE------SAKVCLTDVTI------MERFQMELKDVERKIAQQAAKLQGSD-----LDRTVQQVNQEKQE-- 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2227 kqksqvevelarvriQMEELVKLKLKIEEeNRRLMQKDKDSTQKLlaeeaekmKSLAEEAGRLSVEAEETARQRQIAESN 2306
Cdd:TIGR00606 834 ---------------KQHELDTVVSKIEL-NRKLIQDQQEQIQHL--------KSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2307 LAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQ---AQETAKRLQEDKQQIQQRLDKETEGFQKSLEaerkrqle 2383
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEElisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE-------- 961
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2384 asaeaeklklrvkelSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEI------VVQKLETQRLQSTREADDLKSAIA 2457
Cdd:TIGR00606 962 ---------------NKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKInedmrlMRQDIDTQKIQERWLQDNLTLRKR 1026
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2458 DLEEERKKLKKEAEELQrkSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLedemkKAKALKDE 2537
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL-----REPQFRDA 1099
|
1050 1060
....*....|....*....|
gi 1389908282 2538 QERQRKLMEEERKKLQAIMD 2557
Cdd:TIGR00606 1100 EEKYREMMIVMRTTELVNKD 1119
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
156-256 |
2.30e-15 |
|
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: 75.11 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 235
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1389908282 236 ED-VDVPHPDEKSIITYVSSLY 256
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1796-2560 |
2.46e-15 |
|
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: 83.86 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1796 NTEKSKQLLEsEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE 1875
Cdd:TIGR00618 161 KSKEKKELLM-NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1876 AENERLkRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLqtssdSELGRQKNIVEETLKQKKVVEEEIHIIKINFhKASKE 1955
Cdd:TIGR00618 240 QSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAAHIKAVTQIEQ-QAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1956 KADLESELKKLKGIADETQKSkLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQckaaQEEVERLKKKAED 2035
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAH-VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ----HTLTQHIHTLQQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2036 ANKQKEKAEKEAEKQVVLAKEAAQkcTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQ 2115
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQAT--IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2116 KAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELT 2195
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2196 VVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVEL-------ARVRIQMEELVKLKLKIEEENRRLMQK--DKD 2266
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpnlqnitVRLQDLTEKLSEAEDMLACEQHALLRKlqPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2267 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQ--------IAESNLAEQRALAEKILKEKMQAI--------QEATK 2330
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVrehalsirVLPKELLASRQLALQKMQSEKEQLtywkemlaQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2331 LKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgFQKSLEAERKRQLEASAEAEK---LKLRVKELSLAQ-TKAE 2406
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFnnnEEVTAALQTGAElSHLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2407 DEAKKFKKQADEVKAQLQRTE-KHTTEI--VVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKemana 2483
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEaEIGQEIpsDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK----- 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2484 QQEQIEQQKAELQQsflTEKGLLLKREKEVEGEKKRFEKQLEDEM-KKAKALKDEQERQ---RKLMEEERKKLQAIMDEA 2559
Cdd:TIGR00618 860 QLAQLTQEQAKIIQ---LSDKLNGINQIKIQFDGDALIKFLHEITlYANVRLANQSEGRfhgRYADSHVNARKYQGLALL 936
|
.
gi 1389908282 2560 V 2560
Cdd:TIGR00618 937 V 937
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1432-1760 |
2.54e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 83.25 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1432 NIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQElrdRAAEAEKLRKAAQD-E 1510
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME---RERELERIRQEERKrE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1511 AERLRKQ-VAEETQRKKnaedELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkIRQIRVVEEVAQKSA 1589
Cdd:pfam17380 362 LERIRQEeIAMEISRMR----ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE-MEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1590 ATQLQTKAMSFSEQTtKLEESLKKEQGNVLKLQEEADKLKKQQKEantaREEAEqeleiwRQKANEALRLRLQAEEEAQK 1669
Cdd:pfam17380 437 VRRLEEERAREMERV-RLEEQERQQQVERLRQQEEERKRKKLELE----KEKRD------RKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1670 KSHAQEEAEKQKLEAERDAK--------KRGKAEEAALKQKENAEKeldkqrkfaEQIAQQKLSAEQECIRLKADFEHAE 1741
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERqkaiyeeeRRREAEEERRKQQEMEER---------RRIQEQMRKATEERSRLEAMERERE 576
|
330
....*....|....*....
gi 1389908282 1742 QQRGLLDNELQRLKNEVNS 1760
Cdd:pfam17380 577 MMRQIVESEKARAEYEATT 595
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1361-1785 |
2.65e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.55 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1361 DDEKASEKLKEEERRKmAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHL 1440
Cdd:PRK02224 308 DAEAVEARREELEDRD-EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1441 KSLsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQ------------ 1508
Cdd:PRK02224 387 EEL-EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsp 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1509 --DEAERLRKQVAEETQRKKNAEDELKRKsDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVaq 1586
Cdd:PRK02224 466 hvETIEEDRERVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL-- 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1587 KSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANT------AREEAEQELEIWRQkanealRLR 1660
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLRE------KRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1661 LQAEEEAQKKSHAQEEAE-KQKLEAERDakkrGKAEEAALKQKENAEKELDKqrkfaeqiaqqklsAEQECIRLKADFEH 1739
Cdd:PRK02224 617 ALAELNDERRERLAEKRErKRELEAEFD----EARIEEAREDKERAEEYLEQ--------------VEEKLDELREERDD 678
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1389908282 1740 AEQQRGLLDNELQRLknevNSTEKQRKQLE---DELNKVRSEMDSLLQM 1785
Cdd:PRK02224 679 LQAEIGAVENELEEL----EELRERREALEnrvEALEALYDEAEELESM 723
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1540-2034 |
2.79e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.19 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1540 KEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQK--------SAATQLQTKAMSFSEQTTKLEESL 1611
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSElpelreelEKLEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1612 KKEQGNVLKLQEEADKLKKQQKEANTAREEAEQ---ELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDA 1688
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1689 KKRGKAEEAALKQKENAEKELDKQRKFAEqiAQQKLSAEQECIRLKADFEHAEQQRGllDNELQRLKNEVNSTEKQRKQL 1768
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1769 EDELNKVRSEMDSLLQMKINAEKASM---------------VNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQ 1833
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1834 ------IAEEEAARQRSEAEKI--LKEKLAAINeATRLKTEAEMALKAKE------AENERLKRQAEE-EAYQRKLLE-- 1896
Cdd:PRK03918 484 elekvlKKESELIKLKELAEQLkeLEEKLKKYN-LEELEKKAEEYEKLKEkliklkGEIKSLKKELEKlEELKKKLAEle 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1897 ---DQAAQHKQDIEEKITQLQTSS----DSELGRQKNIVEETLKQKKVV------EEEIHIIKINFHKASKEKADLESEL 1963
Cdd:PRK03918 563 kklDELEEELAELLKELEELGFESveelEERLKELEPFYNEYLELKDAEkelereEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 1964 KKLKGIADETQKSklKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAE 2034
Cdd:PRK03918 643 EELRKELEELEKK--YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4049-4087 |
4.58e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 4.58e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 4049 LLEAQIATGGIIDPQESHRLPVETAYERGLFDEEMNEIL 4087
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
156-256 |
5.83e-15 |
|
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: 73.91 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 235
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1389908282 236 ED-VDVPHPDEKSIITYVSSLY 256
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1396-2224 |
6.45e-15 |
|
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: 82.08 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1396 KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKS--KNQQLEDALVSRRkieeEIHIIR 1473
Cdd:pfam05483 9 KSFNKCTEDDFEFPFAKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGDCHYQEglKDSDFENSEGLSR----LYSKLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1474 IQLEKTTAHKAKSEAELQELRDRAAEAEKL----RKAAQD---EAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQK 1546
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIieaqRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1547 QRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEE--VAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlklQEE 1624
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEElrVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1625 ADKLKKQQKEANTAREEAEQELEIWRQKANE-ALRLRLQAE---EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1700
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKLQDEnlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1701 QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQqrgLLDNELQRLKNevnsTEKQRKQLEDELNKVRSEMD 1780
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEK----NEDQLKIITMELQKKSSELE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1781 SLLQMKINAEkasmVNTEKSKQLLESEalkmKQLADEAARMRSVAEEAK-KQRQIAEEEAARQRSEAEKILKEKLAAINE 1859
Cdd:pfam05483 395 EMTKFKNNKE----VELEELKKILAED----EKLLDEKKQFEKIAEELKgKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1860 ATRLKTEAEMAlkaKEAENERLKRQAEEEAYQRKLLEDQaaqhkqdieeKITQLQTSSDSELGRQKNIVEETLKQKKVVE 1939
Cdd:pfam05483 467 EHYLKEVEDLK---TELEKEKLKNIELTAHCDKLLLENK----------ELTQEASDMTLELKKHQEDIINCKKQEERML 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1940 EEIHIIKinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQC 2019
Cdd:pfam05483 534 KQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2020 KAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKedvLAQEKLRDEFENAKKLAQEA 2099
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK---ISEEKLLEEVEKAKAIADEA 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2100 EKAkekaekeaallrQKAEEAEKQKKAAENEA-AKQAKAQNDtekqrkeaeeeaarraaaeaaalKQKQQADAEMSKHKK 2178
Cdd:pfam05483 688 VKL------------QKEIDKRCQHKIAEMVAlMEKHKHQYD-----------------------KIIEERDSELGLYKN 732
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1389908282 2179 EAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVND 2224
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1354-1932 |
6.72e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1354 DAQRRLEDDEKASEKLKEEE--------RRKMAEIQAELDK---QKQMAEA---HAKSVAKAEQEALELKMKMKEEASKR 1419
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEKDlherlnglESELAELDEEIERyeeQREQAREtrdEADEVLEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1420 QDVAADAEKQKQNIQQELQHLKslsdqeiksknQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAE 1499
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLR-----------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1500 AEKLRKAAQDEAERLRKQVA---EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIR 1576
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADdleERAEELREEAAELESELEEAREAVEDRREEIEELEE---EIEELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1577 QIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESLKKEQGNVlklqEEADKLKKQQK--EANTAREEAE--QELEIWRQK 1652
Cdd:PRK02224 410 AEDFLEELREERDELR---------EREAELEATLRTARERV----EEAEALLEAGKcpECGQPVEGSPhvETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1653 ANEALRLRLQAEEEaqkkshaqEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIR 1732
Cdd:PRK02224 477 VEELEAELEDLEEE--------VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1733 LKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNtEKSKQLLESEALKMK 1812
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLR-EKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1813 QLADEAARMRSVAEEAKKQRQiaeEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEeayqR 1892
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER----R 700
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1389908282 1893 KLLEDQaAQHKQDIEEKITQLQTSS---DSELgRQKNIveETL 1932
Cdd:PRK02224 701 EALENR-VEALEALYDEAEELESMYgdlRAEL-RQRNV--ETL 739
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
41-141 |
7.79e-15 |
|
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: 73.10 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 41 QKKTFTKWVNKHLVK--AQRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 112
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1389908282 113 KLVNIRNDDIADGNPKLTLGLIWTIILHF 141
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2294-2626 |
1.37e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2294 EETARQRQIAESNLAEqralAEKILKEkmqaiqeatkLKAEAEKLQKQKDQAQEtAKRLQEDKQQIQQRL--------DK 2365
Cdd:COG1196 175 EEAERKLEATEENLER----LEDILGE----------LERQLEPLERQAEKAER-YRELKEELKELEAELlllklrelEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2366 ETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQS 2445
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---DIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2446 TREADDLKsaiADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLE 2525
Cdd:COG1196 317 RLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2526 DEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKK-RLEQEKQLAEENKKLREQLQT 2604
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEaELEEEEEALLELLAELLEEAA 473
|
330 340
....*....|....*....|..
gi 1389908282 2605 FEISSKTVSQTKESQTVSVEKL 2626
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLL 495
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
625-815 |
1.53e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.56 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 625 QLHAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAF 704
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 705 TAALQTQWSWLLQLCCCIETHLKENTAHFQFFTDVKEAEEKLKKMQDTMKRKYTCDrsiTVTRLEDLLQDAADEKEQLAE 784
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1389908282 785 FKTNLEALKRRAKTVIQLKPRNPTTPLKGKM 815
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
158-253 |
1.90e-14 |
|
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: 72.03 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 158 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLDPE 236
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1389908282 237 DVDVPHPDEKSIITYVS 253
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1490-1990 |
2.13e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1490 LQELRDRAAEA----EKLRKAAQDEAERLRKQVAEetqrkKNAEDELKRKSDAEKEAAKQKqralDDLQKYKMQAEEAER 1565
Cdd:PRK02224 164 LEEYRERASDArlgvERVLSDQRGSLDQLKAQIEE-----KEEKDLHERLNGLESELAELD----EEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1566 RMKQAE------EEKIRQIRVVEEVAQKSAAtqlqTKAMSFSEQTTkLEESLKKEQGNVLKLQEE--------------A 1625
Cdd:PRK02224 235 TRDEADevleehEERREELETLEAEIEDLRE----TIAETEREREE-LAEEVRDLRERLEELEEErddllaeaglddadA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1626 DKLKKQQKEANTAREEAEQELEIWRQKA----NEALRLR---LQAEEEAQKKSHAQEEAEKQKLEAERDAKKRG------ 1692
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAqahnEEAESLRedaDDLEERAEELREEAAELESELEEAREAVEDRReeieel 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1693 -KAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAE------------------------------ 1741
Cdd:PRK02224 390 eEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkcpecgqpvegsphvet 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1742 -----QQRGLLDNELQRLKNEVNSTEKQRKQLEDeLNKVRSEMDSLLQMKINAEKAsmvnTEKSKQLLESEALKMKQLAD 1816
Cdd:PRK02224 470 ieedrERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEEL----IAERRETIEEKRERAEELRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1817 EAARMRSVAEEAKKQRQIAEEEAARQRSEAeKILKEKLAAINEA-TRLKTEAEMALKAKEAENERLKRQAEEEAYQRKll 1895
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEV-AELNSKLAELKERiESLERIRTLLAAIADAEDEIERLREKREALAEL-- 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1896 EDQAAQHKQDIEEKITQLQTSSDSELgrqkniVEETLKQKKVVEEEIhiikinfhkaskekADLESELKKLKGIADETQK 1975
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEAR------IEEAREDKERAEEYL--------------EQVEEKLDELREERDDLQA 681
|
570
....*....|....*
gi 1389908282 1976 SKLKAEEEAEKLKKL 1990
Cdd:PRK02224 682 EIGAVENELEELEEL 696
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3066-3104 |
2.86e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 2.86e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 3066 FLEAQAATGFVIDPIKNERVPVDEAVKSGLVGPEIHERL 3104
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1621-2444 |
4.33e-14 |
|
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: 79.78 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1621 LQEEADKLKKQQKEANTAREEAEQELEIWRQKANEaLRLRLQaeeEAQKKSHAQEEAEKQKLEAERDAKKRGKAE----E 1696
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVID-LQTKLQ---EMQMERDAMADIRRRESQSQEDLRNQLQNTvhelE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1697 AALKQKENAEKELDKQrkfAEQIAQQKLSAE---QECIRLKADFEHAEQQR----------------GLLDNELQRLKNE 1757
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQ---IEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyehdsmstmhfrslgSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1758 VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE 1837
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQ------DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1838 EAARQRSEAEKILKEKLAAINEatrLKTEAEMALKAKEAENERLKRQ---AEEEAYQRKLLEDQAAQHKQDIEEKITQLQ 1914
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1915 TSSDSelgRQKNIVEETLKQKKVVEEEIHiIKINFHKASKEKADLESELKKLKGIAdETQKSKLKAEEEAEklkklaAEE 1994
Cdd:pfam15921 384 ADLHK---REKELSLEKEQNKRLWDRDTG-NSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQ------MAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1995 ERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANkqkekaekeaekqvvlaKEAAQKCTAAEQKAQDVLSK 2074
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE-----------------RTVSDLTASLQEKERAIEAT 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2075 NKEDVlaqeKLRDEFEnakklaqeaekakekaEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDtekqrkeaeeeaar 2154
Cdd:pfam15921 516 NAEIT----KLRSRVD----------------LKLQELQHLKNEGDHLRNVQTECEALKLQMAEKD-------------- 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2155 raaAEAAALKQKQQADAEM-SKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDafkqksqVE 2233
Cdd:pfam15921 562 ---KVIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-------LE 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2234 VELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKL--LAEEAEKMK-SLAEEAGRLSVEAEETARQRQIAESNLAEQ 2310
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2311 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE---DKQQIQQRLDKETEGFQKSLEAERKRQLEASAE 2387
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 2388 AEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQ-KLETQRLQ 2444
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQhTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1776-2617 |
9.49e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.57 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1776 RSEMDSLL-QMKINAEKASMVNTEKSKQLLESEALKMKQLADEAArmrSVAE-EAKKQRQIAEEEAARQRSE-AEKILKE 1852
Cdd:TIGR02169 119 LSEIHDFLaAAGIYPEGYNVVLQGDVTDFISMSPVERRKIIDEIA---GVAEfDRKKEKALEELEEVEENIErLDLIIDE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1853 KlaaINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQ---HKQDIEEKITQLqTSSDSELGRQKNIVE 1929
Cdd:TIGR02169 196 K---RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAierQLASLEEELEKL-TEEISELEKRLEEIE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1930 ETLKQ-----KKVVEEEIHIIKinfhkasKEKADLESELKKLKGIADEtqkSKLKAEEEAEKLKKLAAEEERRRKEAEEK 2004
Cdd:TIGR02169 272 QLLEElnkkiKDLGEEEQLRVK-------EKIGELEAEIASLERSIAE---KERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2005 VKRItaaeEEAARQCKAAQEEVERLKKKAEDAnkqkekaekeaekqvvlakeaaqkctaaEQKAQDVLSKNKEDVLAQEK 2084
Cdd:TIGR02169 342 EREI----EEERKRRDKLTEEYAELKEELEDL----------------------------RAELEEVDKEFAETRDELKD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2085 LRDEFEnakKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAArraaaeaaalk 2164
Cdd:TIGR02169 390 YREKLE---KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW----------- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2165 QKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQElQRVKGEVNDAFKQKSQVEVELARVRIQME 2244
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVHGTVAQLGSVG 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2245 ELVKLKLKIEEENRR---LMQKDKDSTQ--KLLAEEA---------EKMKSLAEEAGRLS-----------VEAEETAR- 2298
Cdd:TIGR02169 535 ERYATAIEVAAGNRLnnvVVEDDAVAKEaiELLKRRKagratflplNKMRDERRDLSILSedgvigfavdlVEFDPKYEp 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2299 ------QRQIAESNLAEQRALAEKI--------LKEKMQAIQE-ATKLKAEAEKLQKQKDQAQETAKRLQEdkqqiqqrL 2363
Cdd:TIGR02169 615 afkyvfGDTLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGgSRAPRGGILFSRSEPAELQRLRERLEG--------L 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2364 DKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEkhtteivvQKLETQRl 2443
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE--------QEIENVK- 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2444 qstREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQIEQQKAELQQSFLTEKGLLLK-------------RE 2510
Cdd:TIGR02169 758 ---SELKELEARIEEL------------------EEDLHKLEEALNDLEARLSHSRIPEIQAELSkleeevsriearlRE 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2511 KEVEGEKKRFEKQ-LEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEK 2589
Cdd:TIGR02169 817 IEQKLNRLTLEKEyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
890 900
....*....|....*....|....*...
gi 1389908282 2590 QLAEENKKLREQLQTFEISSKTVSQTKE 2617
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKA 924
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
59-138 |
1.76e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 69.54 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 59 HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 130
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1389908282 131 LGLIWTII 138
Cdd:cd21223 105 LALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3730-3768 |
2.10e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.97 E-value: 2.10e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 3730 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPELHDKL 3768
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1347-2037 |
2.24e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 77.47 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1347 QYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKE-----EASK--R 1419
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNtvhelEAAKclK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1420 QDVAADAEKQKQNIQQ-ELQHLKSLsdQEIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKAKS----EAELQELR 1494
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmMLSHEGVL--QEIRSILVDFEEA--SGKKIYEHDSMSTMHFRSLGSAISKIlrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1495 DR----AAEAEKLRKAAQDEAERLRKQ------------------VAEETQRKKNAEDELKRKSDAEKEAAKQKQ----R 1548
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQhqdrieqliseheveitgLTEKASSARSQANSIQSQLEIIQEQARNQNsmymR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1549 ALDDLQKYKMQAEEAERRMKQAEEEKIRQIRvVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKL 1628
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELE-KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1629 KKQQKEA------------NTAREEAEQELEIWRQkanEALRLRLqaeeeaqkKSHAQEEAEKQKleaerdAKKRGKAEE 1696
Cdd:pfam15921 397 KEQNKRLwdrdtgnsitidHLRRELDDRNMEVQRL---EALLKAM--------KSECQGQMERQM------AAIQGKNES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1697 AALKQKENAEKELDKQ--RKFAEQIAQQKL---SAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDE 1771
Cdd:pfam15921 460 LEKVSSLTAQLESTKEmlRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1772 LNKVRSemdslLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQrqiAEEEAARQRSEAE--KI 1849
Cdd:pfam15921 540 GDHLRN-----VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ---LEKEINDRRLELQefKI 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1850 LKEKL-AAINEATRLKTEAEM-ALKAKEAENERLKRQaeeeayqrklledqaaqhkQDIEEKITQLQtssdselgrqkNI 1927
Cdd:pfam15921 612 LKDKKdAKIRELEARVSDLELeKVKLVNAGSERLRAV-------------------KDIKQERDQLL-----------NE 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1928 VEETLKQKKVVEEEIHIIKINFHKASKEkadLESELKKLKGiadETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKR 2007
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEE---METTTNKLKM---QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQ 735
|
730 740 750
....*....|....*....|....*....|
gi 1389908282 2008 ITAAEEeaarQCKAAQEEVERLKKKAEDAN 2037
Cdd:pfam15921 736 ITAKRG----QIDALQSKIQFLEEAMTNAN 761
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1329-1913 |
2.32e-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: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1329 QEYVNLRTRYSELMTLtnqyikfiiDAQRRLEDDEKASEKLKEEERRkmaeIQAELDKQKQMAEAHAKSVAKAEQEALEL 1408
Cdd:COG4913 262 ERYAAARERLAELEYL---------RAALRLWFAQRRLELLEAELEE----LRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1409 kmkmkeeaskRQDVAADAEKQKQNIQQELQHLKSLSDqEIKSKNQQLEDALVS-RRKIEEEIHIIRIQLEKTTAHKAKSE 1487
Cdd:COG4913 329 ----------EAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAAlGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1488 AELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALD---DLqkykMQAEEAE 1564
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPfvgEL----IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1565 RRMKQAEEEKIRQIR---VVEEVAQKSAA-----TQLQTKAmsfseQTTKLEESLKKEQGNVLKLQEEADKLkkqQKEAN 1636
Cdd:COG4913 474 ERWRGAIERVLGGFAltlLVPPEHYAAALrwvnrLHLRGRL-----VYERVRTGLPDPERPRLDPDSLAGKL---DFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1637 TAREEAEQEL-----------------------------------EIWRQKA----------NEALRLRLQAEEEAQKKS 1671
Cdd:COG4913 546 PFRAWLEAELgrrfdyvcvdspeelrrhpraitragqvkgngtrhEKDDRRRirsryvlgfdNRAKLAALEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1672 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKADFEHAEQQRGLLDNEL 1751
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1752 QRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEkasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQ 1831
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE-------DLARLELRALLEERFAAALGDAVERELRENLEER 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1832 RQIAEEEAARQRSEAEKILKE--------------KLAAINEA----TRLKTEaemALKAKEAE-NERLKRQAEEEayqR 1892
Cdd:COG4913 775 IDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEYlallDRLEED---GLPEYEERfKELLNENSIEF---V 848
|
650 660
....*....|....*....|.
gi 1389908282 1893 KLLEDQAAQHKQDIEEKITQL 1913
Cdd:COG4913 849 ADLLSKLRRAIREIKERIDPL 869
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1259-1920 |
2.71e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 77.14 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1259 LREQLTDEKKLLGEIEKNKDKIDdchknakayiDSVKDYEFQILTYKALQDPIASPLKKPKMECASddiiqeyvnLRTRY 1338
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKRKLE----------GESTDLQEQIAELQAQIAELRAQLAKKEEELQA---------ALARL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1339 SELMTLTNQYIKFIIDAQRRLED------DEKASEKLKEEERRKMAE----IQAELDKQKQMAEAHAKSVAKAEQEALEL 1408
Cdd:pfam01576 253 EEETAQKNNALKKIRELEAQISElqedleSERAARNKAEKQRRDLGEeleaLKTELEDTLDTTAAQQELRSKREQEVTEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1409 KMKMKEEaSKRQDVAADAEKQKQNiqqelQHLKSLSDQ-----EIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHK 1483
Cdd:pfam01576 333 KKALEEE-TRSHEAQLQEMRQKHT-----QALEELTEQleqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1484 -AKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEE 1562
Cdd:pfam01576 407 rKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLN 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1563 AERRMKQAEEEK--IRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEE---SLKKEQGNVLKLQEEADKLKKQQKEANT 1637
Cdd:pfam01576 487 LSTRLRQLEDERnsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagTLEALEEGKKRLQRELEALTQQLEEKAA 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1638 AREEAEQELEIWRQKANEAL------RLRLQAEEEAQKKSH---AQEEAEKQKLEAERD---AKKRGKAEEA-----ALK 1700
Cdd:pfam01576 567 AYDKLEKTKNRLQQELDDLLvdldhqRQLVSNLEKKQKKFDqmlAEEKAISARYAEERDraeAEAREKETRAlslarALE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1701 QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHA----EQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVR 1776
Cdd:pfam01576 647 EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSkralEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALK 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1777 SEMDSLLQMKINAekasmvNTEKSKQLLEsEALKMKQLADEAARMRSVAEEAKKQRQIAEEE-------AARQRSEAEKI 1849
Cdd:pfam01576 727 AQFERDLQARDEQ------GEEKRRQLVK-QVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqidaANKGREEAVKQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1850 LK--------------EKLAAINEATRLKTEAEMALKAKEAE----------NERLKRQAEEEayqRKLLEDQAA----- 1900
Cdd:pfam01576 800 LKklqaqmkdlqreleEARASRDEILAQSKESEKKLKNLEAEllqlqedlaaSERARRQAQQE---RDELADEIAsgasg 876
|
730 740
....*....|....*....|....*
gi 1389908282 1901 -----QHKQDIEEKITQLQTSSDSE 1920
Cdd:pfam01576 877 ksalqDEKRRLEARIAQLEEELEEE 901
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
43-144 |
2.74e-13 |
|
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: 69.19 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 43 KTFTKWVNKHLVKAqrHVTDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21298 9 KTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHFQIS 144
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
35-140 |
2.94e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 68.85 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 35 DERDrvqKKTFTKWVNKHLVKAQRHvtDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALDF 106
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVDL 73
|
90 100 110
....*....|....*....|....*....|....
gi 1389908282 107 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 140
Cdd:cd21219 74 AKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1892-2607 |
3.70e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1892 RKLLEDQA--AQHKQDIEEKITQLQTSSDSeLGRQKNIVEETLKQKKVVEEEIHI-IKINFHKASKEKADLESELKKLKG 1968
Cdd:TIGR02168 158 RAIFEEAAgiSKYKERRKETERKLERTREN-LDRLEDILNELERQLKSLERQAEKaERYKELKAELRELELALLVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1969 IADETQKSKLKAEEEAEKLKKLAAEEERrrkeAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAE 2048
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQE----LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2049 KQVVLAKEAAQKCTAAEQKAQDVL-----SKNKEDVLAQEK--LRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAE 2121
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAeelaeLEEKLEELKEELesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2122 KQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQadAEMSKHKKEAEQALQQKSQVEKELTVVKLQL 2201
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2202 DETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKL---------KLKIEEENRRLMQKD-KDSTQKL 2271
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlseLISVDEGYEAAIEAAlGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2272 LAEEAEKMKSLAE-----EAGRLSVEAEETARQRQIaESNLAEQRALAEKILKEKMQAIQEATKLK-------------- 2332
Cdd:TIGR02168 551 VVENLNAAKKAIAflkqnELGRVTFLPLDSIKGTEI-QGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvd 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2333 --AEAEKLQKQKD----------------------------QAQETAKRLQEDKQQIQQRLDKETEGfQKSLEAERKRQL 2382
Cdd:TIGR02168 630 dlDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnsSILERRREIEELEEKIEELEEKIAEL-EKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2383 EASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQklETQRLQSTREADDLKSAIADLEEE 2462
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE--IEELEERLEEAEEELAEAEAEIEE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2463 RKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKR---EKEVEGEKKRFEKQLEDEMKKAKALKDEQE 2539
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaatERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 2540 RQRKLmEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKL---REQLQTFEI 2607
Cdd:TIGR02168 867 LIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLaqlELRLEGLEV 936
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1347-1643 |
4.46e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.93 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1347 QYIKFIIDAQRRLEDDEKasEKLKE-EERRKMAEI----QAELDKQKQMAEAHAKSVAKAEQEALELKM---KMKEEASK 1418
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKE--EKAREvERRRKLEEAekarQAEMDRQAAIYAEQERMAMERERELERIRQeerKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1419 RQDVAADAEKQKqniqqELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELR---- 1494
Cdd:pfam17380 367 QEEIAMEISRMR-----ELERLQ----MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrev 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1495 -----DRAAEAEKLRKAA-----------QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKM 1558
Cdd:pfam17380 438 rrleeERAREMERVRLEEqerqqqverlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1559 QAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT--QLQTKAMSFSEQTTKLeESLKKEQgnvlklqeeadKLKKQQKEAN 1636
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRL-EAMERER-----------EMMRQIVESE 585
|
....*..
gi 1389908282 1637 TAREEAE 1643
Cdd:pfam17380 586 KARAEYE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1348-1984 |
6.24e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1348 YIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmkmkeeaskrqdvaadae 1427
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE------------------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1428 kqkqniqqelqhlkslsdqEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKaksEAELQELRDRAAEAEKLRKAA 1507
Cdd:PRK03918 235 -------------------ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL---KKEIEELEEKVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1508 qDEAERLRKQVAEETQRKKNAEDELKRKSdaekEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRqirvveevaqk 1587
Cdd:PRK03918 293 -EEYIKLSEFYEEYLDELREIEKRLSRLE----EEINGIEERIKELEEKEERLEELKKKLKELEKRLEE----------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1588 saatqLQTKAMSFSEQTTKLE--ESLKKEQGNvlklqEEADKLKKQQKEANTAREEAEQELEIWRQKANE------ALRL 1659
Cdd:PRK03918 357 -----LEERHELYEEAKAKKEelERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEISKITARIGElkkeikELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1660 RLQAEEEAQKK----------SHAQEEAEKQKLEAERDAKKRGKAEEA---ALKQKENAEKELDKQRKFA--EQIAQQKL 1724
Cdd:PRK03918 427 AIEELKKAKGKcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKerkLRKELRELEKVLKKESELIklKELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1725 SAEQECirLKADFEHAEQQRglldNELQRLKNEVNSTEKQRKQLEDELNkvrsemdsllqmKINAEKASMVNTEKSKQLL 1804
Cdd:PRK03918 507 ELEEKL--KKYNLEELEKKA----EEYEKLKEKLIKLKGEIKSLKKELE------------KLEELKKKLAELEKKLDEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1805 ESEalkMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQ 1884
Cdd:PRK03918 569 EEE---LAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1885 AEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKinfhKASKEKADLESELK 1964
Cdd:PRK03918 646 RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE----KAKKELEKLEKALE 721
|
650 660
....*....|....*....|
gi 1389908282 1965 KLKGIADETQKSKLKAEEEA 1984
Cdd:PRK03918 722 RVEELREKVKKYKALLKERA 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1920-2626 |
6.29e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1920 ELGRQKNIVEETLKQKKVVEEE---IHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLaaeeer 1996
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEaagISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERY------ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1997 rrkeaeekvKRITAAEEEA-----ARQCKAAQEEVERLKKKAedankqkekaekeaekqvvlaKEAAQKCTAAEQKAQDV 2071
Cdd:TIGR02168 216 ---------KELKAELRELelallVLRLEELREELEELQEEL---------------------KEAEEELEELTAELQEL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2072 LSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQakaqndtekqrkeaeee 2151
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL----------------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2152 aarraaaeaaaLKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQ 2231
Cdd:TIGR02168 329 -----------ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2232 VEVELARVRIQMEELvklklkiEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQR 2311
Cdd:TIGR02168 398 LNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2312 ALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD------KETEGFQKSLEA--------- 2376
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAalggrlqav 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2377 ------ERKRQLEASAEAEKLKLRVKELSLAQ-TKAEDEAKKFKKQADEVKAQLQRTEKHTTEIvvQKLETQRLQSTREA 2449
Cdd:TIGR02168 551 vvenlnAAKKAIAFLKQNELGRVTFLPLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKL--RKALSYLLGGVLVV 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2450 DDLKSAIADLEEERKKL--------------------KKEAEELQRKSKEMANAQQE-----------QIEQQKAELQQS 2498
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYrivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKieeleekiaelEKALAELRKELE 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2499 FLTEKGLLLKREKE--------VEGEKKRFEK---QLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAE 2567
Cdd:TIGR02168 709 ELEEELEQLRKELEelsrqisaLRKDLARLEAeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2568 EEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL 2626
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1257-1914 |
6.40e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1257 RALREQLTDEKK--LLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDpiASPLKKPKMECASDDIIQEYVNL 1334
Cdd:TIGR02168 216 KELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE--ELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1335 RTRYSELmtltNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKE 1414
Cdd:TIGR02168 294 ANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1415 EASKRQDVAADAEKQKQNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKttAHKAKSEAELQELR 1494
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1495 DRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKS-----------------DAEKEAAKQKQR--------- 1548
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslerlqenlegfsEGVKALLKNQSGlsgilgvls 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1549 --------------------------------------------------ALDDLQKYKMQAEEAERRMKQAE------- 1571
Cdd:TIGR02168 527 elisvdegyeaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtflPLDSIKGTEIQGNDREILKNIEGflgvakd 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1572 ----EEKIR--------QIRVVEEVAQksaATQLQTK-------------------AMSFSEQTT------------KLE 1608
Cdd:TIGR02168 607 lvkfDPKLRkalsyllgGVLVVDDLDN---ALELAKKlrpgyrivtldgdlvrpggVITGGSAKTnssilerrreieELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1609 ESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEA-------------LRLRLQAEEEAQKKSHAQE 1675
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarleaeveqLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1676 EAEKQKLEAERDAKKRGKAEEAALKQK---------------ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHA 1740
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQieqlkeelkalrealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1741 EQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEA-- 1818
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEELre 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1819 --ARMRSVAEEAKKQR-QIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmALKAKEAENERLKRQAEEEAYQRKLL 1895
Cdd:TIGR02168 923 klAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK-RLENKIKELGPVNLAAIEEYEELKER 1001
|
810
....*....|....*....
gi 1389908282 1896 EDQAAQHKQDIEEKITQLQ 1914
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLE 1020
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3473-3509 |
7.10e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 7.10e-13
10 20 30
....*....|....*....|....*....|....*..
gi 1389908282 3473 LLEAQLATGGIIDPASSHRVPTDVAIQRGYFSKQMAK 3509
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1607-2035 |
8.32e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1607 LEESLKKEQGNVLKLQEEADKLKKQQ-KEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEK-QKLEA 1684
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1685 ERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLD-NELQRLKNEVNSTEK 1763
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1764 QRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEAL---------------------------------- 1809
Cdd:COG4717 207 RLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1810 -------KMKQLADEAARMRSVAEEAKKQRqIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLK 1882
Cdd:COG4717 286 lallfllLAREKASLGKEAEELQALPALEE-LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1883 RQAEEEAYQRKLLEDQA------------AQHKQDIEEKITQLQTSSDSELGRQKNIVEETlkQKKVVEEEIHIIKINFH 1950
Cdd:COG4717 365 LEELEQEIAALLAEAGVedeeelraaleqAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1951 KASKEKADLESELKKLkgiadETQKSKLKAEEEAEKLKklaaeeerrrKEAEEKVKRITAAEEEAARqCKAAQEEVERLK 2030
Cdd:COG4717 443 ELEEELEELREELAEL-----EAELEQLEEDGELAELL----------QELEELKAELRELAEEWAA-LKLALELLEEAR 506
|
....*
gi 1389908282 2031 KKAED 2035
Cdd:COG4717 507 EEYRE 511
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1333-1935 |
1.08e-12 |
|
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: 74.79 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1333 NLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDkqkqmAEAHAKSVAKAEQEALELKMKM 1412
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----ALAVAEKAGQAEAEGLRAALAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1413 KEEASKRQDVAAdaekqkqniQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAElqe 1492
Cdd:pfam07111 127 AEMVRKNLEEGS---------QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAE--- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1493 lrdraaeaeklrkaAQDEAERLRKQVAE------------ETQRKKNAEDELKRKSDAEKEAAKQK--------QRALDD 1552
Cdd:pfam07111 195 --------------AQKEAELLRKQLSKtqeeleaqvtlvESLRKYVGEQVPPEVHSQTWELERQElldtmqhlQEDRAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1553 LQK---------------YKMQAEEAERRMKQA---EEEKIRQIR-VVEEVAQKSAATQLQTKAmsfseQTTKLEESLKK 1613
Cdd:pfam07111 261 LQAtvellqvrvqslthmLALQEEELTRKIQPSdslEPEFPKKCRsLLNRWREKVFALMVQLKA-----QDLEHRDSVKQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1614 EQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKAnEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGK 1693
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSA-KGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1694 A---------EEAALK------------QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKAD----FEHAEQQRGLLD 1748
Cdd:pfam07111 415 IwlettmtrvEQAVARipslsnrlsyavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADlsleLEQLREERNRLD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1749 NELQR----LKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKinaeKASMVNTeksKQLLESEALKMKQLADEAARMRsv 1824
Cdd:pfam07111 495 AELQLsahlIQQEVGRAREQGEAERQQLSEVAQQLEQELQRA----QESLASV---GQQLEVARQGQQESTEEAASLR-- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1825 aEEAKKQRQIAEEEAARQRSEAEKILKEKLA----AINEATRLKTEAEMALKAKEAENERLKRQAEEeayQRKLLEDQAA 1900
Cdd:pfam07111 566 -QELTQQQEIYGQALQEKVAEVETRLREQLSdtkrRLNEARREQAKAVVSLRQIQHRATQEKERNQE---LRRLQDEARK 641
|
650 660 670
....*....|....*....|....*....|....*
gi 1389908282 1901 QHKQDIEEKItqlqtssdSELGRQKNIVEETLKQK 1935
Cdd:pfam07111 642 EEGQRLARRV--------QELERDKNLMLATLQQE 668
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1364-1989 |
1.34e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.37 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1364 KASEKLK--EEERRKMAEIQAELDKQ-KQMAEAHAKSVAKAEQEALELKMKMKEEASKrqdvaadaekqkqniqqeLQHL 1440
Cdd:pfam05483 166 RSAEKTKkyEYEREETRQVYMDLNNNiEKMILAFEELRVQAENARLEMHFKLKEDHEK------------------IQHL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1441 KSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEkttahkakseaelqELRDRAAEAEKLRKAAQDEAERLRKQVAE 1520
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE--------------ESRDKANQLEEKTKLQDENLKELIEKKDH 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1521 ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYkmqAEEAERRMKQAEEEKIRQIRVVEEVaqKSAATQLQTKAMSF 1600
Cdd:pfam05483 294 LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL---TEEKEAQMEELNKAKAAHSFVVTEF--EATTCSLEELLRTE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1601 SEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE-----AEQELEIWRQKANEALRLRLQAEEEAQKKSHAQE 1675
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElkkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1676 EAEKQKLEAERDAKKrgKAEEAALKQKENAEKELDKQR-KFAEQIAQ-QKLSAEQECIRLKAD---FEHAEQQRGLLDNE 1750
Cdd:pfam05483 449 EKEIHDLEIQLTAIK--TSEEHYLKEVEDLKTELEKEKlKNIELTAHcDKLLLENKELTQEASdmtLELKKHQEDIINCK 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1751 LQ--RLKNEVNSTEKQRKQLEDELNKVRSEmdslLQMKINAEKASMVNTEKSKQLLESEALK----MKQLADEAARMRSV 1824
Cdd:pfam05483 527 KQeeRMLKQIENLEEKEMNLRDELESVREE----FIQKGDEVKCKLDKSEENARSIEYEVLKkekqMKILENKCNNLKKQ 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1825 AEEAKKQRQIAEEE--AARQRSEAE-------KILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQA-EEEAYQRKL 1894
Cdd:pfam05483 603 IENKNKNIEELHQEnkALKKKGSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKA 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1895 LEDQAAQHKQDI----EEKITQLQTSSDSELGRQKNIVEETlkqkkvvEEEIHIIKINFHKASKEKADLESELKKLKGIA 1970
Cdd:pfam05483 683 IADEAVKLQKEIdkrcQHKIAEMVALMEKHKHQYDKIIEER-------DSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
650
....*....|....*....
gi 1389908282 1971 DETQKSKLKAEEEAEKLKK 1989
Cdd:pfam05483 756 LSLKKQLEIEKEEKEKLKM 774
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2310-2603 |
1.41e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 74.39 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2310 QRALAEKILKEKMQaiqeatklKAEAEKLQKQKDQ-AQETAKR--LQEDKQQIQQRLDKetegfQKSLEAERKR-QLEAS 2385
Cdd:pfam17380 281 QKAVSERQQQEKFE--------KMEQERLRQEKEEkAREVERRrkLEEAEKARQAEMDR-----QAAIYAEQERmAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2386 AEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHttEIVVQKLETQRLQSTREADdlksaiadleeERKK 2465
Cdd:pfam17380 348 RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN--ERVRQELEAARKVKILEEE-----------RQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2466 LKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgekkRFEKQLEDEMKKAKALKDEQERQRKLM 2545
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVE----RLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 2546 EEERKKLQAIMDEavRKQKEAEEEMKNKQREMDVLDKKRL---EQEKQLAEENKKLREQLQ 2603
Cdd:pfam17380 491 EQRRKILEKELEE--RKQAMIEEERKRKLLEKEMEERQKAiyeEERRREAEEERRKQQEME 549
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3397-3435 |
1.45e-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: 1.45e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 3397 LLEAQAATGFITDPVKDKKCSVDDAVKEGIVGPELHEKL 3435
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2740-2778 |
1.81e-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: 1.81e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 2740 LLEAQAASGFIVDPVKNKFLSVDEAVKDKVIGPELHDRL 2778
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2084-2629 |
1.87e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 73.99 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2084 KLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEaarraaaeaaaL 2163
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN-----------L 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2164 KQKQQADAEMSKHKKEAEQALQQKSQVEKELtvvKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQM 2243
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKAL---EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2244 EELVKlklkieeenrrlmqkdkdSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRalaeKILKEKMQ 2323
Cdd:pfam05483 362 EELLR------------------TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK----KILAEDEK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2324 AIQEATKLKAEAEKLQKQKdqaQETAKRLQEDKQQI-------------QQRLDKETEGFQKSLEAERKRQLEASAEAEK 2390
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKE---QELIFLLQAREKEIhdleiqltaiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2391 LKLRVKELS-------LAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVvQKLETQRLQSTREADDLKSAIADLEEER 2463
Cdd:pfam05483 497 LLLENKELTqeasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR-DELESVREEFIQKGDEVKCKLDKSEENA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2464 KKLKKEAEELQ-------------RKSKEMANAQQEQIEQQKAELQQSFLTEKGLLL-------KREKEVEGEKKRFEKQ 2523
Cdd:pfam05483 576 RSIEYEVLKKEkqmkilenkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeikvnKLELELASAKQKFEEI 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2524 LEDEMKKAKALKDEQERqrklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENK------K 2597
Cdd:pfam05483 656 IDNYQKEIEDKKISEEK----LLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDselglyK 731
|
570 580 590
....*....|....*....|....*....|...
gi 1389908282 2598 LREQLQ-TFEISSKTVSQTKESQTVSVEKLVAV 2629
Cdd:pfam05483 732 NKEQEQsSAKAALEIELSNIKAELLSLKKQLEI 764
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
158-257 |
4.15e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.44 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 158 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSN---QENLEQAFSVAERE-LGVTKLL 233
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
|
90 100
....*....|....*....|....
gi 1389908282 234 DPEDVdVPHPDEKSIITYVSSLYD 257
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1378-1838 |
4.22e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1378 AEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAAdAEKQKQNIQQELQHLKSLSDQeiKSKNQQLED 1457
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEK--LEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1458 ALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD 1537
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1538 AEKEAAKQKQRALDDLQKYKMQAEEAERRmkQAEEEKIRQIRVV------------EEVAQKSAATQLQTKAMSFSEQTT 1605
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEA--AALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1606 KLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAE 1685
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1686 RDAKKRGKAEEAALKQKENAEKELDKQRKFaEQIAQQKLSAEQECIRLKADFEHAEQQRGL--LDNELQRLKNEVNSTEK 1763
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 1764 QRKQLEDELNKVRSEMDSLLQMKINAEKasmvnteksKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEE 1838
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGELAEL---------LQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
36-135 |
4.40e-12 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 65.91 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 36 ERDRvQKKTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 107
Cdd:cd21300 4 EGER-EARVFTLWLNSLDVEPA--VNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIW 135
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4319-4357 |
4.63e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.63e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 4319 LLEAQACTGGIIDPNTGEKFSVVDAMNKGLVDKIMVDRI 4357
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1488-1923 |
1.29e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.52 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1488 AELQELRDRAAEAEKLRKAAqdeaerlRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYkMQAeeaerrM 1567
Cdd:COG3096 278 NERRELSERALELRRELFGA-------RRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLV-QTA------L 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1568 KQAEeeKIrqIRVVEEVAQKSAATQLQtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQ----------QKEANT 1637
Cdd:COG3096 344 RQQE--KI--ERYQEDLEELTERLEEQ------EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyqqaldvQQTRAI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1638 AREEAEQELEiwrqKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELdkqRKFAE 1717
Cdd:COG3096 414 QYQQAVQALE----KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV---CKIAG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1718 QI-AQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEdELNKvrsemdsllQMKINAEKASMVN 1796
Cdd:COG3096 487 EVeRSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE-EFCQ---------RIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1797 TEKSKQllesEAlkmkQLADEAARMRSVAEEAKKQRQiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 1876
Cdd:COG3096 557 ELLAEL----EA----QLEELEEQAAEAVEQRSELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQE 627
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1389908282 1877 ENERLKRQAEEEAyQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGR 1923
Cdd:COG3096 628 VTAAMQQLLERER-EATVERDELAARKQALESQIERLSQPGGAEDPR 673
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1505-1729 |
1.34e-11 |
|
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: 69.49 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1505 KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLqKYKMQAEEAERRMKQAEEEKIRQIRVVEEV 1584
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL-EQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1585 AQKSAAtqlqtkamsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEqeleiwRQKANEAlrlrlQAE 1664
Cdd:TIGR02794 125 KAKQAA-----------EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK------KKAEAEA-----KAK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908282 1665 EEAQKKshAQEEAEKQKLEAerdAKKRGKAEEAALKQKENAEK-ELDKQRKFAEQIAQQKLSAEQE 1729
Cdd:TIGR02794 183 AEAEAK--AKAEEAKAKAEA---AKAKAAAEAAAKAEAEAAAAaAAEAERKADEAELGDIFGLASG 243
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
158-256 |
1.35e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 63.91 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 158 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 237
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1389908282 238 VdVPHPDEKSIITYVSSLY 256
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2816-2854 |
1.51e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.51e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 2816 FLDVQLATGGIIDPVNSHRVPLQTAYSQGQFDADMNKKL 2854
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3806-3844 |
1.55e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.55e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 3806 LLEAQNATGGYMDPEYYFRLPIDVAMQRGYINKETHERL 3844
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1349-1909 |
1.77e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.91 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1349 IKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQ---MAEAHAKSVAKAEQEALELKMK----MKEEASKRQD 1421
Cdd:pfam05483 259 LTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdikMSLQRSMSTQKALEEDLQIATKticqLTEEKEAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1422 VAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE 1501
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1502 KLrkaaQDEAERLRKqVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQaeEAERRMKQAEEEKIRQIrvv 1581
Cdd:pfam05483 419 KL----LDEKKQFEK-IAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNI--- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1582 eEVAQKSAATQLQTKAMsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKanealrLRL 1661
Cdd:pfam05483 489 -ELTAHCDKLLLENKEL--TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE------FIQ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1662 QAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAAlkqkENAEKELDKQRKFAEQIAQqklsaeqecirlkadfehae 1741
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC----NNLKKQIENKNKNIEELHQ-------------------- 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1742 qqrglldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM---KINAEKASMVNTEKSKQLLESEALKMKQLADEA 1818
Cdd:pfam05483 616 --------ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1819 ARMRSVAEEaKKQRQIAEEEA--ARQRSEAEKILKEKLAAI-------NEATRLKTEAEMALKAKEAENERLKRQAEEEA 1889
Cdd:pfam05483 688 VKLQKEIDK-RCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEK 766
|
570 580
....*....|....*....|
gi 1389908282 1890 YQRKLLEDQAAQHKQDIEEK 1909
Cdd:pfam05483 767 EEKEKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2164-2394 |
1.94e-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: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2164 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQM 2243
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2244 EELVKLKLKIEEENR---RLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiaesNLAEQRALAEKILKE 2320
Cdd:COG4942 107 AELLRALYRLGRQPPlalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA----ELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 2321 KMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLR 2394
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1926-2594 |
2.91e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1926 NIVEETLKQKKVVEEEIHIIKinFHKASKEKADLESELKKLKgiadETQKSKLKAEEEAEKLKKlaaEEERRRKEAEEKV 2005
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIK---EKEKELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2006 KRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDV--LSKNKEDVLAQE 2083
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2084 KLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKeaEEEAARRAAAEAAAL 2163
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK--RLEELEERHELYEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2164 KQKQqadAEMSKHKKEAEqalqqksqvEKELTVVKLQLDETDKQKVLLDQELQRVKGEvndafkqKSQVEVELARVRIQM 2243
Cdd:PRK03918 368 KAKK---EELERLKKRLT---------GLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2244 EELVKLKLKIEEENRRLMQKDKdstQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRAL-AEKILKEKM 2322
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEHR---KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELiKLKELAEQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2323 QAIQEATKlKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDketegfqkslEAERKRQLEASAEAEKLKLRVKELSLAQ 2402
Cdd:PRK03918 506 KELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK----------ELEKLEELKKKLAELEKKLDELEEELAE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2403 TKAEDEAKKFkKQADEVKAQLQRTEKHTTEIVVQKLETQRLQST-READDLKSAIADLeeerkklkkeaeelqRKSKEMA 2481
Cdd:PRK03918 575 LLKELEELGF-ESVEELEERLKELEPFYNEYLELKDAEKELEREeKELKKLEEELDKA---------------FEELAET 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2482 NAQQEQIEQQKAELQQSFLTE-----KGLLLKREKEVEGEKKRFEkQLEDEMKKAKALKDEQERQRKLMEEERKKLqaim 2556
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEeyeelREEYLELSRELAGLRAELE-ELEKRREEIKKTLEKLKEELEEREKAKKEL---- 713
|
650 660 670
....*....|....*....|....*....|....*....
gi 1389908282 2557 dEAVRKQKEAEEEMKNKQREMDVLDKKR-LEQEKQLAEE 2594
Cdd:PRK03918 714 -EKLEKALERVEELREKVKKYKALLKERaLSKVGEIASE 751
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2269-2609 |
3.02e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.15 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2269 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQ----RQIAESNLAEQRALAEK--ILKEK----MQAIQEATKLKAEAEKL 2338
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREverrRKLEEAEKARQAEMDRQaaIYAEQermaMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2339 QKQKDQAQETA---------KRLQEDKQQIQQRLDKETEGF--QKSLEAERKRQL-EASAEAEKLKLRVKELSLAQTKAE 2406
Cdd:pfam17380 361 ELERIRQEEIAmeisrmrelERLQMERQQKNERVRQELEAArkVKILEEERQRKIqQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2407 DEAKKfkKQADEVKAQLQRtEKHTTEIVVQKLETQRlqstreaddlksaiadleeerkKlkkeaeelqrKSKEManaQQE 2486
Cdd:pfam17380 441 EEERA--REMERVRLEEQE-RQQQVERLRQQEEERK----------------------R----------KKLEL---EKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2487 QIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRfeKQLEDEMKKAKALKDEQERQRKLMEEERKKLQaiMDEAVRKQKEA 2566
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKR--KLLEKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQM 558
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1389908282 2567 EEEMKNKQReMDVLDKKRlEQEKQLAEENKKLREQLQTFEISS 2609
Cdd:pfam17380 559 RKATEERSR-LEAMERER-EMMRQIVESEKARAEYEATTPITT 599
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1483-1732 |
3.70e-11 |
|
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: 67.95 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1483 KAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEEtQRKKNAEDELKRKSDAEKEAAKQKQRALDDlqkyKMQAEE 1562
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE-KAAKQAEQAAKQAEEKQKQAEEAKAKQAAE----AKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1563 AERRMKQAEEEKIRQirvvEEVAQKSAATQLQTKAmsfseqttklEESLKKEqgnvlklqeEADKLKKQQKEANTAREEA 1642
Cdd:TIGR02794 138 AEAERKAKEEAAKQA----EEEAKAKAAAEAKKKA----------EEAKKKA---------EAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1643 EQELEIWRQKanealrlrlqAEEEAQKKShAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQ 1722
Cdd:TIGR02794 195 KAKAEAAKAK----------AAAEAAAKA-EAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
250
....*....|
gi 1389908282 1723 KLSAEQECIR 1732
Cdd:TIGR02794 264 YAAIIQQAIQ 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2163-2602 |
4.44e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2163 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKvlldQELQRVKGEVNDAFKQKSQVEVELARVRIQ 2242
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2243 MEELVKLKLKIEEENRRLMQKDKDSTQ------------KLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2310
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKElkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2311 RALAEKI---------LKEKMQAIQEATKLKAEAEKLQKQK-----DQAQETAKRLQEDKQQIQQRLDKETE--GFQKSL 2374
Cdd:PRK03918 341 EELKKKLkelekrleeLEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITAriGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2375 EAERKRQLEASAEA--------------------EKLKLRVKELSLAQTKAEDEAKKFKKQADEVKA------------- 2421
Cdd:PRK03918 421 IKELKKAIEELKKAkgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliklke 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2422 ---QLQRTEKHTTEIVVQKLEtqrlQSTREADDLKSAIADLEEERKKLKKEAEELQ--RKSKEMANAQQEQIEQQKAELQ 2496
Cdd:PRK03918 501 laeQLKELEEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2497 QSfLTEKGL-----LLKREKEVEGEKKRF------EKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE 2565
Cdd:PRK03918 577 KE-LEELGFesveeLEERLKELEPFYNEYlelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510
....*....|....*....|....*....|....*...
gi 1389908282 2566 -AEEEMKNKQREMDVLDKKRLEQEKQLaEENKKLREQL 2602
Cdd:PRK03918 656 ySEEEYEELREEYLELSRELAGLRAEL-EELEKRREEI 692
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1738-2434 |
4.52e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 69.28 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1738 EHAEQQrglLDNELQRLKNEVNSTEKQRKQLEDELNKvRSEMDSLLQMKINAEKASmVNTEKSKQLLESEalKMKQLADE 1817
Cdd:TIGR04523 32 DTEEKQ---LEKKLKTIKNELKNKEKELKNLDKNLNK-DEEKINNSNNKIKILEQQ-IKDLNDKLKKNKD--KINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1818 AARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEaemaLKAKEAENERLKRQAEEEAYQRKLLED 1897
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1898 QaaqhKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfHKASKEKADLESELKKLKGIADETQKSK 1977
Cdd:TIGR04523 181 E----KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN-NQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1978 LKAEEEAEKLKKlaaeeerrrkeaeekvkritaaeeeaarQCKAAQEEVERLKKKAEDANKQkekaekeaekqvvLAKEA 2057
Cdd:TIGR04523 256 NQLKDEQNKIKK----------------------------QLSEKQKELEQNNKKIKELEKQ-------------LNQLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2058 AQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA---------------KKLAQEAEKAKEKAEKEAALLRQKAEEAEK 2122
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnnkiisqlneqiSQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2123 QKKaaENEAAKQAKAQ-----NDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVV 2197
Cdd:TIGR04523 375 LKK--ENQSYKQEIKNlesqiNDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2198 KLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAE 2277
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2278 KMKslaeeagrlsVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEatkLKAEAEKLQKQKDQAQETAKRLQEDKQ 2357
Cdd:TIGR04523 533 KKE----------KESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 2358 QIQQRLDKETEgfqksLEAERKRQLE-ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV 2434
Cdd:TIGR04523 600 DLIKEIEEKEK-----KISSLEKELEkAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1837-2619 |
5.25e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1837 EEAA------RQRSEAEKilkeKLAAINEA-TRLkteaEMALKAKEAENERLKRQAEE-EAYQRKLLEDQAAQH---KQD 1905
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAEKaERYKELKAELRELELallVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1906 IEEKITQLQTSsDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAE 1985
Cdd:TIGR02168 234 LEELREELEEL-QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1986 KLKKlaaeeerrrkeaeeKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAE 2065
Cdd:TIGR02168 313 NLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2066 QKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2145
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2146 KeaeeeaarraaaeaaalkqkQQADAEMSKHKKEAEQALQQKSQvekeltvvklQLDETDKQKVLLDQELQRVKGE---V 2222
Cdd:TIGR02168 459 L--------------------EEALEELREELEEAEQALDAAER----------ELAQLQARLDSLERLQENLEGFsegV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2223 NDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLaeeaGRLSVEAEETARQR 2300
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvVENLNAAKKAIAFLKQNEL----GRVTFLPLDSIKGT 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2301 QIaESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQ------KDQAQETAKRLQEDKQQIQQRLDKETEGFQKSL 2374
Cdd:TIGR02168 585 EI-QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddLDNALELAKKLRPGYRIVTLDGDLVRPGGVITG 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2375 EAERKRQ--LEASAEAEKLKLRVKELslaqtkaEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQStreaddl 2452
Cdd:TIGR02168 664 GSAKTNSsiLERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS------- 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2453 ksaiadleeerkklkkeaeeLQRKSKEMANAQQEQIEQQKAELQqsfltekglllKREKEVEGEKKRFEKQLEDEMKKAK 2532
Cdd:TIGR02168 730 --------------------ALRKDLARLEAEVEQLEERIAQLS-----------KELTELEAEIEELEERLEEAEEELA 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2533 ALkdeqerqrklmEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTV 2612
Cdd:TIGR02168 779 EA-----------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
....*..
gi 1389908282 2613 SQTKESQ 2619
Cdd:TIGR02168 848 EELSEDI 854
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1475-1897 |
6.86e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1475 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRK--QVAEETQRKKNAEDELKRKsDAEKEAAKQKQRALDD 1552
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAEL-PERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1553 LQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQtkamSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQ 1632
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE----ELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1633 KEANTAREEAEQE--------------------------------------LEIWRQKANEALRLRLQAEEEAQKKSHAQ 1674
Cdd:COG4717 237 EAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1675 EEAEKQKLEAERDAKKRGKAEEA--ALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNelq 1752
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELleLLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ--- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1753 rlKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMkinaekasmVNTEKSKQLLESEALKMKQLADEAARMRsvAEEAKKQR 1832
Cdd:COG4717 394 --AEEYQELKEELEELEEQLEELLGELEELLEA---------LDEEELEEELEELEEELEELEEELEELR--EELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 1833 QIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKeaenERLKRQAEEEaYQRKLLED 1897
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELL----EEAREEYREE-RLPPVLER 520
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
34-141 |
6.95e-11 |
|
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: 62.60 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 34 QDERDRVQ--KKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFL 107
Cdd:cd21222 8 DEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 141
Cdd:cd21222 88 EDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3142-3180 |
7.00e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 7.00e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 3142 LLEAQLSTGGIVDPVKSYRIPHEVACKRGYFDDKMSKTL 3180
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1252-1989 |
7.54e-11 |
|
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: 68.92 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1252 PISDSRALREQLTD---EKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASplkKPKMECASDDII 1328
Cdd:TIGR00606 164 PLSEGKALKQKFDEifsATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITS---KEAQLESSREIV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1329 QEYVN----LRTRYSELMTLTNQYIKfIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQ-KQMAEAHAKSVAKAEQ 1403
Cdd:TIGR00606 241 KSYENeldpLKNRLKEIEHNLSKIMK-LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQlNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1404 EALELKMKMKEEASKRQDVaaDAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHK 1483
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLL--NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHT 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1484 AKSEAElqelRDRAAEAEKLRKAAQDEaERLRKQVAEETQRKKNAedeLKRKSDAEKEAAKQKQRALDDLQKYKMQAEEA 1563
Cdd:TIGR00606 398 LVIERQ----EDEAKTAAQLCADLQSK-ERLKQEQADEIRDEKKG---LGRTIELKKEILEKKQEELKFVIKELQQLEGS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1564 ERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQkeaNTAREEAE 1643
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME---MLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1644 QELEIWRQKANEALRLRLQAEEEAQKKS-----HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR-KFAE 1717
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLsSYED 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1718 QIAQQKLSAEQECI--RLKADFEHAEQQRGLL-------------------------------DNELQ----RLKNEVNS 1760
Cdd:TIGR00606 627 KLFDVCGSQDEESDleRLKEEIEKSSKQRAMLagatavysqfitqltdenqsccpvcqrvfqtEAELQefisDLQSKLRL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1761 TEKQRKQLEDELNKVRSEMDSLLqmkINAEKASMVNTEKSKQLLESEAlKMKQLADEAARMRSVAEEAKKQRQ--IAEEE 1838
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEML---GLAPGRQSIIDLKEKEIPELRN-KLQKVNRDIQRLKNDIEEQETLLGtiMPEEE 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1839 AAR--------------QRSEAEKILkEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhKQ 1904
Cdd:TIGR00606 783 SAKvcltdvtimerfqmELKDVERKI-AQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ-IQ 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1905 DIEEKITQLQT---SSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAE 1981
Cdd:TIGR00606 861 HLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
....*...
gi 1389908282 1982 EEAEKLKK 1989
Cdd:TIGR00606 941 DKVNDIKE 948
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1475-1783 |
7.90e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1475 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDaEKEAAKQKQRALD--- 1551
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELEari 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1552 -----DLQKYKMQAEEAERRMKQAEEEKI-RQIRVVEEVAQK--SAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQE 1623
Cdd:TIGR02169 768 eeleeDLHKLEEALNDLEARLSHSRIPEIqAELSKLEEEVSRieARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1624 EADKLKKQQKEANTAREEAEQELEiwrqkanealrlRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEeaaLKQKE 1703
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELE------------ELEAALRDLESRLGDLKKERDELEAQLRELERKIEE---LEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1704 NAEKELDKQRKFAEQIAQQKLS-------AEQECIRLKADFEHAEQQRGLLDNELQRLK-------NEVNSTEKQRKQLE 1769
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSeiedpkgEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELK 992
|
330
....*....|....
gi 1389908282 1770 DELNKVRSEMDSLL 1783
Cdd:TIGR02169 993 EKRAKLEEERKAIL 1006
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2187-2617 |
9.33e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2187 KSQVEKELTVVKLQLDETDKQKVLLDQELQRvkgEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKD 2266
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2267 STQKLlAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQkdqAQ 2346
Cdd:pfam05483 280 QDENL-KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE---FE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2347 ETAKRLQEDKQQIQQRLDKETEGFQ--------KSLEAERKRQLEASAEAEKLKLrvKELSLAQTKAEDEAKKFKKQADE 2418
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKiitmelqkKSSELEEMTKFKNNKEVELEEL--KKILAEDEKLLDEKKQFEKIAEE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2419 VKA---------QLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEerkklkkeaeelqRKSKEMANAQQEQIE 2489
Cdd:pfam05483 434 LKGkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL-------------KNIELTAHCDKLLLE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2490 QQKAELQQSFLTekgLLLKREKE----VEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE 2565
Cdd:pfam05483 501 NKELTQEASDMT---LELKKHQEdiinCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 2566 AEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLRE-QLQTFEISSKTVSQTKE 2617
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElHQENKALKKKGSAENKQ 630
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1528-1787 |
9.50e-11 |
|
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: 66.79 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1528 AEDELKRKSDAEKEAAKQKQRALDDLQKykmQAEEAERRmKQAEEEKIRQIRvveevaQKSAAtqlqtkamsfsEQTTKL 1607
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQ-RAAEQARQKELE------QRAAA-----------EKAAKQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1608 EESLKKEQgnvLKLQEEADKLKKQQKEANTAREEAEQEleiwrQKANEALRLrlQAEEEAQKKshAQEEAEKQKLEAERD 1687
Cdd:TIGR02794 107 AEQAAKQA---EEKQKQAEEAKAKQAAEAKAKAEAEAE-----RKAKEEAAK--QAEEEAKAK--AAAEAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1688 AKKRGKAEEAALKQK--ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1765
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAkaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
250 260
....*....|....*....|..
gi 1389908282 1766 KQLEDELNKVRSEMDSLLQMKI 1787
Cdd:TIGR02794 255 AAAGSEVDKYAAIIQQAIQQNL 276
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2172-2600 |
1.03e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2172 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSqvevELARVRIQMEELVKLKL 2251
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2252 KIEEENRRLMQKDKDsTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAEsnlaeqraLAEKILKEKMQAIQEATKL 2331
Cdd:PRK03918 249 SLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--------FYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2332 KAEAEKLQKQKDQAQETAKRLQEDKQQIQQrLDKETEGFQKSLEA-ERKRQLEAsaEAEKLKLRVKELSLAQTKAE-DEA 2409
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKE-LEKRLEELEERHELyEEAKAKKE--ELERLKKRLTGLTPEKLEKElEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2410 KKFKKQ-ADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQqEQI 2488
Cdd:PRK03918 397 EKAKEEiEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE-EKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2489 EQQKAELqqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAE- 2567
Cdd:PRK03918 476 RKLRKEL-----RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEk 550
|
410 420 430
....*....|....*....|....*....|....
gi 1389908282 2568 -EEMKNKQREmdvLDKKRLEQEKQLAEENKKLRE 2600
Cdd:PRK03918 551 lEELKKKLAE---LEKKLDELEEELAELLKELEE 581
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1953-2604 |
1.14e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 68.46 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1953 SKEKADLESELKKL---KGIADETQKSKLKAEEEAEKLKK---LAAEEERRRKEAEEKVKRITAAE----EEAARQCKAA 2022
Cdd:TIGR00618 162 SKEKKELLMNLFPLdqyTQLALMEFAKKKSLHGKAELLTLrsqLLTLCTPCMPDTYHERKQVLEKElkhlREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2023 QEEVERLKKKAEDANKQKEkaekeaekqvvLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRdEFENAKKLAQEAEKA 2102
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQ-----------LLKQLRARIEELRAQEAVLEETQERINRARKAAP-LAAHIKAVTQIEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2103 KEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQ 2182
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2183 ALQQKSQVEKELTvvkLQLDETDKQKVLLDQELQRVKGEVNDAFKQK--SQVEVELARVRIQmEELVKLKLKIEEENRrL 2260
Cdd:TIGR00618 390 TLTQKLQSLCKEL---DILQREQATIDTRTSAFRDLQGQLAHAKKQQelQQRYAELCAAAIT-CTAQCEKLEKIHLQE-S 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2261 MQKDKDSTQKLLAEEA----EKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQA-IQEATKLKAEA 2335
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQihlqETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2336 EKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE-AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2414
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2415 QADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAiadleEERKKLKKEAEELQRKSKEMANaQQEQIEQQKAE 2494
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL-----SIRVLPKELLASRQLALQKMQS-EKEQLTYWKEM 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2495 LQQsflteKGLLLKREKEVEGEKKRFEKQLEDEMKKAKA-----LKDEQERQRKLMEEERKKLQAimdeavrkqKEAEEE 2569
Cdd:TIGR00618 699 LAQ-----CQTLLRELETHIEEYDREFNEIENASSSLGSdlaarEDALNQSLKELMHQARTVLKA---------RTEAHF 764
|
650 660 670
....*....|....*....|....*....|....*
gi 1389908282 2570 MKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQT 2604
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1684-1917 |
1.22e-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: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1684 AERDAKKRGKAE-EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTE 1762
Cdd:COG4942 17 AQADAAAEAEAElEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1763 KQRKQLEDELNKVrseMDSLLQMKINAEKASMVNTEKSKQLLESEALkMKQLADeaARMRSVAEEAKKQRQIAE--EEAA 1840
Cdd:COG4942 97 AELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAP--ARREQAEELRADLAELAAlrAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1841 RQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSS 1917
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4317-4354 |
1.44e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 58.65 E-value: 1.44e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1389908282 4317 QRLLEAQACTGGIIDPNTGEKFSVVDAMNKGLVDKIMV 4354
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1524-2146 |
1.68e-10 |
|
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: 67.74 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1524 RKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEaerrMKQAEEEKIRQIRvVEEVAQKSAATQLQTKAMSFSEQ 1603
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE----KINNSNNKIKILE-QQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1604 TTKLEESLKKEQGNVLKLQEEADKLKKQQKEANtareeaEQELEIwrqkANEALRLrlqaEEEAQKKSHAQEEAEKQKLE 1683
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENK------KNIDKF----LTEIKKK----EKELEKLNNKYNDLKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1684 AERDAKKrgkaeeaALKQKENAEKELDKQRKfAEQIAQQKLSAEQECIR----LKADFEHAEQQRGLLDN-------ELQ 1752
Cdd:TIGR04523 171 LENELNL-------LEKEKLNIQKNIDKIKN-KLLKLELLLSNLKKKIQknksLESQISELKKQNNQLKDniekkqqEIN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1753 RLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLAdEAARMRSVAEEAKKQR 1832
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSE-KQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNKELKSELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1833 qiaeeeaaRQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQ 1912
Cdd:TIGR04523 321 --------KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1913 -----LQTSSDSELGRQKNIVEETLKQ-KKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEK 1986
Cdd:TIGR04523 393 indleSKIQNQEKLNQQKDEQIKKLQQeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1987 LKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKaekeaekqvvLAKEAAQKCTAAEQ 2066
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK----------LESEKKEKESKISD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2067 KAQDVLSKNkeDVLAQEKLRDEF----ENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTE 2142
Cdd:TIGR04523 543 LEDELNKDD--FELKKENLEKEIdeknKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
....
gi 1389908282 2143 KQRK 2146
Cdd:TIGR04523 621 KAKK 624
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1491-1936 |
1.81e-10 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 67.77 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1491 QELRDraAEAEKlrKAAQDEaerlrkqVAEETQRKKNAEDElkRKSDAEKeaAKQKQRALDDLQKYKMQAeeaeRRMKQA 1570
Cdd:PRK10929 30 QELEQ--AKAAK--TPAQAE-------IVEALQSALNWLEE--RKGSLER--AKQYQQVIDNFPKLSAEL----RQQLNN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1571 EEEKIRQIRvveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQeleiwr 1650
Cdd:PRK10929 91 ERDEPRSVP------PNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIER------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1651 qkanealrlRLQAeeeAQKKSHAQEEAEKQKLeaerdakkrgKAEEAALKQKENaekELDkqrkfaeqIAQqkLSA--EQ 1728
Cdd:PRK10929 159 ---------RLQT---LGTPNTPLAQAQLTAL----------QAESAALKALVD---ELE--------LAQ--LSAnnRQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1729 ECIRLKADFEHAEQQRglLDNELQRLKNEVNStekQRKQledelnkvrsemdsllqmkiNAEKAsmvnTEKSKQLLESEA 1808
Cdd:PRK10929 204 ELARLRSELAKKRSQQ--LDAYLQALRNQLNS---QRQR--------------------EAERA----LESTELLAEQSG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1809 LKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKIL--KEKLAAINEATRLKTEAEM---ALKAKEA------E 1877
Cdd:PRK10929 255 DLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLqvRQALNTLREQSQWLGVSNAlgeALRAQVArlpempK 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1878 NERLKRQAEEEAYQRKLLEDQAAQHKQDieekiTQLQTSSDSEL-GRQKNIVEETLKQKK 1936
Cdd:PRK10929 335 PQQLDTEMAQLRVQRLRYEDLLNKQPQL-----RQIRQADGQPLtAEQNRILDAQLRTQR 389
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1477-1728 |
1.83e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 67.28 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1477 EKTTAHKAKS--EAELQEL-RDRAAEAEKLRKAAQDEAERLRKQVAEetqrkknAEDELKRKSDAEKEAAKQKQRALDDl 1553
Cdd:PRK05035 444 EKKKAEEAKArfEARQARLeREKAAREARHKKAAEARAAKDKDAVAA-------ALARVKAKKAAATQPIVIKAGARPD- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1554 QKYKMQAEEAERRMKQAEEEKIRQirvVEEVAQKSAA-------TQLQTKAMSFSEQTTKLEESLKKEQgnVLKLQEEAd 1626
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQA---AAAADPKKAAvaaaiarAKAKKAAQQAANAEAEEEVDPKKAA--VAAAIARA- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1627 KLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE 1706
Cdd:PRK05035 590 KAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEP 669
|
250 260
....*....|....*....|....*.
gi 1389908282 1707 KELDKQRK--FAEQIA--QQKLSAEQ 1728
Cdd:PRK05035 670 EEAEDPKKaaVAAAIAraKAKKAAQQ 695
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2164-2614 |
1.95e-10 |
|
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: 67.35 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2164 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVevelarvriqM 2243
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD----------W 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2244 EELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRALAEKILKEKMQ 2323
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE-------LEEKQNEIEKLKKENQS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2324 AIQEATKLKAEAEKLQKQKDQAQETAkrlqedkqqiqQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2403
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLN-----------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2404 KAEDEAKKFKKQADEVKAQLQrtekhTTEIVVQKLETQRLQSTREADDLKSAIadleeerkklkkeaeelqrkskEMANA 2483
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLK-----VLSRSINKIKQNLEQKQKELKSKEKEL----------------------KKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2484 QQEQIEQQKAELQQsfltEKGLLLKREKEVEGEKKRFEKQLEDemKKAKALKDEQERQRKLMEEERKKLQaimdEAVRKQ 2563
Cdd:TIGR04523 504 EKKELEEKVKDLTK----KISSLKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKN----KEIEEL 573
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 2564 KEAEEEMKNKQREMDvldkkrlEQEKQLAEENKKLREQLQTFEISSKTVSQ 2614
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQ-------ELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1490-1710 |
1.98e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 66.37 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1490 LQELRDRAAEAEKLR-KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDlQKykmQAEEAERRMK 1568
Cdd:PRK09510 67 QQQQQKSAKRAEEQRkKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK-QK---QAEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1569 QAEEEKIRQIRVVEEVAQKSAAtqlqtkamsfseqttklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEqelei 1648
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAA-----------------AEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK----- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 1649 wrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELD 1710
Cdd:PRK09510 201 --KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2163-2606 |
2.03e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2163 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVkgevnDAFKQKSQVEVELARVRIQ 2242
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2243 MEELvklKLKIEEENRRLMQKDKdstqkLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRalaEKILKEKM 2322
Cdd:COG4717 148 LEEL---EERLEELRELEEELEE-----LEAELAELQEELEELLEQLSLATEEELQD-------LAEEL---EELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2323 QAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAE-AEKLKLRVKELSLA 2401
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2402 QTKAEDEAKKFKKQADEVKAQLQRtekhtteivvQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMA 2481
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPAL----------EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2482 NAQ--QEQIEQQKAELQQSF-------LTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRklMEEERKKL 2552
Cdd:COG4717 360 EEElqLEELEQEIAALLAEAgvedeeeLRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEEL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 2553 QAimdeavrKQKEAEEEMKNKQREmdvldKKRLEQEKQLAEENKKLREQLQTFE 2606
Cdd:COG4717 438 EE-------ELEELEEELEELREE-----LAELEAELEQLEEDGELAELLQELE 479
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3973-4011 |
2.09e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.49 E-value: 2.09e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 3973 LLEAQAATGYVIDPIKNLKLNVTEAVKMGIVGTEFKDKL 4011
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
530-719 |
2.33e-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: 63.62 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 530 LRYTQDLLGWVEENQRRVDEGEWGSDLPTVESLLGSHRGLHQCVEEFRSKIERAKADESQV---SPASKAAYRDYLGKLE 606
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 607 LQYGKLLTSSKARLRYLD---QLHAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAV 683
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1389908282 684 QTTGDKLLRDGHP-ARKTIEAFTAALQTQWSWLLQLC 719
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2191-2610 |
2.41e-10 |
|
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: 66.97 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2191 EKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLmqkdkdstQK 2270
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK--------EK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2271 LLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAE---QRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQE 2347
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2348 TAKRLQEDKQQIQQRLDKETEGFQ--KSLEAERKRQLEA-SAEAEKLKLRVKELS--LAQTKAEDEAKKFKKQAD---EV 2419
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNqlKDEQNKIKKQLSEkQKELEQNNKKIKELEkqLNQLKSEISDLNNQKEQDwnkEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2420 KAQLQRTEKHTTEIvvqklETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEmanaQQEQIEQQKAElQQSF 2499
Cdd:TIGR04523 313 KSELKNQEKKLEEI-----QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKLKKE-NQSY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2500 LTEKGLLLKREKEVEGE---KKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNkqre 2576
Cdd:TIGR04523 383 KQEIKNLESQINDLESKiqnQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN---- 458
|
410 420 430
....*....|....*....|....*....|....
gi 1389908282 2577 mdvLDKKRLEQEKQLAEENKKLREQLQTFEISSK 2610
Cdd:TIGR04523 459 ---LDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1534-1978 |
2.80e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1534 RKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKK 1613
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1614 EQGNVLKLQEEADKLKKQQKEantaREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGK 1693
Cdd:COG4717 144 LPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1694 AEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRL------KADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQ 1767
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1768 LEDELNKVR--SEMDSLLQMKINAEKAS-MVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEA--ARQ 1842
Cdd:COG4717 300 LGKEAEELQalPALEELEEEELEELLAAlGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1843 RSEAEKILKEKLAAINEATRLK---TEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhkQDIEEKITQLQTssds 1919
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKeelEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--EELEEELEELRE---- 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 1920 ELGRQKNIVEETLKQKKVVE--EEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKL 1978
Cdd:COG4717 454 ELAELEAELEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1918-2606 |
4.52e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1918 DSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLEsELKKLKGIADETQ-----KSKLKAEEEAEKLKK--- 1989
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERqla 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1990 -LAAEEERRRKEAEEKVKRITAAE----EEAARQCKAAQEEVERLKKKAEDankqKEKAEKEAEKQVVLAKEAAQKCTAA 2064
Cdd:TIGR02169 248 sLEEELEKLTEEISELEKRLEEIEqlleELNKKIKDLGEEEQLRVKEKIGE----LEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2065 EQKAQDVLSKNKEDVlaqEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQ 2144
Cdd:TIGR02169 324 LAKLEAEIDKLLAEI---EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2145 RkeaeeeaARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKL-------QLDETDKQKVLLDQELQR 2217
Cdd:TIGR02169 401 I-------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALeikkqewKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2218 VKGEVNDAFKQKSQVEVELARV---RIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAG-RLS--- 2290
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAeaqARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGnRLNnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2291 VEAEETA-------RQRQIAE----------------------------------------------------SNLAEQR 2311
Cdd:TIGR02169 554 VEDDAVAkeaiellKRRKAGRatflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2312 ALAEKI--------LKEKMQAI-----------QEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD-------- 2364
Cdd:TIGR02169 634 RLMGKYrmvtlegeLFEKSGAMtggsraprggiLFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDelsqelsd 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2365 --KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQR 2442
Cdd:TIGR02169 714 asRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2443 LQSTREADDLK------SAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgE 2516
Cdd:TIGR02169 794 PEIQAELSKLEeevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-E 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2517 KKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQE-------- 2588
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeels 952
|
810
....*....|....*....
gi 1389908282 2589 -KQLAEENKKLREQLQTFE 2606
Cdd:TIGR02169 953 lEDVQAELQRVEEEIRALE 971
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
156-255 |
5.69e-10 |
|
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: 59.70 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYrQSNQ--ENLEQAFSVAERELGVTKLL 233
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCPDWESW-DPNQpvQNAREAMQQADDWLGVPQVI 86
|
90 100
....*....|....*....|..
gi 1389908282 234 DPEDVDVPHPDEKSIITYVSSL 255
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQF 108
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
42-138 |
5.93e-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: 59.51 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 42 KKTFTKWVNKHLVKAQ---------RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFL 107
Cdd:cd21217 3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 138
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2269-2590 |
5.95e-10 |
|
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: 64.17 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2269 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQET 2348
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2349 AKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEklkLRVKELSLAQTKAEDEAKKFKKQADEVKaqlqrtEK 2428
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED---ERILEYLKEKAEREEEREAEREEIEEEK------ER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2429 HTTEIVVQKLETQRLQSTREADDLKSAIADLeeerkklkkeaeelQRKSKEMANAQQEQIEQQKAELQQSFLTEKGL-LL 2507
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQ--------------ERKERQKEREEAEKKARQRQELQQAREEQIELkER 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2508 KREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDE---AVRKQKEAEEEMKNKQREMDVLDKKR 2584
Cdd:pfam13868 251 RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEreeQRAAEREEELEEGERLREEEAERRER 330
|
....*.
gi 1389908282 2585 LEQEKQ 2590
Cdd:pfam13868 331 IEEERQ 336
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1360-1714 |
6.73e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 65.27 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1360 EDDEKASEKLKE----EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQN-IQ 1434
Cdd:pfam02029 1 IEDEEEAARERRrrarEERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKrLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1435 QELQHLK---------SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRK 1505
Cdd:pfam02029 81 EALERQKefdptiadeKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1506 AAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRalddLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVA 1585
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG----HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1586 QKSAATQLQTkamsfsEQttKLEESLKKEQGnvlKLQEEADKLKKQQkeantarEEAEQELEIWRQKANEalRLRLQAEE 1665
Cdd:pfam02029 237 EEEAEVFLEA------EQ--KLEELRRRRQE---KESEEFEKLRQKQ-------QEAELELEELKKKREE--RRKLLEEE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 1666 EAQKKshaQEEAEKQKLEAERdaKKRGKAE------EAALKQKENAEKELDKQRK 1714
Cdd:pfam02029 297 EQRRK---QEEAERKLREEEE--KRRMKEEierrraEAAEKRQKLPEDSSSEGKK 346
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2172-2603 |
7.19e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 65.76 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2172 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKL 2251
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2252 KIEEENRRL--MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAEsnLAEQRALAEKILKEKMQAIQEAT 2329
Cdd:TIGR00618 240 QSHAYLTQKreAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2330 KLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRqlEASAEAEKLKLRVKELSLAQTKAEDE- 2408
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR--EISCQQHTLTQHIHTLQQQKTTLTQKl 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2409 ----AKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMAN-- 2482
Cdd:TIGR00618 396 qslcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQql 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2483 AQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFE-----------------------KQLEDEMKKAKALKDEQE 2539
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNparqdidnpgpltrrmqrgeqtyAQLETSEEDVYHQLTSER 555
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 2540 RQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK---KRLEQEKQLAEENKKLREQLQ 2603
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQ 622
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2240-2654 |
7.63e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.76 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2240 RIQMEELV---KLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAgrlsVEAEETARQRQIAESNLAEQRALAEK 2316
Cdd:pfam02463 155 RLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKE----QAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2317 ILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQqRLDKETEGFQKSLEAERKRQLEaSAEAEKLKLRVK 2396
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN-KEEEKEKKLQEEELKLLAKEEE-ELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2397 ELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQSTREADDLksaiADLEEERKKLKKEAEELQRK 2476
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEEL---EKELKELEIKREAEEEEEEEL----EKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2477 SKEMANAQQEQIEQQKAELqqsfltekgllLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQaim 2556
Cdd:pfam02463 382 ESERLSSAAKLKEEELELK-----------SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT--- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2557 deaVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSK 2636
Cdd:pfam02463 448 ---EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410
....*....|....*...
gi 1389908282 2637 GVLNGSTEVDGVKKEGDS 2654
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYK 542
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1544-1967 |
8.00e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1544 KQKQRALDDL------QKYKMQAEEAE---RRMKQAEEEKIRQIRvvEEVAQKSAA------TQLQTKAMSFSEQTTKLE 1608
Cdd:PRK02224 149 SDRQDMIDDLlqlgklEEYRERASDARlgvERVLSDQRGSLDQLK--AQIEEKEEKdlherlNGLESELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1609 EslKKEQGNVLKlqEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDA 1688
Cdd:PRK02224 227 E--QREQARETR--DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1689 KKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQL 1768
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1769 EDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE----------- 1837
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1838 -----EAARQRSEAEKILKEKLAAINEA-TRLKTEAEMALKAKEAEnerlkRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 1911
Cdd:PRK02224 463 gsphvETIEEDRERVEELEAELEDLEEEvEEVEERLERAEDLVEAE-----DRIERLEERREDLEELIAERRETIEEKRE 537
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908282 1912 QLQtssdsELGRQKNIVEETLKQKKVVEEEIHiikINFHKASKEKADLESELKKLK 1967
Cdd:PRK02224 538 RAE-----ELRERAAELEAEAEEKREAAAEAE---EEAEEAREEVAELNSKLAELK 585
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1503-1914 |
8.34e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1503 LRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVE 1582
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1583 EVAQKSAATQLQTKAMSFSEQTTKLEESLKKeqgnvlkLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRlRLQ 1662
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEE-------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1663 AEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIA---------------------- 1720
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1721 ------------QQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVN-STEKQRKQLEDELNKVRSEMDSLLQMKI 1787
Cdd:COG4717 279 lflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1788 NAEKASMVNTEKSKQLLeseaLKMKQLADEAArMRSVAEEAKKQRQIAEE--EAARQRSEAEKILKEKLAAINEATRLKT 1865
Cdd:COG4717 359 LEEELQLEELEQEIAAL----LAEAGVEDEEE-LRAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 1866 EAEMALKAKEAENER---LKRQAEEEAYQRKLLEDQAAQH-KQDIEEKITQLQ 1914
Cdd:COG4717 434 LEELEEELEELEEELeelREELAELEAELEQLEEDGELAElLQELEELKAELR 486
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1476-1897 |
8.88e-10 |
|
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: 65.03 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1476 LEKTTAHKAKSEAELqelrdraaeAEKLRKAAQDEAERLRKQVAEETqrKKNAEDElKRKSDAEKEAAKQKQralDDLQK 1555
Cdd:NF033838 101 LYELNVLKEKSEAEL---------TSKTKKELDAAFEQFKKDTLEPG--KKVAEAT-KKVEEAEKKAKDQKE---EDRRN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1556 Y--------KMQAEEAERRMKQAEEEkirqirVVEEVAQKSaatqlqtkamsfseqttKLEESLKKEQGNVLKLQEEADK 1627
Cdd:NF033838 166 YptntyktlELEIAESDVEVKKAELE------LVKEEAKEP-----------------RDEEKIKQAKAKVESKKAEATR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1628 LKKqqkeANTAREEAEQeleiwrqkanEALRLRLQAEEEAQKKSHAQEEAEKQKleaeRDAKKRGKAEEAALKQKENAEK 1707
Cdd:NF033838 223 LEK----IKTDREKAEE----------EAKRRADAKLKEAVEKNVATSEQDKPK----RRAKRGVLGEPATPDKKENDAK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1708 ELDKQRKfAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRlknevNSTEKQRKQLEDELNKVRSEMDSLLQMKI 1787
Cdd:NF033838 285 SSDSSVG-EETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR-----NYPTNTYKTLELEIAESDVKVKEAELELV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1788 NAEKASMVNTEKSKQLLESEALKMKqladEAARMrsvaEEAKKQRQIAEEEAARQRSEAEKIlKEKLAAINEATRLKTEA 1867
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVESKKA----EATRL----EKIKTDRKKAEEEAKRKAAEEDKV-KEKPAEQPQPAPAPQPE 429
|
410 420 430
....*....|....*....|....*....|....
gi 1389908282 1868 EMALK----AKEAENERLKRQAEEEAYQRKLLED 1897
Cdd:NF033838 430 KPAPKpekpAEQPKAEKPADQQAEEDYARRSEEE 463
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2080-2493 |
9.77e-10 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 65.02 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2080 LAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAE 2159
Cdd:COG5281 15 AAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAEDAAAAAAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2160 AAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARV 2239
Cdd:COG5281 95 AEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2240 RIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILK 2319
Cdd:COG5281 175 AAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2320 EKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRvKELS 2399
Cdd:COG5281 255 AAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQ-ALAA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2400 LAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKE 2479
Cdd:COG5281 334 LAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQAATSAFSG 413
|
410
....*....|....
gi 1389908282 2480 MANAQQEQIEQQKA 2493
Cdd:COG5281 414 LTDALAGAVTTGKL 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1372-1736 |
1.45e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1372 EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKeeaskrqdvaaDAEKQKQNIQQELQHLkslsDQEIKSK 1451
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-----------DASRKIGEIEKEIEQL----EQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1452 NQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE-KLR----KAAQDEAERLRKQVAEETQRKK 1526
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLShsriPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1527 NAEDELKRKSDAEKEAAKQKQraldDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT--QLQTKAMSFSEQT 1604
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQ----ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlrDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1605 TKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELeiwrqkanEALRLRLQAEEEAQKKSHAQEEAEKQKLEA 1684
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 1685 ERDAKKRGKAEEAALKQKENAEKELDKQRKfaeqiAQQKLSAEQECIRLKAD 1736
Cdd:TIGR02169 964 EEEIRALEPVNMLAIQEYEEVLKRLDELKE-----KRAKLEEERKAILERIE 1010
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1354-1644 |
1.66e-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: 64.69 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1354 DAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEAS--------------KR 1419
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEErleeaeeelaeaeaEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1420 QDVAADAEKQKQNIQQELQHLKSLSDQ------EIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQEL 1493
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAEltllneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1494 RDRAAEAEKLRKAAQDEaerlRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEE 1573
Cdd:TIGR02168 865 EELIEELESELEALLNE----RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1574 KIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLE--ESLKKEQGNV--------LKLQEEADKLKKQQKEANTAREEAE 1643
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKrlENKIKELGPVnlaaieeyEELKERYDFLTAQKEDLTEAKETLE 1020
|
.
gi 1389908282 1644 Q 1644
Cdd:TIGR02168 1021 E 1021
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1264-1972 |
1.83e-09 |
|
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: 64.27 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1264 TDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKalqdpiaSPLKKPKMECASDDIIQEYVNLR-TRYSELM 1342
Cdd:TIGR04523 82 QQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE-------VELNKLEKQKKENKKNIDKFLTEiKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1343 TLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMaeahAKSVAKAEQEALELKMKMKEEASKRQDV 1422
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL----LSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1423 aadaEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRdraAEAEK 1502
Cdd:TIGR04523 231 ----KDNIEKKQQEINEKT----TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK---SEISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1503 LRKAAQDEaerLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVE 1582
Cdd:TIGR04523 300 LNNQKEQD---WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1583 EVAQ--KSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEalrLR 1660
Cdd:TIGR04523 377 KENQsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV---KE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1661 LQAEEEAQKKSHAQEEAEKQKLEAerdakkrgKAEEAALKQKenaEKELDKQRKFAEQIAQQKLSAEQECIRLKadfeha 1740
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSI--------NKIKQNLEQK---QKELKSKEKELKKLNEEKKELEEKVKDLT------ 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1741 eQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSllqmkinaekasmVNTEKSKQLLESEALKMKQLADEAar 1820
Cdd:TIGR04523 517 -KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-------------ENLEKEIDEKNKEIEELKQTQKSL-- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1821 mrsvaeeAKKQRQiAEEEAARQRSEAEKILKEklaaINEATRLKTEAEMALKAKEAENERL----------KRQAEEEAY 1890
Cdd:TIGR04523 581 -------KKKQEE-KQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAKKENEKLssiiknikskKNKLKQEVK 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1891 QRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEiHIIKINFHKASKEKADLESELKKLKGIA 1970
Cdd:TIGR04523 649 QIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITR-MIRIKDLPKLEEKYKEIEKELKKLDEFS 727
|
..
gi 1389908282 1971 DE 1972
Cdd:TIGR04523 728 KE 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2247-2607 |
2.73e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2247 VKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ 2326
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2327 EATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQ--RLDKETEGFQKsLEAERKRQLEASAEAEKLKLRVKELSLAQTK 2404
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2405 AEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTR-EADDLKSAIADleeerkklkkeaeelqrKSKEMANA 2483
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKeELERLKKRLTG-----------------LTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2484 QQEQIEQQKAELQQSFLTekglLLKREKEVEGEKKRFEKQLEdEMKKAK-------ALKDEQERQRkLMEEERKKLQAIM 2556
Cdd:PRK03918 392 ELEELEKAKEEIEEEISK----ITARIGELKKEIKELKKAIE-ELKKAKgkcpvcgRELTEEHRKE-LLEEYTAELKRIE 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 2557 DEaVRKQKEAEEEMKNKQREMD--VLDKKRLEQEKQLAEENKKLREQLQTFEI 2607
Cdd:PRK03918 466 KE-LKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1493-1868 |
3.00e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.82 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1493 LRDRAAEAEKLRKAAQDEAERL--RKQVAEETQRKKNAEDELKRKSDAEKE--------------------AAKQKQRAL 1550
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYtsRRQLAAEQYRLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1551 DDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQ--KSAATQL----------QTKAMSFSEQTTKLEESLKKEQGNV 1618
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEevDELKSQLadyqqaldvqQTRAIQYQQAVQALERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1619 L---KLQEEADKLKKQQKEANTAREEAEQEL----EIWRQ--KANEALRlRLQAE-EEAQKKSHAQE---EAEKQKLEAE 1685
Cdd:PRK04863 435 LtadNAEDWLEEFQAKEQEATEELLSLEQKLsvaqAAHSQfeQAYQLVR-KIAGEvSRSEAWDVAREllrRLREQRHLAE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1686 RDAKKRGKAEEaaLKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1765
Cdd:PRK04863 514 QLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDE---LEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1766 KQLEDELNKVRSEMDSLLQMKinaEKASMVNTEKSKQLLESEALkmkqlaDEAarMRSVAEEAKKQRQIAEEEAARQRSE 1845
Cdd:PRK04863 589 EQLQARIQRLAARAPAWLAAQ---DALARLREQSGEEFEDSQDV------TEY--MQQLLERERELTVERDELAARKQAL 657
|
410 420
....*....|....*....|...
gi 1389908282 1846 AEKILKEKLAAINEATRLKTEAE 1868
Cdd:PRK04863 658 DEEIERLSQPGGSEDPRLNALAE 680
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
34-140 |
3.14e-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: 57.51 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 34 QDERDrvqKKTFTKWVNKhlVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLK 108
Cdd:cd21299 1 ETSRE---ERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 109 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 140
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1707-2598 |
3.77e-09 |
|
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: 63.53 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1707 KELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLL---DNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL 1783
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQItskEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1784 QM--KINAEKASMVNTEKSKQLLESEALKMKQLADEaaRMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAT 1861
Cdd:TIGR00606 266 KLdnEIKALKSRKKQMEKDNSELELKMEKVFQGTDE--QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1862 RLKTE-AEMALKAKEAENERLKRQAEEEAYQRKLlEDQAAQHKQDIEEKITQLQT-----SSDSELGRQKNIVE----ET 1931
Cdd:TIGR00606 344 ELLVEqGRLQLQADRHQEHIRARDSLIQSLATRL-ELDGFERGPFSERQIKNFHTlvierQEDEAKTAAQLCADlqskER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1932 LKQKKVVEEEIHIiKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAA 2011
Cdd:TIGR00606 423 LKQEQADEIRDEK-KGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2012 EEEAARQCKAaqeEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKctaaEQKAQDVLSKNKEDVLAQEKlrdEFEN 2091
Cdd:TIGR00606 502 EVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK----DEQIRKIKSRHSDELTSLLG---YFPN 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2092 AKKLAQEAEKakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQkQQADA 2171
Cdd:TIGR00606 572 KKQLEDWLHS-----------KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEES 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2172 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVkgevndaFKQKSQVEvELARVRIQMEELVKLKL 2251
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV-------FQTEAELQ-EFISDLQSKLRLAPDKL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2252 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQralaEKILKEKMQAIQEATKL 2331
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVC 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2332 KAEAEKLQKQKDQAQETAKRLQedkqqiQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKK 2411
Cdd:TIGR00606 788 LTDVTIMERFQMELKDVERKIA------QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2412 FKKQADEVKAQlqRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEqiEQQ 2491
Cdd:TIGR00606 862 LKSKTNELKSE--KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET--SNK 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2492 KAELQQSFLTEK-----GLLLKREKEVEGEKKRFEKQLEDEMKKAKA-LKDEQERQRKLMEEERKKLQAIMDEAVR---- 2561
Cdd:TIGR00606 938 KAQDKVNDIKEKvknihGYMKDIENKIQDGKDDYLKQKETELNTVNAqLEECEKHQEKINEDMRLMRQDIDTQKIQerwl 1017
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1389908282 2562 -----------KQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKL 2598
Cdd:TIGR00606 1018 qdnltlrkrenELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL 1065
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
43-137 |
4.46e-09 |
|
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: 56.96 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 43 KTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 114
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1389908282 115 VNIRNDDIADGNPKLTLGLIWTI 137
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1361-1607 |
4.79e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1361 DDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEeaskRQDVAADAEKQKQNIQQELQHL 1440
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1441 KslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQEL-RDRAAEAEKLRkAAQDEAERLRKQVA 1519
Cdd:COG4942 96 R----AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELR-ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1520 EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKyKMQAEEAERRMKQAEEEKIRqiRVVEEVAQKSAATQLQTKAMS 1599
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEK-ELAELAAELAELQQEAEELE--ALIARLEAEAAAAAERTPAAG 247
|
....*...
gi 1389908282 1600 FSEQTTKL 1607
Cdd:COG4942 248 FAALKGKL 255
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1561-1970 |
4.85e-09 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 62.47 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1561 EEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTARE 1640
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1641 EAEQELEiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAK------KRGKAEEAALKQKENAEKELDKQRK 1714
Cdd:pfam09731 132 EVLKEAI---SKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISRekatdsALQKAEALAEKLKEVINLAKQSEEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1715 FA-EQIAQQKLSAEQECIRLKADFEhaeqqrglldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL-QMKINAEKA 1792
Cdd:pfam09731 209 AApPLLDAAPETPPKLPEHLDNVEE-----------KVEKAQSLAKLVDQYKELVASERIVFQQELVSIFpDIIPVLKED 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1793 SMVNTEKSKQLLESEALKMKQLADEAARMRsVAEEAKKQRQIAEEEAARQRSEAEKI--LKEKLAAINEATRLKTEAEMA 1870
Cdd:pfam09731 278 NLLSNDDLNSLIAHAHREIDQLSKKLAELK-KREEKHIERALEKQKEELDKLAEELSarLEEVRAADEAQLRLEFERERE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1871 LKAKEAENE---RLKRQAEE-EAYQRKLLEDQAAQ----HKQDIEEKITQLQTSSDSELGRQK---NIVEETLKQKKVVE 1939
Cdd:pfam09731 357 EIRESYEEKlrtELERQAEAhEEHLKDVLVEQEIElqreFLQDIKEKVEEERAGRLLKLNELLanlKGLEKATSSHSEVE 436
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1389908282 1940 EE----------IHIIKINFHKAS--KEKADLESELKKLKGIA 1970
Cdd:pfam09731 437 DEnrkaqqlwlaVEALRSTLEDGSadSRPRPLVRELKALKELA 479
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2203-2606 |
5.50e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2203 ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELvklklkieEENRRLMQKDKDSTQKLLAEEAEK---M 2279
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERreeL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2280 KSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKD----QAQETAKRLQED 2355
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeledRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2356 KQQIQQrldketegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVV 2435
Cdd:PRK02224 334 RVAAQA--------HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2436 Q--KLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQR--------------KSKEMANA---QQEQIEQQKAEL- 2495
Cdd:PRK02224 406 DlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETieeDRERVEELEAELe 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2496 ----QQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMK 2571
Cdd:PRK02224 486 dleeEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430
....*....|....*....|....*....|....*
gi 1389908282 2572 NKQREMDVLdkKRLEQEKQlaeENKKLREQLQTFE 2606
Cdd:PRK02224 566 EAEEAREEV--AELNSKLA---ELKERIESLERIR 595
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1367-1819 |
5.57e-09 |
|
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: 62.53 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1367 EKLKEEERRKMAEIQA------ELDKQ----KQMAEAHAKSVAKAEQ---------EALELKMKMKEEA-SKRQDVAADA 1426
Cdd:pfam10174 292 DQLKQELSKKESELLAlqtkleTLTNQnsdcKQHIEVLKESLTAKEQraailqtevDALRLRLEEKESFlNKKTKQLQDL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1427 EKQKQNIQQELQHLKSLSDQE------IKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHkakSEAELQELRDRAAEA 1500
Cdd:pfam10174 372 TEEKSTLAGEIRDLKDMLDVKerkinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN---TDTALTTLEEALSEK 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1501 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAekeaakqkqralddlqkykMQAEEAERrmkqaeeekirqirv 1580
Cdd:pfam10174 449 ERIIERLKEQREREDRERLEELESLKKENKDLKEKVSA-------------------LQPELTEK--------------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1581 veevaqKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwrqkaneALRLR 1660
Cdd:pfam10174 495 ------ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-------NDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1661 LQAEEEAQKKshaqEEAEKQKLEAERDAKKRGKAE-EAALKQKENAEKELDKQRKFAEQ-IAQQKLSAEQECIRLKAdfe 1738
Cdd:pfam10174 562 LLEQEVARYK----EESGKAQAEVERLLGILREVEnEKNDKDKKIAELESLTLRQMKEQnKKVANIKHGQQEMKKKG--- 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1739 haeqqRGLLDNELQRLKNEV-NSTEKQRKQLEDELNKVRSEMDSlLQMKIN------AEKASMVNT---EKSKQLleSEA 1808
Cdd:pfam10174 635 -----AQLLEEARRREDNLAdNSQQLQLEELMGALEKTRQELDA-TKARLSstqqslAEKDGHLTNlraERRKQL--EEI 706
|
490
....*....|.
gi 1389908282 1809 LKMKQLADEAA 1819
Cdd:pfam10174 707 LEMKQEALLAA 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2178-2416 |
5.81e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2178 KEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRiqmEELVKLKLKIEEen 2257
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2258 rrlMQKDKDSTQKLLAE---EAEKMKSLAEEAGRLSVE-AEETARQRQIAESNLAEQRALAEKILKEKmqaiqeatklkA 2333
Cdd:COG4942 95 ---LRAELEAQKEELAEllrALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADL-----------A 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2334 EAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFK 2413
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1389908282 2414 KQA 2416
Cdd:COG4942 241 ERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1334-1688 |
5.95e-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: 62.78 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1334 LRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMaeahaksvakaEQEALELKMKMK 1413
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL-----------EQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1414 EEASKRQDVAADAEKqkqnIQQELQHLK-SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE 1492
Cdd:TIGR02169 762 ELEARIEELEEDLHK----LEEALNDLEaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1493 LRDRAAEAEKLRKAAQDEAERLRKQVAEetqrkknAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEE 1572
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1573 EkirqirvVEEvaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlklqEEADKLKKQQKEantaREEAEQELEiwrqk 1652
Cdd:TIGR02169 911 Q-------IEK--KRKRLSELKAKLEALEEELSEIEDPKGEDEEIP----EEELSLEDVQAE----LQRVEEEIR----- 968
|
330 340 350
....*....|....*....|....*....|....*.
gi 1389908282 1653 ANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDA 1688
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1354-1553 |
5.98e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.75 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1354 DAQRRLEDDEKASEKLKEEERRKMAEIQ---AELDKQKQMAEAHAKSVAKAEQEALElKMKMKEEASKRQDVAADAEKQK 1430
Cdd:PRK09510 73 SAKRAEEQRKKKEQQQAEELQQKQAAEQerlKQLEKERLAAQEQKKQAEEAAKQAAL-KQKQAEEAAAKAAAAAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1431 QNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKieeeihiiriQLEKTTAHKAKSEAElqelrdRAAEAEKLRKAAQD- 1509
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKK----------KAEAEAAAKAAAEAK------KKAEAEAKKKAAAEa 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1389908282 1510 --EAERLRKQVAEETQRKKNAEDELKRKSDA-EKEAAKQKQRALDDL 1553
Cdd:PRK09510 216 kkKAAAEAKAAAAKAAAEAKAAAEKAAAAKAaEKAAAAKAAAEVDDL 262
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2014-2392 |
6.81e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2014 EAARQCKAAQEEVERLKK-KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA 2092
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2093 KKLAQEAEKAKEKAEKEAALLRQKAEEAEKQkkaaENEAAKQAKAQnDTEKQRKEaeeeaarraaaeaaalkqkQQADAE 2172
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQ----ELEAARKVKIL-EEERQRKI-------------------QQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2173 MSKHKKEAEQALQQKSQV---EKELTVVKLQLDETDKQkvlldQELQRVKgevndafkqksQVEVELARVRIQMEELVKL 2249
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRleeERAREMERVRLEEQERQ-----QQVERLR-----------QQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2250 KLKIEEENRRLMQKDKdstqkllaeEAEKMKSLAEEAGRLSVEAEETARQRQIAESnlaEQRALAEKiLKEKMQAIQeat 2329
Cdd:pfam17380 486 RKRAEEQRRKILEKEL---------EERKQAMIEEERKRKLLEKEMEERQKAIYEE---ERRREAEE-ERRKQQEME--- 549
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 2330 klkaEAEKLQKQKDQAQETAKRLQEdkqqiqqrLDKETEGFQKSLEAERKRQ-LEASAEAEKLK 2392
Cdd:pfam17380 550 ----ERRRIQEQMRKATEERSRLEA--------MEREREMMRQIVESEKARAeYEATTPITTIK 601
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4395-4433 |
7.42e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 53.87 E-value: 7.42e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 4395 FLEVQYLTGGLIEPDATNRVAIDEAVKKGTLDARTAQKL 4433
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1549-1779 |
8.71e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1549 ALDDLQKYKMQAEEAERRMKQAEEeKIRQIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESlkKEQGNVLKLQEEADKL 1628
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE-QIELLEPIRELAERYAAAR---------ERLAELEYL--RAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1629 KKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQK------ 1702
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalgl 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1703 --ENAEKELDKQRkfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEM 1779
Cdd:COG4913 374 plPASAEEFAALR---AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
151-255 |
8.98e-09 |
|
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: 56.25 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 151 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGV 229
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*.
gi 1389908282 230 TKLLDPEDVDVPHPDEKSIITYVSSL 255
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQF 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2324-2597 |
1.00e-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: 60.93 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2324 AIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2403
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2404 KAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVqkletqrLQSTREADDLKSAIAdleeerkklkkeaeelqrkSKEMANA 2483
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALL-------LSPEDFLDAVRRLQY-------------------LKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2484 QQEQIEQQKAELQQsfLTEKglllkrekevegekkrfEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQ 2563
Cdd:COG4942 148 RREQAEELRADLAE--LAAL-----------------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
250 260 270
....*....|....*....|....*....|....
gi 1389908282 2564 KEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKK 2597
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2212-2422 |
1.34e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2212 DQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLmQKDKDSTQKLLAEEAEKMKSLAEEAGRLSV 2291
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2292 EAEETARQRQIAE--------SNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRL 2363
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2364 DKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQ 2422
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1406-1965 |
1.39e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 61.20 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1406 LELKmKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQ-EIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKA 1484
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEA--QAKQDSELAKLRVEEMEQGIADEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1485 K--SEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEE 1562
Cdd:pfam05701 119 SvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLES 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1563 AERRMKQAEEEKIRqirvveevaqksaatqlqtKAMSFSEQTTKLEESLKkeqgnvlKLQEEADKLKKQQkeanTAREEA 1642
Cdd:pfam05701 199 AHAAHLEAEEHRIG-------------------AALAREQDKLNWEKELK-------QAEEELQRLNQQL----LSAKDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1643 EQELEiwrqkANEALRLRLQAEEEAQKKSHAQEEAEKQKLEaerdaKKRGKAEEAALKQkenAEKELDKQRKFAEqiaqq 1722
Cdd:pfam05701 249 KSKLE-----TASALLLDLKAELAAYMESKLKEEADGEGNE-----KKTSTSIQAALAS---AKKELEEVKANIE----- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1723 KLSAEQECIRLKAdfehaeqqrGLLDNELQRLKNEVNSTeKQRK--------QLEDELNKVRSEMdSLLQMKINAEKASM 1794
Cdd:pfam05701 311 KAKDEVNCLRVAA---------ASLRSELEKEKAELASL-RQREgmasiavsSLEAELNRTKSEI-ALVQAKEKEAREKM 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1795 VNTEKSKQLLESEALKMKQLAdEAARmrsvaEEAKKQRQIAEE-EAARQRSEA--EKILKEKLAAiNEATRLKTEAEMAL 1871
Cdd:pfam05701 380 VELPKQLQQAAQEAEEAKSLA-QAAR-----EELRKAKEEAEQaKAAASTVESrlEAVLKEIEAA-KASEKLALAAIKAL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1872 KAKEAENE----------------------RLKRQAEEEAYQRklledqaaqhkqdIEEKITQLQTSSDSELgRQKNIVE 1929
Cdd:pfam05701 453 QESESSAEstnqedsprgvtlsleeyyelsKRAHEAEELANKR-------------VAEAVSQIEEAKESEL-RSLEKLE 518
|
570 580 590
....*....|....*....|....*....|....*.
gi 1389908282 1930 ETLKQKKVVEEEIHIIKINFHKASKEKADLESELKK 1965
Cdd:pfam05701 519 EVNREMEERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
32-143 |
1.50e-08 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 56.16 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 32 KNQD------ERDRVQKKTFTKWVNKHLVKAqrHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhK 96
Cdd:cd21331 8 ENQDidwtllEGETREERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--K 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1389908282 97 LQNVQIALDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 143
Cdd:cd21331 84 LENCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1680-2145 |
1.53e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1680 QKLEAERDA--KKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqklsAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1757
Cdd:COG4717 49 ERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1758 VN--STEKQRKQLEDELNKVRSEMDSLLQmkinaekasmvntekskqllesealKMKQLADEAARMRSVAEEAKKQRQIA 1835
Cdd:COG4717 125 LQllPLYQELEALEAELAELPERLEELEE-------------------------RLEELRELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1836 EEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEayqRKLLEDQAAQHKQDIEEKITQLQT 1915
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEARLLLLIAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1916 SSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIAdetQKSKLKAEEEAEKLKKLAAEEE 1995
Cdd:COG4717 257 ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP---ALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1996 RRRKEAEEKVKRITAAEEEAARQCKAAQE-EVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSK 2074
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 2075 NKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2145
Cdd:COG4717 414 LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1717-2443 |
1.65e-08 |
|
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: 61.28 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1717 EQIAQQKLSAEQECIRlKADFEHAEQQRGL---LDNELQRLKNEVNSTEKQRKQLEDELNKVRSemdsLLQMKINAEKAS 1793
Cdd:pfam05483 51 EQVANSGDCHYQEGLK-DSDFENSEGLSRLyskLYKEAEKIKKWKVSIEAELKQKENKLQENRK----IIEAQRKAIQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1794 MVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmALKA 1873
Cdd:pfam05483 126 QFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1874 kEAENERLKR--QAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNI---VEETLKQKKVVEEEIHIIKIN 1948
Cdd:pfam05483 205 -QAENARLEMhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDEN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1949 FHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVER 2028
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2029 LKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEK 2108
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2109 EAALLRQKAEEAEKQ---KKAAENEAAKQA---KAQNDTEKQRKEAEEEAARRAAAEAAALKQ----------KQQADae 2172
Cdd:pfam05483 444 LLQAREKEIHDLEIQltaIKTSEEHYLKEVedlKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlelkKHQED-- 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2173 MSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQkvlLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVK---- 2248
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENkcnn 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2249 LKLKIEEENRRL--MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEeTARQRQIAESNLAEQRALAEKILKEKM-QAI 2325
Cdd:pfam05483 599 LKKQIENKNKNIeeLHQENKALKKKGSAENKQLNAYEIKVNKLELELA-SAKQKFEEIIDNYQKEIEDKKISEEKLlEEV 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2326 QEATKLKAEAEKLQKQKDqaqetaKRLQEDKQQIQQRLDKETEGFQKSLEaerkrqlEASAEAEKLKLRVKELSLAQTKA 2405
Cdd:pfam05483 678 EKAKAIADEAVKLQKEID------KRCQHKIAEMVALMEKHKHQYDKIIE-------ERDSELGLYKNKEQEQSSAKAAL 744
|
730 740 750
....*....|....*....|....*....|....*...
gi 1389908282 2406 EDEAKKFKKQADEVKAQLQrtekhtteivVQKLETQRL 2443
Cdd:pfam05483 745 EIELSNIKAELLSLKKQLE----------IEKEEKEKL 772
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1544-1726 |
1.67e-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: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1544 KQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIrvveevaQKSAATQLQTKAmsfseqttklEESLKKEQGNVLKLQE 1623
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEI-------AIAQANREAEEA----------ELEQEREIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1624 EADKLKKQ---QKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1700
Cdd:COG2268 243 EAELAKKKaeeRREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
170 180
....*....|....*....|....*.
gi 1389908282 1701 QKENAEKELDKQRKFAEQIAQQKLSA 1726
Cdd:COG2268 323 AEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
156-253 |
1.68e-08 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 55.56 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 156 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLD 234
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1389908282 235 PEDVDVPHPDEKSIITYVS 253
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
160-255 |
1.70e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.16 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 160 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ-----------------------EN 215
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 216 LEQAFSVAER-----------ELG-VTKLLDPEDVDVPHPDEKSIITYVSSL 255
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1504-1722 |
1.87e-08 |
|
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: 60.74 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1504 RKAAQDEAERLRKQVAE----ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKmqAEEAERRMKQAEEEKIRQir 1579
Cdd:pfam15709 328 REQEKASRDRLRAERAEmrrlEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRR--FEEIRLRKQRLEEERQRQ-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1580 vveEVAQKSAATQLQTKamsfSEQTTKLEESLKKeqgnvlKLQEEadKLKKQQKEANTAREEAEQELEIWRQKANEALRL 1659
Cdd:pfam15709 404 ---EEEERKQRLQLQAA----QERARQQQEEFRR------KLQEL--QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 1660 RLQAEEEaqkkshaQEEAEKQKLEAErdAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQ 1722
Cdd:pfam15709 469 MEMAEEE-------RLEYQRQKQEAE--EKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2168-2409 |
2.11e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2168 QADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELV 2247
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2248 klklkieeenrRLMQKDKDSTQKLLA-EEAEkmkSLAEEAGRLSVEAEETARQRQIAESnLAEQRALAEKILKEKMQAIQ 2326
Cdd:COG3883 93 -----------RALYRSGGSVSYLDVlLGSE---SFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2327 EATKLKAEAEK----LQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQ 2402
Cdd:COG3883 158 ELEALKAELEAakaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*..
gi 1389908282 2403 TKAEDEA 2409
Cdd:COG3883 238 AAAAAAA 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1689-1890 |
2.46e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 60.18 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1689 KKRGKAEEAALKQKENAEKEldkqrkfAEQIAQQKLS-AEQECIRLKADFEhaeqqrglldNELQRLKNEVNSTEKQRKQ 1767
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-------AEAIKKEALLeAKEEIHKLRNEFE----------KELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1768 LEDELNKvrsEMDSLlqmkinaekasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEA-KKQRQIAEEEAARQRSEA 1846
Cdd:PRK12704 94 KEENLDR---KLELL---------------EKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1389908282 1847 EKILKEKLaaineatRLKTEAEMALKAKEAENErLKRQAEEEAY 1890
Cdd:PRK12704 156 KEILLEKV-------EEEARHEAAVLIKEIEEE-AKEEADKKAK 191
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1582-2371 |
2.76e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.62 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1582 EEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQ-----------EEADKLKKQQKEANTAREEAEQELEIWR 1650
Cdd:pfam12128 221 QQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLShlhfgyksdetLIASRQEERQETSAELNQLLRTLDDQWK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1651 QKANEaLRLRLQAEEEA-QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQiAQQKLSAEQE 1729
Cdd:pfam12128 301 EKRDE-LNGELSAADAAvAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTG-KHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1730 CIRLKADFEHAeqqRGLLDNElQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINaekasmvNTEKSKQLLESEAL 1809
Cdd:pfam12128 379 RRRSKIKEQNN---RDIAGIK-DKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-------EFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1810 KMKQLADEAarmrSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERL--KRQAEE 1887
Cdd:pfam12128 448 ELKLRLNQA----TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLeeRQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1888 EAYQR---------KLLEDQAAQHKQDIEEKITQ---LQTSSDSELGRQKNIVEETLKQKKVVEEEIHIikinfhkasKE 1955
Cdd:pfam12128 524 ELELQlfpqagtllHFLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDV---------PE 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1956 KADLESELKKLKGIADETqkskLKAEEEaeklkklaaeeerrrkeaeekvkRITAAEEEAArqckAAQEEVERLKKKAED 2035
Cdd:pfam12128 595 WAASEEELRERLDKAEEA----LQSARE-----------------------KQAAAEEQLV----QANGELEKASREETF 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2036 ANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLrdefeNAKKLAQEAEKAKEKAEKEAALLRQ 2115
Cdd:pfam12128 644 ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ-----LDKKHQAWLEEQKEQKREARTEKQA 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2116 KAEEAEKQKKAAEnEAAKQAKAQndTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELT 2195
Cdd:pfam12128 719 YWQVVEGALDAQL-ALLKAAIAA--RRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2196 VVKLQLDETdkqkvlLDQELQRVKGEVNDAFKQKSQVEVELARvriqMEELVKLKLKIEEENRrlmqKDKDSTQKLLAEE 2275
Cdd:pfam12128 796 RYFDWYQET------WLQRRPRLATQLSNIERAISELQQQLAR----LIADTKLRRAKLEMER----KASEKQQVRLSEN 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2276 AEKMKSLAEEAGRLSVEAEETARQRQIAESNlaeqRALAEkiLKEKMQAIQEATKLKAEAEKLQKQKDQAQ---ETAKRL 2352
Cdd:pfam12128 862 LRGLRCEMSKLATLKEDANSEQAQGSIGERL----AQLED--LKLKRDYLSESVKKYVEHFKNVIADHSGSglaETWESL 935
|
810 820
....*....|....*....|..
gi 1389908282 2353 QEDKQQI---QQRLDKETEGFQ 2371
Cdd:pfam12128 936 REEDHYQndkGIRLLDYRKLVP 957
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2071-2619 |
2.76e-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: 60.47 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2071 VLSKNKEDVLAQ-EKLRDEFENAKK-LAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEA 2148
Cdd:TIGR02169 227 ELLKEKEALERQkEAIERQLASLEEeLEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2149 EEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQ 2228
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2229 KSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKL------LAEEAEKMKSLAEEAGRLSVEAEETARQRQI 2302
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagieakINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2303 AESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQ---QRLDKETEGFQKSLEAERK 2379
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHgtvAQLGSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2380 RQLEA--------SAEAEKLKLRVK--------------ELSLAQTKAEDEAKKF--------KKQADEVKAQLQRTekh 2429
Cdd:TIGR02169 547 NRLNNvvveddavAKEAIELLKRRKagratflplnkmrdERRDLSILSEDGVIGFavdlvefdPKYEPAFKYVFGDT--- 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2430 tteIVVQKLETQRLQS-------------------TREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQ--I 2488
Cdd:TIGR02169 624 ---LVVEDIEAARRLMgkyrmvtlegelfeksgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELrrI 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2489 EQQKAELQQSFLTEKGLLLKREKEVE---GEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVR---- 2561
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKleea 780
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 2562 ----KQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVsQTKESQ 2619
Cdd:TIGR02169 781 lndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-QELQEQ 841
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1482-1690 |
2.82e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 59.79 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1482 HKAKSEAELQELRdraAEAEKLRKAAQDEAERLRKQVAEETQrkknaEDELKRKSDAEKEAaKQKQRALDDLqkykmqae 1561
Cdd:PRK12704 25 RKKIAEAKIKEAE---EEAKRILEEAKKEAEAIKKEALLEAK-----EEIHKLRNEFEKEL-RERRNELQKL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1562 eaERRMKQAEEekirqirvveevaqksaatQLQTKamsfSEQTTKLEESLKKEQGNVLKLQEEadkLKKQQKEANTAREE 1641
Cdd:PRK12704 88 --EKRLLQKEE-------------------NLDRK----LELLEKREEELEKKEKELEQKQQE---LEKKEEELEELIEE 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 1642 AEQELE----IWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1690
Cdd:PRK12704 140 QLQELErisgLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKE 192
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1476-1981 |
3.49e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.24 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1476 LEKTTAHKAKSEAELQElrdraaeaEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQK 1555
Cdd:pfam12128 258 LRLSHLHFGYKSDETLI--------ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1556 YKMQAEEAERRMKQAEEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQEEADKLKKQQKEA 1635
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLPSWQ--SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ-NNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1636 NTAREEAEQELEiwrqkaneALRLRLQAEEEAQKKShAQEEAEKQKLEAErDAKKR---GKAEEAALKQKENAEKELDKQ 1712
Cdd:pfam12128 407 DRQLAVAEDDLQ--------ALESELREQLEAGKLE-FNEEEYRLKSRLG-ELKLRlnqATATPELLLQLENFDERIERA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1713 RKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ------------RKQL---EDELNKV-- 1775
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflRKEApdwEQSIGKVis 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1776 -----RSEMD------------SLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAarmRSVAEEAKKQ------- 1831
Cdd:pfam12128 557 pellhRTDLDpevwdgsvggelNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSA---REKQAAAEEQlvqange 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1832 --RQIAEEEAARQrseAEKILKEKLAaineatRLKTEAEMALKAKEAENERLKRQAEEE----AYQRKLLEDqaaQHKQD 1905
Cdd:pfam12128 634 leKASREETFART---ALKNARLDLR------RLFDEKQSEKDKKNKALAERKDSANERlnslEAQLKQLDK---KHQAW 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1906 IEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfHKA--SKEKADLESELKKLkGIaDETQKSKLKAE 1981
Cdd:pfam12128 702 LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG-AKAelKALETWYKRDLASL-GV-DPDVIAKLKRE 776
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1362-1603 |
3.61e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1362 DEKASEKLKEEERRKMAEIQAELDKQKQMAEahaksvakaeQEalelkmKMKEEASKRQdvaADAEKQKQNIQQElqhlk 1441
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAE----------QE------RLKQLEKERL---AAQEQKKQAEEAA----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1442 slsdQEIKSKNQQLEDAlvsrrkieeeihiiriqlEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEE 1521
Cdd:PRK09510 125 ----KQAALKQKQAEEA------------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1522 TQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRqirvveevAQKSAATQLQTKAMSFS 1601
Cdd:PRK09510 183 AKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA--------AEKAAAAKAAEKAAAAK 254
|
..
gi 1389908282 1602 EQ 1603
Cdd:PRK09510 255 AA 256
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1537-1854 |
3.62e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.50 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1537 DAEKEAAKQKQRalddlqkykmQAEEAERRMKQaEEEKIRQIRVVEEVAQKSAATQLQTKAMS----------FSEQTTK 1606
Cdd:pfam02029 2 EDEEEAARERRR----------RAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSgqggldeeeaFLDRTAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1607 LEESLKKEQGNVLKLQEEADKLKKQQKE--ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKShaQEEAEKQKLEA 1684
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIADEKEsvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE--KEYQENKWSTE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1685 ERDAKKRGKAEEaalkQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRglldnelqRLKNEVNSTEKQ 1764
Cdd:pfam02029 149 VRQAEEEGEEEE----DKSEEAEEVPTENFAKEEVKDEKIKKEKK---VKYESKVFLDQK--------RGHPEVKSQNGE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1765 RKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEK-------SKQLLESEAL-KMKQLADEAA-----------RMRSVA 1825
Cdd:pfam02029 214 EEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQkleelrrRRQEKESEEFeKLRQKQQEAEleleelkkkreERRKLL 293
|
330 340
....*....|....*....|....*....
gi 1389908282 1826 EEAKKQRQIAEEEAARQRSEAEKILKEKL 1854
Cdd:pfam02029 294 EEEEQRRKQEEAERKLREEEEKRRMKEEI 322
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2236-2606 |
3.72e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2236 LARVRIQMEELVKLKLKIEEENRRLMQKdkdsTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiAESNLAEQRALAE 2315
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEEELEELEA-ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2316 KIL------KEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAE 2389
Cdd:COG4717 123 KLLqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2390 KLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhtteivVQKLETQR------------LQSTREADDLKSAIA 2457
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL------EERLKEARlllliaaallalLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2458 DLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKA------ELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKA 2531
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAleeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2532 KALkdEQERQRKLMEEERKKL----QAIMDEAVRKQKEAEEEMKNKQREMDVLdkkrleqEKQLAEENKKLREQLQTFE 2606
Cdd:COG4717 357 EEL--EEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEEL-------EEQLEELLGELEELLEALD 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1481-1915 |
4.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1481 AHKAKSEAELQELRDRAA--EAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELK----RKSDAEKEAAKQKQRALDDLQ 1554
Cdd:COG4913 265 AAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDalreELDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAA--TQLQTKAMSFSEQTTKLEEslkkeqgnvlKLQEEADKLKKQQ 1632
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPASAEefAALRAEAAALLEALEEELE----------ALEEALAEAEAAL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1633 KEANTAREEAEQELEIWRQKAN----EALRLRLQAEEEAQKKS------------HAQEE-----AEK------------ 1679
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEaelpfvgelievRPEEErwrgaIERvlggfaltllvp 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1680 ----------------------QKLEAERDAKKRGKAEEAALKQK----EN-----AEKELDKQRKFA-----EQIAQQK 1723
Cdd:COG4913 495 pehyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKldfkPHpfrawLEAELGRRFDYVcvdspEELRRHP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1724 LSAEQEC-IRLKAD-FEH---------------AEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMK 1786
Cdd:COG4913 575 RAITRAGqVKGNGTrHEKddrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1787 ------INAEKASMVNTEKSKQL--LESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEaekilkeklaaIN 1858
Cdd:COG4913 655 eyswdeIDVASAEREIAELEAELerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-----------LE 723
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1859 EATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQT 1915
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1375-1722 |
4.42e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.12 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1375 RKMAEIQAELdkqKQMAEAHAKSVAKaeqealelKMKMKEEASKRQDVAadaEKQKQNIQQELQ----HLKSLSDQEIKS 1450
Cdd:COG2268 116 RDPEEIEELA---EEKLEGALRAVAA--------QMTVEELNEDREKFA---EKVQEVAGTDLAknglELESVAITDLED 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1451 KNQQLeDALvSRRKIEEEihiiriqleKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERlrkqvaeetqrkknaed 1530
Cdd:COG2268 182 ENNYL-DAL-GRRKIAEI---------IRDARIAEAEAE-RETEIAIAQANREAEEAELEQER----------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1531 ELKRKSDAEKEAAKQKQRAlddlqkykmqaeEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAmsfseqttklees 1610
Cdd:COG2268 233 EIETARIAEAEAELAKKKA------------EERREAETARAEAEAAYEIAEANAEREVQRQLEIAE------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1611 lkkeqgnvlklQEEADKLKKQQKEantaREEAEQELEIwrQKANEALRLRLQAEEEAqkkshaqeEAEKQKLEAERDAKK 1690
Cdd:COG2268 288 -----------REREIELQEKEAE----REEAELEADV--RKPAEAEKQAAEAEAEA--------EAEAIRAKGLAEAEG 342
|
330 340 350
....*....|....*....|....*....|....
gi 1389908282 1691 RGKAEEAALKQKENAEKE--LDKQRKFAEQIAQQ 1722
Cdd:COG2268 343 KRALAEAWNKLGDAAILLmlIEKLPEIAEAAAKP 376
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1374-1784 |
4.44e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 59.81 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1374 RRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMkeeASKRQDVaadaeKQKQniqQELQHLKSLSDQEIKSKNQ 1453
Cdd:PRK10246 425 RQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL---NEMRQRY-----KEKT---QQLADVKTICEQEARIKDL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1454 QLEDALVSRRKIEEeihiiriqLEKTTAHKAKSEAELQELRD---RAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAED 1530
Cdd:PRK10246 494 EAQRAQLQAGQPCP--------LCGSTSHPAVEAYQALEPGVnqsRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1531 ELKRKSDAEKEAAKQKQRAL----------DDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT-QLQTKAMS 1599
Cdd:PRK10246 566 EAQSLRQEEQALTQQWQAVCaslnitlqpqDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQ 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1600 FSEQTTKLEESLKKEQGNVLKL---QEEADKLKKQQKEANTAREEAEQ---------------------ELEIWRQKANE 1655
Cdd:PRK10246 646 LLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRIQQltplletlpqsddlphseetvALDNWRQVHEQ 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1656 ALRL-------RLQAEEEAQKKSHAQ---EEAEKQKLEAERDAKKRGKAEEAAL----KQKENAEKELDKQRKFAEQiAQ 1721
Cdd:PRK10246 726 CLSLhsqlqtlQQQDVLEAQRLQKAQaqfDTALQASVFDDQQAFLAALLDEETLtqleQLKQNLENQRQQAQTLVTQ-TA 804
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1722 QKLSAEQ----ECIRLKADFEHAEQQRGLLDnelQRLKNEVNSTEKQRKQL-EDELNkvRSEMDSLLQ 1784
Cdd:PRK10246 805 QALAQHQqhrpDGLDLTVTVEQIQQELAQLA---QQLRENTTRQGEIRQQLkQDADN--RQQQQALMQ 867
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4047-4083 |
4.49e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.71 E-value: 4.49e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1389908282 4047 IRLLEAQIATGGIIDPQESHRLPVETAYERGLFDEEM 4083
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1374-1642 |
4.69e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.12 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1374 RRKMAEIQAELDKQKQMAEAHA-KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQ--KQNIQQELQHLKSLSDQEIKS 1450
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAkkKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1451 KNQQLEDALvsrrKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAErlrkqvAEETQRKKNAED 1530
Cdd:COG2268 271 AEANAEREV----QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE------AEAIRAKGLAEA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1531 ELKRksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAeeEKIRQIRVVEEVAQKSAATQLQTKAMsfseqtTKLEES 1610
Cdd:COG2268 341 EGKR---ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPL--EKIDKITIIDGGNGGNGAGSAVAEAL------APLLES 409
|
250 260 270
....*....|....*....|....*....|..
gi 1389908282 1611 LKKEQGnvLKLQEEADKLKKQQKEANTAREEA 1642
Cdd:COG2268 410 LLEETG--LDLPGLLKGLTGAGAAAPAGEPAE 439
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1605-1966 |
5.16e-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: 59.14 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1605 TKLEESLKkEQGNVLKLQEEADKLKKQQKEAntaREEAEQELEIWRQkaneALRLRLQ-AEEEAQKKSHAQEEAEKQKLE 1683
Cdd:pfam07888 34 NRLEECLQ-ERAELLQAQEAANRQREKEKER---YKRDREQWERQRR----ELESRVAeLKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1684 AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEK 1763
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1764 QRKQLEDELNKVRSEMD----SLLQMKINAEKASMVNTEKSKQLLESEALKmkqladeaARMRSVAEEAKKQRQIAE--- 1836
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALL--------EELRSLQERLNASERKVEglg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1837 ---EEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA----ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEK 1909
Cdd:pfam07888 258 eelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1910 ITQLQtSSDSELGRQKNIveeTLKQKKVVEEEIHIIKINFHKASKEKADLESELKKL 1966
Cdd:pfam07888 338 RMERE-KLEVELGREKDC---NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1402-1738 |
6.96e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.73 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1402 EQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLS------DQEIKSKNQQLEDalvSRRKIEEEIHIIRIQ 1475
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGqggldeEEAFLDRTAKREE---RRQKRLQEALERQKE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1476 LEKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaEDELKRKSDAEKEAAKQKQralddlQK 1555
Cdd:pfam02029 89 FDPTIADEKESVAE-RKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREK--EYQENKWSTEVRQAEEEGE------EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1556 YKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEA 1635
Cdd:pfam02029 160 EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1636 NTAREEAEQELEIWRQKANEAlrlrlqAEEEAQKKSHAQEEAEkqkLEAERDAKKRgkaeeaalKQKENAEKELDKQRKF 1715
Cdd:pfam02029 240 AEVFLEAEQKLEELRRRRQEK------ESEEFEKLRQKQQEAE---LELEELKKKR--------EERRKLLEEEEQRRKQ 302
|
330 340
....*....|....*....|...
gi 1389908282 1716 AEqiAQQKLSAEQECIRLKADFE 1738
Cdd:pfam02029 303 EE--AERKLREEEEKRRMKEEIE 323
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1542-1714 |
6.99e-08 |
|
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: 56.47 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1542 AAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvVEEVAQKSAAtqLQTKAMSFSEQTTKLEESLKKEQGNVLKL 1621
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAE-------LAELEDELAA--LEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1622 QEEADKLKKQQKEANTARE--EAEQELEIW--RQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKrgKAEEA 1697
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyeALQKEIESLkrRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK--AELDE 149
|
170
....*....|....*..
gi 1389908282 1698 ALKQKENAEKELDKQRK 1714
Cdd:COG1579 150 ELAELEAELEELEAERE 166
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1396-2056 |
7.33e-08 |
|
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: 58.96 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1396 KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQ---ELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHII 1472
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1473 RIQLEKTTAHKAKSEAELQELRDRAAEAEK-------LRKAAQDEAERLRKQVAEETQRKKNAEDELKRK-SDAEKEAA- 1543
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKmilafeeLRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEiNDKEKQVSl 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1544 -----KQKQRALDDLQkykMQAEEAERRMKQAEEEKIRQIRVVEEVAQKS--AATQLQTKAMSFSEQTTK---LEESLKK 1613
Cdd:pfam05483 245 lliqiTEKENKMKDLT---FLLEESRDKANQLEEKTKLQDENLKELIEKKdhLTKELEDIKMSLQRSMSTqkaLEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1614 EQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL---RLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1690
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1691 RGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLkadFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLED 1770
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL---LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1771 ELNK----------------------VRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMK--QLADEaarMRSVAE 1826
Cdd:pfam05483 479 ELEKeklknieltahcdklllenkelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKemNLRDE---LESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1827 EAKKQRQ-------IAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE---AENERLKRQAEEE-----AYQ 1891
Cdd:pfam05483 556 EFIQKGDevkckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEelhQENKALKKKGSAEnkqlnAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1892 RKL--LEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGI 1969
Cdd:pfam05483 636 IKVnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1970 ADETQKSKlkaEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLkkkaedankqkekaEKEAEK 2049
Cdd:pfam05483 716 YDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL--------------KMEAKE 778
|
....*..
gi 1389908282 2050 QVVLAKE 2056
Cdd:pfam05483 779 NTAILKD 785
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1554-1764 |
7.40e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.28 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1554 QKYKMQAEEAERRMKQAEEEKirqirvvEEVAQKSAATQLQTKAMsfsEQTTKLEESLKKEQGNVLKL----QEEADKLK 1629
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQA-------EELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQaalkQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1630 KQQKEANTAREEAEQE-LEIWRQKANEALRLRLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAeEAALKQKENAEK 1707
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaEAAAKAAAEAKKKAEA-EAKKKAAAEAKK 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1708 ELDKQRKFAEQ--IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ 1764
Cdd:PRK09510 218 KAAAEAKAAAAkaAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGKNAPKTG 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1422-1681 |
8.55e-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: 57.85 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1422 VAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE 1501
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1502 KLRKAAQDEAERLRKQVAEE--TQRKKNAEDELKRKSDAEkeAAKQKQRALDDLQKYkmqaeeAERRMKQAEEekirqir 1579
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYL------APARREQAEE------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1580 vveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL 1659
Cdd:COG4942 155 ------LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 1389908282 1660 --RLQAEEEAQKKSHAQEEAEKQK 1681
Cdd:COG4942 229 iaRLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1363-1573 |
9.45e-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: 57.55 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1363 EKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQdvAADAEKQKQNiqqelqhlks 1442
Cdd:TIGR02794 79 EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA--EAEAERKAKE---------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1443 lsdqeiKSKNQQLEDALVSrrkieeeihiiriqlEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDE----AERLRKQV 1518
Cdd:TIGR02794 147 ------EAAKQAEEEAKAK---------------AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAKA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 1519 AEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEE 1573
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1697-1919 |
1.08e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1697 AALKQKENAEKELdkqrkfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVR 1776
Cdd:COG4942 17 AQADAAAEAEAEL-------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1777 SEMDSLlQMKINAEKASMvntekSKQLleSEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAA 1856
Cdd:COG4942 90 KEIAEL-RAELEAQKEEL-----AELL--RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 1857 INEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDS 1919
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1608-1767 |
1.09e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 58.09 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1608 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEeeAQKKSHAQEEAEKQKLEAERD 1687
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPAD--TSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1688 AKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKlsaeqecirlkadfeHAEQQRGLLD--NELQRLKNEVNSTEKQR 1765
Cdd:pfam05262 287 QIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK---------------ELEAQKKREPvaEDLQKTKPQVEAQPTSL 351
|
..
gi 1389908282 1766 KQ 1767
Cdd:pfam05262 352 NE 353
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1694-1942 |
1.21e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1694 AEEAALKQKENAEKeLDKQRKFAEQIAQQKLSAE-QECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDEL 1772
Cdd:COG4913 240 AHEALEDAREQIEL-LEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1773 NKVRSEMDSLLQmkinaekasmvntekskQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKE 1852
Cdd:COG4913 319 DALREELDELEA-----------------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1853 KLAAINEATRLKTEAemalkakeaenERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdselGRQKNIVEETL 1932
Cdd:COG4913 382 FAALRAEAAALLEAL-----------EEELEALEEALAEAEAALRDLRRELRELEAEIASLE-------RRKSNIPARLL 443
|
250
....*....|
gi 1389908282 1933 KQKKVVEEEI 1942
Cdd:COG4913 444 ALRDALAEAL 453
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1608-1968 |
1.29e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1608 EESLKKEQGNVLKLQEEADklkkQQKEANTAREEAEQELEIWRQKANEALRL-----RLQAE-EEAQKKSHAQEEA--EK 1679
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAASDHLNLVQTALRQqekieRYQADlEELEERLEEQNEVveEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1680 QKLEAERDAKKRgKAEEAAL---KQKENAEKELDKQRKFAEQI--AQQKLSAEQECIRLK-----------ADFEHAEQQ 1743
Cdd:PRK04863 375 DEQQEENEARAE-AAEEEVDelkSQLADYQQALDVQQTRAIQYqqAVQALERAKQLCGLPdltadnaedwlEEFQAKEQE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1744 rglLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSllqmkINAEKASmvntEKSKQLLEsEALKMKQLADEAARMRS 1823
Cdd:PRK04863 454 ---ATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGE-----VSRSEAW----DVARELLR-RLREQRHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1824 VAEEAKkQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALkakeaenERLKRQAEEEAYQRKLLEDQAAQHK 1903
Cdd:PRK04863 521 RLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1904 QDIEE---KITQLQTSSDSeLGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKG 1968
Cdd:PRK04863 593 ARIQRlaaRAPAWLAAQDA-LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1367-1724 |
1.33e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 56.85 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1367 EKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEaskRQDVAADAEKQKQNIQQELQhlkslsdq 1446
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY---RQELEEQIEEREQKRQEEYE-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1447 eiksknQQLEDALVSRRKIEEEIHIIRIQLEKttahKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK 1526
Cdd:pfam13868 95 ------EKLQEREQMDEIVERIQEEDQAEAEE----KLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1527 NAEDELKRKSDAEKEAAKQKQRAlddlqkyKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKamsfsEQTTK 1606
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIA-------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEA-----EKKAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1607 LEESLKKEQgnvlkLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEAlrlRLQAEEEAQKKSHAQEEAEKQKLEAER 1686
Cdd:pfam13868 233 QRQELQQAR-----EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE---QEEAEKRRMKRLEHRRELEKQIEEREE 304
|
330 340 350
....*....|....*....|....*....|....*...
gi 1389908282 1687 dakKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKL 1724
Cdd:pfam13868 305 ---QRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1717-2375 |
1.73e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1717 EQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQ----RLKNEVNSTEKQRKQLEDELN-----------KVRSEMDS 1781
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaELNQLLRTLDDQWKEKRDELNgelsaadaavaKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1782 LLQMKINAEKAsmvNTEKSKQLLESEALKMKQLADEAARM-------RSVAEEAKKQRQIAEEEAARQRSEaekiLKEKL 1854
Cdd:pfam12128 327 LEDQHGAFLDA---DIETAAADQEQLPSWQSELENLEERLkaltgkhQDVTAKYNRRRSKIKEQNNRDIAG----IKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1855 AAINEA-TRLKTEAEMALKAKEAE-NERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKItqlqtssdselgrqknIVEETL 1932
Cdd:pfam12128 400 AKIREArDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT----------------ATPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1933 KQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKklaaeeerrrkeaeekvkriTAAE 2012
Cdd:pfam12128 464 LQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ--------------------SALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2013 EEAARQCKAAQEEVERLKKKAEDANKQKEKaekeaekqvVLAKEAAQKC------TAAEQKAQDVLSKNKEDVLA----- 2081
Cdd:pfam12128 524 ELELQLFPQAGTLLHFLRKEAPDWEQSIGK---------VISPELLHRTdldpevWDGSVGGELNLYGVKLDLKRidvpe 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2082 ----QEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKqkkaaENEAAKQAKAQND------TEKQRKEAEEE 2151
Cdd:pfam12128 595 waasEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR-----EETFARTALKNARldlrrlFDEKQSEKDKK 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2152 AARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQ-----LDETDKQKVLLDQELQRVKGEVNDAF 2226
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAywqvvEGALDAQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2227 KQ-KSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDST-----------------QKLLAEEAEKMKSLAEEAGR 2288
Cdd:pfam12128 750 KAlETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQevlryfdwyqetwlqrrPRLATQLSNIERAISELQQQ 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2289 LSVEAEETARQRQIAESNLAEQRALAEKIlkekmqaIQEATKLKAEAEKLQKQK-----DQAQETAKRLQEDKQQIQQRL 2363
Cdd:pfam12128 830 LARLIADTKLRRAKLEMERKASEKQQVRL-------SENLRGLRCEMSKLATLKedansEQAQGSIGERLAQLEDLKLKR 902
|
730
....*....|..
gi 1389908282 2364 DKETEGFQKSLE 2375
Cdd:pfam12128 903 DYLSESVKKYVE 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1597-1820 |
1.86e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1597 AMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwRQKANEALRLRLQAEEEAQKKSHAQEE 1676
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1677 AEKQKLEAERD--------AKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLD 1748
Cdd:COG4942 94 ELRAELEAQKEelaellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE---LRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 1749 NELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAAR 1820
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1346-2552 |
2.17e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.75 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1346 NQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEAL--ELKMKMKEEA------- 1416
Cdd:TIGR01612 616 NEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDIDALynELSSIVKENAidntedk 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1417 SKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIriQLEKTTAHKAKSEAEL-QELRD 1495
Cdd:TIGR01612 696 AKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINK--DLNKILEDFKNKEKELsNKIND 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1496 RAAEAEKLRKAAQDEAErLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmqaeeAERRMKQAEEEKI 1575
Cdd:TIGR01612 774 YAKEKDELNKYKSKISE-IKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFK-------IINEMKFMKDDFL 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1576 RQIRVVEEVaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLklQEEADKLKKQQKEANTAREEAEQELEIWRqKANE 1655
Cdd:TIGR01612 846 NKVDKFINF-ENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDY--EKKFNDSKSLINEINKSIEEEYQNINTLK-KVDE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1656 ALRLrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQK-----ENAEKELDKqrKFAEQIAQQKLSAEQEC 1730
Cdd:TIGR01612 922 YIKI-CENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKfdntlIDKINELDK--AFKDASLNDYEAKNNEL 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1731 IRLKADFehaeqQRGLLDNELQRLKNEVNSTEKQRKQLE---DELNKVRSEMDSLLQMKI-NAEKASMVNTEKSKQLLES 1806
Cdd:TIGR01612 999 IKYFNDL-----KANLGKNKENMLYHQFDEKEKATNDIEqkiEDANKNIPNIEIAIHTSIyNIIDEIEKEIGKNIELLNK 1073
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1807 EALKMKQLAdeAARMRSVAEEAKKQR--QIAEEEAARQRSEAEKI------LKEKL-AAINEATRLKTEAEMALKAKEAE 1877
Cdd:TIGR01612 1074 EILEEAEIN--ITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIkddiknLDQKIdHHIKALEEIKKKSENYIDEIKAQ 1151
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1878 NERLKRQAEEEAYQrklledqaaQHKQDIEEKITQLQTSSDselgRQKNIVEETlkqKKVVEEeihIIKInfhkaSKEKA 1957
Cdd:TIGR01612 1152 INDLEDVADKAISN---------DDPEEIEKKIENIVTKID----KKKNIYDEI---KKLLNE---IAEI-----EKDKT 1207
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1958 DLEselkKLKGIADETQKS--KLKAEEEAEKLKKlaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERLKKKAED 2035
Cdd:TIGR01612 1208 SLE----EVKGINLSYGKNlgKLFLEKIDEEKKK----------------------SEHMIKAMEAYIEDLDEIKEKSPE 1261
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2036 ANKQKEKAEKEAEKQVVLakeaaqKCTAAEQKAQDVLSKNKEdvlaqEKLRDEFENAKKLAQEAEKAKEKaekeaallrq 2115
Cdd:TIGR01612 1262 IENEMGIEMDIKAEMETF------NISHDDDKDHHIISKKHD-----ENISDIREKSLKIIEDFSEESDI---------- 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2116 kaeeaekqkkaaeneaakqakaqNDTEKQRkeaeeeaarraaaeaaalkQKQQADAEmsKHKKEAEQALQQKSQVEKELT 2195
Cdd:TIGR01612 1321 -----------------------NDIKKEL-------------------QKNLLDAQ--KHNSDINLYLNEIANIYNILK 1356
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2196 VVKLQ--LDETDKQKVLLDQELQRVKGEVNdafkqKSQVEVELARVRIQMEELvklKLKIEEEnrrLMQKDKDSTQKLLA 2273
Cdd:TIGR01612 1357 LNKIKkiIDEVKEYTKEIEENNKNIKDELD-----KSEKLIKKIKDDINLEEC---KSKIEST---LDDKDIDECIKKIK 1425
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2274 EEaeKMKSLAEEAGRLSV--EAEETARQRQIAESNLAEQRALAEKILK-EKMQAIQEA----TKLKAEAEKLQKQKDQAQ 2346
Cdd:TIGR01612 1426 EL--KNHILSEESNIDTYfkNADENNENVLLLFKNIEMADNKSQHILKiKKDNATNDHdfniNELKEHIDKSKGCKDEAD 1503
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2347 ETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASA-EAEKLKLRVKEL----SLAQTKAEDEAKKFKKQADEVKA 2421
Cdd:TIGR01612 1504 KNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKkDSEIIIKEIKDAhkkfILEAEKSEQKIKEIKKEKFRIED 1583
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2422 QLQRTEKHTTEIV-----VQKLETQRLQST----------READDLKSAIA----DLEEERKKLKKEAEELQRKSKEMAN 2482
Cdd:TIGR01612 1584 DAAKNDKSNKAAIdiqlsLENFENKFLKISdikkkindclKETESIEKKISsfsiDSQDTELKENGDNLNSLQEFLESLK 1663
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 2483 AQQEQIEQQKAELQQsfLTEKglLLKREKEVEGEKKRFEKQLEDEMKK-AKALKDEQERQRKLMEEERKKL 2552
Cdd:TIGR01612 1664 DQKKNIEDKKKELDE--LDSE--IEKIEIDVDQHKKNYEIGIIEKIKEiAIANKEEIESIKELIEPTIENL 1730
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1476-1826 |
2.18e-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: 57.65 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1476 LEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQrkknAEDELKRKsdaekeaAKQKQRALDDLQK 1555
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ----ALDVQQTR-------AIQYQQAVQALEK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1556 YKMQAEEAERRMKQAEeekirqirvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKlkkqQKEA 1635
Cdd:COG3096 425 ARALCGLPDLTPENAE----------DYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAG----EVER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1636 NTAREEAEQELEIWRQKANEALRLR-LQAE-EEAQKKSHAQEEAEKQkleAERDAKKRGKAEEAALkQKENAEKELDKQR 1713
Cdd:COG3096 491 SQAWQTARELLRRYRSQQALAQRLQqLRAQlAELEQRLRQQQNAERL---LEEFCQRIGQQLDAAE-ELEELLAELEAQL 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1714 kfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLL----------DNELQRLKNEVNSTekqrkqLEDelnkvRSEMDSLL 1783
Cdd:COG3096 567 ---EELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaQDALERLREQSGEA------LAD-----SQEVTAAM 632
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1389908282 1784 QMKINAEKASMVNTEKS---KQLLESEALKMKQLA-DEAARMRSVAE 1826
Cdd:COG3096 633 QQLLEREREATVERDELaarKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1429-1724 |
2.41e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 56.58 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1429 QKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTtAHKAKSEAELQELRDR----AAEAEKLR 1504
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKE-QRKARLGREERRRADRrekqVIEKESRW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1505 KAAQDEAERLRKQ-----VAEETQRKKNAEDELKrksdaEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirQIR 1579
Cdd:pfam15558 97 REQAEDQENQRQEkleraRQEAEQRKQCQEQRLK-----EKEEELQALREQNSLQLQERLEEACHKRQLKEREE---QKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1580 VVEEVAQKSAATQLQTKAMSFSEQTTK------LEESLKKEQGN--------VLKLQEEADKLKKQQKEANTAREEAEQE 1645
Cdd:pfam15558 169 VQENNLSELLNHQARKVLVDCQAKAEEllrrlsLEQSLQRSQENyeqlveerHRELREKAQKEEEQFQRAKWRAEEKEEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1646 LEIWrqkanealrLRLQAEEEAQKKSHAQEEAEKQKLE-AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKL 1724
Cdd:pfam15558 249 RQEH---------KEALAELADRKIQQARQVAHKTVQDkAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKE 319
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1886-2606 |
2.63e-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: 57.49 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1886 EEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKqkkvVEEEIhiikinFHKASKEKADLESELKK 1965
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETEL------CAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1966 LKGIADETQKsklKAEEEAEKLKKLAAEEERRRKEAEEKVKRItaAEEEAARQcKAAQEEVE---RLKKKAEDankqkek 2042
Cdd:pfam01576 73 LEEILHELES---RLEEEEERSQQLQNEKKKMQQHIQDLEEQL--DEEEAARQ-KLQLEKVTteaKIKKLEED------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2043 aekeaekqvVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKlrdefENAKKLAQEAEKAKEKAEKEAALLRQKA---EE 2119
Cdd:pfam01576 140 ---------ILLLEDQNSKLSKERKLLEERISEFTSNLAEEE-----EKAKSLSKLKNKHEAMISDLEERLKKEEkgrQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2120 AEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKL 2199
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2200 QLDETDKQKVLLDQELQRVKGEVNDAFkQKSQVEVELARVRIQmeELVKLKLKIEEENRRLMQKDKDSTQK------LLA 2273
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTL-DTTAAQQELRSKREQ--EVTELKKALEEETRSHEAQLQEMRQKhtqaleELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2274 EEAEKMK-----------SLAEEAGRLSVE-------AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEA 2335
Cdd:pfam01576 363 EQLEQAKrnkanlekakqALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2336 EKLQKQKDQAQETAKRLQEDK-------QQIQQRLDKETEgfQKSLEAERKRQLeasaEAEKLKLRvkelslAQTKAEDE 2408
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVsslesqlQDTQELLQEETR--QKLNLSTRLRQL----EDERNSLQ------EQLEEEEE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2409 AKK-FKKQADEVKAQLQRTEKHTTEI--VVQKLETQRLQSTREADDLKSaiadleeerkklkkeaeelQRKSKEMAnaqQ 2485
Cdd:pfam01576 511 AKRnVERQLSTLQAQLSDMKKKLEEDagTLEALEEGKKRLQRELEALTQ-------------------QLEEKAAA---Y 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2486 EQIEQQKAELQQSfLTEKGLLLKREKEV----EGEKKRFEKQLEDEmkKAKALKDEQERQRKLMEEERKKLQAI-----M 2556
Cdd:pfam01576 569 DKLEKTKNRLQQE-LDDLLVDLDHQRQLvsnlEKKQKKFDQMLAEE--KAISARYAEERDRAEAEAREKETRALslaraL 645
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2557 DEAVRKQKEAEEEMKNKQREMDVLDKKR---------LEQEKQLAEEN-KKLREQLQTFE 2606
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKddvgknvheLERSKRALEQQvEEMKTQLEELE 705
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2266-2458 |
2.81e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2266 DSTQKLLAEEAEKMKSLA---EEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ-EATKLKAEAEKLQKQ 2341
Cdd:COG4913 238 ERAHEALEDAREQIELLEpirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRaELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2342 KDQAQEtakRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAqtkAEDEAKKFKKQADEVKA 2421
Cdd:COG4913 318 LDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP---LPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*....
gi 1389908282 2422 QLQRTEKHTTEIVVQ--KLETQRLQSTREADDLKSAIAD 2458
Cdd:COG4913 392 LLEALEEELEALEEAlaEAEAALRDLRRELRELEAEIAS 430
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1484-1714 |
2.84e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1484 AKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaekeaaKQKQRALDDLQKykmQAEEA 1563
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-----------EALQAEIDKLQA---EIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1564 ERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLE--ESLKKEQGNVLKLQEEA-DKLKKQQKEANTARE 1640
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSalSKIADADADLLEELKADkAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 1641 EAEQeleiwRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1714
Cdd:COG3883 158 ELEA-----LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1397-1967 |
2.91e-07 |
|
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: 57.06 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1397 SVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQL 1476
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKR-IRLLEKREAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1477 EktTAHKAKSEAELQElrdraAEAEKLRKAAQDEAERLRKQVAE---ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDL 1553
Cdd:pfam05557 86 E--ALNKKLNEKESQL-----ADAREVISCLKNELSELRRQIQRaelELQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1554 QKYKMQAEEAERRMKQAEEEkirqirvveevAQKSAATQLQTKAMsfseqttkleeslKKEQGNVLKLQEEADKLKKQQK 1633
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELEFE-----------IQSQEQDSEIVKNS-------------KSELARIPELEKELERLREHNK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1634 EANTAREEAeqelEIWRQKANEaLRLRLQAEEEAQKKShAQEEAEKQKLEAERDA-KKRGKAEEAALKQKENAekeldkq 1712
Cdd:pfam05557 215 HLNENIENK----LLLKEEVED-LKRKLEREEKYREEA-ATLELEKEKLEQELQSwVKLAQDTGLNLRSPEDL------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1713 RKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNE-------LQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM 1785
Cdd:pfam05557 282 SRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1786 KINAEKaSMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRS-----EAEKILKEKLAAINEA 1860
Cdd:pfam05557 362 LESYDK-ELTMSNYSPQLLE----RIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQqaqtlERELQALRQQESLADP 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1861 TRLKTEAEmALKAK----EAENERLKRQAEE---EAYQRKLLEDQ--------------AAQHKQDIEEKITQLQtssdS 1919
Cdd:pfam05557 437 SYSKEEVD-SLRRKletlELERQRLREQKNElemELERRCLQGDYdpkktkvlhlsmnpAAEAYQQRKNQLEKLQ----A 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1389908282 1920 ELGRQKNIVEE-TLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK 1967
Cdd:pfam05557 512 EIERLKRLLKKlEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQ 560
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2164-2651 |
2.93e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.05 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2164 KQKQQADAEMSKHKKEAEQALQQ-KSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEvNDAFKQKS-----QVEVELA 2237
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTVSQlRSELREAKRMYEDKIEELEKQLVLANSELTEARTE-RDQFSQESgnlddQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2238 RVRIQMEELVKLKlkieEENRRLMQKDKDSTQKLlaeeaekmkslaeeaGRLSVEAEETARQRQIAESNLAEQRALAEKI 2317
Cdd:pfam15921 385 DLHKREKELSLEK----EQNKRLWDRDTGNSITI---------------DHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2318 LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED---KQQIQQRLDKETEGFQKSLEaERKRQLEAS-AEAEKLKL 2393
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQ-EKERAIEATnAEITKLRS 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2394 RV----KELSLAQTKaEDEAKKFKKQADEVKAQLQRTEKhTTEIVVQKLE--TQRL-QSTREADDLKSaiadleeerkkl 2466
Cdd:pfam15921 525 RVdlklQELQHLKNE-GDHLRNVQTECEALKLQMAEKDK-VIEILRQQIEnmTQLVgQHGRTAGAMQV------------ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2467 kkeaeelqrkskEMANAQQEqIEQQKAELQQSfltekgLLLKREKEveGEKKRFEKQLED-EMKKAKALKDEQERQRKLM 2545
Cdd:pfam15921 591 ------------EKAQLEKE-INDRRLELQEF------KILKDKKD--AKIRELEARVSDlELEKVKLVNAGSERLRAVK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2546 EEERKKlqaimDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEK 2625
Cdd:pfam15921 650 DIKQER-----DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
490 500
....*....|....*....|....*.
gi 1389908282 2626 LVAVtTVGTSKGVLNGSTEVDGVKKE 2651
Cdd:pfam15921 725 AMKV-AMGMQKQITAKRGQIDALQSK 749
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1508-1907 |
2.97e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.41 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1508 QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAER-----RMKQAEEEKIRqirvve 1582
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEeafldRTAKREERRQK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1583 evaqksaatqlqtkamsfseqttKLEESLKKEQGNVLKLQEEADKLkkqqkeANTAREEAEQELEIWRQKANEALRLRLQ 1662
Cdd:pfam02029 78 -----------------------RLQEALERQKEFDPTIADEKESV------AERKENNEEEENSSWEKEEKRDSRLGRY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1663 AEEEAQKKShaQEEAEKQKLEAERDAKKRGKAEEaalkQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQ 1742
Cdd:pfam02029 129 KEEETEIRE--KEYQENKWSTEVRQAEEEGEEEE----DKSEEAEEVPTENFAKEEVKDEKIKKEKK---VKYESKVFLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1743 QRglldnelqRLKNEVNStekqrKQLEDELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLESEALKmkqladeaarmr 1822
Cdd:pfam02029 200 QK--------RGHPEVKS-----QNGEEEVTKLKVTTKRRQGGLSQSQERE----EEAEVFLEAEQKL------------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1823 svaEEAKKQRQIAEEEaarqrsEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnERLKRQAEEEAYQRKllEDQAAQH 1902
Cdd:pfam02029 251 ---EELRRRRQEKESE------EFEKLRQKQQEAELELEELKKKREERRKLLEEE-EQRRKQEEAERKLRE--EEEKRRM 318
|
....*
gi 1389908282 1903 KQDIE 1907
Cdd:pfam02029 319 KEEIE 323
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1428-1989 |
3.14e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1428 KQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAA 1507
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1508 QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIR---QIRVVEEV 1584
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlelLLSNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1585 AQKSaaTQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADK-------LKKQQKEANTAREEAEQELEIWRQK----- 1652
Cdd:TIGR04523 210 IQKN--KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqlnqLKDEQNKIKKQLSEKQKELEQNNKKikele 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1653 ------ANEALRLRLQAEEEAQKKSHAQ-EEAEKQKLEAERDAKKRGKA------------EEAALKQKENAEK--ELDK 1711
Cdd:TIGR04523 288 kqlnqlKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQNQISQNNKIisqlneqisqlkKELTNSESENSEKqrELEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1712 QRKFAEQIAQQKLSAEQECIRLKAD-------FEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQ 1784
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQindleskIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1785 mKINAEKASMVNTEKSKQLLESealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEaEKILKEKLAAINEATRLK 1864
Cdd:TIGR04523 448 -QDSVKELIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1865 TEAEMALKAKEAENERLKRQAEEE------AYQRKLLEDQAAQHKQDIEEkITQLQTSSDSELGRQKNIVEETLKQKKVV 1938
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDElnkddfELKKENLEKEIDEKNKEIEE-LKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 1939 EEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKK 1989
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1487-1851 |
3.84e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.41 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1487 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKrksDAEKEAAKQKQRALDDLQKykmQAEEAERR 1566
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELK---PSGQGGLDEEEAFLDRTAK---REERRQKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1567 MKQAEEEkirqirvveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTaREEAEQEl 1646
Cdd:pfam02029 79 LQEALER------------QKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE-KEYQENK- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1647 eiWRQKANealrlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQklsA 1726
Cdd:pfam02029 145 --WSTEVR-------QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---G 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1727 EQECIRLKadFEHAEQQRGLLDNELQRLKNEV-----NSTEKQRKQLEDelnKVRSEMDSLLQMKINAE------KASMv 1795
Cdd:pfam02029 213 EEEVTKLK--VTTKRRQGGLSQSQEREEEAEVfleaeQKLEELRRRRQE---KESEEFEKLRQKQQEAEleleelKKKR- 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1796 ntEKSKQLLESEALKMKQLADEaarmRSVAEEAKKQRQiaEEEAARQRSEA-EKILK 1851
Cdd:pfam02029 287 --EERRKLLEEEEQRRKQEEAE----RKLREEEEKRRM--KEEIERRRAEAaEKRQK 335
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2315-2600 |
3.85e-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: 56.11 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2315 EKILKEKMQAIQEATKLKAEAEKLQKQKDqAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLR 2394
Cdd:pfam15709 214 ESKAEKKSELISKGKKTGAKRKRTQKERN-LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVS 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2395 VKELSLAQtkaedeakkfkkQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQ 2474
Cdd:pfam15709 293 IDGRSSPT------------QTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2475 RKSKEmanAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRfekQLEDEMKKAKALKDEQERQRKLMEEERKKLQA 2554
Cdd:pfam15709 361 RRLQQ---EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR---QEEEERKQRLQLQAAQERARQQQEEFRRKLQE 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1389908282 2555 IMDEavRKQKEAEEEMKNKQRemdvldkkRLEQEKQLAEENKKLRE 2600
Cdd:pfam15709 435 LQRK--KQQEEAERAEAEKQR--------QKELEMQLAEEQKRLME 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1475-1691 |
4.51e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1475 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQ 1554
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 K-----YKMQAEEAERRMKQAEE--EKIRQIRVVEEVAQksaatQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADK 1627
Cdd:COG4942 108 EllralYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAP-----ARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 1628 LKKQQKEANTAREEAEQELEIWRQKANEalrlrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1691
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAE-----LAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
627-719 |
4.87e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 50.79 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 627 HAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAFTA 706
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1389908282 707 ALQTQWSWLLQLC 719
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2252-2601 |
4.89e-07 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 56.17 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2252 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSlaeEAGRLSVEAEETARQRQIAESNlAEQRALAEKILKEKMQ---AIQEA 2328
Cdd:NF033838 69 KILSEIQKSLDKRKHTQNVALNKKLSDIKT---EYLYELNVLKEKSEAELTSKTK-KELDAAFEQFKKDTLEpgkKVAEA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2329 TKLKAEAEKlqKQKDQAQEtakrlqedkqqiqQRLDKETEGFqKSLEAERkrqleasAEAEkLKLRVKELSLAQTKAEDE 2408
Cdd:NF033838 145 TKKVEEAEK--KAKDQKEE-------------DRRNYPTNTY-KTLELEI-------AESD-VEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2409 AKKFKKQADEVKAQLQRTEKHTTEivvqKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQ--E 2486
Cdd:NF033838 201 RDEEKIKQAKAKVESKKAEATRLE----KIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPatP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2487 QIEQQKAELQQSFLTEKGL---LLKREKEV-EGEKKRFEKQledemKKAKALKDEQERQ-----RKLMEEE--------- 2548
Cdd:NF033838 277 DKKENDAKSSDSSVGEETLpspSLKPEKKVaEAEKKVEEAK-----KKAKDQKEEDRRNyptntYKTLELEiaesdvkvk 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 2549 RKKLQAIMDEAVR-----KQKEAEEEMKNKQREMDVLD------KKRLEQEKQLAEENKKLREQ 2601
Cdd:NF033838 352 EAELELVKEEAKEprneeKIKQAKAKVESKKAEATRLEkiktdrKKAEEEAKRKAAEEDKVKEK 415
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4150-4178 |
5.25e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.86 E-value: 5.25e-07
10 20
....*....|....*....|....*....
gi 1389908282 4150 IVDPESGKEMSVYEAYQKGLIDHQTYLEL 4178
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1339-1622 |
6.32e-07 |
|
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: 56.38 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1339 SELMTLTNQYIKFIID---AQRRLEDDEKA---SEKLKEEERRKMAEI---QAEL---DKQKQMAEAHAKSVA-KAEQEA 1405
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAeadRQRLEQEKQQQLAAIsgsQSQLestDQNALETNGQAQRDAiLEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1406 L--ELKMKMKE-EASKRQDVAAD----------AEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIeeeihii 1472
Cdd:NF012221 1618 VtkELTTLAQGlDALDSQATYAGesgdqwrnpfAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDA------- 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1473 riqLEKTTAHKAKSEAELQELRDRAAEAEKlrKAAQDEAERLRKQvaeetQRKKNAEdelkrkSDAEKEAAKQKQRALDD 1552
Cdd:NF012221 1691 ---VAKSEAGVAQGEQNQANAEQDIDDAKA--DAEKRKDDALAKQ-----NEAQQAE------SDANAAANDAQSRGEQD 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1553 LQKYKMQAEEAE---RRMKQAEEEKIRQIRV-----------VEEVAQKSAA--TQLQTKAMS-FSEQTTKLE-ESLKKE 1614
Cdd:NF012221 1755 ASAAENKANQAQadaKGAKQDESDKPNRQGAagsglsgkaysVEGVAEPGSHinPDSPAAADGrFSEGLTEQEqEALEGA 1834
|
....*...
gi 1389908282 1615 QGNVLKLQ 1622
Cdd:NF012221 1835 TNAVNRLQ 1842
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2213-2570 |
6.77e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.26 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2213 QELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRL---MQKDKDSTQKLLAEEAEKMKSLAEEAGRL 2289
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFldrTAKREERRQKRLQEALERQKEFDPTIADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2290 SVEAEETARQRQIAESNLAEQRalaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQqiqqrldketeg 2369
Cdd:pfam02029 97 KESVAERKENNEEEENSSWEKE---EKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEED------------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2370 fqKSLEAERKRQLEASAEAEKLKLRVKELslaqtKAEDEAKKF---KKQADEVKAQlqRTEKHTTEIVVQKLETQRLQST 2446
Cdd:pfam02029 162 --KSEEAEEVPTENFAKEEVKDEKIKKEK-----KVKYESKVFldqKRGHPEVKSQ--NGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2447 READDLKSAiadlEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELqqsfltEKGLLLKREKEVEGEKKRFEKQLED 2526
Cdd:pfam02029 233 SQEREEEAE----VFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAEL------ELEELKKKREERRKLLEEEEQRRKQ 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1389908282 2527 EMKKAKALKDEQERQRKlMEEERKKLQAimdeAVRKQKEAEEEM 2570
Cdd:pfam02029 303 EEAERKLREEEEKRRMK-EEIERRRAEA----AEKRQKLPEDSS 341
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1740-1910 |
6.85e-07 |
|
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: 53.78 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1740 AEQQRGLLDneLQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEalkMKQLADEAA 1819
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELE---IEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1820 RMRSVAEEAKKQRQIA-----EEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKL 1894
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1389908282 1895 LEDQAAQHKQDIEEKI 1910
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1622-1757 |
7.21e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1622 QEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKShAQEEAEKQ-KLEAERDAKKRGKAEEAALK 1700
Cdd:COG2268 210 RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET-ARAEAEAAyEIAEANAEREVQRQLEIAER 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 1701 QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADfEHAEQQ----RGLLDNELQRLKNE 1757
Cdd:COG2268 289 EREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE-AEAEAEairaKGLAEAEGKRALAE 348
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1705-1901 |
7.89e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1705 AEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQ 1784
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1785 -MKINAEKASMVNtekskQLLESE--------ALKMKQLAD-------EAARMRSVAEEAKKQRQIAEEEAARQRSEAEK 1848
Cdd:COG3883 94 aLYRSGGSVSYLD-----VLLGSEsfsdfldrLSALSKIADadadlleELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 1849 ILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQ 1901
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2164-2355 |
8.09e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2164 KQKQQADAEMSKHKKEAEQA--LQQKSQVE----KELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAfkQKSQVEVELA 2237
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEqerlKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA--AAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2238 RVRIQMEELVKLKLKIEEENRRLMQKDKDSTQ----KLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRAL 2313
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAaaeaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA-------EAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908282 2314 AEKilkeKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED 2355
Cdd:PRK09510 221 AEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2113-2617 |
8.57e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2113 LRQKAEEAEKQKKAAENEAAKQAKAQndtEKQRKEaeeeaarraaaeaaalkqkqqadaeMSKHKKEAEQALQQKSQVEK 2192
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKEL---EEELKE-------------------------AEEKEEEYAELQEELEELEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2193 ELTVVKLQLDETDKQKVLLDQELQRVkgevnDAFKQKSQVEVELARVRIQMEElvkLKLKIEEENRRLMQKdkdstQKLL 2272
Cdd:COG4717 103 ELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLEE---LEERLEELRELEEEL-----EELE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2273 AEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRalaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2352
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQD-------LAEEL---EELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2353 QEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAE-AEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtekhtt 2431
Cdd:COG4717 240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2432 eivvQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQ--QEQIEQQKAELQQSF-------LTE 2502
Cdd:COG4717 314 ----EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqLEELEQEIAALLAEAgvedeeeLRA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2503 KGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK 2582
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1389908282 2583 -----KRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKE 2617
Cdd:COG4717 468 dgelaELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1981-2368 |
8.86e-07 |
|
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: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1981 EEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQK 2060
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2061 ctaaeqkaQDVLSKNKEDvlAQEKLRDEFENAKKLAQEAEKAKEKAEKeaalLRQKAEEAEKQKKAAENE-AAKQAKAQN 2139
Cdd:pfam07888 117 --------KDALLAQRAA--HEARIRELEEDIKTLTQRVLERETELER----MKERAKKAGAQRKEEEAErKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2140 dTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKkeaeQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVK 2219
Cdd:pfam07888 183 -TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT----QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2220 GEVNDAFKQKSQVEVELARVRIQMEE----LVKLKLKIEEENRRlMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEE 2295
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRAR-WAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 2296 TARQRQIAESNLAEQRALAEKILKEKMQAIQEatkLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETE 2368
Cdd:pfam07888 337 ERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1478-1775 |
9.36e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.15 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1478 KTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD----AEKEAAKQKQRALDDL 1553
Cdd:pfam09731 94 QSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDdaiqAVKAHTDSLKEASDTA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1554 QKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTkleESLKKEQGNVLKLQEEADKLKKQQK 1633
Cdd:pfam09731 174 EISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLP---EHLDNVEEKVEKAQSLAKLVDQYKE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1634 EANTAREEAEQELE---------------IWRQKAN----------EALRLRLQaEEEAQKKSHAQEEAEKQKLE----- 1683
Cdd:pfam09731 251 LVASERIVFQQELVsifpdiipvlkednlLSNDDLNsliahahreiDQLSKKLA-ELKKREEKHIERALEKQKEEldkla 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1684 -----------AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLS---AEQEcIRLKADF-----EHAEQQR 1744
Cdd:pfam09731 330 eelsarleevrAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKdvlVEQE-IELQREFlqdikEKVEEER 408
|
330 340 350
....*....|....*....|....*....|....
gi 1389908282 1745 GLLDNELQRLKNEVNSTEKQ---RKQLEDELNKV 1775
Cdd:pfam09731 409 AGRLLKLNELLANLKGLEKAtssHSEVEDENRKA 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1329-1708 |
9.65e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1329 QEYVNLRTRYSELMTLTNQyIKFIIDAQRRLEDDEKASEKLKEEERR------KMAEIQAELDKQKQMAEAHAKSVAKAE 1402
Cdd:COG4717 102 EELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPERleeleeRLEELRELEEELEELEAELAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1403 QEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQ------- 1475
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ----EELEELEEELEQLENELEAAALEERLKEARlllliaa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1476 ----LEKTTAHKAKSEAELQEL-----------RDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEK 1540
Cdd:COG4717 257 allaLLGLGGSLLSLILTIAGVlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1541 EAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQ-----IRVVEEVAQKSAATQLQtKAMSFSEQTTKLEESLKKEQ 1615
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1616 GNVLKLQEEADK--LKKQQKEANTAREEAEQELEIWRQK--ANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1691
Cdd:COG4717 416 GELEELLEALDEeeLEEELEELEEELEELEEELEELREElaELEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL 495
|
410
....*....|....*..
gi 1389908282 1692 GKAEEAALKQKENAEKE 1708
Cdd:COG4717 496 KLALELLEEAREEYREE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2251-2606 |
1.01e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2251 LKIEEENRRL------MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLA---EQRALAEKI---- 2317
Cdd:PRK04863 275 MRHANERRVHleealeLRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqTALRQQEKIeryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2318 ---------LKEKMQAIQEATKLKAEAEKlqkQKDQAQETAKRLQEDKQQIQQRLD---KETEGFQKSLEA-ERKRQLEA 2384
Cdd:PRK04863 355 adleeleerLEEQNEVVEEADEQQEENEA---RAEAAEEEVDELKSQLADYQQALDvqqTRAIQYQQAVQAlERAKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2385 SAeaeklklrvkelSLAQTKAEDEAKKFKKQADEVKAQLQRTEkhtteivvqkletQRLQSTREADD-------LKSAIA 2457
Cdd:PRK04863 432 LP------------DLTADNAEDWLEEFQAKEQEATEELLSLE-------------QKLSVAQAAHSqfeqayqLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2458 DLEEERKKLKKEAEELQRKSKEMANAQQ-EQIEQQKAELQQS-------------FLTEKGLLLKREKEVEGEKKRFEKQ 2523
Cdd:PRK04863 487 GEVSRSEAWDVARELLRRLREQRHLAEQlQQLRMRLSELEQRlrqqqraerllaeFCKRLGKNLDDEDELEQLQEELEAR 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2524 LED---EMKKAKALKDEQERQRKLMEEERKKLQAI------MDEAV-RKQKEAEEEMKNKQREMDVLdKKRLEQEKQLAE 2593
Cdd:PRK04863 567 LESlseSVSEARERRMALRQQLEQLQARIQRLAARapawlaAQDALaRLREQSGEEFEDSQDVTEYM-QQLLERERELTV 645
|
410
....*....|...
gi 1389908282 2594 ENKKLREQLQTFE 2606
Cdd:PRK04863 646 ERDELAARKQALD 658
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1084-1974 |
1.09e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.44 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1084 LTLKKMEQVYGLSSVYLDKLKTVDVVIRNTADAEEtlkNYEARLRDVSK--------VPSEQKEVEKHRSQMKSMRSEAE 1155
Cdd:TIGR00606 196 QTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKE---AQLESSREIVKsyeneldpLKNRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1156 ADQVMFDRLQDDLRKATTVHDKMTRIHSERDADLEHYRQLVNGLLERwqaVFAQIELRLRELDLLGRHMNSYRDSYEWLI 1235
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER---ELVDCQRELEKLNKERRLLNQEKTELLVEQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1236 RWLT-EARQRQEKIQAvpiSDSRALREQLTDEKKLLGEIEKNKDKIDDCHK--------NAKAYIDSVKDYEFQILTYKA 1306
Cdd:TIGR00606 350 GRLQlQADRHQEHIRA---RDSLIQSLATRLELDGFERGPFSERQIKNFHTlvierqedEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1307 LQDPIasplkKPKMECASDDIIQEYVNLRTRYSELmtltnqyiKFIIDAQRRLEDDEKASEKLKEEERRKMAEIqaELDK 1386
Cdd:TIGR00606 427 QADEI-----RDEKKGLGRTIELKKEILEKKQEEL--------KFVIKELQQLEGSSDRILELDQELRKAEREL--SKAE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1387 QKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQniQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIE 1466
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ--MEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1467 EEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQR------KKNAEDELKRKSDAEK 1540
Cdd:TIGR00606 570 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1541 EAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSaaTQLQTKAMSFSEQTTKLEESLKKE------ 1614
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFI--SDLQSKLRLAPDKLKSTESELKKKekrrde 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1615 -------QGNVL--------KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL--------RLQAEEEAQKKS 1671
Cdd:TIGR00606 728 mlglapgRQSIIdlkekeipELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKDVERK 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1672 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKAD---FEHAEQQRGLLD 1748
Cdd:TIGR00606 808 IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqIGTNLQRRQQFE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1749 NELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMkiNAEKASMVNTEKSKQLLESEALKmKQLADEAARMRSVAEEa 1828
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE--KEELISSKETSNKKAQDKVNDIK-EKVKNIHGYMKDIENK- 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1829 kkqrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmalkakeaENERLKRQAEEEAYQR-KLLEDQAAQHKqdIE 1907
Cdd:TIGR00606 964 ------IQDGKDDYLKQKETELNTVNAQLEECEKHQEKIN--------EDMRLMRQDIDTQKIQeRWLQDNLTLRK--RE 1027
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1908 EKITQLQTSSDSELGR--QKNIVEETLKQKKvVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQ 1974
Cdd:TIGR00606 1028 NELKEVEEELKQHLKEmgQMQVLQMKQEHQK-LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1437-1771 |
1.12e-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: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1437 LQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRK 1516
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1517 QVAEEtqrkknaedelKRKSDAEKEAAKQKQRALDDLQK---YKMQAEEAE-RRMKQAEEEKIRQIRVVEEVAQKSAATQ 1592
Cdd:pfam07888 112 ELSEE-----------KDALLAQRAAHEARIRELEEDIKtltQRVLERETElERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1593 LQTKA--MSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWR---------QKANEALRLRL 1661
Cdd:pfam07888 181 QQTEEelRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRslqerlnasERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1662 qaEEEAQKKSHAQEEAEKQKLEAE-------------RDAKKRGKAEEAALKQkeNAEKELDKQRKFAEQIAQ-QKLSAE 1727
Cdd:pfam07888 261 --SSMAAQRDRTQAELHQARLQAAqltlqladaslalREGRARWAQERETLQQ--SAEADKDRIEKLSAELQRlEERLQE 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1728 QECIRLKADFEHAEQ------QRGLLDNELQRLKNEVNSTEKQRKQLEDE 1771
Cdd:pfam07888 337 ERMEREKLEVELGREkdcnrvQLSESRRELQELKASLRVAQKEKEQLQAE 386
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2221-2409 |
1.15e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 54.62 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2221 EVNDAFKQKSQVEVELARVRIQMEELvklklKIEEENRRLMQKDKDSTQKllAEEAEKMKSLAEEAGRLSVEAEETARQR 2300
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKER-----ESQEDAKRAQQLKEELDKK--QIDADKAQQKADFAQDNADKQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2301 QIAESNLAEQRALAEKILKEKMQAIQeatklKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGF--QKSLEAER 2378
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKQVAENQ-----KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEaeDKELEAQK 328
|
170 180 190
....*....|....*....|....*....|.
gi 1389908282 2379 KRqLEASAEAEKLKLRVKelslAQTKAEDEA 2409
Cdd:pfam05262 329 KR-EPVAEDLQKTKPQVE----AQPTSLNED 354
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1253-1686 |
1.18e-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: 55.03 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1253 ISDSRALREQLTDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDyefQILTYKALQDPIASPL--KKPKMECASDDIIQE 1330
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT---QLNQLKDEQNKIKKQLseKQKELEQNNKKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1331 YVNLRTRYSELMTLTNQYIKfiiDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKM 1410
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKEQ---DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1411 KMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSD--QEIKSKNQQLEDALvsrRKIEEEIHIIRIQLEKTTAHKAKSEA 1488
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESkiQNQEKLNQQKDEQI---KKLQQEKELLEKEIERLKETIIKNNS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1489 ELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKsdaeKEAAKQKQRALDDLQKYKMQAEEAERRMK 1568
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1569 QAEEEKIRQIRVVEevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQ--GNVLKLQEEADKLKKQQKEANTAREEAEQEL 1646
Cdd:TIGR04523 517 KKISSLKEKIEKLE-----SEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1389908282 1647 EiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAER 1686
Cdd:TIGR04523 592 D---QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1491-1793 |
1.30e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1491 QELRDRAAEAEKLRKAAQDEAERLRKQVA------EETQRK--------KNAEDELKRKSDAEKEAAKQKQRALddlqky 1556
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVqangelEKASREetfartalKNARLDLRRLFDEKQSEKDKKNKAL------ 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1557 kmqaeeaERRMKQAEeekirqirvveevaqksaatqlqtkamsfsEQTTKLEESLKKeqgNVLKLQEEADKLKKQQKEAN 1636
Cdd:pfam12128 674 -------AERKDSAN------------------------------ERLNSLEAQLKQ---LDKKHQAWLEEQKEQKREAR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1637 TAREEAEQELEIWRQKANEALRLRLQAEEEAQKkshAQEEAEKQklEAERDAKKRGKAEEAALKQK---ENAEKELDKQR 1713
Cdd:pfam12128 714 TEKQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELKALET--WYKRDLASLGVDPDVIAKLKreiRTLERKIERIA 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1714 KFAEQIAQ----QKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEV-----------NSTEKQRKQLEDELNKVRSE 1778
Cdd:pfam12128 789 VRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTklrraklemerKASEKQQVRLSENLRGLRCE 868
|
330
....*....|....*
gi 1389908282 1779 MDSLLQMKINAEKAS 1793
Cdd:pfam12128 869 MSKLATLKEDANSEQ 883
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
31-137 |
1.43e-06 |
|
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: 50.35 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 31 RKNQDERDRVQKKTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDF 106
Cdd:cd21285 1 GKSWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSF 80
|
90 100 110
....*....|....*....|....*....|.
gi 1389908282 107 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 137
Cdd:cd21285 81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1353-1661 |
1.43e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1353 IDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQN 1432
Cdd:pfam13868 45 LDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1433 IQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAE 1512
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1513 RLRKQVAEETQRKKNAEdelkrksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQ 1592
Cdd:pfam13868 205 ELRAKLYQEEQERKERQ--------KEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1593 LQtkamsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1661
Cdd:pfam13868 277 EQ-------EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2286-2628 |
1.49e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 54.76 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2286 AGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKL----------KAEAEKLQKQKDQAQETAKRLQED 2355
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELdalavaekagQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2356 KQQI--------QQRLDKETEGFQKSLE--AERKRQLEASAEAEKLKL--RVKELSLAQTKAEDEAKKFKKQADEVKAQL 2423
Cdd:pfam07111 138 SQREleeiqrlhQEQLSSLTQAHEEALSslTSKAEGLEKSLNSLETKRagEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2424 QRTE---KHTTEIVVQKLETQRLQSTREA--DDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIE--QQKAELQ 2496
Cdd:pfam07111 218 TLVEslrKYVGEQVPPEVHSQTWELERQEllDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRkiQPSDSLE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2497 QSFLTEKGLLLKREKE-VEGEKKRFEKQLEDEMKKAKALKDE-QERQRKLMEEERKklQAIMDEAVR-KQKEAEEE---M 2570
Cdd:pfam07111 298 PEFPKKCRSLLNRWREkVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQVTSQSQE--QAILQRALQdKAAEVEVErmsA 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2571 KNKQREMDVLDKKRLEQEKQLAEENKKLReqlqtFEISSKTVSQTK-ESQTVSVEKLVA 2628
Cdd:pfam07111 376 KGLQMELSRAQEARRRQQQQTASAEEQLK-----FVVNAMSSTQIWlETTMTRVEQAVA 429
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2113-2603 |
1.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2113 LRQKAEEAEKQKKA---AENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQA-DAEMSKHKKEAEQALQQKS 2188
Cdd:COG4913 240 AHEALEDAREQIELlepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEElRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2189 QVEKELTVVKLQLDETDkqkvllDQELQRVKGEVNDAFKQKSQVEVELARvriQMEELVKLKLKIEEEnRRLMQKDKDST 2268
Cdd:COG4913 320 ALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRAR---LEALLAALGLPLPAS-AEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2269 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKI---LKEKMQAIQEATKLKAE-----AEKLQ- 2339
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAelpfvGELIEv 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2340 KQKDQAQETA----------------KRLQE-----DKQQIQQRLDkeTEGFQKSLEAERKRQLEASAEAEKLKLRVKEL 2398
Cdd:COG4913 470 RPEEERWRGAiervlggfaltllvppEHYAAalrwvNRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDFKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2399 S------LAQTKA------EDEAKKFKK---QADEVKAQLQRTEKHTTEIV-------------VQKLETQRLQSTREAD 2450
Cdd:COG4913 548 RawleaeLGRRFDyvcvdsPEELRRHPRaitRAGQVKGNGTRHEKDDRRRIrsryvlgfdnrakLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2451 DLKSAIADLEEERKKLKKEAEELQRKSK--------EMANAQQEQIEQQKAELQQSF--LTEkglLLKREKEVEGEKKRF 2520
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDASSddLAA---LEEQLEELEAELEEL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2521 EKQLEDEMKKAKALKDEQERqrklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLRE 2600
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQ----AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780
|
...
gi 1389908282 2601 QLQ 2603
Cdd:COG4913 781 RLN 783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1841-2449 |
1.84e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1841 RQRSEAEKILKEKLAAINEatrlKTEAEMALKAKEAENERLKRQAEEEAYQRKllEDQAAQHKQDIEEKITQLqtssdse 1920
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEE----KEEKDLHERLNGLESELAELDEEIERYEEQ--REQARETRDEADEVLEEH------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1921 lgrqknivEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEklkklaaeeerrrke 2000
Cdd:PRK02224 247 --------EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2001 aeekvkrITAAEEEAArqcKAAQEEVERLKKKAEDAnkqkekaekeAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVL 2080
Cdd:PRK02224 304 -------LDDADAEAV---EARREELEDRDEELRDR----------LEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2081 AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEa 2160
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2161 aalkQKQQADAEMSKHkKEAEQALQQKSQVEKeltvvklqLDETDKQKVLLDQELQRVKGEVNDafkqksqVEVELARVr 2240
Cdd:PRK02224 443 ----EEAEALLEAGKC-PECGQPVEGSPHVET--------IEEDRERVEELEAELEDLEEEVEE-------VEERLERA- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2241 iqmEELVKLKLKIE--EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNlAEQRALAEKIL 2318
Cdd:PRK02224 502 ---EDLVEAEDRIErlEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVAEL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2319 KEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKslEAERKRQLEASAEA---EKLKLRV 2395
Cdd:PRK02224 578 NSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAE--KRERKRELEAEFDEariEEAREDK 655
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 2396 KELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREA 2449
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1492-1878 |
2.06e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 53.96 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1492 ELRDRAAEAEKLRKaaqdEAERLRKQVAEETQRKK--------NAEDELKRKSDAEKEAakqkQRALDDLQKYKMQAeea 1563
Cdd:pfam03528 5 DLQQRVAELEKENA----EFYRLKQQLEAEFNQKRakfkelylAKEEDLKRQNAVLQEA----QVELDALQNQLALA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1564 errmkQAEEEKIRQIRVVEEVAQKSAATQLQTKamsFSEQTTKLEeSLKKEQGNVLKLQEEAdKLKKQQKEANTAREEAE 1643
Cdd:pfam03528 74 -----RAEMENIKAVATVSENTKQEAIDEVKSQ---WQEEVASLQ-AIMKETVREYEVQFHR-RLEQERAQWNQYRESAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1644 QELEIWRQKANEAlrlrlQAEEEAQKK-SHAQEEAEKQkleaeRDAKKRGKAEEAALKQK-ENAEKELDKQRKFAEQIAQ 1721
Cdd:pfam03528 144 REIADLRRRLSEG-----QEEENLEDEmKKAQEDAEKL-----RSVVMPMEKEIAALKAKlTEAEDKIKELEASKMKELN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1722 QKLSAEQECirlKADFEhaeQQRGLLDNELQRLKNEvnsTEKQRKQLEDELNKVRSEMDSLLQMKINAEKAsmvntekSK 1801
Cdd:pfam03528 214 HYLEAEKSC---RTDLE---MYVAVLNTQKSVLQED---AEKLRKELHEVCHLLEQERQQHNQLKHTWQKA-------ND 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1802 QLLESEALKMKQLadeaARMRSV--------AEEAKKQRQIAEEEA-ARQRSEAEKILKEKLAAINEATRLKTEAEMALK 1872
Cdd:pfam03528 278 QFLESQRLLMRDM----QRMESVltseqlrqVEEIKKKDQEEHKRArTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
....*.
gi 1389908282 1873 AKEAEN 1878
Cdd:pfam03528 354 SNVEEQ 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1489-1963 |
2.08e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1489 ELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAE-DELKRKSDAEKEAAKQKQRALDDLQKYKMQA-----EE 1562
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAElARLEAELERLEARLDALREELDELEAQIRGNggdrlEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1563 AERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAM--SFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTARE 1640
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGLPLPASaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1641 EAEQELEIWRQKAN----EALRLRLQAEEEAQKKS------------HAQEE-----AEK-------------------- 1679
Cdd:COG4913 423 ELEAEIASLERRKSnipaRLLALRDALAEALGLDEaelpfvgelievRPEEErwrgaIERvlggfaltllvppehyaaal 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1680 --------------QKLEAERDAKKRGKAEEAALKQK----EN-----AEKELDKQRKFA-----EQIAQQKLSAEQEC- 1730
Cdd:COG4913 503 rwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKldfkPHpfrawLEAELGRRFDYVcvdspEELRRHPRAITRAGq 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1731 IRLKAD-FEHAEQQRGLLDNELQRlknevnSTEKQRKQLEDELNKVRSEMDSLlqmkinaekasmvntEKSKQLLESEAL 1809
Cdd:COG4913 583 VKGNGTrHEKDDRRRIRSRYVLGF------DNRAKLAALEAELAELEEELAEA---------------EERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1810 KMKQLADEAARMRSVAEEAKKQRQIAEEEAArqrseaekiLKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEA 1889
Cdd:COG4913 642 ALQERREALQRLAEYSWDEIDVASAEREIAE---------LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELK 712
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1890 YQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ---KKVVEEEIHIIKINFHKASKEKADLESEL 1963
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1835-2603 |
2.21e-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: 54.35 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1835 AEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnerLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQ 1914
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVID---LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1915 TSSdSELGRQKNIVEETLKQKKV--------------VEEEIHIIKINFHKASKEKA----------------------- 1957
Cdd:pfam15921 149 NTV-HELEAAKCLKEDMLEDSNTqieqlrkmmlshegVLQEIRSILVDFEEASGKKIyehdsmstmhfrslgsaiskilr 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1958 DLESELKKLKG--IADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAAR---QCKAAQEEVERLKKK 2032
Cdd:pfam15921 228 ELDTEISYLKGriFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSarsQANSIQSQLEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2033 AEDANKQKEKAEKEAEKQVvlakeaaqkctaaeqkaqdvlsknkedvlaqEKLRDEFENAKKLAQeaekakekaekeaal 2112
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTV-------------------------------SQLRSELREAKRMYE--------------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2113 lrQKAEEAEKQKKAAENEAAkQAKAQNDTEKQRKEAEEeaarraaaeaaalKQKQQADAEMSKHKKEAEQALQQKSQVEK 2192
Cdd:pfam15921 342 --DKIEELEKQLVLANSELT-EARTERDQFSQESGNLD-------------DQLQKLLADLHKREKELSLEKEQNKRLWD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2193 ELTVVKLQLDETDKQKVLLDQELQRVKGEVNdAFKQKSQVEVELARVRIQ-----MEELVKLKLKIEEENRRLMQKDKDS 2267
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNMEVQRLEALLK-AMKSECQGQMERQMAAIQgknesLEKVSSLTAQLESTKEMLRKVVEEL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2268 T-QKLLAEEAEKMKSlaeeagRLSVEAEETARQRQIAESNLAEQRALAEkiLKekmqaIQEATKLKAEAEKLQKQkdQAQ 2346
Cdd:pfam15921 485 TaKKMTLESSERTVS------DLTASLQEKERAIEATNAEITKLRSRVD--LK-----LQELQHLKNEGDHLRNV--QTE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2347 ETAKRLQ-EDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLaqtkaedEAKKFKKQADEVKAQLQR 2425
Cdd:pfam15921 550 CEALKLQmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL-------ELQEFKILKDKKDAKIRE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2426 TEKHTTEIVVQKLE-----TQRLQSTREA--------DDLKSAIADLEEERKKLKKEAEELQRKSKEM---ANAQQEQIE 2489
Cdd:pfam15921 623 LEARVSDLELEKVKlvnagSERLRAVKDIkqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMettTNKLKMQLK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2490 QQKAELQQSFLTEKGL----------LLKREKEVEGEKKRFEKqLEDEMKKAKALKDEQERQRKLMEEERKKL-QAIMDE 2558
Cdd:pfam15921 703 SAQSELEQTRNTLKSMegsdghamkvAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLsQELSTV 781
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2559 AVRKQKEA---------EEEMKNKQREMDV-LDKKRLE----QEKQLAEENKKLREQLQ 2603
Cdd:pfam15921 782 ATEKNKMAgelevlrsqERRLKEKVANMEVaLDKASLQfaecQDIIQRQEQESVRLKLQ 840
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1475-1757 |
2.38e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.00 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1475 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVaEETQRKKNAEDELKRKSDAEKeaakqKQRALDDLQ 1554
Cdd:pfam13868 60 EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEK-----QRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERRMKQAEEEKIRQIRvveevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1634
Cdd:pfam13868 134 EFNEEQAEWKELEKEEEREEDERIL--------EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1635 ANTAREEAEQElEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRG------KAEEAALKQKENAEKE 1708
Cdd:pfam13868 206 LRAKLYQEEQE-RKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEfermlrKQAEDEEIEQEEAEKR 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1709 LDKQRKFAEQIAQQKLSAEQECIRLKAD-FEHAEQQRGLLDNELQRLKNE 1757
Cdd:pfam13868 285 RMKRLEHRRELEKQIEEREEQRAAEREEeLEEGERLREEEAERRERIEEE 334
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1487-1743 |
2.46e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 53.45 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1487 EAELQELRDRAAEAEKLRkAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERR 1566
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEE-ARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1567 MKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQEL 1646
Cdd:PRK07735 83 EEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1647 EIWRQKANEALRLR---LQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAAL-KQKEN-----AEKELDKQRKFAE 1717
Cdd:PRK07735 163 EKAKAKAAAAAKAKaaaLAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALaKQKASqgngdSGDEDAKAKAIAA 242
|
250 260
....*....|....*....|....*.
gi 1389908282 1718 QIAQQKLSAEQECIRLKADFEHAEQQ 1743
Cdd:PRK07735 243 AKAKAAAAARAKTKGAEGKKEEEPKQ 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2077-2561 |
2.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2077 EDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRA 2156
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2157 AAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKV-LLDQELQRVKGEVNDAFKQKSQVEVE 2235
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2236 LARVRiqmEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAE 2315
Cdd:COG4717 208 LAELE---EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2316 KILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE-AERKRQLEASAEAEKLKLR 2394
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDrIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2395 VKE--------LSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLeeerkkl 2466
Cdd:COG4717 365 LEEleqeiaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2467 kkeaeelqRKSKEMANAQQEQIEQQKAELQQ--SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKL 2544
Cdd:COG4717 438 --------EEELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
490
....*....|....*..
gi 1389908282 2545 MEEerkKLQAIMDEAVR 2561
Cdd:COG4717 510 REE---RLPPVLERASE 523
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2067-2351 |
2.84e-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: 53.49 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2067 KAQDVLSKNKEDvLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEK--- 2143
Cdd:pfam05667 204 VVPSLLERNAAE-LAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAElls 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2144 ------QRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSqvEKELTVVKLQLDETDKQKVLLDQELQR 2217
Cdd:pfam05667 283 sfsgssTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQR--EEELEELQEQLEDLESSIQELEKEIKK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2218 VKGEVndafkqkSQVEVELARVRIQMEEL---VKLK------LKIEEENRRLMQKD-KDSTQKL--LAEEAEKMKS-LAE 2284
Cdd:pfam05667 361 LESSI-------KQVEEELEELKEQNEELekqYKVKkktldlLPDAEENIAKLQALvDASAQRLveLAGQWEKHRVpLIE 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2285 EAGRLSVeaeetarqrQIAESNLAEQRALAE-KILKEKMQAIQEATKLKAEAEK-LQKQKDQAQETAKR 2351
Cdd:pfam05667 434 EYRALKE---------AKSNKEDESQRKLEEiKELREKIKEVAEEAKQKEELYKqLVAEYERLPKDVSR 493
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1500-1854 |
2.91e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.61 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1500 AEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRksdaEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIRQIR 1579
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEK----EEERKEERKRYRQELEE---QIEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1580 VVEEVAQKsaatqlqtkamsfseqttkleeslkkeqgnvLKLQEEADKLKKQQKEANTARE--EAEQELEIWRQKANEAL 1657
Cdd:pfam13868 102 QMDEIVER-------------------------------IQEEDQAEAEEKLEKQRQLREEidEFNEEQAEWKELEKEEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1658 RLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELdkqrkfAEQIAQQKLSAEQECIRLKADF 1737
Cdd:pfam13868 151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE------RDELRAKLYQEEQERKERQKER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1738 EHAEQQRGLLDNELQRLKNEVnstEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADE 1817
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQI---ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
330 340 350
....*....|....*....|....*....|....*..
gi 1389908282 1818 AARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKL 1854
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1327-1984 |
3.37e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.93 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1327 IIQEYVNLRTRYSEL--MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKqkqmAEAHAKSVAKAEQE 1404
Cdd:COG5022 792 KWRLFIKLQPLLSLLgsRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGR----SLKAKKRFSLLKKE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1405 ALELKMKMKEEASKRQDVaadaEKQKQNiqQELQHLKSLS---DQEIKSKNQQLEDalvSRRKIEEEIHIIRIQLEKtta 1481
Cdd:COG5022 868 TIYLQSAQRVELAERQLQ----ELKIDV--KSISSLKLVNlelESEIIELKKSLSS---DLIENLEFKTELIARLKK--- 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1482 HKAKSEAELQELRdraaEAEKLRKAAQD-EAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQA 1560
Cdd:COG5022 936 LLNNIDLEEGPSI----EYVKLPELNKLhEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1561 EEAERRMKQaeeekiRQIRVVEevaqksaatqlQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTARE 1640
Cdd:COG5022 1012 QESTKQLKE------LPVEVAE-----------LQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRE 1074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1641 -EAEQELEIWRQKANEALRLRLQA-EEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQ 1718
Cdd:COG5022 1075 nSLLDDKQLYQLESTENLLKTINVkDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQL 1154
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1719 IA-----QQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNStekqrkqLEDELNKVRSEMDSLLQMKI---NAE 1790
Cdd:COG5022 1155 ELdglfwEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVND-------LKNELIALFSKIFSGWPRGDklkKLI 1227
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1791 KASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKqrqiaeeeaARQRSEAEKILKEKLAAI--NEATRLKTEAE 1868
Cdd:COG5022 1228 SEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNS---------IDNLLSSYKLEEEVLPATinSLLQYINVGLF 1298
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1869 MALKAKEAENERlkRQAEEEAYQRKLLEDQAAQHK-QDIEEKITQLQTSSDSELGRQKNIveETLKQKKVVEEEIHIIKI 1947
Cdd:COG5022 1299 NALRTKASSLRW--KSATEVNYNSEELDDWCREFEiSDVDEELEELIQAVKVLQLLKDDL--NKLDELLDACYSLNPAEI 1374
|
650 660 670
....*....|....*....|....*....|....*....
gi 1389908282 1948 NFHKASKEKADLESELKK--LKGIADETQKSKLKAEEEA 1984
Cdd:COG5022 1375 QNLKSRYDPADKENNLPKeiLKKIEALLIKQELQLSLEG 1413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1484-1647 |
3.76e-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: 51.46 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1484 AKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQ-----KQRALDDLQKykm 1558
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEYEALQK--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1559 QAEEAERRMKQAEEEkirQIRVVEEVAQKSAATQLQTKAMSfseqttKLEESLKKEQGnvlKLQEEADKLKKQQKEANTA 1638
Cdd:COG1579 97 EIESLKRRISDLEDE---ILELMERIEELEEELAELEAELA------ELEAELEEKKA---ELDEELAELEAELEELEAE 164
|
....*....
gi 1389908282 1639 REEAEQELE 1647
Cdd:COG1579 165 REELAAKIP 173
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1357-1642 |
3.93e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.41 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1357 RRLEDDEKASEKLKE--EERrkmaeiQAELDKQKQMAEAHAKsvAKAEQEAlelkmkmkeeASKRQDVAADAEKQKQNIQ 1434
Cdd:PRK05035 439 RAIEQEKKKAEEAKArfEAR------QARLEREKAAREARHK--KAAEARA----------AKDKDAVAAALARVKAKKA 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1435 QELQhlKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERL 1514
Cdd:PRK05035 501 AATQ--PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1515 RKQVAEETQRKKNaedelKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAerRMKQAEEEKIRQIRVVEEVAQKSAATQlq 1594
Cdd:PRK05035 579 KAAVAAAIARAKA-----KKAAQQAASAEPEEQVAEVDPKKAAVAAAIA--RAKAKKAEQQANAEPEEPVDPRKAAVA-- 649
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1389908282 1595 tKAMSFSeqttkleESLKKEQGNVLKLQEEADKLKKQQKEANTAREEA 1642
Cdd:PRK05035 650 -AAIARA-------KARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1699-1900 |
4.22e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1699 LKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlkadfehAEQQRglldneLQRLKNEVNSTEKQRKQLEDELNKVRSE 1778
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER------LKQLEKERLAAQEQKKQAEEAAKQAALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1779 MDsllqmkiNAEKASMVNTEKSKQLLESEAlkmKQLADEAARmrsVAEEAKKQrqiAEEEAARQRSEAEKILKEKLAAIN 1858
Cdd:PRK09510 131 QK-------QAEEAAAKAAAAAKAKAEAEA---KRAAAAAKK---AAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908282 1859 EATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 1900
Cdd:PRK09510 195 AAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2116-2448 |
5.05e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2116 KAEEAEKQKKAAENEAAKQAKAQND---TEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEK 2192
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2193 ELTVVKLQLD-ETDKQKVLLDQ-ELQRVKGEVNDAFKQKSQVEVElarvriqmEELVKLKLKIEEENRRLMQKDKDSTQK 2270
Cdd:pfam07888 128 EARIRELEEDiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEEELRSLSKEFQELRN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2271 LLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKmqaiQEATKLKAEAEKLQKQKDQAQ---- 2346
Cdd:pfam07888 200 SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE----RKVEGLGEELSSMAAQRDRTQaelh 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2347 --------------ETAKRLQEDKQQIQQrldkETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKF 2412
Cdd:pfam07888 276 qarlqaaqltlqlaDASLALREGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGRE 351
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1389908282 2413 KkqaDEVKAQLQRTEKHTTEI-----VVQKLETQRLQSTRE 2448
Cdd:pfam07888 352 K---DCNRVQLSESRRELQELkaslrVAQKEKEQLQAEKQE 389
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1779-2320 |
5.19e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1779 MDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILKEKLAAI 1857
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1858 NEATRLKTEAEMALKAKEAENERLKRQAEEeayqRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKV 1937
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1938 VEEEIHIIKINFHKASKEKADLESELKKLkgiadetqKSKLKAEEEAEKLKKLAAEEERrrkeaeekvkritaaeeeAAR 2017
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLLI------------------AAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2018 QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQkctaAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQ 2097
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS----LGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2098 EAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQrkeaeeeaarraAAEAAALKQKQQADAEMSKHK 2177
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG------------VEDEEELRAALEQAEEYQELK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2178 KEAEQAlqqKSQVEKELTVVKLQLDETDKQKvlLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELvklklkieEEN 2257
Cdd:COG4717 402 EELEEL---EEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQL--------EED 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 2258 RRLMQKdkdstQKLLAEEAEKMKSLAEEAGRLSVEAE--ETARQRQIaESNLAEQRALAEKILKE 2320
Cdd:COG4717 469 GELAEL-----LQELEELKAELRELAEEWAALKLALEllEEAREEYR-EERLPPVLERASEYFSR 527
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1562-1941 |
5.24e-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: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1562 EAERRMKQAEEEKIRQI---RVVEEVAQKSAATQLQTKAMSFSEQTTKLE-------ESLKKEQGNVL---KLQEEADKL 1628
Cdd:NF012221 1468 DFARRAGLSTNNGIEVLwngEVVFASSGDASAWQQKTLKLTAKAGSNRLEfkgtghnDGLGYILDNVVatsESSQQADAV 1547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1629 KKQQKEaNTAREEAEQEleiwrQKANEALRLRLQAEEEAQ----KKSHAQEEA-EKQKLEaerdakKRGKAEEAALKQKE 1703
Cdd:NF012221 1548 SKHAKQ-DDAAQNALAD-----KERAEADRQRLEQEKQQQlaaiSGSQSQLEStDQNALE------TNGQAQRDAILEES 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1704 NA-EKELDKQRKFAEQIAQQKLSAEQECIRLKADFehAEqqrGLLDNelqrlknevnstekqrkqledelnkVRSEMDsl 1782
Cdd:NF012221 1616 RAvTKELTTLAQGLDALDSQATYAGESGDQWRNPF--AG---GLLDR-------------------------VQEQLD-- 1663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1783 lqmkiNAEKASMVNTEKSKQLLESEALKMKqlaDEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATR 1862
Cdd:NF012221 1664 -----DAKKISGKQLADAKQRHVDNQQKVK---DAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQ 1735
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1863 LKTEAEMALKAKEAENERLKRQAEEEAYQrklLEDQAAQHKQDIEEKITQlQTSSDSELGRQKNIVEETLKQKKVVEEE 1941
Cdd:NF012221 1736 AESDANAAANDAQSRGEQDASAAENKANQ---AQADAKGAKQDESDKPNR-QGAAGSGLSGKAYSVEGVAEPGSHINPD 1810
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
36-144 |
5.82e-06 |
|
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: 48.44 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 36 ERDRVQKKTFTKWVNKhlVKAQRHVTDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 106
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908282 107 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 144
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1487-1782 |
6.04e-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: 53.03 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1487 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVaeetqrkknaedelkrksdaekEAAKQKQRALDDLQKYKM-------- 1558
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQL----------------------DQLKEQLQLLNKLLPQANlladetla 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1559 -QAEEAERRMKQAEEEK--IRQirvveevaQKSAATQLQTKAMSFsEQTTKLEESLKKEqgnVLKLQEEADKLKKQ---- 1631
Cdd:COG3096 893 dRLEELREELDAAQEAQafIQQ--------HGKALAQLEPLVAVL-QSDPEQFEQLQAD---YLQAKEQQRRLKQQifal 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1632 ----QKEANTAREEAEQELEIwRQKANEALRLRL-QAEEEAQKKSHAQEEAEKQKLEAerdakkrgKAEEAALKQKENAe 1706
Cdd:COG3096 961 sevvQRRPHFSYEDAVGLLGE-NSDLNEKLRARLeQAEEARREAREQLRQAQAQYSQY--------NQVLASLKSSRDA- 1030
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908282 1707 keldKQRKFAEqiAQQKLSAeqecIRLKADFEHAEQQRGlldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSL 1782
Cdd:COG3096 1031 ----KQQTLQE--LEQELEE----LGVQADAEAEERARI----RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2169-2570 |
6.70e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2169 ADAEMSKHKKEAEQAlqQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVK 2248
Cdd:PRK02224 307 ADAEAVEARREELED--RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2249 LKLKIEEENRRLMQKDKDSTQKLlAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEK------------ 2316
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDL-GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpveg 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2317 -----ILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQqRLDKETEGFQKSLEAERKRQLEASAEAEKL 2391
Cdd:PRK02224 464 sphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEEL 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2392 KLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIvvqKLETQRLQSTREADDLKSAIADLEEERKKLKKEAE 2471
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL---KERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2472 ELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKE----VEGEKKRFEKQLEDEMKKAKALKDEQERQRKLmEE 2547
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEyleqVEEKLDELREERDDLQAEIGAVENELEELEEL-RE 698
|
410 420
....*....|....*....|....*
gi 1389908282 2548 ERKKLQAIMD--EAVRKQKEAEEEM 2570
Cdd:PRK02224 699 RREALENRVEalEALYDEAEELESM 723
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2197-2403 |
6.78e-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: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2197 VKLQLDETDKQKVLLDQELQRVKGEVNDA------FKQKS-------QVEVELARVRIQMEELVKLKLKIEEENRRLmqk 2263
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAeaaleeFRQKNglvdlseEAKLLLQQLSELESQLAEARAELAEAEARL--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2264 dkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAES------------NLAEQRALAEKILKEKMQAIQEATK- 2330
Cdd:COG3206 243 --AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpdviALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 2331 ----LKAEAEKLQKQKDQAQETAKRLQEdKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2403
Cdd:COG3206 321 eleaLQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVV 396
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1801-1962 |
6.82e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1801 KQLLESEALKMKQLAD---EAARMRsvAEEAKKQRQI-AEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 1876
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKE--AEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1877 ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQT--SSDSELGRQ--KNIVEETLKqKKVVEEEIHIIKiNFHKA 1952
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLTAEeaKEILLEKVE-EEARHEAAVLIK-EIEEE 181
|
170
....*....|
gi 1389908282 1953 SKEKADLESE 1962
Cdd:PRK12704 182 AKEEADKKAK 191
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2281-2495 |
6.93e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2281 SLAEEAGRLSvEAEETARQRQIAESNLAEQRA--LAEKILKEKmqaiQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQ 2358
Cdd:PRK09510 59 AVVEQYNRQQ-QQQKSAKRAEEQRKKKEQQQAeeLQQKQAAEQ----ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2359 IQQRLDKETEGFQKSLEAERKRQLEASAEAEklklrvkelSLAQTKAEDEAKKfkKQADEVKAQLQRTEKHTTEIVVQKL 2438
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---------AEAKKKAEAEAAK--KAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 2439 ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAEL 2495
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1587-1784 |
7.07e-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: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1587 KSAATQLQTKAMSFSEQTTKLEESLK--KEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANealRLRLQAE 1664
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA---ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1665 EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE-KELDKQRkfAEQIAQQKLSAEQECIRLKADFEHAEQQ 1743
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDvIALRAQI--AALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1389908282 1744 RGLLDNELQRLKNEV---NSTEKQRKQLEDELNKVRSEMDSLLQ 1784
Cdd:COG3206 329 EASLQAQLAQLEARLaelPELEAELRRLEREVEVARELYESLLQ 372
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1661-1866 |
7.30e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1661 LQAEEEAQK-KSHAQEEAEKQKLEAERDAKkrgkaeEAALKQKENAEKEL-DKQRKFAEQiaqqklsaEQeciRLKADFE 1738
Cdd:PRK12704 34 KEAEEEAKRiLEEAKKEAEAIKKEALLEAK------EEIHKLRNEFEKELrERRNELQKL--------EK---RLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1739 HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEdelnKVRSEMDSLLQMKINA-EKASMVNTEKSKQLLesealkMKQLADE 1817
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQELE----KKEEELEELIEEQLQElERISGLTAEEAKEIL------LEKVEEE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1818 AarmrsVAEEAKKQRQIaEEEAarqRSEAEKILKEKLA-AIneaTRLKTE 1866
Cdd:PRK12704 167 A-----RHEAAVLIKEI-EEEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2262-2432 |
7.30e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2262 QKDKDSTQKLLAE--EAEKMKSLAEEAGRL-SVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ-EATKLKAEAEK 2337
Cdd:PRK09510 74 AKRAEEQRKKKEQqqAEELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAaAAAKAKAEAEA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2338 lqkqkDQAQETAKRLQEDKQQiqqrldKETEGFQKSLEAERKRQLEASAEAeklklrvkelslaqtKAEDEAKKFKKQAD 2417
Cdd:PRK09510 154 -----KRAAAAAKKAAAEAKK------KAEAEAAKKAAAEAKKKAEAEAAA---------------KAAAEAKKKAEAEA 207
|
170
....*....|....*
gi 1389908282 2418 EVKAQLQRTEKHTTE 2432
Cdd:PRK09510 208 KKKAAAEAKKKAAAE 222
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1110-1670 |
7.94e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1110 IRNTADAEETLKNYEARL----RDVSKVPSEQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLRKATTVHDKMTRIHSER 1185
Cdd:PRK03918 185 IKRTENIEELIKEKEKELeevlREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1186 DADLEHYRQLVNGLLERWQAVfAQIELRLRELDLLGRHMNSYRDSYEWLIRWLTEARQRQEKIQAVpISDSRALREQLTD 1265
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1266 EKKLLGEIEKNKDKIDDchknakayidSVKDYEfqilTYKALQDPIASpLKKPKMECASDDIIQEYVNLRTRYSELMTLT 1345
Cdd:PRK03918 343 LKKKLKELEKRLEELEE----------RHELYE----EAKAKKEELER-LKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1346 NQYIKFIIDAQRRLEDDEKASEKLK---------------EEERRKMAEIQAELDK-QKQMAEAHAK-SVAKAEQEALEL 1408
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteEHRKELLEEYTAELKRiEKELKEIEEKeRKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1409 KMKMKEEASKRQDVAadaeKQKQNIQQELqhlKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEA 1488
Cdd:PRK03918 488 VLKKESELIKLKELA----EQLKELEEKL---KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1489 ---ELQELRDRAAEAEK-LRKAAQDEAERLRKQVAE------ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKM 1558
Cdd:PRK03918 561 lekKLDELEEELAELLKeLEELGFESVEELEERLKElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1559 QAEEAERRMKQAE----EEKIRQIRvveevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1634
Cdd:PRK03918 641 RLEELRKELEELEkkysEEEYEELR--------EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
570 580 590
....*....|....*....|....*....|....*.
gi 1389908282 1635 ANTArEEAEQELEIWRQKaneALRLRLQAEEEAQKK 1670
Cdd:PRK03918 713 LEKL-EKALERVEELREK---VKKYKALLKERALSK 744
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1525-1784 |
8.22e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 50.38 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1525 KKNAEDELKRKsdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkIRQIRvvEEVAQKSAATQLQTKAMSFSEQT 1604
Cdd:pfam12795 6 EKAKLDEAAKK--KLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAE-LRELR--QELAALQAKAEAAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1605 TKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEaLRLRLQAEEEAQKkshAQEEAEKQKLEA 1684
Cdd:pfam12795 81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQ-IRNRLNGPAPPGE---PLSEAQRWALQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1685 ERdakkrgkaeeAALKQkenaekELDKQRKfaeqiAQQKLSAEQECIRLKADFEHAEQQRglLDNELQRLKNEVNS---- 1760
Cdd:pfam12795 157 EL----------AALKA------QIDMLEQ-----ELLSNNNRQDLLKARRDLLTLRIQR--LEQQLQALQELLNEkrlq 213
|
250 260
....*....|....*....|....*
gi 1389908282 1761 -TEKQRKQLEDELNKVRSEMDSLLQ 1784
Cdd:pfam12795 214 eAEQAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
41-148 |
8.31e-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: 48.50 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 41 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 148
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
1361-1858 |
8.47e-06 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 51.96 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1361 DDEKASEKLKEEERRKMAEIQAELDKQKQmAEAHAKSVAKAE---QEALELKMKMKEEASKRQDVAADAEKQKQNIQQEL 1437
Cdd:pfam01271 69 EASHLSSRSRDGLSDEDMQIITEALRQAE-NEPGGHSRENQPyalQVEKEFKTDHSDDYETQQWEEEKLKHMRFPLRYEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1438 QHLKSLSDQEIKSKNQQLedalvsrrkieeeIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLrkaAQDEAERLRKQ 1517
Cdd:pfam01271 148 NSEEKHSEREGELSEVFE-------------NPRSQATLKKVFEEVSRLDTPSKQKREKSDEREKS---SQESGEDTYRQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1518 --VAEETQRKKNAEDElkrksDAEKEaakqkqralddlqkyKMQAEEAERRMKQaEEEKIRQIrvvEEVAQKSAATQLQT 1595
Cdd:pfam01271 212 enIPQEDQVGPEDQEP-----SEEGE---------------EDATQEEVKRSRP-RTHHGRSL---PDESSRGGQLGLEE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1596 KAMSFSEQTTKLEESLKKEQGNVLKLqEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL--RLQAEEEAQKK--- 1670
Cdd:pfam01271 268 EASEEEEEYGEESRGLSAVQTYLLRL-VNARGRGRSEKRAERERSEESEEEELKRASPYEELEItaNLQIPPSEEERmlk 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1671 ----SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDK--QRKFAEQIAQQ-------KLSAEQECIRLKADF 1737
Cdd:pfam01271 347 kagrSPRGRVDEAGALEALEALEEKRKLDLDHSRVFESSEDGAPRapQGAWVEALRNYlsygeegMEGKWNQQGPYFPNE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1738 EHAEQQRGLLDNELQRLKNE-------VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSkqlLESEALK 1810
Cdd:pfam01271 427 ENREEARFRLPQYLGELSNPwedpkqwKPSDFERKELTADKFLEGEEENEYTLSMKNSFPEYNYDGYEKR---VPSPGLD 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 1811 MKQLADEAAR---------------MRSVAEEAKKQRQIA--EEEAARQRSEAEKILKEKLAAIN 1858
Cdd:pfam01271 504 LKRQYDPVARedqllhyrkkssefpDFYDSEEKKEPPVGAekEEDSANRQTRDEDKELENLAAMD 568
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2296-2602 |
9.06e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2296 TARQRQIAEsnlAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE 2375
Cdd:pfam13868 22 KERDAQIAE---KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2376 AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVvqkLETQRLQSTREADdlksa 2455
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI---LEYLKEKAEREEE----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2456 iadleeeRKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQsfltekgLLLKREKEvEGEKKRFEKQLEDEMKKAKALK 2535
Cdd:pfam13868 171 -------REAEREEIEEEKEREIARLRAQQEKAQDEKAERDE-------LRAKLYQE-EQERKERQKEREEAEKKARQRQ 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 2536 DEQERQRKLMEEERKKLQaimdEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2602
Cdd:pfam13868 236 ELQQAREEQIELKERRLA----EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1110-1934 |
9.43e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1110 IRNTADaEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLR-KATTVHDKMT----RIHSE 1184
Cdd:TIGR01612 801 IDNIKD-EDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKeKIDSEHEQFAeltnKIKAE 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1185 -RDADLEHYRQLVNGllerwqaVFAQIELRLRELDLLGRHMNSYR--DSYEWLIRWLTEARQRQEKIQAVpisdsraLRE 1261
Cdd:TIGR01612 880 iSDDKLNDYEKKFND-------SKSLINEINKSIEEEYQNINTLKkvDEYIKICENTKESIEKFHNKQNI-------LKE 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1262 QLTDEKKLLGE---IEKN-KDKIDDCHKNAKAYID------SVKDYEFQILTYKALQDPIASPLKKPK----------ME 1321
Cdd:TIGR01612 946 ILNKNIDTIKEsnlIEKSyKDKFDNTLIDKINELDkafkdaSLNDYEAKNNELIKYFNDLKANLGKNKenmlyhqfdeKE 1025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1322 CASDDIIQEYVNLRTRYSELMTLTNQYIKFIID--------------------AQRRLEDDEKASEKLK--------EEE 1373
Cdd:TIGR01612 1026 KATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDeiekeigkniellnkeileeAEINITNFNEIKEKLKhynfddfgKEE 1105
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1374 RRKMA----EIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADA---------EKQKQNIQQELQHL 1440
Cdd:TIGR01612 1106 NIKYAdeinKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnddpeeiEKKIENIVTKIDKK 1185
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1441 KSLSDQ---------EIKSKNQQLEDalVSRRKIEEEIHIIRIQLEKTTAHKAKSE----------AELQELRDRAAEAE 1501
Cdd:TIGR01612 1186 KNIYDEikkllneiaEIEKDKTSLEE--VKGINLSYGKNLGKLFLEKIDEEKKKSEhmikameayiEDLDEIKEKSPEIE 1263
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1502 KLRKAAQDEAERLR-------KQVAEETQRKKNAED--ELKRKSDAEKEAAKQKQRALD---DLQKYKMQAEEAERRMKQ 1569
Cdd:TIGR01612 1264 NEMGIEMDIKAEMEtfnishdDDKDHHIISKKHDENisDIREKSLKIIEDFSEESDINDikkELQKNLLDAQKHNSDINL 1343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1570 AEEE--------KIRQIR-VVEEVaqKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlKLQEEADKLK----------- 1629
Cdd:TIGR01612 1344 YLNEianiynilKLNKIKkIIDEV--KEYTKEIEENNKNIKDELDKSEKLIKKIKDDI-NLEECKSKIEstlddkdidec 1420
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1630 -KQQKEANTAREEAEQELEIWRQKA---NEALRLRLQAEEEAQKKSHAQEEAEK-----------QKLEAERDAKKRGKA 1694
Cdd:TIGR01612 1421 iKKIKELKNHILSEESNIDTYFKNAdenNENVLLLFKNIEMADNKSQHILKIKKdnatndhdfniNELKEHIDKSKGCKD 1500
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1695 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAeqecIRLKADFEHAEQQRGLLDNELQRLKN----EVNSTEKQRKQLED 1770
Cdd:TIGR01612 1501 EADKNAKAIEKNKELFEQYKKDVTELLNKYSA----LAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKK 1576
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1771 ElnKVRSEMDSllqMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKqrQIAEEEAARQRSEaekiL 1850
Cdd:TIGR01612 1577 E--KFRIEDDA---AKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEK--KISSFSIDSQDTE----L 1645
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1851 KEKLAAINEatrLKTEAEmALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIE----EKITQLQTSSDSELGRQKN 1926
Cdd:TIGR01612 1646 KENGDNLNS---LQEFLE-SLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKE 1721
|
....*...
gi 1389908282 1927 IVEETLKQ 1934
Cdd:TIGR01612 1722 LIEPTIEN 1729
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
40-141 |
9.70e-06 |
|
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: 47.80 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 40 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHF 141
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1538-1793 |
9.80e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1538 AEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESLKKEQGN 1617
Cdd:COG4942 17 AQADAAAEAEAELEQLQQ---EIAELEKELAALKKEEKALLKQLAALERRIAALA---------RRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1618 VLKLQEEADKLKKQQKEanTAREEAEQELEIWRQKANEALRLRLQAEEEAQkkshaqeeaekqkleAERDA---KKRGKA 1694
Cdd:COG4942 85 LAELEKEIAELRAELEA--QKEELAELLRALYRLGRQPPLALLLSPEDFLD---------------AVRRLqylKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1695 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLdneLQRLKNEVNSTEKQRKQLEDELNK 1774
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*....
gi 1389908282 1775 VRSEMDSLLQMKINAEKAS 1793
Cdd:COG4942 225 LEALIARLEAEAAAAAERT 243
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1876-1988 |
1.03e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 52.14 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1876 AENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ-KKVVEEEIHIIKI---NFHK 1951
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEaKKEADEIIKELRQlqkGGYA 602
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908282 1952 ASKEKaDLESELKKLKGIADETQKSKLKAEEEAEKLK 1988
Cdd:PRK00409 603 SVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2777-2813 |
1.07e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 1.07e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908282 2777 RLLSAERAATGFKDPYTGAKISLFEAMNKGLIEKEQA 2813
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1442-1614 |
1.11e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 51.54 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1442 SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAelQELRDRAAEAEKLRKAAQDEAERLRKQVAEE 1521
Cdd:pfam05262 176 SISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEEL--DKKQIDADKAQQKADFAQDNADKQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1522 TQRKKNAEDELKRKSDAEKE--AAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAtQLQTKAMS 1599
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKqvAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKEL-EAQKKREP 332
|
170
....*....|....*
gi 1389908282 1600 FSEQTTKLEESLKKE 1614
Cdd:pfam05262 333 VAEDLQKTKPQVEAQ 347
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3103-3139 |
1.12e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.12e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908282 3103 RLLSAEKAVSGYHDPYTGKKVSLFEALKLGLIKKDHG 3139
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
145-255 |
1.18e-05 |
|
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: 47.49 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 145 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVA 223
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 224 ERELGVTKLLDPEDVDVPHPDEKSIITYVSSL 255
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2164-2619 |
1.21e-05 |
|
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: 51.71 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2164 KQKQQADAEMSKHKKEaEQALQQKSQVEKELTVVKLQLDETDkqkvLLDQELQRVKGEvndafKQKSQVEVELARVRIQM 2243
Cdd:pfam01576 99 KKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKIKKLEED----ILLLEDQNSKLS-----KERKLLEERISEFTSNL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2244 EElvklklkiEEENRRLMQKDKDSTQKLLAEEAEKMKSlaEEAGRLSVEAEETARQRQIAE--SNLAEQRALAEKILKEK 2321
Cdd:pfam01576 169 AE--------EEEKAKSLSKLKNKHEAMISDLEERLKK--EEKGRQELEKAKRKLEGESTDlqEQIAELQAQIAELRAQL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2322 MQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQrlDKETEGFQKSLEAERKRQLEASAEAEKLKL-------- 2393
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE--DLESERAARNKAEKQRRDLGEELEALKTELedtldtta 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2394 --------RVKELSLAQTKAEDEAKKFKKQADEV-KAQLQRTEKHTTEIVVQKLETQRLQSTREAddLKSAIADLEEERK 2464
Cdd:pfam01576 317 aqqelrskREQEVTELKKALEEETRSHEAQLQEMrQKHTQALEELTEQLEQAKRNKANLEKAKQA--LESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2465 KLKKEAEELQRKSKEMANAQQE-QIEQQKAELQQSFLTEKGLLLKREKE-VEGEKKRFEKQLEDEMKKAKALKDE-QERQ 2541
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSELEsVSSLLNEAEGKNIKLSKDVSSLESQlQDTQ 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 2542 RKLMEEERKKLQAimdeaVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQ 2619
Cdd:pfam01576 475 ELLQEETRQKLNL-----STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGK 547
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3935-3973 |
1.27e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.27e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1389908282 3935 YLEGSSCIAGVYVESSKDRLSIYQAMKKNMIRPGTAFEL 3973
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1952-2612 |
1.30e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.76 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1952 ASKEKADLESELKKLKG--IADETQKSKLKaEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERL 2029
Cdd:pfam12128 249 EFNTLESAELRLSHLHFgyKSDETLIASRQ-EERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2030 ---KKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAA-EQKAQDVLSKNKedvlAQEKLRDEfENAKKLAQEAEKAKEK 2105
Cdd:pfam12128 328 edqHGAFLDADIETAAADQEQLPSWQSELENLEERLKAlTGKHQDVTAKYN----RRRSKIKE-QNNRDIAGIKDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2106 AekeaallrqkaEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALK--------------QKQQADA 2171
Cdd:pfam12128 403 R-----------EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKlrlnqatatpelllQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2172 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAfkqksqvevelarvriqMEELVKLKL 2251
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL-----------------ELQLFPQAG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2252 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETA-----RQRQI-------AESNLAEQRALAEKIL- 2318
Cdd:pfam12128 535 TLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvklDLKRIdvpewaaSEEELRERLDKAEEALq 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2319 --KEKMQAIQEA-TKLKAEAEKLQKQK-------DQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEaERKRQLEasAEA 2388
Cdd:pfam12128 615 saREKQAAAEEQlVQANGELEKASREEtfartalKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ERLNSLE--AQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2389 EKLKLRVKELSLAQTKAEDEAKKFKKQADEVkaqLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKK 2468
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQV---VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2469 EAEELQRKSKEMaNAQQEQIEQQKAE-------LQQSFLTEKGLLLKREKEVEGEKKRFEKQLedemkkaKALKDEQERQ 2541
Cdd:pfam12128 769 VIAKLKREIRTL-ERKIERIAVRRQEvlryfdwYQETWLQRRPRLATQLSNIERAISELQQQL-------ARLIADTKLR 840
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2542 RKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQR--------EMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTV 2612
Cdd:pfam12128 841 RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedanseQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNV 919
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1484-1574 |
1.62e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1484 AKSEAELQELRDRAAEAEKLRKaaqdEAERLRKQVAEETQRKKNAEDELKRKSDAE--------KEAAKQKQRALDDLQK 1555
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQK 598
|
90 100
....*....|....*....|....*
gi 1389908282 1556 YKM------QAEEAERRMKQAEEEK 1574
Cdd:PRK00409 599 GGYasvkahELIEARKRLNKANEKK 623
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1417-1670 |
1.65e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 50.85 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1417 SKRQDVaadAEKQKqNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKseaelqeLRDR 1496
Cdd:PRK11637 51 SIQQDI---AAKEK-SVRQQQQQRASLLAQ-LKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAK-------LEQQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1497 AAEAEKLRKAAQDEAERLRKQVA-------EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEaerrmKQ 1569
Cdd:PRK11637 119 QAAQERLLAAQLDAAFRQGEHTGlqlilsgEESQRGERILAYFGYLNQARQETIAELKQTREELAAQKAELEE-----KQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1570 AEEEKIrqirvveeVAQKSAATQLQTKAMSFSEQT-TKLEESLKKEQGNVLKL-QEEA---DKLKKQQKEantAREEAEQ 1644
Cdd:PRK11637 194 SQQKTL--------LYEQQAQQQKLEQARNERKKTlTGLESSLQKDQQQLSELrANESrlrDSIARAERE---AKARAER 262
|
250 260
....*....|....*....|....*.
gi 1389908282 1645 EleiwrqkANEALRLRlQAEEEAQKK 1670
Cdd:PRK11637 263 E-------AREAARVR-DKQKQAKRK 280
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1603-1813 |
1.76e-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: 50.23 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1603 QTTKLEESLKKEQGNVLKlQEEADKLKKQQKEANTAREEAEQELEiwRQKANEA----LRLRLQAEEEAQKKSHAQEEAE 1678
Cdd:TIGR02794 39 QAVLVDPGAVAQQANRIQ-QQKKPAAKKEQERQKKLEQQAEEAEK--QRAAEQArqkeLEQRAAAEKAAKQAEQAAKQAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1679 KQKLEAERdAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAE----QECIRLKADFEHAEQQrgllDNELQRL 1754
Cdd:TIGR02794 116 EKQKQAEE-AKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakkkAEEAKKKAEAEAKAKA----EAEAKAK 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1755 KNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQ 1813
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1668-1877 |
1.95e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1668 QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKADFEHAEQQRgll 1747
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ----KQAEEAAAKAA--- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1748 dnELQRLKnevnsTEKQRKQLEDELNKVRSEMDsllqmKINAEKASMVNTEKSKQLLESEAlkmKQLADEAARMRSVAEE 1827
Cdd:PRK09510 143 --AAAKAK-----AEAEAKRAAAAAKKAAAEAK-----KKAEAEAAKKAAAEAKKKAEAEA---AAKAAAEAKKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 1828 AKKQRQIAEEEAARQ-RSEAEKILKEKLAAINEATRLKTEAEMALKAKEAE 1877
Cdd:PRK09510 208 KKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2280-2494 |
1.97e-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: 50.23 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2280 KSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKilkekmQAIQEATKLKAEAEKLQKQKD--QAQETAKRLQEDKQ 2357
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAakQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2358 QIQQRLDKETEGFQKSLEAERKRQLEA----SAEAEKLKlrvKELSLAQTKAEdEAKkfKKQADEVKAQLQRTEKHTTEI 2433
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEeaakQAEEEAKA---KAAAEAKKKAE-EAK--KKAEAEAKAKAEAEAKAKAEE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 2434 VVQKLETQRLQSTRE----ADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2494
Cdd:TIGR02794 194 AKAKAEAAKAKAAAEaaakAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3933-3970 |
2.07e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.07e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1389908282 3933 KKYLEGSSCIAGVYVESSKDRLSIYQAMKKNMIRPGTA 3970
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
178-255 |
2.20e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 46.14 E-value: 2.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 178 DNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSvAERELGVTKLLDPEDVDVPHPDEKSIITYVSSL 255
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3473-3508 |
2.35e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.35e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1389908282 3473 LLEAQLATGGIIDPASSHRVPTDVAIQRGYFSKQMA 3508
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1626-1990 |
2.37e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.51 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1626 DKLKKQQKEANTAREEAEqeleiwrqkaNEALRLRLQAEEEAQKKSHAQEEAEK-QKLEAERDAKKRGKAEEAALKQK-- 1702
Cdd:pfam05557 16 NEKKQMELEHKRARIELE----------KKASALKRQLDRESDRNQELQKRIRLlEKREAEAEEALREQAELNRLKKKyl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1703 ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLkNEVNSTEKQRKQledELNKVRSEMDSL 1782
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL-QERLDLLKAKAS---EAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1783 LQMKINAEkASMVNTEKSKQLLESEALKMKQLADEAARMRSVaeEAKKQRQIAEEEAARQRSEAEKILKEKLAAINeaTR 1862
Cdd:pfam05557 162 QSSLAEAE-QRIKELEFEIQSQEQDSEIVKNSKSELARIPEL--EKELERLREHNKHLNENIENKLLLKEEVEDLK--RK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1863 LKTEAEMALKAKEAENERLKRQAEEEAYQrKLLEDQAAQHK--QDIEEKITQLQtSSDSELGRQKNIVEETLKQKKVVEE 1940
Cdd:pfam05557 237 LEREEKYREEAATLELEKEKLEQELQSWV-KLAQDTGLNLRspEDLSRRIEQLQ-QREIVLKEENSSLTSSARQLEKARR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1941 EIHIIKINfhkASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKL 1990
Cdd:pfam05557 315 ELEQELAQ---YLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI 361
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2211-2565 |
2.44e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.82 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2211 LDQELQRVKGEVNDAfkQKSQVEVELARVRIQMEElvklklKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEagRLS 2290
Cdd:PRK10929 28 ITQELEQAKAAKTPA--QAEIVEALQSALNWLEER------KGSLERAKQYQQVIDNFPKLSAELRQQLNNERDE--PRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2291 VEAEETARqrqiaesnlaeqrALAEKILKEKMQAIQEATKLKAEAEKLQKQKD------QAQETAKRLQEDkqqIQQRLd 2364
Cdd:PRK10929 98 VPPNMSTD-------------ALEQEILQVSSQLLEKSRQAQQEQDRAREISDslsqlpQQQTEARRQLNE---IERRL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2365 ketEGFQKSLEAERKRQLEA-SAEAEKLKLRVKELSLAQTKAED-------EAKKFKKQADEVKAQLQRTEKHTTEIVVQ 2436
Cdd:PRK10929 161 ---QTLGTPNTPLAQAQLTAlQAESAALKALVDELELAQLSANNrqelarlRSELAKKRSQQLDAYLQALRNQLNSQRQR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2437 KLEtQRLQSTR----EADDLKSAIADlEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQ--SFLTEKGLLLKrE 2510
Cdd:PRK10929 238 EAE-RALESTEllaeQSGDLPKSIVA-QFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQalNTLREQSQWLG-V 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908282 2511 KEVEGEKKRFE----------KQLEDEMKK--AKALK--DEQERQRKLMEEERKKLQA-------IMDEAVRKQKE 2565
Cdd:PRK10929 315 SNALGEALRAQvarlpempkpQQLDTEMAQlrVQRLRyeDLLNKQPQLRQIRQADGQPltaeqnrILDAQLRTQRE 390
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3434-3470 |
2.60e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.60e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908282 3434 KLLSAEKAITGYRDPYTGNKISLFQAMKKELVLREHA 3470
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2327-2584 |
2.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2327 EATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQ--QRLDKETEGFQKSL-EAERKRQLEASAEAEKLKLRVKELSLAQT 2403
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAAReRLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2404 KAEDEAKKFKKQADEVKAQLQRTEKHtteivVQKLETQRLQS-TREADDLKSAIADleeerkklkkeaeelqrkskemAN 2482
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREE-----LDELEAQIRGNgGDRLEQLEREIER----------------------LE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2483 AQQEQIEQQKAELQQsFLTEKGLllkrekEVEGEKKRFEKQLEdemkKAKALKDEQERQRKLMEEERkklqaimDEAVRK 2562
Cdd:COG4913 352 RELEERERRRARLEA-LLAALGL------PLPASAEEFAALRA----EAAALLEALEEELEALEEAL-------AEAEAA 413
|
250 260
....*....|....*....|..
gi 1389908282 2563 QKEAEEEMKNKQREMDVLDKKR 2584
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRK 435
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1475-1704 |
2.78e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1475 QLEKTTAHKAKSEAELQELRDRA-AEAEKLRkaAQDEAERLRKQVAEeTQRKKNAEDE--LKRKSDAEKEAAKQKQRA-- 1549
Cdd:NF012221 1543 QADAVSKHAKQDDAAQNALADKErAEADRQR--LEQEKQQQLAAISG-SQSQLESTDQnaLETNGQAQRDAILEESRAvt 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1550 ---------LDDLQKYKMQAEEAERRMKQAEEEKIRQiRVVEEV--AQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNV 1618
Cdd:NF012221 1620 kelttlaqgLDALDSQATYAGESGDQWRNPFAGGLLD-RVQEQLddAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGV 1698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1619 LKLQEeadklKKQQKEANTAREEAEQEleiwrQKANEALRlrlqAEEEAQK-KSHAQEEAEKQKLEAERDAKKRG----- 1692
Cdd:NF012221 1699 AQGEQ-----NQANAEQDIDDAKADAE-----KRKDDALA----KQNEAQQaESDANAAANDAQSRGEQDASAAEnkanq 1764
|
250
....*....|...
gi 1389908282 1693 -KAEEAALKQKEN 1704
Cdd:NF012221 1765 aQADAKGAKQDES 1777
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4143-4171 |
2.84e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 2.84e-05
10 20
....*....|....*....|....*....
gi 1389908282 4143 VRKRRVVIVDPESGKEMSVYEAYQKGLID 4171
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1378-1790 |
3.11e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.68 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1378 AEIQAELD---KQKQmAEAHAKSVAKAEQEALEL---KMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSK 1451
Cdd:PRK11281 39 ADVQAQLDalnKQKL-LEAEDKLVQQDLEQTLALldkIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1452 -----NQQLEDALVSRRkieeeihiiriqlekttahkakseAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK 1526
Cdd:PRK11281 118 lstlsLRQLESRLAQTL------------------------DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1527 NAEDELKrKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRM-------------KQAEEEKIRQIRVVEEVAqksaatQL 1593
Cdd:PRK11281 174 QIRNLLK-GGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKslegntqlqdllqKQRDYLTARIQRLEHQLQ------LL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1594 QT----KAMSFSEQTTKLEESLKKEQgnvlklQEEADKLKKQQKEANTareEAEQELEIWRQKANEALRLRLQAeeeaqk 1669
Cdd:PRK11281 247 QEainsKRLTLSEKTVQEAQSQDEAA------RIQANPLVAQELEINL---QLSQRLLKATEKLNTLTQQNLRV------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1670 kshaqeeaeKQKLE----AERDAKKRGKAEEAAL-------KQKENAEKeLDKQRKFAEQIAQqklsaeqecIRLKAdFE 1738
Cdd:PRK11281 312 ---------KNWLDrltqSERNIKEQISVLKGSLllsrilyQQQQALPS-ADLIEGLADRIAD---------LRLEQ-FE 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1739 hAEQQRGLL-------DNELQRLKNEVNSTEKQ--------RKQLEDELNKvrsEMDSLLQMKINAE 1790
Cdd:PRK11281 372 -INQQRDALfqpdayiDKLEAGHKSEVTDEVRDallqlldeRRELLDQLNK---QLNNQLNLAINLQ 434
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2193-2592 |
3.21e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2193 ELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIeeenrrlmqKDKDSTQKLL 2272
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI---------KTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2273 AEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2352
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2353 QEDKQQIQQRLDKETE--GFQKSLEAERKRQLEASAEAEKLKlrvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHT 2430
Cdd:PRK01156 349 DDLNNQILELEGYEMDynSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEINVKLQDISSKV 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2431 TEIvvqkleTQRLQSTRE-ADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQsfltekgllLKR 2509
Cdd:PRK01156 426 SSL------NQRIRALREnLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIRE---------IEI 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2510 EKEVEGEKKRFEKQLEDEMKKAKAlkDEQERQRKLMEEERKKLQAIMD-EAVRKQKEAE-EEMKNKQREMDV--LDKKRL 2585
Cdd:PRK01156 491 EVKDIDEKIVDLKKRKEYLESEEI--NKSINEYNKIESARADLEDIKIkINELKDKHDKyEEIKNRYKSLKLedLDSKRT 568
|
....*..
gi 1389908282 2586 EQEKQLA 2592
Cdd:PRK01156 569 SWLNALA 575
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1820-2620 |
3.30e-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: 50.43 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1820 RMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAlKAKEAENERLKRQaeeeayQRKLLEDQA 1899
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV-KSYENELDPLKNR------LKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1900 AQHKqdIEEKITQLQTSsdsELGRQKNIVEETLKQKKV---VEEEIHIIKINFHKASKEK----ADLESELKKLkgiade 1972
Cdd:TIGR00606 263 KIMK--LDNEIKALKSR---KKQMEKDNSELELKMEKVfqgTDEQLNDLYHNHQRTVREKerelVDCQRELEKL------ 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1973 TQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRitaaeeEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVV 2052
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRAR------DSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2053 LAKEAAQKCTaaeqkaqDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAA 2132
Cdd:TIGR00606 406 EAKTAAQLCA-------DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2133 KQAKAQNDTEKQRKEAEEEAARRAAAEAaalkQKQQADAEMSKhKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLD 2212
Cdd:TIGR00606 479 ELRKAERELSKAEKNSLTETLKKEVKSL----QNEKADLDRKL-RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRK 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2213 QELQRV------------KGEVNDAF----KQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLaeEA 2276
Cdd:TIGR00606 554 IKSRHSdeltsllgyfpnKKQLEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF--DV 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2277 EKMKSLAEEAGRLSVEAEETARQRQI--AESNLAEQRAL------------------AEKILKEKMQAIQEATKL----K 2332
Cdd:TIGR00606 632 CGSQDEESDLERLKEEIEKSSKQRAMlaGATAVYSQFITqltdenqsccpvcqrvfqTEAELQEFISDLQSKLRLapdkL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2333 AEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQksleaERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKK- 2411
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-----NKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKv 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2412 ----------FKKQADEVK----AQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKS 2477
Cdd:TIGR00606 787 cltdvtimerFQMELKDVErkiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2478 KEM---------ANAQQEQIEQQKAELQ---QSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLM 2545
Cdd:TIGR00606 867 NELkseklqigtNLQRRQQFEEQLVELStevQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI 946
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908282 2546 EEERKKLQAIMDEAVRK-QKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQT 2620
Cdd:TIGR00606 947 KEKVKNIHGYMKDIENKiQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT 1022
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2069-2627 |
3.65e-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: 50.43 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2069 QDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAEneaAKQAKAQNDTEKQRKEA 2148
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELE---LKMEKVFQGTDEQLNDL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2149 EEEAARRAAAEAAALKQKQQadaEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVN-DAFK 2227
Cdd:TIGR00606 307 YHNHQRTVREKERELVDCQR---ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2228 QKSQVEvelarvrIQMEELVKLKlkieeenRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNL 2307
Cdd:TIGR00606 384 RGPFSE-------RQIKNFHTLV-------IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2308 AEQRALAEKILKEKMQAIQEATK-LKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASA 2386
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRiLELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2387 EAEKLKlrvKELSLAQTKAEDEAKKFK---KQADEVKAQL---------------QRTEKHTTE-------IVVQKLETQ 2441
Cdd:TIGR00606 530 HTTTRT---QMEMLTKDKMDKDEQIRKiksRHSDELTSLLgyfpnkkqledwlhsKSKEINQTRdrlaklnKELASLEQN 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2442 RLQSTREADDLK---SAIADLEEERKKLKKEAEELQRKSKEMANA-QQEQIEQQKAELQQSFLTEKGL-------LLKRE 2510
Cdd:TIGR00606 607 KNHINNELESKEeqlSSYEDKLFDVCGSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQFITQLTDenqsccpVCQRV 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2511 KEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKL-------QAIMDEAVRKQKEAEEEMKNKQREMDVLDKK 2583
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 2584 RLEQEKQLAEENKKL--------------REQLQTFEISSKTVSQTKESQTVSVEKLV 2627
Cdd:TIGR00606 767 IEEQETLLGTIMPEEesakvcltdvtimeRFQMELKDVERKIAQQAAKLQGSDLDRTV 824
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1514-1950 |
3.70e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 49.90 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1514 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQ---AEEEKIRQIRVVEEVAQKSAA 1590
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKelaSQQEKRAQEKEALRKEMKKER 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1591 TQLQTKAMSFSEqttkleeslkkeqgNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEAL-RLRLQAEEEAQK 1669
Cdd:pfam15964 399 EELGATMLALSQ--------------NVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCgEMRYQLNQTKMK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1670 KshaqEEAEKQKLEAErdaKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDN 1749
Cdd:pfam15964 465 K----DEAEKEHREYR---TKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1750 E----LQRLKNEVNSTEKQRKQLEDELNKvrsemdSLLQMKINAEKAsmVNTEKSkqLLESEALKMKQLADEAARMrsva 1825
Cdd:pfam15964 538 EkesiQQSFSNEAKAQALQAQQREQELTQ------KMQQMEAQHDKT--VNEQYS--LLTSQNTFIAKLKEECCTL---- 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1826 eeAKKQRQIAEeeaaRQRSEAEKILKEKLAAINEAtrlkteaemalkakeaenERLKRQAEEeayqrklLEDQAAQH--- 1902
Cdd:pfam15964 604 --AKKLEEITQ----KSRSEVEQLSQEKEYLQDRL------------------EKLQKRNEE-------LEEQCVQHgrm 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 1903 KQDIEEKITQL----QTSSdSELGRQKNIVEETLKQKKVVEEEIHIIKINFH 1950
Cdd:pfam15964 653 HERMKQRLRQLdkhcQATA-QQLVQLLSKQNQLFKERQNLTEEVQSLRSQVP 703
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
41-149 |
3.74e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 46.97 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 41 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 149
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
47-137 |
3.83e-05 |
|
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: 45.75 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 47 KWVNKHLVKAQR---HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 119
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1389908282 120 DDIADGNPKLTLGLIWTI 137
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2384-2603 |
3.84e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2384 ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKH--TTEIVVQKLETQRLQSTREADDLKSAIADlee 2461
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELEKEIAE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2462 erkklkkeaeelQRKSKEmanAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgekkrfekQLEDEMKKAKALKDEQERQ 2541
Cdd:COG4942 95 ------------LRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFL--------DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 2542 RKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQ 2603
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1434-1731 |
3.93e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1434 QQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAER 1513
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1514 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQL 1593
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1594 QTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHA 1673
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1674 QEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECI 1731
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2193-2388 |
4.29e-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: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2193 ELTVVKLQlDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVElARVRI----QMEELVKLKLKIEEENRRLMQKDKDsT 2268
Cdd:COG2268 170 ELESVAIT-DLEDENNYLDALGRRKIAEIIRDARIAEAEAERE-TEIAIaqanREAEEAELEQEREIETARIAEAEAE-L 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2269 QKLLAE---EAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQA 2345
Cdd:COG2268 247 AKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1389908282 2346 QEtakrlqedKQQIQQRLDKETEGFQKSLEAERKRQLEASAEA 2388
Cdd:COG2268 327 AE--------AEAIRAKGLAEAEGKRALAEAWNKLGDAAILLM 361
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3064-3100 |
4.46e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.46e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908282 3064 LNFLEAQAATGFVIDPIKNERVPVDEAVKSGLVGPEI 3100
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1440-1589 |
4.51e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1440 LKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERLRKQVA 1519
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1520 EETQRKKNAEDELKRKSDAEKEAAKQK-------QRALDDLQKY-KMQAEEA-ERRMKQAEE----EKIRQIRVVEEVAQ 1586
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEeeleeliEEQLQELERIsGLTAEEAkEILLEKVEEearhEAAVLIKEIEEEAK 183
|
...
gi 1389908282 1587 KSA 1589
Cdd:PRK12704 184 EEA 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1360-1604 |
4.51e-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: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1360 EDDEKASEKLKEEERRKMAEIQAELDKQKQmaeahakSVAKAEQEALELKMKMKEeaskrqdvaadAEKQKQNIQQELQH 1439
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEA-----------LQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1440 LKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAE-LQELRDRAAEAEKLRKAAQDEAERLRKQV 1518
Cdd:COG3883 77 AE----AEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSaLSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1519 AEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAM 1598
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
....*.
gi 1389908282 1599 SFSEQT 1604
Cdd:COG3883 233 AAAAAA 238
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1505-1850 |
4.52e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1505 KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEV 1584
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1585 AQksaatqlqtkamsfseQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAE 1664
Cdd:COG4372 121 QK----------------ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1665 EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQR 1744
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1745 GLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSV 1824
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330 340
....*....|....*....|....*.
gi 1389908282 1825 AEEAKKQRQIAEEEAARQRSEAEKIL 1850
Cdd:COG4372 345 LLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2341-2648 |
4.63e-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: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2341 QKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVK 2420
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDA----LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2421 AQLQRTEKHTTEIVVqkletqrLQSTREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQIEQQKAELQqsfl 2500
Cdd:COG3883 93 RALYRSGGSVSYLDV-------LLGSESFSDFLDRLSAL------------------SKIADADADLLEELKADKA---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2501 tekglllkrekevegEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVL 2580
Cdd:COG3883 144 ---------------ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 2581 DKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSKGVLNGSTEVDGV 2648
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA 276
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1604-1792 |
4.70e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.62 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1604 TTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEaeqeleiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLE 1683
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQ---------QLKEELDKKQIDADKAQQKADFAQDNADKQRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1684 AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKlsAEQECIRLKADFEHAEQQrglldnelqrLKNEVNSTEK 1763
Cdd:pfam05262 250 VRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIE--IKKNDEEALKAKDHKAFD----------LKQESKASEK 317
|
170 180
....*....|....*....|....*....
gi 1389908282 1764 QRKQLEDELNKVRSEMDSLLQMKINAEKA 1792
Cdd:pfam05262 318 EAEDKELEAQKKREPVAEDLQKTKPQVEA 346
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2020-2498 |
4.75e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2020 KAAQEEVERLKKKAEdankqkekaekeaekqvVLA--KEAAQKCTAAEQKA---QDVLSKNK--EDVLAQEKLRDEFENA 2092
Cdd:COG4913 238 ERAHEALEDAREQIE-----------------LLEpiRELAERYAAARERLaelEYLRAALRlwFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2093 KKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAE 2172
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2173 -MSKHKKEAEQALQQKSQVEKELTVvklQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVR----------- 2240
Cdd:COG4913 381 eFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRdalaealglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2241 ---------IQMEE------------------------------------------LVKLKLKIEEENRRLMQKDKDS-T 2268
Cdd:COG4913 458 aelpfvgelIEVRPeeerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSlA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2269 QKLLAEE----AEKMKSLAEEAGRLSVEAEET-----------------------------ARQRQIAESNlAEQRALAE 2315
Cdd:COG4913 538 GKLDFKPhpfrAWLEAELGRRFDYVCVDSPEElrrhpraitragqvkgngtrhekddrrriRSRYVLGFDN-RAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2316 KILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE------DKQQIQQRLDketegfqkSLEAERKRQLEASAEAE 2389
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIA--------ELEAELERLDASSDDLA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2390 KLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtekhtteivvqkLETQRLQSTREADDLKSAIADLEEERKKLKKE 2469
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ------------AEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
570 580
....*....|....*....|....*....
gi 1389908282 2470 AEELQRKSKEMANAQQEQIEQQKAELQQS 2498
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRA 785
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
42-107 |
5.35e-05 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 45.34 E-value: 5.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 42 KKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 107
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1501-1771 |
5.47e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 49.61 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1501 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQaeeAERRMKQAEEEKIRQIRv 1580
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIP---AERKGEQEGEGEIEAKE- 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1581 vEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLR 1660
Cdd:TIGR00927 704 -ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1661 LQAEEEAQKKShaqEEAEKQKLEAERDAKKRGKAEEaalkqkENAEKELDKQRKFAEQIAQQKLSAEQECiRLKADFEHA 1740
Cdd:TIGR00927 783 IQAGEDGEMKG---DEGAEGKVEHEGETEAGEKDEH------EGQSETQADDTEVKDETGEQELNAENQG-EAKQDEKGV 852
|
250 260 270
....*....|....*....|....*....|...
gi 1389908282 1741 EQQRGLL--DNELQRLKNEVNSTEKQRKQLEDE 1771
Cdd:TIGR00927 853 DGGGGSDggDSEEEEEEEEEEEEEEEEEEEEEE 885
|
|
| Selenoprotein_S |
pfam06936 |
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ... |
1631-1708 |
5.57e-05 |
|
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.
Pssm-ID: 462043 [Multi-domain] Cd Length: 192 Bit Score: 47.14 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1631 QQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQ------KKSHAQEEAEKQKLEaERDAKKRGKAEEAALKQKEN 1704
Cdd:pfam06936 62 RQRSSDHSAATVDPDLVVKRQEALEASRLRMQEELDAQaekfkeKQKQLEEEKRRQKIE-MWESMQEGKSYKGNAKLAQE 140
|
....
gi 1389908282 1705 AEKE 1708
Cdd:pfam06936 141 ETEE 144
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1706-1860 |
5.93e-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: 47.61 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1706 EKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRS--EMDSLL 1783
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1784 QmkinaEKASMvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEA 1860
Cdd:COG1579 96 K-----EIESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2522-2604 |
6.08e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2522 KQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQ 2601
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
...
gi 1389908282 2602 LQT 2604
Cdd:COG4942 110 LRA 112
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2214-2653 |
6.96e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2214 ELQRVKGEVNDAFKQKSQVEVELARVRIQMEELV---KLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLS 2290
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKAsalKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2291 VEAEETARQRQIAESNLAEQRALAEKILKEkmqaiqeatkLKAEAEKLQKQKDQAQETAKRLQEdkqqIQQRLDKETEGF 2370
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNE----------LSELRRQIQRAELELQSTNSELEE----LQERLDLLKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2371 Q-----------------------KSLEAERKRQLEASAEAEKLK---LRVKELSLAQTKAEDEAKKF----------KK 2414
Cdd:pfam05557 149 SeaeqlrqnlekqqsslaeaeqriKELEFEIQSQEQDSEIVKNSKselARIPELEKELERLREHNKHLnenienklllKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2415 QADEVKAQLQRTEKHTTEIVVQKLETQRLQstREADDLKSAIADLEEERkklkkeaeelqrKSKEMANAQQEQIEQQKAE 2494
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLELEKEKLE--QELQSWVKLAQDTGLNL------------RSPEDLSRRIEQLQQREIV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2495 LQQ---SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQER-QRK--LMEEERKKLQAIMDEAVRKQKEAEE 2568
Cdd:pfam05557 295 LKEensSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRvlLLTKERDGYRAILESYDKELTMSNY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2569 EMKNKQREMDVLDkkrLEQEKQLAEENKKLR-EQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSKgvlngsTEVDG 2647
Cdd:pfam05557 375 SPQLLERIEEAED---MTQKMQAHNEEMEAQlSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK------EEVDS 445
|
....*.
gi 1389908282 2648 VKKEGD 2653
Cdd:pfam05557 446 LRRKLE 451
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1660-1935 |
7.45e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1660 RLQAEEEAQKKshAQEEAEKQKLEAERDAKKRGKAEEAALKQKEnAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEh 1739
Cdd:TIGR02794 54 RIQQQKKPAAK--KEQERQKKLEQQAEEAEKQRAAEQARQKELE-QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1740 AEQQRGLLDNELQRLKnevnstEKQRKQLEDElnkvrsemdsllqmkinaekasmvntekskqllesealkmkQLADEAA 1819
Cdd:TIGR02794 130 AEAKAKAEAEAERKAK------EEAAKQAEEE-----------------------------------------AKAKAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1820 RMRSVAEEAKKQrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQA 1899
Cdd:TIGR02794 163 EAKKKAEEAKKK---AEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 1389908282 1900 AQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQK 1935
Cdd:TIGR02794 240 LASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1891-2089 |
7.46e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1891 QRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLK---QKKVVEEEIHIIKINfHKASKEKADLESELKKLK 1967
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAaqeQKKQAEEAAKQAALK-QKQAEEAAAKAAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1968 GIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEkvkritaAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEA 2047
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAK-------KKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908282 2048 EKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEF 2089
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2521-2670 |
7.64e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2521 EKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQ--------KEAEEEMKNKQREMDVLDKKRLEQ--EKQ 2590
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAHE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2591 LAEENKKLREQLQTFEisSKTVSQTKESQTVSVEKLVAVTTVGtSKGvlngstEVDGVKKEGDSPLSFEGIREKVPAERL 2670
Cdd:PRK00409 609 LIEARKRLNKANEKKE--KKKKKQKEKQEELKVGDEVKYLSLG-QKG------EVLSIPDDKEAIVQAGIMKMKVPLSDL 679
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1354-1727 |
7.72e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1354 DAQRRLEDDEKASEKLKEEERRKMAEIQAeLDKQKQMAEAHAKSVAKAEQ----------EALELKMKMKEEASKRQDVA 1423
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALRGQLDA-LTKQLQRDESEAQSLRQEEQaltqqwqavcASLNITLQPQDDIQPWLDAQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1424 ADAEKQKQNIQQELQHLKSLSDQEikSKNQQLEDALVSRRkieeeiHIIRIQLEKTTAHKAKSEAELQELRDRAAEAeKL 1503
Cdd:PRK10246 606 EEHERQLRLLSQRHELQGQIAAHN--QQIIQYQQQIEQRQ------QQLLTALAGYALTLPQEDEEASWLATRQQEA-QS 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1504 RKAAQDEAERLRKQVAeetqRKKNAEDELKRKSDAEKEAAKQkqrALDDLQKYKMQ--AEEAERRMKQAEEEKIRQiRVV 1581
Cdd:PRK10246 677 WQQRQNELTALQNRIQ----QLTPLLETLPQSDDLPHSEETV---ALDNWRQVHEQclSLHSQLQTLQQQDVLEAQ-RLQ 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1582 EEVAQKSAATQlqtkAMSFSEQTTKLEESLKKEqgNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1661
Cdd:PRK10246 749 KAQAQFDTALQ----ASVFDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTV 822
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908282 1662 QAEEeaqkkSHAQEEAEKQKLeaeRDAKKRGKAEEAALKQKENAEKEldkQRKFAEQIAQQKLSAE 1727
Cdd:PRK10246 823 TVEQ-----IQQELAQLAQQL---RENTTRQGEIRQQLKQDADNRQQ---QQALMQQIAQATQQVE 877
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1460-1677 |
7.91e-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: 48.79 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1460 VSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE--------LRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaEDE 1531
Cdd:pfam15709 350 VERKRREQEEQRRLQQEQLERAEKMREELELEQqrrfeeirLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ--QEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1532 LKRKsdaekeaakqkqraLDDLQKyKMQAEEAERrmkqAEEEKIRQirvveevaqksaatqlqtkamsfseqtTKLEESL 1611
Cdd:pfam15709 428 FRRK--------------LQELQR-KKQQEEAER----AEAEKQRQ---------------------------KELEMQL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908282 1612 KKEQGNVLKLQEEADKLKKQQKEanTAREEAEQELEIWRQKANEALRLrlqAEEEAQKKshAQEEA 1677
Cdd:pfam15709 462 AEEQKRLMEMAEEERLEYQRQKQ--EAEEKARLEAEERRQKEEEAARL---ALEEAMKQ--AQEQA 520
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2308-2582 |
8.48e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2308 AEQRALAEKILKEKMQAIQEATklkaeaekLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAE 2387
Cdd:COG3206 144 SPDPELAAAVANALAEAYLEQN--------LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNGLVDLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2388 AEKLKL--RVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEI----VVQKLETQRLQSTREADDLKSaiadlee 2461
Cdd:COG3206 212 EEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspVIQQLRAQLAELEAELAELSA------- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2462 erkklkkeaeELQRKSKEMANAQQE------QIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEmkkakalk 2535
Cdd:COG3206 285 ----------RYTPNHPDVIALRAQiaalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL-------- 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1389908282 2536 DEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK 2582
Cdd:COG3206 347 PELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2289-2427 |
8.87e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.12 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2289 LSVEAEETARQRQIAESNLAEQRALAEKiLKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE-DKQQI--QQRLDk 2365
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLAR-LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlYKKGAvsQQELD- 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 2366 etegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTK-AEDEAKKFKKQADEVKAQLQRTE 2427
Cdd:COG1566 152 -----EARAALDAAQAQLEAAQAQLAQAQAGLREEEELAaAQAQVAQAEAALAQAELNLARTT 209
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1584-1728 |
9.00e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1584 VAQKSAATQL---QTKAMSFSEQTTKLEESLKKEQgnVLKLQEEADKLkkqqkeantaREEAEQELEIWRQKANEALRlR 1660
Cdd:PRK12704 24 VRKKIAEAKIkeaEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKL----------RNEFEKELRERRNELQKLEK-R 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1661 LQAEEEAQKKShaQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqkLSAEQ 1728
Cdd:PRK12704 91 LLQKEENLDRK--LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE 154
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1505-1990 |
9.69e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1505 KAAQDEAERLRKQVAEETQRKKNAEDELKRKS----------DAEKEAAKQKQRALDDLQKYKMQAEEAERRmKQAEEEK 1574
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSieynnamddyNNLKSALNELSSLEDMKNRYESEIKTAESD-LSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1575 IRQIRVVEE---------------------------VAQKSAATQLQTKAMSFSEQTTKLEEsLKKEQGNVLKLQEEADK 1627
Cdd:PRK01156 272 NNYYKELEErhmkiindpvyknrnyindyfkykndiENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1628 LKKQQKEA-------NTAREEAEQeLEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1700
Cdd:PRK01156 351 LNNQILELegyemdyNSYLKSIES-LKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1701 QKENAEKE-LDKQRKFAEQiaqqkLSAEQECIRLKADF--EHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRS 1777
Cdd:PRK01156 430 QRIRALREnLDELSRNMEM-----LNGQSVCPVCGTTLgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1778 EMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE------------------AKKQRQIAEEEA 1839
Cdd:PRK01156 505 RKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslkledldskrtswlnALAVISLIDIET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1840 ARQRSEaekilkEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAY----QRKLLEDQAAQhKQDIEEKITQLQT 1915
Cdd:PRK01156 585 NRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQENKIL-IEKLRGKIDNYKK 657
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 1916 SSDSELGRQKNIVEETLKQKKvVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKL 1990
Cdd:PRK01156 658 QIAEIDSIIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1732-1986 |
9.93e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1732 RLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEALKM 1811
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-KVKELKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1812 KQLADEAARMRsvAEEAKKQRQIAEEEAARQRS----EAEKILKEKLAAINE-ATRLKTEAEMALKAKEAENE--RLKRQ 1884
Cdd:COG1340 98 RKELAELNKAG--GSIDKLRKEIERLEWRQQTEvlspEEEKELVEKIKELEKeLEKAKKALEKNEKLKELRAElkELRKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1885 AEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEetlKQKKVVEEEIHIIKInfhkaSKEKADLESELK 1964
Cdd:COG1340 176 AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE---AQEKADELHEEIIEL-----QKELRELRKELK 247
|
250 260
....*....|....*....|..
gi 1389908282 1965 KLKGIADETQKSKLKAEEEAEK 1986
Cdd:COG1340 248 KLRKKQRALKREKEKEELEEKA 269
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2292-2603 |
1.05e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2292 EAEETARQRqiaesnlaEQRALAEKI-LKEKMQAIQEATKLKAEAEKLQKQKDQ-AQETAKRLQEDKQQIQQRLDKETEG 2369
Cdd:pfam02029 3 DEEEAARER--------RRRAREERRrQKEEEEPSGQVTESVEPNEHNSYEEDSeLKPSGQGGLDEEEAFLDRTAKREER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2370 FQKSLE--AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTR 2447
Cdd:pfam02029 75 RQKRLQeaLERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2448 EADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQ--IEQQK-----AELQQSFLTEKGLLLKREKEVEGEKKRF 2520
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESkvFLDQKrghpeVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2521 EKQLEDEMKKAKALKDEQERQR--KLMEEERKKLQaimdeavRKQKEAEEEM---------KNKQREMDVLDKKRLEQEK 2589
Cdd:pfam02029 235 EREEEAEVFLEAEQKLEELRRRrqEKESEEFEKLR-------QKQQEAELELeelkkkreeRRKLLEEEEQRRKQEEAER 307
|
330
....*....|....*.
gi 1389908282 2590 QLA--EENKKLREQLQ 2603
Cdd:pfam02029 308 KLReeEEKRRMKEEIE 323
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1541-1901 |
1.07e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.49 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1541 EAAKQKQRALDDLQK----YKMQAEEAERRMKQAEEEKIRQIRVVEEvaqksaatqlqtkamsfseqttkLEESLKKEQG 1616
Cdd:pfam05701 35 ERRKLVELELEKVQEeipeYKKQSEAAEAAKAQVLEELESTKRLIEE-----------------------LKLNLERAQT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1617 NVLKLQEEAD--KLKKQQKEANTAREE---AEQELEIWRQKANEALrlrlqAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1691
Cdd:pfam05701 92 EEAQAKQDSElaKLRVEEMEQGIADEAsvaAKAQLEVAKARHAAAV-----AELKSVKEELESLRKEYASLVSERDIAIK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1692 gKAEEAALKQKE------------NAEKELDKQRKFAEQIAQQK-----LSAEQECIRLKADFEHAEQqrglldnELQRL 1754
Cdd:pfam05701 167 -RAEEAVSASKEiektveeltielIATKESLESAHAAHLEAEEHrigaaLAREQDKLNWEKELKQAEE-------ELQRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1755 KNEVNSTEKQRKQLE---DELNKVRSEMDSLLQMKINAEKASMVNTEKS-----------KQLLESEALKMKQLADEAAR 1820
Cdd:pfam05701 239 NQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEKKTstsiqaalasaKKELEEVKANIEKAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1821 MRSVAE--EAKKQRQIAEEEAARQRSEAEKILKEKLAAinEATRLKTEAEMA-LKAKEAENERLK-----RQAEEEAYQR 1892
Cdd:pfam05701 319 LRVAAAslRSELEKEKAELASLRQREGMASIAVSSLEA--ELNRTKSEIALVqAKEKEAREKMVElpkqlQQAAQEAEEA 396
|
....*....
gi 1389908282 1893 KLLEdQAAQ 1901
Cdd:pfam05701 397 KSLA-QAAR 404
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4283-4316 |
1.09e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.09e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908282 4283 EETGPIAGILDTDTLEKVSVTEAIHRNLVDNITG 4316
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
41-148 |
1.13e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 45.39 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 41 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 148
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2384-2657 |
1.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2384 ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHtteivVQKLETQRLQSTREADDLKSAIADLeeer 2463
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-----LEALQAEIDKLQAEIAEAEAEIEER---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2464 kklkkeaeelQRKSKEMANAQQEQIEQQK-------AELQQSFLTEKGLLlkrekevegekKRFEKQLEDEMKKAKALKD 2536
Cdd:COG3883 85 ----------REELGERARALYRSGGSVSyldvllgSESFSDFLDRLSAL-----------SKIADADADLLEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2537 EQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTK 2616
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1389908282 2617 ESQTVSVEKLVAVTTVGTSKGVLNGSTEVDGVKKEGDSPLS 2657
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1356-2037 |
1.14e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1356 QRRLEDDEKASEKLKEEErrkmaEIQAELDKQKQMAEAHAKSvakAEQEALELKMKMKEeASKRQDVAADAEKQKQNIQQ 1435
Cdd:PRK04863 351 ERYQADLEELEERLEEQN-----EVVEEADEQQEENEARAEA---AEEEVDELKSQLAD-YQQALDVQQTRAIQYQQAVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1436 ELQHLKSLSD-------------QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK------------------------ 1478
Cdd:PRK04863 422 ALERAKQLCGlpdltadnaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagevsrseawdvarel 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1479 -TTAHKAKSEAE-LQELRDRAAEAEKlRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaEKEAAKQKQRaLDDLQKY 1556
Cdd:PRK04863 502 lRRLREQRHLAEqLQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDEDEL------EQLQEELEAR-LESLSES 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1557 KmqAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTtklEESLKKEQGNVLKLQEEADKLKKQQKEAN 1636
Cdd:PRK04863 574 V--SEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQS---GEEFEDSQDVTEYMQQLLERERELTVERD 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1637 TAREEAEQ-ELEIWR---QKANEALRLRLQAE----------------EEAQKKS-------HA----QEEAEKQKLEAE 1685
Cdd:PRK04863 649 ELAARKQAlDEEIERlsqPGGSEDPRLNALAErfggvllseiyddvslEDAPYFSalygparHAivvpDLSDAAEQLAGL 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1686 RD---------------AKKRGKAEE--AALKQKENA-------------------EKELDKQRKFAEQIAQQ--KLSAE 1727
Cdd:PRK04863 729 EDcpedlyliegdpdsfDDSVFSVEEleKAVVVKIADrqwrysrfpevplfgraarEKRIEQLRAEREELAERyaTLSFD 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1728 -QECIRLKADFEH--------------------AEQQRGLLDNELQRLKNEVNSTEKQRKQLE---DELNKVRSEMDSL- 1782
Cdd:PRK04863 809 vQKLQRLHQAFSRfigshlavafeadpeaelrqLNRRRVELERALADHESQEQQQRSQLEQAKeglSALNRLLPRLNLLa 888
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1783 ---LQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILkekLAAIN 1858
Cdd:PRK04863 889 detLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQfEQLKQDYQQAQQTQRDAKQQAFA---LTEVV 965
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1859 E-ATRLKTEAEMALKAKEAE-NERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKiTQLQTSSDSELGRQKNIVEEtlkqkk 1936
Cdd:PRK04863 966 QrRAHFSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY-NQVLASLKSSYDAKRQMLQE------ 1038
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1937 vveeeihiikinfhkaskekadLESELKKLKGIADETQKSKLKAEEEaeKLKKLAAEEERRRKEAEEKVKRITAAEEEAA 2016
Cdd:PRK04863 1039 ----------------------LKQELQDLGVPADSGAEERARARRD--ELHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
810 820
....*....|....*....|.
gi 1389908282 2017 RQCKAAQEEVERLKKKAEDAN 2037
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAK 1115
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1967-2187 |
1.14e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1967 KGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAA--EEEAARQCKAAQEEVERLKKKAEdankqkekae 2044
Cdd:TIGR02794 60 KPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAkqAEQAAKQAEEKQKQAEEAKAKQA---------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2045 keaekqvvlaKEAAQKCTA-AEQKAQDVLSKNKEdvlaQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQ 2123
Cdd:TIGR02794 130 ----------AEAKAKAEAeAERKAKEEAAKQAE----EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2124 KKA------AENEAAKQA----KAQNDTEKQRKEAEEEAARRAAAEAAALKQKQ------QADAEMSKHKKEAEQALQQK 2187
Cdd:TIGR02794 196 AKAeaakakAAAEAAAKAeaeaAAAAAAEAERKADEAELGDIFGLASGSNAEKQggargaAAGSEVDKYAAIIQQAIQQN 275
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1640-1990 |
1.21e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1640 EEAEQELeiwRQKANEAlRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK----RGKAEEAALKQKEnAEKELDKQRKF 1715
Cdd:pfam02029 5 EEAARER---RRRAREE-RRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgqGGLDEEEAFLDRT-AKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1716 AEQIAQQKlsaeqecirlkadfehaeqqrgLLDNELQRLKNEVNStEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMV 1795
Cdd:pfam02029 80 QEALERQK----------------------EFDPTIADEKESVAE-RKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1796 NTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRqIAEEEAARQRSEAEKILKEKLAAINEATRLKTEA------EM 1869
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEN-FAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVksqngeEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1870 ALKAKEAENERLK-----RQAEEEAYQR----KLLEDQAAQHkQDIE----EKITQLQTSSDSELGRQKNIVEEtlkQKK 1936
Cdd:pfam02029 216 VTKLKVTTKRRQGglsqsQEREEEAEVFleaeQKLEELRRRR-QEKEseefEKLRQKQQEAELELEELKKKREE---RRK 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1937 VVEEEihiikinfhkasKEKADLESELKKLKGiadETQKSKLKAE------EEAEKLKKL 1990
Cdd:pfam02029 292 LLEEE------------EQRRKQEEAERKLRE---EEEKRRMKEEierrraEAAEKRQKL 336
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1492-2318 |
1.25e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1492 ELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD------AEKEAAKQKQRALDDLQKYKMQAEEAER 1565
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDhlnlvqTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1566 RMKQAEEEKIRQIRVVEEVAQ--KSAATQL----------QTKAMSFSEQTTKLEESLKKEQGNVL---KLQEEADKLKK 1630
Cdd:PRK04863 370 VVEEADEQQEENEARAEAAEEevDELKSQLadyqqaldvqQTRAIQYQQAVQALERAKQLCGLPDLtadNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1631 QQKEANTAREEAEQEL----EIWRQ--KANEALRlRLQAE-EEAQKKSHAQE---EAEKQKLEAERDAKKRGKAEEaaLK 1700
Cdd:PRK04863 450 KEQEATEELLSLEQKLsvaqAAHSQfeQAYQLVR-KIAGEvSRSEAWDVAREllrRLREQRHLAEQLQQLRMRLSE--LE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1701 QKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMD 1780
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDEDE---LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1781 SLLQMKinaEKASMVNTEKSKQLLESEALkmkqlaDEAarMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEA 1860
Cdd:PRK04863 604 AWLAAQ---DALARLREQSGEEFEDSQDV------TEY--MQQLLERERELTVERDELAARKQALDEEIERLSQPGGSED 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1861 TRLKTEAEmalkakeaeneRLKRQAEEEAYQRKLLEDQA--------AQHK---QDIEEKITQLQT-------------- 1915
Cdd:PRK04863 673 PRLNALAE-----------RFGGVLLSEIYDDVSLEDAPyfsalygpARHAivvPDLSDAAEQLAGledcpedlyliegd 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1916 -------SSDSELGRQKNIVEETLKQ---KKVVEEEIhiikinFHKASKEK--ADLESElkklkgiADETQKSKLKAEEE 1983
Cdd:PRK04863 742 pdsfddsVFSVEELEKAVVVKIADRQwrySRFPEVPL------FGRAAREKriEQLRAE-------REELAERYATLSFD 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1984 AEKLKKLAAEEERRRKEAEEKVkrITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAekeaekqvvlAKEAAQKCTA 2063
Cdd:PRK04863 809 VQKLQRLHQAFSRFIGSHLAVA--FEADPEAELRQLNRRRVELERALADHESQEQQQRSQ----------LEQAKEGLSA 876
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2064 AEQKAQDVlsknkeDVLAQEKLRDEF----------ENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAEneaak 2133
Cdd:PRK04863 877 LNRLLPRL------NLLADETLADRVeeireqldeaEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQ----- 945
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2134 QAKAQNDTEKQRK---------------EAEEEAARRAAAEAAALKQKQ-QADAEMSKHKKEAEQALQQKSQVEKELTvv 2197
Cdd:PRK04863 946 QAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQRLeQAEQERTRAREQLRQAQAQLAQYNQVLA-- 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2198 KLQLDETDKQKVL--LDQELQRV-----KGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEE----NRRLMQKDKD 2266
Cdd:PRK04863 1024 SLKSSYDAKRQMLqeLKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEmdnlTKKLRKLERD 1103
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 2267 STQ-KLLAEEAEKMKSLAEEAGRLSvEAEETARQRQIAESNLAEQRALAEKIL 2318
Cdd:PRK04863 1104 YHEmREQVVNAKAGWCAVLRLVKDN-GVERRLHRRELAYLSADELRSMSDKAL 1155
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1608-1778 |
1.29e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.02 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1608 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQA-------EEEAQKKSHAQEEAEKQ 1680
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRleeerqrQEEEERKQRLQLQAAQE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1681 KLEAERDAKKRGKAEEAALKQKENAEK-ELDKQRKFAEQIaqqKLSAEQecirlKADFEHAEQQRglldNELQRLKNEvn 1759
Cdd:pfam15709 420 RARQQQEEFRRKLQELQRKKQQEEAERaEAEKQRQKELEM---QLAEEQ-----KRLMEMAEEER----LEYQRQKQE-- 485
|
170
....*....|....*....
gi 1389908282 1760 stEKQRKQLEDELNKVRSE 1778
Cdd:pfam15709 486 --AEEKARLEAEERRQKEE 502
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2163-2444 |
1.36e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.50 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2163 LKQKQQADAEMSKHKKEaeqalqqksqVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQ 2242
Cdd:pfam15905 61 LKKKSQKNLKESKDQKE----------LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2243 MEELVK----LKLKIEEE-NRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKI 2317
Cdd:pfam15905 131 LLELTRvnelLKAKFSEDgTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVST 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2318 LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRlDKETEGFQKSLEAerkRQLEASAEAEKLKLRVKE 2397
Cdd:pfam15905 211 EKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEK-NDEIESLKQSLEE---KEQELSKQIKDLNEKCKL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1389908282 2398 LslaQTKAEDEAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQ 2444
Cdd:pfam15905 287 L---ESEKEELLREYEEKEQTLNAELEELKE---KLTLEEQEHQKLQ 327
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1700-2084 |
1.41e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1700 KQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSem 1779
Cdd:COG5185 142 KLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1780 dslLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEaarmrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINE 1859
Cdd:COG5185 220 ---TLLEKAKEIINIEEALKGFQDPESELEDLAQTSDK-------LEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1860 ATRlKTEAEMALKAKEAENERLKRQAEEEAyQRKLLEDQAAQHKQDIEEKITQLQtssdSELGRQKNIVEEtlKQKKVVE 1939
Cdd:COG5185 290 QFE-NTKEKIAEYTKSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLT----AEIEQGQESLTE--NLEAIKE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1940 EEIHIIKINFHKASKEKAD-LESELKKLKGIADETQKSKLKAEEE-AEKLKKLAAEEERRRKEAEEKVKRITAAEEEAAR 2017
Cdd:COG5185 362 EIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEiLATLEDTLKAADRQIEELQRQIEQATSSNEEVSK 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2018 QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAK--EAAQKCTAAEQKAQDVLSKNKEDVLAQEK 2084
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKkeDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1362-1543 |
1.48e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1362 DEKASEKLKEEErrkmaeiQAELDKQKQMAEAHAKSvakaEQEALELKMKMKEEASKRQDVAAD-----------AEKQK 1430
Cdd:pfam05262 179 DKKVVEALREDN-------EKGVNFRRDMTDLKERE----SQEDAKRAQQLKEELDKKQIDADKaqqkadfaqdnADKQR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1431 QNIQQELQHLKSLSD----QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAkseaelQELRDRAAEAEKLRKA 1506
Cdd:pfam05262 248 DEVRQKQQEAKNLPKpadtSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKA------FDLKQESKASEKEAED 321
|
170 180 190
....*....|....*....|....*....|....*..
gi 1389908282 1507 AQDEAERLRKQVAEETQRKKNaedELKRKSDAEKEAA 1543
Cdd:pfam05262 322 KELEAQKKREPVAEDLQKTKP---QVEAQPTSLNEDA 355
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2127-2361 |
1.53e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2127 AENEAAKQAKAQNDTEKQRKeaeeeaarraaaeaAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDK 2206
Cdd:COG3883 14 ADPQIQAKQKELSELQAELE--------------AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2207 QkvlLDQELQRVKGEVNDAFKQKSQVEVE------------LARVriqmeELVKlklKIEEENRRLMQKDKDSTQKLlae 2274
Cdd:COG3883 80 E---IEERREELGERARALYRSGGSVSYLdvllgsesfsdfLDRL-----SALS---KIADADADLLEELKADKAEL--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2275 eAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE 2354
Cdd:COG3883 146 -EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
....*..
gi 1389908282 2355 DKQQIQQ 2361
Cdd:COG3883 225 AAAAAAA 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1804-2031 |
1.56e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1804 LESEALKMKQLADEAARMRSVAEEAKKQRQIAEE-EAARQRSEAEKILKEKLAAINEATRLKTeAEMALKAKEAENERLK 1882
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1883 RQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSdselGRQKNIVEETLKQKKvveeeihiikinfhkasKEKADLESE 1962
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNG----GDRLEQLEREIERLE-----------------RELEERERR 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1963 LKKLkgiADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKK 2031
Cdd:COG4913 361 RARL---EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1499-1866 |
1.56e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.98 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1499 EAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEKIRQI 1578
Cdd:pfam15964 357 QCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ------NVAQLEAQVEKVTREKNSLV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1579 RVVEEvaqksAATQLQTKAMSFSEQTTKLEESLKKEQgnvLKLQEEADKLKKQQKEANTAREEAEQELEiwrqkanealR 1658
Cdd:pfam15964 431 SQLEE-----AQKQLASQEMDVTKVCGEMRYQLNQTK---MKKDEAEKEHREYRTKTGRQLEIKDQEIE----------K 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1659 LRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKEnaEKElDKQRKFAEQIAQQKLSAEQECIRLKADFE 1738
Cdd:pfam15964 493 LGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRL--EKE-SIQQSFSNEAKAQALQAQQREQELTQKMQ 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1739 HAEQQRGLLDNELQRLKNEVNSTEKQRKQ--------LEDELNKVRSEMDSLLQ----MKINAEKASMVNTEKSKQLLES 1806
Cdd:pfam15964 570 QMEAQHDKTVNEQYSLLTSQNTFIAKLKEecctlakkLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQCVQH 649
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1807 EalKMKQladeaaRMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTE 1866
Cdd:pfam15964 650 G--RMHE------RMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2301-2442 |
1.71e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2301 QIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD------------KETE 2368
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 2369 GFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQrTEKHTTEIVVQKLETQR 2442
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEELEAER 165
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1627-1989 |
1.72e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1627 KLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE 1706
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1707 KELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLK-------NEVNSTEKQRKQLEDELNKVRSEM 1779
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEaqiaelqSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1780 DSLLQMKINAEKASMVNtekskqllesealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINE 1859
Cdd:COG4372 167 AALEQELQALSEAEAEQ-------------ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1860 ATRLKTEAEMALKAKEAENERLK-RQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVV 1938
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVIlKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 1939 EEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKK 1989
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAE 364
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2521-2603 |
1.85e-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: 46.80 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2521 EKQLEDEMKKAKALkdeqERQRKLMEEERKKLQAIMDEAVRKQKEA--------EEEMKNKQREMD-VLDKKRLEQEKQL 2591
Cdd:cd16269 197 EKEIEAERAKAEAA----EQERKLLEEQQRELEQKLEDQERSYEEHlrqlkekmEEERENLLKEQErALESKLKEQEALL 272
|
90
....*....|..
gi 1389908282 2592 AEENKKLREQLQ 2603
Cdd:cd16269 273 EEGFKEQAELLQ 284
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1238-1464 |
1.86e-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: 47.07 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1238 LTEARQRQEKIQAVPISDSRALREQLTDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASPLKK 1317
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1318 PKMECAsDDIIQEYVNlrTRYSELMTLTNQyiKFIIDAQRRLEDDEKASEKLKEEeRRKMAEIQAELDKQKQMAEAHAKS 1397
Cdd:COG4942 102 QKEELA-ELLRALYRL--GRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQ-AEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1398 VAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSlSDQEIKSKNQQLEDALVSRRK 1464
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAAAE 241
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1505-1923 |
2.03e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.87 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1505 KAAQDEAERLRKQVA-----EETQRKKnAEDELKRKSDAEKEAAKQKQRA---------LDDLQKYKMQAEEAERRMKQA 1570
Cdd:PRK10246 194 KSARTELEKLQAQASgvallTPEQVQS-LTASLQVLTDEEKQLLTAQQQQqqslnwltrLDELQQEASRRQQALQQALAA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1571 EEEKIRQIRVVEeVAQksAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWR 1650
Cdd:PRK10246 273 EEKAQPQLAALS-LAQ--PARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLN 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1651 QKANEALRLRLQAEEEA--------QKKSHAQEE-------AEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR-- 1713
Cdd:PRK10246 350 TWLAEHDRFRQWNNELAgwraqfsqQTSDREQLRqwqqqltHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQRlv 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1714 ----------KFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNeVNSTEKQRKQLEDELNKVRSEMDSLL 1783
Cdd:PRK10246 430 alhgqivpqqKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT-ICEQEARIKDLEAQRAQLQAGQPCPL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1784 -----QMKINAEKASMVNTEKSKQL-LESEalkMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEaEKILKEKLAAI 1857
Cdd:PRK10246 509 cgstsHPAVEAYQALEPGVNQSRLDaLEKE---VKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE-EQALTQQWQAV 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1858 NEATRLKTEAEMALKAKEAENERLKRQAEEEAyQRKLLEDQAAQHKQDI---EEKITQLQTSSDSELGR 1923
Cdd:PRK10246 585 CASLNITLQPQDDIQPWLDAQEEHERQLRLLS-QRHELQGQIAAHNQQIiqyQQQIEQRQQQLLTALAG 652
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1413-1644 |
2.07e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.15 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1413 KEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE 1492
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL--EQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1493 lrdrAAEAEKLRKAaqdEAERLRKQvAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmqAEEAERRmKQAEE 1572
Cdd:TIGR02794 127 ----KQAAEAKAKA---EAEAERKA-KEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA----KAEAEAK-AKAEE 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 1573 EKIRQirvveEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQE-EADKLKKQQKEANTAREEAEQ 1644
Cdd:TIGR02794 194 AKAKA-----EAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGlASGSNAEKQGGARGAAAGSEV 261
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1400-1904 |
2.14e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.87 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1400 KAEQEALElkmKMKEEASkrqDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKT 1479
Cdd:PRK10246 194 KSARTELE---KLQAQAS---GVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1480 TAHKAKSEAELQELRDRAAE-AEKLRKAaqdeAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDdlQKYKM 1558
Cdd:PRK10246 268 QALAAEEKAQPQLAALSLAQpARQLRPH----WERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAK--QSAEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1559 QAEEAERRMKQAEEEKIRQIRvvEEVA--------QKSAATQLQTKAMSFSEQTTKL-------------EESLKKEQGN 1617
Cdd:PRK10246 342 QAQQQSLNTWLAEHDRFRQWN--NELAgwraqfsqQTSDREQLRQWQQQLTHAEQKLnalpaitltltadEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1618 --------VLKLQEEADKLKKQQKEANTAREEAEQELeiwrQKANEALRLRLQ-----AEEEAQKKSHAQEEAEKQKLEA 1684
Cdd:PRK10246 420 eqrplrqrLVALHGQIVPQQKRLAQLQVAIQNVTQEQ----TQRNAALNEMRQrykekTQQLADVKTICEQEARIKDLEA 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1685 ERDAKKRGK-------AEEAALKQKENAEKELDKQRKfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1757
Cdd:PRK10246 496 QRAQLQAGQpcplcgsTSHPAVEAYQALEPGVNQSRL--DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1758 VNSTEKQRKQLEDELNKVRSEMDSL----------------------LQMKINAEKASMVN----TEKSKQLLESE---- 1807
Cdd:PRK10246 574 EQALTQQWQAVCASLNITLQPQDDIqpwldaqeeherqlrllsqrheLQGQIAAHNQQIIQyqqqIEQRQQQLLTAlagy 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1808 ALKMKQLADEAARMRSVAEEAKK-QRQIAEEEAARQRSEAEKILKEKLAAINEATrlkTEAEMAL--KAKEAENERLKRQ 1884
Cdd:PRK10246 654 ALTLPQEDEEASWLATRQQEAQSwQQRQNELTALQNRIQQLTPLLETLPQSDDLP---HSEETVAldNWRQVHEQCLSLH 730
|
570 580
....*....|....*....|.
gi 1389908282 1885 AEEEAYQRKL-LEDQAAQHKQ 1904
Cdd:PRK10246 731 SQLQTLQQQDvLEAQRLQKAQ 751
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1229-1672 |
2.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1229 DSYEWLIRWLTEARQRQEKIQAVpISDSRALREQLTDEKKLLG------EIEKNKDKIDDCHKNAKAYIDSVKDYEFQIL 1302
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPlyqeleALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1303 TYKALQDPIASPLKKpKMECASDDIIQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRkmAEIQA 1382
Cdd:COG4717 167 ELEAELAELQEELEE-LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA--AALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1383 ELDKQKQMAEAHAksvakaeqEALELKMKMKEEASKRQDVAADAekqkQNIQQELQHLKSLSDQEIKSKNQQLEDALVSR 1462
Cdd:COG4717 244 RLKEARLLLLIAA--------ALLALLGLGGSLLSLILTIAGVL----FLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1463 RKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaedeLKRKSDAEKEA 1542
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-----LAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1543 AKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQ 1622
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE-AELEQL 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1623 EEADKLKKQQKEANTAREEAEQELEIWRqkaneALRLRLQAEEEAQKKSH 1672
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYR 510
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2179-2497 |
2.15e-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: 47.64 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2179 EAEQALQQKSQVEKELTvvkLQLDETDKQKVLLDQELQRVKGEVNDAfkqkSQVEVELARVRIQMEELVKLKlkieEENR 2258
Cdd:COG3096 358 ELTERLEEQEEVVEEAA---EQLAEAEARLEAAEEEVDSLKSQLADY----QQALDVQQTRAIQYQQAVQAL----EKAR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2259 RLMQKDkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKE--KMQAIQEATKLKAEAE 2336
Cdd:COG3096 427 ALCGLP-DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEveRSQAWQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2337 KLQKQKDQAQETAKRLQEDKQQI--QQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2414
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2415 QADEVKAQLQRTEK-----HTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKeaeelqrkSKEMANAQQEQIE 2489
Cdd:COG3096 586 QLEQLRARIKELAArapawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATV--------ERDELAARKQALE 657
|
....*...
gi 1389908282 2490 QQKAELQQ 2497
Cdd:COG3096 658 SQIERLSQ 665
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1967-2191 |
2.20e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1967 KGIADETQKSKLKAEEEAEKLKklaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERL-----KKKAEDANKQKE 2041
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQ-----------------------QKQAAEQERLKQLEKERLaaqeqKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2042 KAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEdvlAQEKLRDEFENAKKLAQEAEKAKEKAEKEaallRQKAEEAE 2121
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---AEAKKKAEAEAAKKAAAEAKKKAEAEAAA----KAAAEAKK 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2122 KQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAaeaaalkqkqqADAEMSKHKKEAEQALQQKSQVE 2191
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA-----------AEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3730-3763 |
2.21e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.21e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908282 3730 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPE 3763
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1808-2037 |
2.26e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1808 ALKMKQLADEAARMRSvaeEAKKQRQIAEEEA--ARQRSEAEKILKEKLAAINEA-TRLK-----------TEAEMALKA 1873
Cdd:PRK05035 440 AIEQEKKKAEEAKARF---EARQARLEREKAAreARHKKAAEARAAKDKDAVAAAlARVKakkaaatqpivIKAGARPDN 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1874 KEAENERLKRQAEEEAYQRKLLEDQAAQHKQD-IEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfhKA 1952
Cdd:PRK05035 517 SAVIAAREARKAQARARQAEKQAAAAADPKKAaVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAK--KA 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1953 SKEKADLESELKKLkgiADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKK 2032
Cdd:PRK05035 595 AQQAASAEPEEQVA---EVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEE 671
|
....*
gi 1389908282 2033 AEDAN 2037
Cdd:PRK05035 672 AEDPK 676
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1512-1697 |
2.31e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.30 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1512 ERLRKQVAEETQRKKNAEDELKRKSdaeKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEvAQKSAAT 1591
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERES---QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ-KQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1592 QLQTKAMSFSEQTTKLEESLKKEqgnVLKLQEEAdklkkqQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKS 1671
Cdd:pfam05262 260 LPKPADTSSPKEDKQVAENQKRE---IEKAQIEI------KKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|....*.
gi 1389908282 1672 HAQEEaEKQKLEAERDAKKRGKAEEA 1697
Cdd:pfam05262 331 EPVAE-DLQKTKPQVEAQPTSLNEDA 355
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3029-3064 |
2.32e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.16 E-value: 2.32e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1389908282 3029 LQGTPSIAGILDEPTKEKMPFYQAMKKEFLSPETAL 3064
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1620-1727 |
2.41e-04 |
|
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: 44.39 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1620 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALrlrlqaeEEAQKKSHAQEEAEKQKLEAERDAKKRgKAEEAAL 1699
Cdd:COG0711 35 KIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEII-------AEARKEAEAIAEEAKAEAEAEAERIIA-QAEAEIE 106
|
90 100 110
....*....|....*....|....*....|...
gi 1389908282 1700 KQKENAEKELDKQ-----RKFAEQIAQQKLSAE 1727
Cdd:COG0711 107 QERAKALAELRAEvadlaVAIAEKILGKELDAA 139
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2164-2414 |
2.45e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2164 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVndafKQKSQVEVELARVRIQM 2243
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2244 EELVK----LKLKIEEEnRRLMQKDKDSTQKLlaEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILK 2319
Cdd:COG1340 119 ERLEWrqqtEVLSPEEE-KELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2320 EKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASaeaeklklRVKELS 2399
Cdd:COG1340 196 EMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELKKLRKKQRALK--------REKEKE 263
|
250
....*....|....*
gi 1389908282 2400 LAQTKAEDEAKKFKK 2414
Cdd:COG1340 264 ELEEKAEEIFEKLKK 278
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2179-2452 |
2.52e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2179 EAEQALQQKSQVEKEltvVKLQLDETDKQKVLLDQELQRVKGEVND-------------AFKQKSQVeVELARVRIQMEE 2245
Cdd:PRK04863 359 ELEERLEEQNEVVEE---ADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtraiQYQQAVQA-LERAKQLCGLPD 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2246 LV--KLKLKIEEenrrLMQKDKDSTQKLLAEE-----AEKMKSLAEEAGRL------SVEAEETARQRQIAESNLAEQRA 2312
Cdd:PRK04863 435 LTadNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRH 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2313 LAEKI--LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEK 2390
Cdd:PRK04863 511 LAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 2391 LKLRVKEL------------SLAQTKAEDEAKKFKKQA-DEVKAQLQRTEKHTTEiVVQKLETQRLQSTREADDL 2452
Cdd:PRK04863 591 LQARIQRLaarapawlaaqdALARLREQSGEEFEDSQDvTEYMQQLLERERELTV-ERDELAARKQALDEEIERL 664
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2740-2773 |
2.56e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.56e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908282 2740 LLEAQAASGFIVDPVKNKFLSVDEAVKDKVIGPE 2773
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1356-1589 |
2.87e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1356 QRRLEDdekasEKLKEEERRKMAEiqAELDKQKQMAEAHAKSVAKAEQEALELKMKMK-EEASKRQDVAADAEKQKQNIQ 1434
Cdd:PRK05035 459 QARLER-----EKAAREARHKKAA--EARAAKDKDAVAAALARVKAKKAAATQPIVIKaGARPDNSAVIAAREARKAQAR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1435 QELQhlKSLSDQEIKSKNQQLEDALV-SRRKIEEEIHIIRIQLEKTTAHKAKSEAELqelrdraAEAeKLRKAAQDEAER 1513
Cdd:PRK05035 532 ARQA--EKQAAAAADPKKAAVAAAIArAKAKKAAQQAANAEAEEEVDPKKAAVAAAI-------ARA-KAKKAAQQAASA 601
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1514 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALD--DLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSA 1589
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEpvDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAA 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1803-2037 |
2.89e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1803 LLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLK 1882
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1883 RQAEEeayqrklLEDQAAQHKQDIEEKITQLQTSSDSE----LGRQKNIVE-----ETLKQ-KKVVEEEIHIIKINFHKA 1952
Cdd:COG4942 90 KEIAE-------LRAELEAQKEELAELLRALYRLGRQPplalLLSPEDFLDavrrlQYLKYlAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1953 SKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKK 2032
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....*
gi 1389908282 2033 AEDAN 2037
Cdd:COG4942 243 TPAAG 247
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1629-1782 |
2.92e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 47.32 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1629 KKQQKEANTAREEAEQE----LEiwRQKanealrLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKEN 1704
Cdd:PTZ00491 662 KSQEAAARHQAELLEQEargrLE--RQK------MHDKAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAE 733
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1705 AEKELDKQRKFAEQIAQQklsAEQECIRLKADFEHAEQQRgllDNELQRlknevnstEKQRKQLEDELNKVRSEMDSL 1782
Cdd:PTZ00491 734 AEVEQAELRAKALRIEAE---AELEKLRKRQELELEYEQA---QNELEI--------AKAKELADIEATKFERIVEAL 797
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3804-3840 |
2.94e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.94e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1389908282 3804 LRLLEAQNATGGYMDPEYYFRLPIDVAMQRGYINKET 3840
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1356-1989 |
3.06e-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: 47.25 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1356 QRRLEDDEKASEKLKEEErrkmaEIQAELDKQKQMAEAHAKSvakAEQEALELKMKMK--EEASKRQDVAADAEKQKQNI 1433
Cdd:COG3096 350 ERYQEDLEELTERLEEQE-----EVVEEAAEQLAEAEARLEA---AEEEVDSLKSQLAdyQQALDVQQTRAIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1434 QQELQHLKSLSD----------QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK--------------TTAHKAKSE-- 1487
Cdd:COG3096 422 LEKARALCGLPDltpenaedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiageverSQAWQTAREll 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1488 ----------AELQELRDRAAEAEKlRKAAQDEAERLRKQVAEETQRKKNAEDELkrksDAEKEAAKQKQRALDDLQkyk 1557
Cdd:COG3096 502 rryrsqqalaQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRIGQQLDAAEEL----EELLAELEAQLEELEEQA--- 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1558 mqAEEAERRMK-QAEEEKIRQiRVVEEVAQKSAATQLQTKAMSFSEQTtklEESLKKEQGNVLKLQEEADKLKKQQKEAN 1636
Cdd:COG3096 574 --AEAVEQRSElRQQLEQLRA-RIKELAARAPAWLAAQDALERLREQS---GEALADSQEVTAAMQQLLEREREATVERD 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1637 TAREEAEQ-ELEIWRQKA---NEALRLRLQAE----------------EEAQKKS------------------------- 1671
Cdd:COG3096 648 ELAARKQAlESQIERLSQpggAEDPRLLALAErlggvllseiyddvtlEDAPYFSalygparhaivvpdlsavkeqlagl 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1672 ----------------------HAQEEA----------------------------EKQ--KLEAERDAKKRGKAEEAAL 1699
Cdd:COG3096 728 edcpedlyliegdpdsfddsvfDAEELEdavvvklsdrqwrysrfpevplfgraarEKRleELRAERDELAEQYAKASFD 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1700 KQkenaekeldKQRKFAEQIAQqkLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ-RKQLE------DEL 1772
Cdd:COG3096 808 VQ---------KLQRLHQAFSQ--FVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQlRQQLDqlkeqlQLL 876
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1773 NKVRSEM----DSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE-----AKKQRQIAEEEAARQR 1843
Cdd:COG3096 877 NKLLPQAnllaDETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQfeqlqADYLQAKEQQRRLKQQ 956
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1844 SEAEKILKEKLAAINEAtrlktEAEMALKAKEAENERLK---RQAEEEAYQ-RKLLEDQAAQHKQdieekITQLQTSSDS 1919
Cdd:COG3096 957 IFALSEVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREaREQLRQAQAQYSQ-----YNQVLASLKS 1026
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 1920 ELgRQKNiveETLKQkkvVEEEIHIIKINF-----HKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKK 1989
Cdd:COG3096 1027 SR-DAKQ---QTLQE---LEQELEELGVQAdaeaeERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQK 1094
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3397-3430 |
3.09e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.09e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908282 3397 LLEAQAATGFITDPVKDKKCSVDDAVKEGIVGPE 3430
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1355-1613 |
3.14e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 46.29 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1355 AQRRLEDDEKASEKLKE----EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMkeeaskrQDVAADAEKQK 1430
Cdd:pfam09787 16 AARILQSKEKLIASLKEgsgvEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTEL-------QELEAQQQEEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1431 QNIQQELQHLKSlsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahkakseaeLQE-LRDRAAEAEKlrkaaqd 1509
Cdd:pfam09787 89 ESSREQLQELEE--QLATERSARREAEAELERLQEELRYLEEELRRSKAT---------LQSrIKDREAEIEK------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1510 eaerLRKQVAEETQrKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYK----MQAEEAERRMKQAEEEKIRQIRVVEEVA 1585
Cdd:pfam09787 151 ----LRNQLTSKSQ-SSSSQSELENRLHQLTETLIQKQTMLEALSTEKnslvLQLERMEQQIKELQGEGSNGTSINMEGI 225
|
250 260
....*....|....*....|....*...
gi 1389908282 1586 QKSAATQLQTKAMSFSEQTTKLEESLKK 1613
Cdd:pfam09787 226 SDGEGTRLRNVPGLFSESDSDRAGMYGK 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2288-2602 |
3.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2288 RLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKEt 2367
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2368 egfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTR 2447
Cdd:COG4372 93 ---QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2448 EADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDE 2527
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 2528 MKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2602
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1831-2514 |
3.31e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1831 QRQIAEEEAARQrsEAEKILKEKLAA--------INEATRLKTEAEMALKAKEAENERLKRQA----EEEAYQRKLLEDQ 1898
Cdd:pfam12128 271 ETLIASRQEERQ--ETSAELNQLLRTlddqwkekRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1899 AAQHKQDIE--EKITQLQTSSDSEL-----GRQKNIVEETLKQKKVVEEEIHIIKinfHKASKEKADLESELKKLKG-IA 1970
Cdd:pfam12128 349 LPSWQSELEnlEERLKALTGKHQDVtakynRRRSKIKEQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESeLR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1971 DETQKSKLKAEEEAEKLKklaaeeeRRRKEAEEKVKRITAAEEEAARQcKAAQEEVERLKKKAEDANKQKEkaekeaekq 2050
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLK-------SRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQEAANAEVE--------- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2051 vvlakeAAQKctaaEQKAQDVLSKNKEDVLAQEKLRDEfENAKKLAQEAEKAKEKAEKEAALLRQkaeEAEKQKKAAENE 2130
Cdd:pfam12128 489 ------RLQS----ELRQARKRRDQASEALRQASRRLE-ERQSALDELELQLFPQAGTLLHFLRK---EAPDWEQSIGKV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2131 AAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSkhkkeaEQALQQK-SQVEKELTVVKLQLDETDKQKV 2209
Cdd:pfam12128 555 ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAAS------EEELRERlDKAEEALQSAREKQAAAEEQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2210 LLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEElvkLKLKIEEENRRLMQKDKDSTQKLLAE----EAEKMKSLAEE 2285
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQS---EKDKKNKALAERKDSANERLNSLEAQlkqlDKKHQAWLEEQ 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2286 AGRLSVEAEETARQRQIAESNLAEQRA-LAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD 2364
Cdd:pfam12128 706 KEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2365 KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtEKHTTEivvqKLETQRLQ 2444
Cdd:pfam12128 786 RIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEM-ERKASE----KQQVRLSE 860
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 2445 STREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQ--IEQQKAELQQSFLTEKGLLLKREKEVE 2514
Cdd:pfam12128 861 NLRGLRCEMSKLATL------------------KEDANSEQAQgsIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1798-1986 |
3.58e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1798 EKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAe 1877
Cdd:TIGR02794 69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEE- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1878 nerLKRQAEEEAyqrKLLEDQAAQHKQDIEEKITqlqtssdselgrqknivEETLKQKKVVEEeihiikinfhKASKEKA 1957
Cdd:TIGR02794 148 ---AAKQAEEEA---KAKAAAEAKKKAEEAKKKA-----------------EAEAKAKAEAEA----------KAKAEEA 194
|
170 180 190
....*....|....*....|....*....|...
gi 1389908282 1958 DLESELKKLKGIADETQK----SKLKAEEEAEK 1986
Cdd:TIGR02794 195 KAKAEAAKAKAAAEAAAKaeaeAAAAAAAEAER 227
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2300-2449 |
3.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2300 RQIAESNLAEQRALAEKILKE---KMQAIQEATKLKAEaEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEA 2376
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEakkEAEAIKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2377 ERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ--------ADEVKAQ-LQRTE---KHTTEIVVQKLETQ-RL 2443
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEIlLEKVEeeaRHEAAVLIKEIEEEaKE 184
|
....*.
gi 1389908282 2444 QSTREA 2449
Cdd:PRK12704 185 EADKKA 190
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2122-2388 |
3.72e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.14 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2122 KQKKAAENEAAKQAKAQNDteKQRkeaeeeaarraaaeaaaLKQ-KQQADAEMSKHKKEAE----QALQQKSQVEKEltV 2196
Cdd:NF012221 1552 KQDDAAQNALADKERAEAD--RQR-----------------LEQeKQQQLAAISGSQSQLEstdqNALETNGQAQRD--A 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2197 VKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELA---RVRIQmEELVKLKLKIEEENRRLMQKDKDSTQKLla 2273
Cdd:NF012221 1611 ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAgglLDRVQ-EQLDDAKKISGKQLADAKQRHVDNQQKV-- 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2274 eeaekMKSLAE-EAGrlsveAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLK----AEAEKLQKQKDQAQET 2348
Cdd:NF012221 1688 -----KDAVAKsEAG-----VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAEsdanAAANDAQSRGEQDASA 1757
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1389908282 2349 AK----RLQEDKQQIQQRLDK--ETEGFQKSLEAERKRQLEASAEA 2388
Cdd:NF012221 1758 AEnkanQAQADAKGAKQDESDkpNRQGAAGSGLSGKAYSVEGVAEP 1803
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
33-138 |
4.00e-04 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 43.21 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 33 NQDERdrvqkKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETL-------PREKGRM--RF 94
Cdd:cd21294 4 NEDER-----REFTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1389908282 95 HKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 138
Cdd:cd21294 79 QMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2270-2595 |
4.07e-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: 46.87 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2270 KLLAEEAEkmkSLAEEAGRLSVEAEETARQRQIAESNLAEQRALA-----EKILKEKMQAIQEATK-LKAEAEKLQKQKD 2343
Cdd:COG3096 788 EELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELEReLAQHRAQEQQLRQ 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2344 QAQETAKRLQE-----------DKQQIQQRLDKETEGFQKSLEAER--KRQLEASAEAEKL--KLRVKELSLAQTKAEDE 2408
Cdd:COG3096 865 QLDQLKEQLQLlnkllpqanllADETLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLvaVLQSDPEQFEQLQADYL 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2409 akkfkkQADEVKAQLQRTEKHTTEIVvqkletQRLQ--STREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQE 2486
Cdd:COG3096 945 ------QAKEQQRRLKQQIFALSEVV------QRRPhfSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQA 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2487 QIEQQKAELQQ---SFLTEKGLLlkreKEVEGEKKRFEKQLEDEMK-KAKALKDE------QERQRK-LMEEERKKLQAI 2555
Cdd:COG3096 1013 QYSQYNQVLASlksSRDAKQQTL----QELEQELEELGVQADAEAEeRARIRRDElheelsQNRSRRsQLEKQLTRCEAE 1088
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1389908282 2556 MDEAVRKQKEAEEEMKNkQREMDVLDKKRLEQEKQLAEEN 2595
Cdd:COG3096 1089 MDSLQKRLRKAERDYKQ-EREQVVQAKAGWCAVLRLARDN 1127
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1613-2193 |
4.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1613 KEQGNVLK-LQEEADKLKKQQKEANTARE--------EAEQELEIWRQK--ANEALRLRLQAEEEAQKKSHAQEEAEKQK 1681
Cdd:COG4913 248 REQIELLEpIRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAEleELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1682 LEAERDAKKrGKAEEAALKQKENAEKELDKQR----KFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1757
Cdd:COG4913 328 LEAQIRGNG-GDRLEQLEREIERLERELEERErrraRLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1758 VNSTEKQRKQLEDELNKVRSEMDSLlqmkinaekasmvntEKSKQLLESEALKM-KQLADE----AARMRSVAEEAkkqr 1832
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASL---------------ERRKSNIPARLLALrDALAEAlgldEAELPFVGELI---- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1833 QIAEEEAARQRSeAEKILKeklaaiNEATRLKTEAEMALKAKEA-ENERLKRQ-------AEEEAYQRKLLEDQAAQHKQ 1904
Cdd:COG4913 468 EVRPEEERWRGA-IERVLG------GFALTLLVPPEHYAAALRWvNRLHLRGRlvyervrTGLPDPERPRLDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1905 DIEEkiTQLQTSSDSELGRQKNIV----EETLKQ-KKVVEEEIHIikinfhKASKEKADleselkklKGIADETQKSKLK 1979
Cdd:COG4913 541 DFKP--HPFRAWLEAELGRRFDYVcvdsPEELRRhPRAITRAGQV------KGNGTRHE--------KDDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1980 AEEEAEKLKKLAAEeerrrkeaeekVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEaekqvVLAKEAAQ 2059
Cdd:COG4913 605 GFDNRAKLAALEAE-----------LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-----IDVASAER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2060 KCTAAEQKAQDvLSKNKEDVLAQEKLRDEfenakklaqeaekakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQN 2139
Cdd:COG4913 669 EIAELEAELER-LDASSDDLAALEEQLEE------------------------LEAELEELEEELDELKGEIGRLEKELE 723
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 2140 DTEKQRKEAEEEAARRAAAEAAALKQ---KQQADAEMSKHKKEAEQALQQKSQVEKE 2193
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERELRENLEERIDALRA 780
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2163-2329 |
4.40e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2163 LKQKQQADAEMSKHKKEA-EQALQQKSQVEKELTVVKLQLDETDKQKVLLD-QELQRvkgEVNDAFKQKSQVEVELARVR 2240
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARRErEELQR---EEERLVQKEEQLDARAEKLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2241 IQMEELVKLKLKIEEENRRLMQKDKDSTQKLlaEEAEKMKS---LAEEAGRLSVEAEETARQR--QIAESNLAEQRALAE 2315
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEEKAQRvkKIEEEADLEAERKAQ 179
|
170
....*....|....
gi 1389908282 2316 KILKEKMQAIQEAT 2329
Cdd:PRK12705 180 NILAQAMQRIASET 193
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3029-3063 |
4.57e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.57e-04
10 20 30
....*....|....*....|....*....|....*
gi 1389908282 3029 LQGTPSIAGILDEPTKEKMPFYQAMKKEFLSPETA 3063
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1335-1747 |
4.59e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1335 RTRYSELMTLTNQYIKF---IIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMK 1411
Cdd:COG5278 106 QARLDELEALIDQWLAEleqVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1412 MKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQ 1491
Cdd:COG5278 186 LALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1492 ELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRkkNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAE 1571
Cdd:COG5278 266 ALLALAALLLALAAAAALAAAAALELAAAEALA--LAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1572 EEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQ 1651
Cdd:COG5278 344 LALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1652 KANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECI 1731
Cdd:COG5278 424 LAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLAL 503
|
410
....*....|....*.
gi 1389908282 1732 RLKADFEHAEQQRGLL 1747
Cdd:COG5278 504 ALAALLLAAAEAALAA 519
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2814-2850 |
4.85e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.85e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1389908282 2814 TKFLDVQLATGGIIDPVNSHRVPLQTAYSQGQFDADM 2850
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1396-1642 |
4.98e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 46.58 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1396 KSVAKAEQEALELKMK----MKEEASKRQDVAadaekqkqniQQELQ-HLKSLSDQeiksKNQQLEDalvsrrkieeeih 1470
Cdd:pfam10168 524 KLSSPSPQECLQLLSRatqvFREEYLKKHDLA----------REEIQkRVKLLKLQ----KEQQLQE------------- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1471 iiriqlekttahkakseaeLQELRDraaEAEKLRKAAQDEAERLR----KQvaEETQRK-----KNAEDELKRKSDAEKE 1541
Cdd:pfam10168 577 -------------------LQSLEE---ERKSLSERAEKLAEKYEeikdKQ--EKLMRRckkvlQRLNSQLPVLSDAERE 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1542 AAKQKQRALDDLQKYKMQAEEAerRMKQaeEEKIRQIRVVEEVAQKSAAtqlqtkamsfseqttkleeSLKKEQGNVLK- 1620
Cdd:pfam10168 633 MKKELETINEQLKHLANAIKQA--KKKM--NYQRYQIAKSQSIRKKSSL-------------------SLSEKQRKTIKe 689
|
250 260
....*....|....*....|...
gi 1389908282 1621 -LQEEADKLKKQQKEANTAREEA 1642
Cdd:pfam10168 690 iLKQLGSEIDELIKQVKDINKHV 712
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1343-1619 |
5.20e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1343 TLTNQYIKFIIDAQRrlEDDEKASEKLKEEerrkMAEIQAELDKqkqmaeahaksvakAEQEALELKMKMKEEASKRQdv 1422
Cdd:COG3206 156 ALAEAYLEQNLELRR--EEARKALEFLEEQ----LPELRKELEE--------------AEAALEEFRQKNGLVDLSEE-- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1423 AADAEKQKQNIQQELQHLKSLSdQEIKSKNQQLEDALvSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEK 1502
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAEL-AEAEARLAALRAQL-GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1503 LRKAAQDEAERLRKQVAEETQRkknaedeLKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEKIRQIRVVE 1582
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQR-------ILASLEAELEALQAREASLQA------QLAQLEARLAELPELEAELRRLER 358
|
250 260 270
....*....|....*....|....*....|....*...
gi 1389908282 1583 EV-AQKSAATQLQTKAmsfseQTTKLEESLKKEQGNVL 1619
Cdd:COG3206 359 EVeVARELYESLLQRL-----EEARLAEALTVGNVRVI 391
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2295-2496 |
5.21e-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: 45.20 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2295 ETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQ-KQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKS 2373
Cdd:pfam17045 57 EIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQrKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2374 LEAERKR----QLEASAEAEKlKLRVKELSLAQTKAEDEAKKFKKQADE-VKAQLQR----TEKHTTEIVVQKLETQRLQ 2444
Cdd:pfam17045 137 LEWEQQRlqyqQQVASLEAQR-KALAEQSSLIQSAAYQVQLEGRKQCLEaSQSEIQRlrskLERAQDSLCAQELELERLR 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 2445 StreaddLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQ 2496
Cdd:pfam17045 216 M------RVSELGDSNRKLLEEQQRLLEELRMSQRQLQVLQNELMELKATLQ 261
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2301-2495 |
5.21e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2301 QIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfQKSLEAERKR 2380
Cdd:TIGR02794 36 EIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKA--AKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2381 QLEASAEAEKLKLrvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIvvqKLETQRLQSTREADDLKSAIADLE 2460
Cdd:TIGR02794 114 AEEKQKQAEEAKA--KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEA---KKKAEEAKKKAEAEAKAKAEAEAK 188
|
170 180 190
....*....|....*....|....*....|....*
gi 1389908282 2461 EERKKLKKEAEELQRKSKEMANAQQEQIEQQKAEL 2495
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1491-1613 |
5.57e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 45.75 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1491 QELRDRAAEAEKLRKAAQDEAERLRKQVAEEtqRKKNAEDELKRKSDAEKEAAKQKQRALddlqkyKMQAEEAERRMKQA 1570
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLERVLEKIAES--AATAEAREEKRKTKAQRNKEKRRKEEE------REAKEEKALKKKLA 269
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1389908282 1571 EEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKK 1613
Cdd:pfam07767 270 QLERLKEIA--KEIAEKEKEREEKAEARKREKRKKKKEEKKLR 310
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
41-138 |
5.60e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 43.42 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 41 QKKTFTKWVNKHLVKAQ--RHV-------TDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 107
Cdd:cd21292 25 EKVAFVNWINKNLGDDPdcKHLlpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1389908282 108 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 138
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1477-1712 |
5.78e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1477 EKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK---------NAEDELKRKSDAEKEAAKQKQ 1547
Cdd:pfam05667 255 QLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEklqftneapAATSSPPTKVETEEELQQQRE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1548 RALDDLQKykmQAEEAERRMKQAEEE------KIRQirVVEEVAQKSAATQLQTKAMSFSEQTTKLeesLKKEQGNVLKL 1621
Cdd:pfam05667 335 EELEELQE---QLEDLESSIQELEKEikklesSIKQ--VEEELEELKEQNEELEKQYKVKKKTLDL---LPDAEENIAKL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1622 QEEADKLKkqQKEANTAREeaeqeleiWrqkanEALRLRLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAEEAALK 1700
Cdd:pfam05667 407 QALVDASA--QRLVELAGQ--------W-----EKHRVPLIEEYRALKEAKSNKEDEsQRKLEEIKELREKIKEVAEEAK 471
|
250
....*....|..
gi 1389908282 1701 QKENAEKELDKQ 1712
Cdd:pfam05667 472 QKEELYKQLVAE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2481-2628 |
5.87e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2481 ANAQQEQIEQQKAELQQsfltEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALkdeQERQRKLmEEERKKLQAIMDEAV 2560
Cdd:COG1196 237 LEAELEELEAELEELEA----ELEELEAELAELEAELEELRLELEELELELEEA---QAEEYEL-LAELARLEQDIARLE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 2561 RKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVA 2628
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2076-2393 |
5.92e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.10 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2076 KEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARR 2155
Cdd:COG5185 261 QNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQN 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2156 AAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAF--------K 2227
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLedtlkaadR 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2228 QKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSlaeeagRLSVEAEETARQRQIAESNL 2307
Cdd:COG5185 421 QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINR------SVRSKKEDLNEELTQIESRV 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2308 AEqralaekiLKEKMQaiQEATKLKAEAEKLQKQKDQAQETAKRLqEDKQQIQQRLDKETE----GFQKSLEAERKRQLE 2383
Cdd:COG5185 495 ST--------LKATLE--KLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLipasELIQASNAKTDGQAA 563
|
330
....*....|
gi 1389908282 2384 ASAEAEKLKL 2393
Cdd:COG5185 564 NLRTAVIDEL 573
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1591-1913 |
5.95e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1591 TQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKK 1670
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1671 SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNE 1750
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1751 LQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKK 1830
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1831 QRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKI 1910
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
...
gi 1389908282 1911 TQL 1913
Cdd:COG4372 368 ADG 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1582-1765 |
5.96e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1582 EEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALR--- 1658
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1659 -------------------------LRLQAEEEAQKK-----SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKE 1708
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlSALSKIADADADlleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1709 LDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1765
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
176-257 |
6.13e-04 |
|
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: 42.29 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 176 RCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQ-AFSVAE--RELGVTKLLDPEDVDVPHPDEksIITYV 252
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTPEDIVSGNPRL--NLAFV 109
|
....*
gi 1389908282 253 SSLYD 257
Cdd:cd21218 110 ATLFN 114
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1817-2034 |
6.25e-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: 45.66 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1817 EAARMRSVAEEAKKQRQIAEEEAARQRSEAE---KILKEKLAAINEATRLKTEAEMALKAKEAEnerLKRQAEEEAYQRK 1893
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKE---LSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1894 LLEDQAAQHKQDIEE------KITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK 1967
Cdd:pfam07888 119 ALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1968 GIADETQKSKLKAEEEAEKLKKLAAEEerrrkeaeekvKRITAAEEEAARQCKAAQEEVERLKKKAE 2034
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTITTLTQKLTTA-----------HRKEAENEALLEELRSLQERLNASERKVE 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1378-1776 |
6.39e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1378 AEIQAELDKQKQMA---EAHAKSVAKAEQEALELKMKMKEEASKRQDVAAdAEKQKQNIQQELQHLKSLsdqeiksknqq 1454
Cdd:PRK04863 897 EEIREQLDEAEEAKrfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQ-AQQTQRDAKQQAFALTEV----------- 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1455 ledalVSRRkieeeihiiriqlekttAHKAKSEA--------ELQE-LRDRAAEAEKLRKAAQDEAERLRKQVAEETQRK 1525
Cdd:PRK04863 965 -----VQRR-----------------AHFSYEDAaemlaknsDLNEkLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVL 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1526 KNAEDELKRKSDAEKEAAKqkqraldDLQKYKMQA-EEAERRMKQAEEEKIRQIRvveevAQKSAATQLQTkamsfseQT 1604
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQ-------ELQDLGVPAdSGAEERARARRDELHARLS-----ANRSRRNQLEK-------QL 1083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1605 TKLEESLKKEQGnvlklqeeadKLKKQQKEANTAREEAEQeleiwrQKANEALRLRLQAEEEAQKKSHAQEEAEkQKLEA 1684
Cdd:PRK04863 1084 TFCEAEMDNLTK----------KLRKLERDYHEMREQVVN------AKAGWCAVLRLVKDNGVERRLHRRELAY-LSADE 1146
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1685 ERDAkkRGKAEEAALKQKENAEKELDKQR-----KFAEQIAQ------QKLS--AEQECIRLKADFEHAEQqrglLDNEL 1751
Cdd:PRK04863 1147 LRSM--SDKALGALRLAVADNEHLRDVLRlsedpKRPERKVQfyiavyQHLRerIRQDIIRTDDPVEAIEQ----MEIEL 1220
|
410 420 430
....*....|....*....|....*....|....*..
gi 1389908282 1752 QRLKNEVNSTEKQ------------RKQLEDELNKVR 1776
Cdd:PRK04863 1221 SRLTEELTSREQKlaissesvaniiRKTIQREQNRIR 1257
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1738-1874 |
6.40e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1738 EHAEQQ-RGLLdnELQRLKNEVnSTEKQRKQLedelnkvrsemdslLQMKinAEKASMVNTEKSKQ--LLESEALKMKQL 1814
Cdd:PTZ00491 673 ELLEQEaRGRL--ERQKMHDKA-KAEEQRTKL--------------LELQ--AESAAVESSGQSRAeaLAEAEARLIEAE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1815 AD-EAARMRSVAE------EAKKQRQIAEEEAARQRSEAE-KILKEKLAAINEATRLK---------TEAEMA-----LK 1872
Cdd:PTZ00491 734 AEvEQAELRAKALrieaeaELEKLRKRQELELEYEQAQNElEIAKAKELADIEATKFErivealgreTLIAIAragpeLQ 813
|
..
gi 1389908282 1873 AK 1874
Cdd:PTZ00491 814 AK 815
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1517-1684 |
6.75e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.31 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1517 QVAEETQRKKNAEDELKRKSDAEKE---AAKQKQRalddlqKYKMQAEEAERRMKQAEEEKiRQirvveEVAQKSAATQL 1593
Cdd:pfam13904 34 QSSSLTYARKLEGLKLERQPLEAYEnwlAAKQRQR------QKELQAQKEEREKEEQEAEL-RK-----RLAKEKYQEWL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1594 QTKAmsfsEQTTKLEESLKKEQGNvLKLQEEADKLKKQQKEantarEEAEQELEIWRQKANEALRLRLQAEEEAQKKSHA 1673
Cdd:pfam13904 102 QRKA----RQQTKKREESHKQKAA-ESASKSLAKPERKVSQ-----EEAKEVLQEWERKKLEQQQRKREEEQREQLKKEE 171
|
170
....*....|.
gi 1389908282 1674 QEEAEKQKLEA 1684
Cdd:pfam13904 172 EEQERKQLAEK 182
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1758-2092 |
6.90e-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: 45.88 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1758 VNSTEKQRKQLEDELNKVRSEMDSLLQmkinaekasmvNTEKSKQLLESEALKMKQLADEAA----RMRSVAEEAKKQRQ 1833
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAR-----------EVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1834 IAEEEAARqrsEAEKILKEKLAAinEATRLKtEAEMALKAKEAENERLkRQAEEEAYQRKLLEDQaaQHKQDIEEKITQL 1913
Cdd:pfam17380 353 IRQEERKR---ELERIRQEEIAM--EISRMR-ELERLQMERQQKNERV-RQELEAARKVKILEEE--RQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1914 QTSSDSELGRQKNIveETLKQKKVVEEEihiikinfhKASKEKADLESELKKLKgiADETQKSKLKAEEEAEKLKKLAAE 1993
Cdd:pfam17380 424 QIRAEQEEARQREV--RRLEEERAREME---------RVRLEEQERQQQVERLR--QQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1994 EERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAA--EQKAQDV 2071
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAteERSRLEA 570
|
330 340
....*....|....*....|....
gi 1389908282 2072 LSKNKE---DVLAQEKLRDEFENA 2092
Cdd:pfam17380 571 MEREREmmrQIVESEKARAEYEAT 594
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2267-2565 |
6.97e-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: 46.10 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2267 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAE-QRAL--AEKI-------------LKEKMQAIQEATK 2330
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvQTALrqQEKIeryqedleelterLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2331 LKAEAEKlqkQKDQAQETAKRLQEDKQQIQQRLD-KETEGFQKsleaerkRQ-LEASAEAEKLkLRVKELSLAQtkAEDE 2408
Cdd:COG3096 376 QLAEAEA---RLEAAEEEVDSLKSQLADYQQALDvQQTRAIQY-------QQaVQALEKARAL-CGLPDLTPEN--AEDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2409 AKKFKKQADEVKAQLQRTEkhtteivvQKL---ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQ 2485
Cdd:COG3096 443 LAAFRAKEQQATEEVLELE--------QKLsvaDAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQALAQRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2486 EQIEQQKAELQQsfltekglLLKREKEVEGEKKRFEKQ----------LEDEMKKAKALKDEQERQRKLMEEERKKLQAI 2555
Cdd:COG3096 515 QQLRAQLAELEQ--------RLRQQQNAERLLEEFCQRigqqldaaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330
....*....|
gi 1389908282 2556 MDEAVRKQKE 2565
Cdd:COG3096 587 LEQLRARIKE 596
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2262-2621 |
7.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2262 QKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQ 2341
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2342 KDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKA 2421
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2422 QLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLT 2501
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2502 EKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLD 2581
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1389908282 2582 KKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTV 2621
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2491-2606 |
7.18e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.97 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2491 QKAELQQSFLTEKglllkreKEVEGEKKRFEKQL---EDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE-- 2565
Cdd:pfam02841 173 KAEEVLQEFLQSK-------EAVEEAILQTDQALtakEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEhv 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 2566 ------AEEEMKNKQREMD-VLDKKRLEQEKQLAE----ENKKLREQLQTFE 2606
Cdd:pfam02841 246 kqliekMEAEREQLLAEQErMLEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1740-2022 |
7.44e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1740 AEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKvrsemdslLQMKINAEKASMVNTEKSKQLLESEalkMKQLADEAA 1819
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--------LERRIAALARRIRALEQELAALEAE---LAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1820 RMRsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAtrlktEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQA 1899
Cdd:COG4942 94 ELR--AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFL-----DAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1900 AQHKQDIEEKITQLQtssdselgrqkniveetlkqkkvveeeihiikinfhKASKEKADLESELKKLKGIADETQKSKLK 1979
Cdd:COG4942 167 AELEAERAELEALLA------------------------------------ELEEERAALEALKAERQKLLARLEKELAE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1389908282 1980 AEEEAEKLKKlaaeeerRRKEAEEKVKRITAAEEEAARQCKAA 2022
Cdd:COG4942 211 LAAELAELQQ-------EAEELEALIARLEAEAAAAAERTPAA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1354-1953 |
7.51e-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: 46.10 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1354 DAQRRLEDDEKASEKLKEEERRKMAEIQA------ELDKQKQMAEAHAKSVAKAeqeaLELKMKMKEEASkrqdvAADAE 1427
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQateevlELEQKLSVADAARRQFEKA----YELVCKIAGEVE-----RSQAW 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1428 KQKQNIQQELQHLKSLSDQE--IKSKNQQLEDALVSRRKIEEEIHIIRIQL-------EKTTAHKAKSEAELQELRDRAA 1498
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLqqLRAQLAELEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1499 EAEKLRKAAQDEAERLRKQVAEETQRKKN---AEDELKR---KSDAEKEAAKQ----KQRALDDLQKYKMQAEEAERRmK 1568
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAwlaAQDALERlreQSGEALADSQEvtaaMQQLLEREREATVERDELAAR-K 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1569 QAEEEKIRQIrvveEVAQKSAATQLQTKAMSF-----SE--QTTKLEE--------------------SLKKEQgnVLKL 1621
Cdd:COG3096 654 QALESQIERL----SQPGGAEDPRLLALAERLggvllSEiyDDVTLEDapyfsalygparhaivvpdlSAVKEQ--LAGL 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1622 QEEADKLKKQQKEANT----AREEAEQELEIWRQKANEALR---------------------LRLQAEEEAQKksHAQEE 1676
Cdd:COG3096 728 EDCPEDLYLIEGDPDSfddsVFDAEELEDAVVVKLSDRQWRysrfpevplfgraarekrleeLRAERDELAEQ--YAKAS 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1677 AEKQKLEAERDAKKRGKAE----------EAALKQKENAEKELDKQR-KFAEQIAQQKLSAEQECIRLKA---------- 1735
Cdd:COG3096 806 FDVQKLQRLHQAFSQFVGGhlavafapdpEAELAALRQRRSELERELaQHRAQEQQLRQQLDQLKEQLQLlnkllpqanl 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1736 -DFEHAEQQRGLLDNELQRL---KNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKAsmvntEKSKQLLESEALKM 1811
Cdd:COG3096 886 lADETLADRLEELREELDAAqeaQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQA-----KEQQRRLKQQIFAL 960
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1812 KQLA--------DEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAK-----EAEN 1878
Cdd:COG3096 961 SEVVqrrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKqqtlqELEQ 1040
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1879 E--RLKRQAEEEAyqrkllEDQAAQHKQDIEEKITQLQ---TSSDSELGRQKNIVEETLKQKKVVEEEIHIIK--INFHK 1951
Cdd:COG3096 1041 EleELGVQADAEA------EERARIRRDELHEELSQNRsrrSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEReqVVQAK 1114
|
..
gi 1389908282 1952 AS 1953
Cdd:COG3096 1115 AG 1116
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2255-2363 |
7.71e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.21 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2255 EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAE 2334
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91
|
90 100
....*....|....*....|....*....
gi 1389908282 2335 AEKLQKQKDQAQETAKRLQEDKQQIQQRL 2363
Cdd:pfam20492 92 IARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1872-2132 |
7.84e-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: 45.22 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1872 KAKEAENERLKRQAEEEAyqrklleDQAAQHKQDIEEKITQLQTSSDSELGRQKNiveetLKQKKVVEEEihiikinfhK 1951
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAA-------KKEQERQKKLEQQAEEAEKQRAAEQARQKE-----LEQRAAAEKA---------A 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1952 ASKEKADLESELKKlkgiadeTQKSKLKAEEEAEKLKKLAaeeerrrkeaeekvkritAAEEEAARQCKAAQEEVERLKK 2031
Cdd:TIGR02794 105 KQAEQAAKQAEEKQ-------KQAEEAKAKQAAEAKAKAE------------------AEAERKAKEEAAKQAEEEAKAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2032 KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAA 2111
Cdd:TIGR02794 160 AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFG 239
|
250 260
....*....|....*....|.
gi 1389908282 2112 LlrQKAEEAEKQKKAAENEAA 2132
Cdd:TIGR02794 240 L--ASGSNAEKQGGARGAAAG 258
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2113-2628 |
8.14e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2113 LRQKAEEAEKQKKAAEN-----EAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQK 2187
Cdd:pfam05557 23 LEHKRARIELEKKASALkrqldRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2188 SQV----EKELTVVKLQLDETDKQKVLLDQELQRVKgEVNDAFKQK-SQVEVELARVRIQMEELVKLKLKIEEENRRLMQ 2262
Cdd:pfam05557 103 REVisclKNELSELRRQIQRAELELQSTNSELEELQ-ERLDLLKAKaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2263 KDKDSTQ-KLLAEEAEKMKSLAEEAGRLSVEAE---ETARQRQIAESNLAEQRALAEKilKEKMQAiqEATKLKAEAEKL 2338
Cdd:pfam05557 182 QEQDSEIvKNSKSELARIPELEKELERLREHNKhlnENIENKLLLKEEVEDLKRKLER--EEKYRE--EAATLELEKEKL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2339 QKQ----KDQAQETA------KRLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASaeaekLKLRVKELSLAQTKAEDE 2408
Cdd:pfam05557 258 EQElqswVKLAQDTGlnlrspEDLSRRIEQLQQR--EIVLKEENSSLTSSARQLEKA-----RRELEQELAQYLKKIEDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2409 AKKFKKQaDEVKAQLQRT---------------EKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEEL 2473
Cdd:pfam05557 331 NKKLKRH-KALVRRLQRRvllltkerdgyrailESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2474 QRKSKEMANAQQEQIE---QQKAELQQSFLTEKGLLLKRE-KEVEGEKKRFEKQledemkkakalKDEQErqrklMEEER 2549
Cdd:pfam05557 410 LGGYKQQAQTLERELQalrQQESLADPSYSKEEVDSLRRKlETLELERQRLREQ-----------KNELE-----MELER 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2550 KKLQAIMDEAVRKQKEAEEEMKNKQREmdvldkKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVA 2628
Cdd:pfam05557 474 RCLQGDYDPKKTKVLHLSMNPAAEAYQ------QRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVL 546
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
36-144 |
8.17e-04 |
|
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: 42.28 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 36 ERDRVQKKTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 106
Cdd:cd21330 9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908282 107 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 144
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1490-1722 |
8.34e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.97 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1490 LQELRDRAAEAEK------LRKAAQDEAERLRKQVAEETQRKKnaeDELKRKSdaEKEAAKQKQRALDDLqkykmqAEEA 1563
Cdd:pfam02841 67 LQELLDLHRDCEKeaiavfMKRSFKDENQEFQKELVELLEAKK---DDFLKQN--EEASSKYCSALLQDL------SEPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1564 ERRMKQAEEEK-------IRQIRVVEEVAQKSAATQLQTKAM--SFSEQTTKLEESLkkeqgnvLKLQEEADKLKKQQKE 1634
Cdd:pfam02841 136 EEKISQGTFSKpggyklfLEERDKLEAKYNQVPRKGVKAEEVlqEFLQSKEAVEEAI-------LQTDQALTAKEKAIEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1635 ANTAREEAEQELEIWRQKANEalrlrLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR 1713
Cdd:pfam02841 209 ERAKAEAAEAEQELLREKQKE-----EEQMMEAQERSYQEHVKQlIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFK 283
|
....*....
gi 1389908282 1714 KFAEQIAQQ 1722
Cdd:pfam02841 284 TEAESLQKE 292
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1602-2029 |
8.44e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1602 EQTTKLEESLKKeQGNVLKLQEEADKLKKQQKEANTAREEAEQELEiwrQKANEALRLRlqaeEEAQKKSHAQEEAEK-- 1679
Cdd:pfam10174 158 ESIKKLLEMLQS-KGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLD---QKEKENIHLR----EELHRRNQLQPDPAKtk 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1680 --QKLEAERDAK----KRG--KAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAE---QECIRLKADFEHAEQQRGLLD 1748
Cdd:pfam10174 230 alQTVIEMKDTKisslERNirDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKfmkNKIDQLKQELSKKESELLALQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1749 NELQRLKNEvNSTEKQRKQLEDELNKVRSEMDSLLQMKINA------EKASMVNtEKSKQLLE---------SEALKMKQ 1813
Cdd:pfam10174 310 TKLETLTNQ-NSDCKQHIEVLKESLTAKEQRAAILQTEVDAlrlrleEKESFLN-KKTKQLQDlteekstlaGEIRDLKD 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1814 LADEAARMRSVAEeaKKQRQIAEEEAARQRSEAEkiLKEKLAAI-----NEATRLKTeAEMALKAKEAENERLKRQAEEE 1888
Cdd:pfam10174 388 MLDVKERKINVLQ--KKIENLQEQLRDKDKQLAG--LKERVKSLqtdssNTDTALTT-LEEALSEKERIIERLKEQRERE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1889 AYQRKLLEDQAAQHKQDIEEKITQLQT------SSDSELGRQKNIVEETLKQKkvvEEEIHIIKINFHKASKEKADLESE 1962
Cdd:pfam10174 463 DRERLEELESLKKENKDLKEKVSALQPeltekeSSLIDLKEHASSLASSGLKK---DSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908282 1963 LKKLKGIADETQKSklkaEEEAEKLKKLAaeeerrrkeaeekvKRITAAEEEAARqckaAQEEVERL 2029
Cdd:pfam10174 540 LKKAHNAEEAVRTN----PEINDRIRLLE--------------QEVARYKEESGK----AQAEVERL 584
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2354-2594 |
8.70e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2354 EDKQQIQQRLdKETEGFQKSLEAERKRQleasAEAEKLKLRVKELslaqtkaedeakkfkKQADEVKAQLQRTEKHTTEI 2433
Cdd:pfam15709 329 EQEKASRDRL-RAERAEMRRLEVERKRR----EQEEQRRLQQEQL---------------ERAEKMREELELEQQRRFEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2434 VvqKLETQRLQSTREaddlksaiadleeerkklkkeaeelQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEV 2513
Cdd:pfam15709 389 I--RLRKQRLEEERQ-------------------------RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2514 E-GEKKRFEKQLEDEMKKAkaLKDEQERQRKLMEEERKKLQaimdeavRKQKEAEE----EMKNKQREMDVLDKKRLEQE 2588
Cdd:pfam15709 442 EeAERAEAEKQRQKELEMQ--LAEEQKRLMEMAEEERLEYQ-------RQKQEAEEkarlEAEERRQKEEEAARLALEEA 512
|
....*.
gi 1389908282 2589 KQLAEE 2594
Cdd:pfam15709 513 MKQAQE 518
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2474-2597 |
9.01e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2474 QRKSKEMANAQQE---QIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERK 2550
Cdd:PRK09510 68 QQQQKSAKRAEEQrkkKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1389908282 2551 KLQAIMDEAVRKQKEAEEEMKnKQREMDVLDKKRLEQEKQLAEENKK 2597
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1483-1555 |
9.09e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.42 E-value: 9.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 1483 KAKSEAELQELRdraAEAEKLRKAAQDEAERLRKQVAEETQRKKNaedelKRKSDAEKEAAKQKQRALDDLQK 1555
Cdd:cd06503 53 LAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKEEAE-----RILEQAKAEIEQEKEKALAELRK 117
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2114-2458 |
9.23e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.52 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2114 RQKAEEAEKQKKAAENEAAK----QAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHK-----------K 2178
Cdd:pfam09731 100 EVAEEEKEATKDAAEAKAQLpkseQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKeasdtaeisreK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2179 EAEQALQQKSQVEKEL--TVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVElarvriQMEELVKLKLKI-EE 2255
Cdd:pfam09731 180 ATDSALQKAEALAEKLkeVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKA------QSLAKLVDQYKElVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2256 ENRRLMQKDKDST-QKLLAEEAEKMKSLAEEAGRL--SVEAEETARQRQIAESNLAEQRALAEKILKekmqaiQEATKLK 2332
Cdd:pfam09731 254 SERIVFQQELVSIfPDIIPVLKEDNLLSNDDLNSLiaHAHREIDQLSKKLAELKKREEKHIERALEK------QKEELDK 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2333 AEAEKLQKQKDQaqetakrLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQ---------- 2402
Cdd:pfam09731 328 LAEELSARLEEV-------RAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIelqreflqdi 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 2403 -TKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVV---QKLETQRLQSTREA--DDLKSAIAD 2458
Cdd:pfam09731 401 kEKVEEERAGRLLKLNELLANLKGLEKATSSHSEvedENRKAQQLWLAVEAlrSTLEDGSAD 462
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2474-2594 |
9.79e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2474 QRKSKEMANAQQEQiEQQKAELQQSflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKAlkdeqERQRKLMEEERKKLQ 2553
Cdd:COG2268 208 AERETEIAIAQANR-EAEEAELEQE--REIETARIAEAEAELAKKKAEERREAETARAEA-----EAAYEIAEANAEREV 279
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1389908282 2554 AIMDEAVRKQKEAEEEMKNKQREMDVLD---KKRLEQEKQLAEE 2594
Cdd:COG2268 280 QRQLEIAEREREIELQEKEAEREEAELEadvRKPAEAEKQAAEA 323
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2255-2514 |
9.91e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2255 EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAgrlsvEAEETARQRQIAESNLAEQRALAEKILKEkmqaiqeatklkae 2334
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSE-------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2335 aekLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEAsaEAEKLKLRVKELSLAQTKAEDEAKKFKK 2414
Cdd:COG3206 224 ---LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA--QLAELEAELAELSARYTPNHPDVIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2415 QADEVKAQLQRTekhtTEIVVQKLETQRLQSTREADDLKSAIADleeerkklkkeaeeLQRKSKEMANAQQEQIE-QQKA 2493
Cdd:COG3206 299 QIAALRAQLQQE----AQRILASLEAELEALQAREASLQAQLAQ--------------LEARLAELPELEAELRRlEREV 360
|
250 260
....*....|....*....|.
gi 1389908282 2494 ELQQSFLTEkglLLKREKEVE 2514
Cdd:COG3206 361 EVARELYES---LLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2267-2458 |
1.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2267 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiaesNLAEQRALAEKILKEKMQAIqEATKLKAEAEKLQKQKDQAQ 2346
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELD----ALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2347 ETAKRLQEDKQQIQQrLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ-ADEVKAQLQR 2425
Cdd:COG4913 682 ASSDDLAALEEQLEE-LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|...
gi 1389908282 2426 TEKHTTeiVVQKLETQRLQSTREADDLKSAIAD 2458
Cdd:COG4913 761 DAVERE--LRENLEERIDALRARLNRAEEELER 791
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1475-1901 |
1.11e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.28 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1475 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRkknaedelKRKSDAEKEAAKQKQRALDDLQ 1554
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL--------LALALAALLLAAAALLLLLLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1634
Cdd:COG5278 183 AALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1635 ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1714
Cdd:COG5278 263 LAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1715 FAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASM 1794
Cdd:COG5278 343 ALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1795 VNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAK 1874
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*..
gi 1389908282 1875 EAENERLKRQAEEEAYQRKLLEDQAAQ 1901
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAE 529
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1363-1597 |
1.13e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1363 EKASEKLKEEERRKMAEIQAELDKQKQMAEahaksvAKAEQEALELKMKMKEEASKRQDVAADAEK-QKQNIQQELQHlk 1441
Cdd:pfam15709 331 EKASRDRLRAERAEMRRLEVERKRREQEEQ------RRLQQEQLERAEKMREELELEQQRRFEEIRlRKQRLEEERQR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1442 slsdQEIKSKNQQLEdalvsrrkieeeihiirIQLEKTTAHKAKSE--AELQELRdraaeaeklRKAAQDEAERlrkqVA 1519
Cdd:pfam15709 403 ----QEEEERKQRLQ-----------------LQAAQERARQQQEEfrRKLQELQ---------RKKQQEEAER----AE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1520 EETQRKKNAEDELKRKSDAEKEAAKQKQralddlQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKA 1597
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEER------LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1481-1555 |
1.15e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1481 AHKAKSEAELQElrdraAEAEKLRKAAQDEAERLRKQVAEETQR-----KKNAEDELKR-KSDAEKEAAKQKQRALDDLQ 1554
Cdd:COG0711 43 AERAKEEAEAAL-----AEYEEKLAEARAEAAEIIAEARKEAEAiaeeaKAEAEAEAERiIAQAEAEIEQERAKALAELR 117
|
.
gi 1389908282 1555 K 1555
Cdd:COG0711 118 A 118
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1394-1714 |
1.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1394 HAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIR 1473
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLR----EELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1474 IQLEKTtahkaksEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDL 1553
Cdd:COG4372 80 EELEEL-------NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1554 QKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQK 1633
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1634 EANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR 1713
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
.
gi 1389908282 1714 K 1714
Cdd:COG4372 313 L 313
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1546-1911 |
1.33e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1546 KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEA 1625
Cdd:COG3064 6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1626 DKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENA 1705
Cdd:COG3064 86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1706 EKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM 1785
Cdd:COG3064 166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1786 KINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKT 1865
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1389908282 1866 EAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 1911
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
40-142 |
1.39e-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: 41.90 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 40 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHFQ 142
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
41-138 |
1.44e-03 |
|
first 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, and are probably involved in the 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 41.36 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 41 QKKTFTKWVNKHLVK---------AQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 106
Cdd:cd21293 2 EKGSYVDHINRYLGDdpflkqflpIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1389908282 107 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 138
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2261-2416 |
1.45e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2261 MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNL--AEQRALAEKILKEKMQAIQEATKLKAEAEKL 2338
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRerEELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 2339 QKQKDQAQETAKRLQEDKQQIQQRLdKETEGF-QKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQA 2416
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNEL-YRVAGLtPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2054-2226 |
1.47e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2054 AKEAAQKCTAAEQKAQDVlskNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAK 2133
Cdd:PRK09510 89 AEELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2134 QAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQ-----KSQVEKELTVVKLQLDETDKQK 2208
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKaaaeaKAAAAKAAAEAKAAAEKAAAAK 245
|
170
....*....|....*...
gi 1389908282 2209 VLLDQELQRVKGEVNDAF 2226
Cdd:PRK09510 246 AAEKAAAAKAAAEVDDLF 263
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1682-2128 |
1.47e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.51 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1682 LEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNST 1761
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1762 EKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAAR 1841
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1842 QRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSEL 1921
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1922 GRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEA 2001
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2002 EEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLA 2081
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1389908282 2082 QEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAE 2128
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAA 524
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1355-1458 |
1.48e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1355 AQRRLEDDEKAseklkEEERRKMAEIQAELDKQKQ--MAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAE--KQK 1430
Cdd:PTZ00491 684 ERQKMHDKAKA-----EEQRTKLLELQAESAAVESsgQSRAEALAEAEARLIEAEAEVEQAELRAKALRIEAEAEleKLR 758
|
90 100
....*....|....*....|....*...
gi 1389908282 1431 QNIQQELQHLKSLSDQEIKsKNQQLEDA 1458
Cdd:PTZ00491 759 KRQELELEYEQAQNELEIA-KAKELADI 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1532-1755 |
1.57e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1532 LKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEkirqirvVEEVAQKSAATQLQTKAMSFSEQTTKLEESL 1611
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE------QLPELRKELEEAEAA-------LEEFRQKNGLVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1612 KKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEA-LRLRLQAEEEAQKKSH-------AQEEAEKQKLE 1683
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAeLEAELAELSARYTPNHpdvialrAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 1684 AERDAKKRG-KAEEAALKQKENA-EKELDKQRKFAEQIAQQklsaEQECIRLKADFEHAEQqrgLLDNELQRLK 1755
Cdd:COG3206 309 QEAQRILASlEAELEALQAREASlQAQLAQLEARLAELPEL----EAELRRLEREVEVARE---LYESLLQRLE 375
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1488-1691 |
1.64e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1488 AELQELRDRAAEAEKLRKAAQDEAERL---RKQVAEETQRKKNAEDELKRKSD---AEKEAAKQKQRALDDLQkYKMQAE 1561
Cdd:COG1340 50 AQVKELREEAQELREKRDELNEKVKELkeeRDELNEKLNELREELDELRKELAelnKAGGSIDKLRKEIERLE-WRQQTE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1562 ----EAERR-MKQAE--EEKIRQIRVVEEVAQK-----SAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLK 1629
Cdd:COG1340 129 vlspEEEKElVEKIKelEKELEKAKKALEKNEKlkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 1630 KQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1691
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1356-1673 |
1.65e-03 |
|
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: 44.26 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1356 QRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmKMKEEASKRQdvaadaekQKQNIQQ 1435
Cdd:pfam15558 61 EQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERA-RQEAEQRKQC--------QEQRLKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1436 ELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahKAKSEAELQELRDRAAEAEKLRKA--------A 1507
Cdd:pfam15558 132 KEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSE--LLNHQARKVLVDCQAKAEELLRRLsleqslqrS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1508 QDEAERLRKQVAEETQRKKNAEDELKRKSdaeKEAAKQKQRALDdlQKYKMQAEEAERRMKQAEEekirqirVVEEVAQK 1587
Cdd:pfam15558 210 QENYEQLVEERHRELREKAQKEEEQFQRA---KWRAEEKEEERQ--EHKEALAELADRKIQQARQ-------VAHKTVQD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1588 SAAtqlqtkamsfseqttkleeslKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEA 1667
Cdd:pfam15558 278 KAQ---------------------RARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEA 336
|
....*.
gi 1389908282 1668 QKKSHA 1673
Cdd:pfam15558 337 RKTARA 342
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1413-1727 |
1.68e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 44.67 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1413 KEEASKRQDVAADAEKQKQNIQQEL-----------QHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTA 1481
Cdd:pfam04747 14 QQLTNRRKNLGRVAKSQRNQFRQWLltavlpnsindQRKEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1482 HKAKSEAELqelrdRAAEAEKLRKAAQdeaerlrkqvaEETQRKKNAEDELKRKSDAEKEAAKQKQRAlddlQKYKMQAE 1561
Cdd:pfam04747 94 AKKAAEKEA-----RRAEAEAKKRAAQ-----------EEEHKQWKAEQERIQKEQEKKEADLKKLQA----EKKKEKAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1562 EAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1641
Cdd:pfam04747 154 KAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1642 AEQELEIWRQKANEALRlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1721
Cdd:pfam04747 234 VEQVVEQPKVVTEEPHQ---QAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPASENQKKNKKDKKKSESEKVVE 310
|
....*.
gi 1389908282 1722 QKLSAE 1727
Cdd:pfam04747 311 EPVQAE 316
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2332-2583 |
1.73e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2332 KAEAeKLQKQKDQAQETAKRLQEDKqqiQQRLDKEtegfqkslEAERKRQLEASAEAeklklRVKELSLAQTKAEDEAKK 2411
Cdd:PRK05035 435 KAEI-RAIEQEKKKAEEAKARFEAR---QARLERE--------KAAREARHKKAAEA-----RAAKDKDAVAAALARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2412 FKKQADEVKAQLQRTEKHTTEIVVQ--------KLETQRLQSTREADDLKSAIA---------DLEEERKKLKKEAEELQ 2474
Cdd:PRK05035 498 KKAAATQPIVIKAGARPDNSAVIAArearkaqaRARQAEKQAAAAADPKKAAVAaaiarakakKAAQQAANAEAEEEVDP 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2475 RKSK---EMANAQQEQIEQQKAELQQSfltekglllkrekEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKK 2551
Cdd:PRK05035 578 KKAAvaaAIARAKAKKAAQQAASAEPE-------------EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPR 644
|
250 260 270
....*....|....*....|....*....|...
gi 1389908282 2552 LQAIMDEAVR-KQKEAEEEMKNKQREMDVLDKK 2583
Cdd:PRK05035 645 KAAVAAAIARaKARKAAQQQANAEPEEAEDPKK 677
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1403-1666 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1403 QEALElKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQ--EIKSKNQQLEDALVSRRKIEEEihiiriqLEKTt 1480
Cdd:COG2433 379 EEALE-ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQveRLEAEVEELEAELEEKDERIER-------LERE- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1481 AHKAKSEAELQELRDRaaEAEKLRKaaqdEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQA 1560
Cdd:COG2433 450 LSEARSEERREIRKDR--EISRLDR----EIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEA 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1561 -EEAERRMKQAEeekiRQIRVVEEV--AQKSAATQL---QTKAMSFSEQT-TKLEESLKKEQGNVLKLQE----EADKLk 1629
Cdd:COG2433 524 iRRLEEEYGLKE----GDVVYLRDAsgAGRSTAELLaeaGPRAVIVPGELsEAADEVLFEEGIPVLPAEDvtiqEVDDL- 598
|
250 260 270
....*....|....*....|....*....|....*..
gi 1389908282 1630 kqqkeANTAREEAEQELEIWRQKANEalRLRLQAEEE 1666
Cdd:COG2433 599 -----AVVDEEELEAAIEDWEERAEE--RRREKKAEM 628
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1555-1879 |
1.90e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERrmKQAEEEKIR----QIRVVEEVAQKSAAtqLQTKAmsfseqttkleESLKKEQGNVLKLQEEADKLKK 1630
Cdd:PRK05035 435 KAEIRAIEQEK--KKAEEAKARfearQARLEREKAAREAR--HKKAA-----------EARAAKDKDAVAAALARVKAKK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1631 QQKEANTArEEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAerdAKKRGKAEEAALKQK--ENAEKE 1708
Cdd:PRK05035 500 AAATQPIV-IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAA---AIARAKAKKAAQQAAnaEAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1709 LDKQRKFAEQIAqqklsaeqeciRLKAdfEHAEQQrglldnelqrlkNEVNSTEKQRKQLEDELNKVRSEMdsllqmkin 1788
Cdd:PRK05035 576 DPKKAAVAAAIA-----------RAKA--KKAAQQ------------AASAEPEEQVAEVDPKKAAVAAAI--------- 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1789 aEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEaarqrsEAEKILKEKLAAineatrlkteAE 1868
Cdd:PRK05035 622 -ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE------EAEDPKKAAVAA----------AI 684
|
330
....*....|.
gi 1389908282 1869 MALKAKEAENE 1879
Cdd:PRK05035 685 ARAKAKKAAQQ 695
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
178-238 |
1.91e-03 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 39.98 E-value: 1.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 178 DNFTTSWRDGKLFSAIIHKHRPALIDMNQV--YRQSNQE----NLEQAFSVAERELGVTKL-LDPEDV 238
Cdd:pfam11971 14 EDLLRDLSDGCALAALIHFYCPQLIDLEDIclKESMSLAdslyNIQLLQEFCQRHLGNRCChLTLEDL 81
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1444-1671 |
1.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1444 SDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAE--- 1520
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1521 ETQRKKNAEDEL-------------------KRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvv 1581
Cdd:COG3883 94 ALYRSGGSVSYLdvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1582 eevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1661
Cdd:COG3883 166 ----LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250
....*....|
gi 1389908282 1662 QAEEEAQKKS 1671
Cdd:COG3883 242 AAASAAGAGA 251
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
639-719 |
1.96e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 40.76 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 639 WLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAFTAALQTQWSWLLQL 718
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 1389908282 719 C 719
Cdd:pfam00435 96 A 96
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1620-1702 |
2.09e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 41.69 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1620 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEalrLRLQAEEEAQK-----KSHAQEEAEKQKLEAERDAKKRGKA 1694
Cdd:PRK05759 39 KIADGLAAAERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQiieeaKAEAEAEAARIKAQAQAEIEQERKR 115
|
....*...
gi 1389908282 1695 EEAALKQK 1702
Cdd:PRK05759 116 AREELRKQ 123
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1572-1823 |
2.10e-03 |
|
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: 43.27 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1572 EEKIRQIRVVeeVAQKSAATQLQTKAMSFSEQTTklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQ 1651
Cdd:pfam17045 9 QELMKQIDIM--VAHKKSEWEGQTRALETRLDIR--EEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1652 KANEALRLRLQAEEEAQKKS--HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQE 1729
Cdd:pfam17045 85 KLQEELSKLKRSYEKLQRKQlkEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1730 CIRLKADF----EHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL--QMKINAEKasmvntEKSKQL 1803
Cdd:pfam17045 165 SLIQSAAYqvqlEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGdsNRKLLEEQ------QRLLEE 238
|
250 260
....*....|....*....|
gi 1389908282 1804 LESEALKMKQLADEAARMRS 1823
Cdd:pfam17045 239 LRMSQRQLQVLQNELMELKA 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1954-2415 |
2.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1954 KEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKA 2033
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2034 EDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAAlL 2113
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE-L 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2114 RQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKE 2193
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2194 LTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRI-----QMEELVKLKLKIEEENRRLMQKD-KDS 2267
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldRIEELQELLREAEELEEELQLEElEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2268 TQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILkekmqAIQEATKLKAEAEKLQKQKDQAQE 2347
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 2348 TAKRLQEDKQQIQQRLdKETEGFQKSLEAERKRQlEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ 2415
Cdd:COG4717 447 ELEELREELAELEAEL-EQLEEDGELAELLQELE-ELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2344-2494 |
2.20e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2344 QAQETAKRLQEDKQQIQQRldketegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQL 2423
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKK--------QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAEN 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 2424 QRTEKHTTEIVVQKLETQRLQST-READDLKSaiaDLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2494
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKdHKAFDLKQ---ESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQ 347
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
43-135 |
2.24e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.16 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 43 KTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLKHRQV 112
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 1389908282 113 KLVNIRNDDIADGNpKLTLGLIW 135
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2279-2616 |
2.42e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2279 MKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEkilkEKMQAIQEATKLKAEAEKLQKQKDQAQ------ETAKRL 2352
Cdd:pfam05622 68 LEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNE----ELTSLAEEAQALKDEMDILRESSDKVKkleatvETYKKK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2353 QED----KQQIQQRLDKETEGFQK--SLEAERKRQLEASAEAEKLKLRVKELslaQTKAEDEAKKFKKQADEVKaqlQRT 2426
Cdd:pfam05622 144 LEDlgdlRRQVKLLEERNAEYMQRtlQLEEELKKANALRGQLETYKRQVQEL---HGKLSEESKKADKLEFEYK---KLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2427 EKHTTeivVQKlETQRLQSTREA-----DDLKSAIADLEEERKKLKkeaeelqrkskeMANAQQEQIEQQKAELQQSFLT 2501
Cdd:pfam05622 218 EKLEA---LQK-EKERLIIERDTlretnEELRCAQLQQAELSQADA------------LLSPSSDPGDNLAAEIMPAEIR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2502 EKGLLLKREKEVEGEKKrfEKQLEDEMKKAKALKDE-QERQRKLMEEERKKLQAIMD--EAVRKQKEAEEEMKNKQREMD 2578
Cdd:pfam05622 282 EKLIRLQHENKMLRLGQ--EGSYRERLTELQQLLEDaNRRKNELETQNRLANQRILElqQQVEELQKALQEQGSKAEDSS 359
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1389908282 2579 VLDKKRLEQEKQLAE---ENKKLREQLQTFEISSKTVSQTK 2616
Cdd:pfam05622 360 LLKQKLEEHLEKLHEaqsELQKKKEQIEELEPKQDSNLAQK 400
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1525-1637 |
2.45e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1525 KKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERR-----MKQAEE-EKIRQIRvvEEVAQ-KSAATQLQTKA 1597
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNyerelVLHAEDiKALQALR--EELNElKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1389908282 1598 MSFSEQTTKLEESLKKEQGnvlKLQEEADKLKKQQKEANT 1637
Cdd:pfam07926 81 ESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNE 117
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4393-4430 |
2.48e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.48e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1389908282 4393 QRFLEVQYLTGGLIEPDATNRVAIDEAVKKGTLDARTA 4430
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1423-1764 |
2.54e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1423 AADAEKQKQNIQQELQHL-KSLSDQEikSKNQQLEDALvsrrkieeeihiiriqlekttahkAKSEAELQELRDRAAEAE 1501
Cdd:PRK04863 832 EADPEAELRQLNRRRVELeRALADHE--SQEQQQRSQL------------------------EQAKEGLSALNRLLPRLN 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1502 KL-RKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAK--QKQRALDDLQKYKMQAEEAERRMKQaeeekirQI 1578
Cdd:PRK04863 886 LLaDETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVlqSDPEQFEQLKQDYQQAQQTQRDAKQ-------QA 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1579 RVVEEVAQKSAAtqlqtkaMSFSEQttklEESLKKEQGNVlklqeeaDKLKKQQKEANTAREEAEQELEIWRQKANEALR 1658
Cdd:PRK04863 959 FALTEVVQRRAH-------FSYEDA----AEMLAKNSDLN-------EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1659 LR--LQAEEEAQKKSHAQEEAEKQKL------EAERDAKKRGKAEEAALKQKENAEKELDKQRKFAE---QIAQQKLSAE 1727
Cdd:PRK04863 1021 VLasLKSSYDAKRQMLQELKQELQDLgvpadsGAEERARARRDELHARLSANRSRRNQLEKQLTFCEaemDNLTKKLRKL 1100
|
330 340 350
....*....|....*....|....*....|....*..
gi 1389908282 1728 QEciRLKADFEHAEQQRGLLDNELQRLKNevNSTEKQ 1764
Cdd:PRK04863 1101 ER--DYHEMREQVVNAKAGWCAVLRLVKD--NGVERR 1133
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1477-1682 |
2.56e-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: 43.26 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1477 EKT--TAHKAKSEAELQELRdRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQ 1554
Cdd:pfam15905 116 EKTslSASVASLEKQLLELT-RVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1555 KYKMQAEEAERRMKQAEEEKIRQ----IRVVEEVAQKSAATQlqtKAMSFSEQTTKLEESLKKEQGNVL----KLQEEAD 1626
Cdd:pfam15905 195 HSKGKVAQLEEKLVSTEKEKIEEksetEKLLEYITELSCVSE---QVEKYKLDIAQLEELLKEKNDEIEslkqSLEEKEQ 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908282 1627 KLKKQQKEANTAREEAEQELEIWRQKaNEALRLRLQAEEEAQKKSHAQEEAEKQKL 1682
Cdd:pfam15905 272 ELSKQIKDLNEKCKLLESEKEELLRE-YEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2180-2431 |
2.61e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2180 AEQALQQKSQVEKeltvvkLQLDETDKQKVLLDQELQRvkGEVNDAFKQKSQVEVELAR-VRIQMEELVKLKLKIEEENR 2258
Cdd:PRK11637 39 SAHASDNRDQLKS------IQQDIAAKEKSVRQQQQQR--ASLLAQLKKQEEAISQASRkLRETQNTLNQLNKQIDELNA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2259 RL--MQKDKDSTQKLLAEEAEKMKSLAEEAG-RLSVEAEETARQRQIaesnLAEQRALAekilkekmQAIQEA-TKLKAE 2334
Cdd:PRK11637 111 SIakLEQQQAAQERLLAAQLDAAFRQGEHTGlQLILSGEESQRGERI----LAYFGYLN--------QARQETiAELKQT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2335 AEKLQKQKD---QAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAerkrqLEASAEAEK---LKLRVKELSLAQT--KAE 2406
Cdd:PRK11637 179 REELAAQKAeleEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTG-----LESSLQKDQqqlSELRANESRLRDSiaRAE 253
|
250 260 270
....*....|....*....|....*....|
gi 1389908282 2407 DEAK----KFKKQADEVKA-QLQRTEKHTT 2431
Cdd:PRK11637 254 REAKaraeREAREAARVRDkQKQAKRKGST 283
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2505-2619 |
2.64e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2505 LLLKR--EKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKlMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREmDVLDK 2582
Cdd:PRK12704 23 FVRKKiaEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKE-ENLDR 100
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1389908282 2583 KRLE---QEKQLAEENKKLREQLQTFEISSKTVSQTKESQ 2619
Cdd:PRK12704 101 KLELlekREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1620-1712 |
2.66e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1620 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALrlrlqaeEEAQKKshAQEEAEKQKLEAERDAKK-RGKAEEAA 1698
Cdd:cd06503 34 KIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEII-------EEARKE--AEKIKEEILAEAKEEAERiLEQAKAEI 104
|
90
....*....|....
gi 1389908282 1699 LKQKENAEKELDKQ 1712
Cdd:cd06503 105 EQEKEKALAELRKE 118
|
|
| CH_PARVG_rpt2 |
cd21307 |
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ... |
42-131 |
2.79e-03 |
|
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409156 [Multi-domain] Cd Length: 122 Bit Score: 40.80 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 42 KKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKgrmrFH--------KLQNVQIALDFLKHRQVK 113
Cdd:cd21307 18 KKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSE----FFltpsstseMLHNVTLALELLKEGGLL 93
|
90
....*....|....*...
gi 1389908282 114 LVNIRNDDIADGNPKLTL 131
Cdd:cd21307 94 NFPVNPEDIVNGDSKATI 111
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2476-2643 |
2.85e-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: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2476 KSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAi 2555
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVR-QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEI- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2556 mdeavrkQKEAEEEMKNKQREMDVLDKKRLEQEKQlaEENKKLREQLQTFEISS---KTVSQTKESQTVSVEKLVAVTTV 2632
Cdd:pfam05262 291 -------KKNDEEALKAKDHKAFDLKQESKASEKE--AEDKELEAQKKREPVAEdlqKTKPQVEAQPTSLNEDAIDSSNP 361
|
170
....*....|.
gi 1389908282 2633 GTSKGVLNGST 2643
Cdd:pfam05262 362 VYGLKVVDPIT 372
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1532-1836 |
2.85e-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: 43.79 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1532 LKRKSDAEKEAAKQ----KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKL 1607
Cdd:COG5185 248 LAQTSDKLEKLVEQntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1608 EESLKKEQGNVLKLQEEADKLKKQQKEA-NTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKS-----HAQEEAEKQK 1681
Cdd:COG5185 328 EESKRETETGIQNLTAEIEQGQESLTENlEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESldeipQNQRGYAQEI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1682 LEAERDAKKRGKAE---------------EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQecirlKADFEHAEQQRGL 1746
Cdd:COG5185 408 LATLEDTLKAADRQieelqrqieqatssnEEVSKLLNELISELNKVMREADEESQSRLEEAY-----DEINRSVRSKKED 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1747 LDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEA--LKMKQLADEAARMRSV 1824
Cdd:COG5185 483 LNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLipASELIQASNAKTDGQA 562
|
330
....*....|..
gi 1389908282 1825 AEEAKKQRQIAE 1836
Cdd:COG5185 563 ANLRTAVIDELT 574
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1505-1695 |
2.90e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1505 KAAQDEAERLRKQVAEETQRKKNAEDELKRKsdaEKEAAKQKQRALDDLQKYKMQAEEAERRMKqaeeeKIRQirvveEV 1584
Cdd:PHA02562 198 KTYNKNIEEQRKKNGENIARKQNKYDELVEE---AKTIKAEIEELTDELLNLVMDIEDPSAALN-----KLNT-----AA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1585 AQKSAATQLQTKAMSFSEQTT---KLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL-- 1659
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEKGGvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELkn 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908282 1660 -----------------RLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAE 1695
Cdd:PHA02562 345 kistnkqslitlvdkakKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2163-2626 |
2.91e-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: 44.06 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2163 LKQKQQADAEmsKHKKEAEQALQQKSQVEKELTVVKLQLD-------ETDKQKVLLDQELQRVKGEVNDAF-KQKSQVEV 2234
Cdd:pfam12128 331 HGAFLDADIE--TAAADQEQLPSWQSELENLEERLKALTGkhqdvtaKYNRRRSKIKEQNNRDIAGIKDKLaKIREARDR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2235 ELARVRIQMEELvklklkiEEENRRLMQKDKDStqklLAEEAEKMKS-LAEEAGRLS--VEAEETARQRQIAESNLAEQR 2311
Cdd:pfam12128 409 QLAVAEDDLQAL-------ESELREQLEAGKLE----FNEEEYRLKSrLGELKLRLNqaTATPELLLQLENFDERIERAR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2312 ALAEKILKEKMQAIQEATKLKA----EAEKLQKQKDQAQETAKRLQEDKQQIQQR-------LDKETEGFQKSLEAERKR 2380
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKrrdqASEALRQASRRLEERQSALDELELQLFPQagtllhfLRKEAPDWEQSIGKVISP 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2381 QL-----------EASAEAEK----LKLRVKEL----SLAQTKA-EDEAKKFKKQADEVKAQLQRTEKHTTEIVVQkLET 2440
Cdd:pfam12128 558 ELlhrtdldpevwDGSVGGELnlygVKLDLKRIdvpeWAASEEElRERLDKAEEALQSAREKQAAAEEQLVQANGE-LEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2441 QRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKE---MANAQQEQIEQQK-----------AELQQSFLTEKGLL 2506
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAErkdSANERLNSLEAQLkqldkkhqawlEEQKEQKREARTEK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2507 LKREKEVEGEKKRFEKQLEDEMKKAKALKD------EQERQRKL------------MEEERKKLQAIMDEAVRKQKEAEE 2568
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKAAIAARRSGAKaelkalETWYKRDLaslgvdpdviakLKREIRTLERKIERIAVRRQEVLR 796
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 2569 EMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL 2626
Cdd:pfam12128 797 YFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2234-2420 |
3.00e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2234 VELARVRIQMEELvKLKLKIE--EENRRLMQKDKDSTQKLLaEEAEKMK-SLAEEAGRLSvEAEETARQRQiaesnlaEQ 2310
Cdd:PRK00409 504 IEEAKKLIGEDKE-KLNELIAslEELERELEQKAEEAEALL-KEAEKLKeELEEKKEKLQ-EEEDKLLEEA-------EK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2311 RAlaEKILKEkmqAIQEATKLKAEAEKLQKQKDQAQeTAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQL-------- 2382
Cdd:PRK00409 574 EA--QQAIKE---AKKEADEIIKELRQLQKGGYASV-KAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVgdevkyls 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 2383 --------------EASAEAEKLKLRVK--ELSLAQTKAEDEAKKFKKQADEVK 2420
Cdd:PRK00409 648 lgqkgevlsipddkEAIVQAGIMKMKVPlsDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1588-1847 |
3.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1588 SAATQLQTKAmsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEiwrqkanealrlrlQAEEEA 1667
Cdd:COG3883 13 FADPQIQAKQ----KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------KLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1668 QKKSHAQEEAEKQKLEAERDAKKRGKAE------------EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKA 1735
Cdd:COG3883 75 AEAEAEIEERREELGERARALYRSGGSVsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAK----KA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1736 DfehAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLA 1815
Cdd:COG3883 151 E---LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270
....*....|....*....|....*....|..
gi 1389908282 1816 DEAARMRSVAEEAKKQRQIAEEEAARQRSEAE 1847
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4288-4319 |
3.21e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.08 E-value: 3.21e-03
10 20 30
....*....|....*....|....*....|..
gi 1389908282 4288 IAGILDTDTLEKVSVTEAIHRNLVDNITGQRL 4319
Cdd:pfam00681 8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
1602-1761 |
3.22e-03 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 43.60 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1602 EQTTKLEESLKKE--QGNVLKLQEEADK----LKKQQKEANTAREEAEQELEIWRQKaNEALRLRLQAEE--------EA 1667
Cdd:PRK11519 240 EQIRDILNSITRNylEQNIERKSEEASKslafLAQQLPEVRSRLDVAENKLNAFRQD-KDSVDLPLEAKAvldsmvniDA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1668 QKKSHAQEEAEKQKLEAerdakKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqklsAEQECIRLKADFEHAEQQRGLL 1747
Cdd:PRK11519 319 QLNELTFKEAEISKLYT-----KEHPAYRTLLEKRKALEDEKAKLNGRVTAMPK----TQQEIVRLTRDVESGQQVYMQL 389
|
170
....*....|....
gi 1389908282 1748 DNELQRLKNEVNST 1761
Cdd:PRK11519 390 LNKQQELKITEAST 403
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1355-1615 |
3.42e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.43 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1355 AQRRLEDDEKASE-KLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKqni 1433
Cdd:PRK07735 28 AKHGAEISKLEEEnREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAK--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1434 QQELQHLKSLSDQEIKSknqqlEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAER 1513
Cdd:PRK07735 105 AAALAKQKREGTEEVTE-----EEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1514 LRKQVAEEtqrkknAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQL 1593
Cdd:PRK07735 180 LAKQKAAE------AGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARA 253
|
250 260
....*....|....*....|..
gi 1389908282 1594 QTKAMSFSEQTTKLEESLKKEQ 1615
Cdd:PRK07735 254 KTKGAEGKKEEEPKQEEPSVNQ 275
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2264-2451 |
3.68e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.45 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2264 DKDSTQKLLaEEAEKMKSLAEEAGRL-SVEAEETARQRQIAESNLAEQRALAEKilkekmqAIQEATKLKAEAEKLQKQK 2342
Cdd:pfam05262 179 DKKVVEALR-EDNEKGVNFRRDMTDLkERESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2343 DQAQETAKRLQEDKQQIQQRLDKETEGFQKSlEAErKRQLEASAEAEKLKlrvKELSLAQTKAEDEAKKFKKQADEVKAQ 2422
Cdd:pfam05262 251 RQKQQEAKNLPKPADTSSPKEDKQVAENQKR-EIE-KAQIEIKKNDEEAL---KAKDHKAFDLKQESKASEKEAEDKELE 325
|
170 180
....*....|....*....|....*....
gi 1389908282 2423 LQRTEKHTTEIVVQKLETQRLQSTREADD 2451
Cdd:pfam05262 326 AQKKREPVAEDLQKTKPQVEAQPTSLNED 354
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2474-2594 |
3.72e-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: 42.00 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2474 QRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQrKLMEEERKKLQ 2553
Cdd:pfam13904 67 QRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERK-VSQEEAKEVLQ 145
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908282 2554 AIMDEAVRKQKEAEEEMKNKQREmdvldKKRLEQE-KQLAEE 2594
Cdd:pfam13904 146 EWERKKLEQQQRKREEEQREQLK-----KEEEEQErKQLAEK 182
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1490-1690 |
3.74e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1490 LQELRDRAAEAEKLRKAAQDEAERLRKQVaeetqrkknaedELKRKSDAEKEAAKQKQRALDDLQKYKmqaeEAERRMKQ 1569
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAA------------LLEAKELLLRERNQQRQEARREREELQ----REEERLVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1570 AEEekirqirvveevaqksaatQLQTKAmsfsEQTTKLEEslkkeqgnvlKLQEEADKLKKQQKEANTAREEAEQELE-- 1647
Cdd:PRK12705 89 KEE-------------------QLDARA----EKLDNLEN----------QLEEREKALSARELELEELEKQLDNELYrv 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1389908282 1648 --IWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1690
Cdd:PRK12705 136 agLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1477-1576 |
3.75e-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: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1477 EKTtahKAKSEAELQELRDRAAEAEklRKAAQDEAERLRkQVAEETQRKKNAEDE-LKRKSDAEKEAAKQKQRALDDLQK 1555
Cdd:cd03406 174 EKT---KLLIAEQHQKVVEKEAETE--RKRAVIEAEKDA-EVAKIQMQQKIMEKEaEKKISEIEDEMHLAREKARADAEY 247
|
90 100
....*....|....*....|.
gi 1389908282 1556 YKMqaeeaerrMKQAEEEKIR 1576
Cdd:cd03406 248 YRA--------LREAEANKLK 260
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2163-2602 |
4.11e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2163 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTvvklQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEV-----ELA 2237
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHerqakELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2238 RVRIQMEELvklKLKIEEENRRLMQKDkDSTQKLLaeEAEKMKSLAEEAGrlsVEAEETARQRQIAESNLAEQRALAEKI 2317
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLL--EMLQSKGLPKKSG---EEDWERTRRIAEAEMQLGHLEVLLDQK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2318 LKEKMQAiqeatklkaeAEKLQKQKDQAQETAKrlqedKQQIQQRLD-KETegfqKSLEAERK-RQLEASAEAEK----L 2391
Cdd:pfam10174 205 EKENIHL----------REELHRRNQLQPDPAK-----TKALQTVIEmKDT----KISSLERNiRDLEDEVQMLKtnglL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2392 KLRVKELSLAQTKAEDEAKKF-KKQADEVKAQLQRTEkhtTEIVV--QKLET---QRLQSTREADDLKSAIA--DLEEER 2463
Cdd:pfam10174 266 HTEDREEEIKQMEVYKSHSKFmKNKIDQLKQELSKKE---SELLAlqTKLETltnQNSDCKQHIEVLKESLTakEQRAAI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2464 KKLKKEAEELQRKSKE-MANAQQEQIE---QQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQE 2539
Cdd:pfam10174 343 LQTEVDALRLRLEEKEsFLNKKTKQLQdltEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908282 2540 RQRKLMEEERKKLQAI--MDEAVRKQKEAEEEMKnKQREMDvlDKKRLEQEKQLAEENKKLREQL 2602
Cdd:pfam10174 423 RVKSLQTDSSNTDTALttLEEALSEKERIIERLK-EQRERE--DRERLEELESLKKENKDLKEKV 484
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2273-2539 |
4.13e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2273 AEEAEKMKslAEEAgRLSVEAEEtARQRQIAESNLAEQRALAEKILKEKMQAIQEA-----TKLKAEAEKLQKQKDQAQE 2347
Cdd:PRK05035 440 AIEQEKKK--AEEA-KARFEARQ-ARLEREKAAREARHKKAAEARAAKDKDAVAAAlarvkAKKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2348 TAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTE 2427
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2428 KHTTEIVVQKLETqrlqstrEADDLKSAIAdleeerkkLKKEAEELQRKSKEMANAQQEQIEQQKAELQ------QSFLT 2501
Cdd:PRK05035 596 QQAASAEPEEQVA-------EVDPKKAAVA--------AAIARAKAKKAEQQANAEPEEPVDPRKAAVAaaiaraKARKA 660
|
250 260 270
....*....|....*....|....*....|....*...
gi 1389908282 2502 EKGLLLKREKEVEGEKKrfeKQLEDEMKKAKALKDEQE 2539
Cdd:PRK05035 661 AQQQANAEPEEAEDPKK---AAVAAAIARAKAKKAAQQ 695
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2055-2437 |
4.16e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 43.13 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2055 KEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKaekeaallrqKAEEAEKQKKAAENEAAKQ 2134
Cdd:pfam04747 52 KEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEA----------RRAEAEAKKRAAQEEEHKQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2135 AKAqndtEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDET---------- 2204
Cdd:pfam04747 122 WKA----EQERIQKEQEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSaapapepktp 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2205 DKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQmEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAE 2284
Cdd:pfam04747 198 TNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPASVE-QVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2285 EAGRLSVEAEETARQRQiAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKL---------QKQKDQAQET-AKRLQE 2354
Cdd:pfam04747 277 TPVEPVVETTPPASENQ-KKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADDNMdfldfvtakEEPKDEPAETpAAPVEE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2355 DKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV 2434
Cdd:pfam04747 356 VVENVVENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQVVETTPPASENKKKNKKDKKKSESEKA 435
|
...
gi 1389908282 2435 VQK 2437
Cdd:pfam04747 436 VEE 438
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1830-1976 |
4.22e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1830 KQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRK------------LLED 1897
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKeeqldaraekldNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1898 Q---AAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQK--KVVEEEIHIIKINFHKASKEKADLESELKKLKGIADE 1972
Cdd:PRK12705 106 QleeREKALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
....
gi 1389908282 1973 TQKS 1976
Cdd:PRK12705 186 MQRI 189
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1501-1678 |
4.33e-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: 43.07 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1501 EKLRKAAQDEAERLRkqvaEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRV 1580
Cdd:pfam05262 184 EALREDNEKGVNFRR----DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1581 VEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEE-ADKLKKQQKEANTAREEAEQELEIWRQKANEALRl 1659
Cdd:pfam05262 260 LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHkAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ- 338
|
170
....*....|....*....
gi 1389908282 1660 RLQAEEEAQKKSHAQEEAE 1678
Cdd:pfam05262 339 KTKPQVEAQPTSLNEDAID 357
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2435-2602 |
4.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2435 VQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEmANAQQEQIEQQKAELQQSFLTEKGLLLK----RE 2510
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2511 -----KEVEGEKKRfEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEavrKQKEAEEEMKNKQREMDVLDKKRL 2585
Cdd:COG1579 91 yealqKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
170
....*....|....*..
gi 1389908282 2586 EQEKQLAEENKKLREQL 2602
Cdd:COG1579 167 ELAAKIPPELLALYERI 183
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1815-2145 |
5.16e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1815 ADEAARMRSVAEEAKKQRQIAEEEAARQRSE----AEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAY 1890
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTEsvepNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1891 QR-KLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEEtlkQKKVVEEEIHIIKINFHKASKEKADLESElkklkgi 1969
Cdd:pfam02029 84 ERqKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR---LGRYKEEETEIREKEYQENKWSTEVRQAE------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1970 aDETQKSKLKAEEEAEKLKklaaeeerrRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEK 2049
Cdd:pfam02029 154 -EEGEEEEDKSEEAEEVPT---------ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2050 QVVLAKEAAQKCTAAEQKAQDVLSKNKEDVL--AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAA 2127
Cdd:pfam02029 224 KRRQGGLSQSQEREEEAEVFLEAEQKLEELRrrRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQE 303
|
330
....*....|....*...
gi 1389908282 2128 EneaaKQAKAQNDTEKQR 2145
Cdd:pfam02029 304 E----AERKLREEEEKRR 317
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2275-2428 |
5.17e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2275 EAEKMKSLAE---EAGRLSVEAEETARQrQIAESN--LAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQK------D 2343
Cdd:COG2268 187 DALGRRKIAEiirDARIAEAEAERETEI-AIAQANreAEEAELEQEREIETARIAEAEAELAKKKAEERREAEtaraeaE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2344 QA---QETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQ---LEASAEAEKLKLRVKEL-----SLAQTKAEDEAKKF 2412
Cdd:COG2268 266 AAyeiAEANAEREVQRQLEIAEREREIELQEKEAEREEAELeadVRKPAEAEKQAAEAEAEaeaeaIRAKGLAEAEGKRA 345
|
170
....*....|....*.
gi 1389908282 2413 KKQADEVKAQLQRTEK 2428
Cdd:COG2268 346 LAEAWNKLGDAAILLM 361
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1018-1517 |
5.22e-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: 43.18 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1018 TVTRLRQPVDKEPLKACALKtSEQKKVQSELEG-LKRDLTCVSEKTEEV----LMSPQQSSSAPLLRSELD-LTLKKMeq 1091
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLE-ALLKAMKSECQGqMERQMAAIQGKNESLekvsSLTAQLESTKEMLRKVVEeLTAKKM-- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1092 vyglssvyldklktvdvvirntadaeeTLKNYEARLRDVS-KVPSEQKEVEKHRSQMKSMRSEAEADQVMFDRLQ---DD 1167
Cdd:pfam15921 490 ---------------------------TLESSERTVSDLTaSLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDH 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1168 LRKATTVHDKMTRIHSERDADLEHYRQlvngllerwqavfaQIELRLRELDLLGRhmnsyrdsyewlirwlTEARQRQEK 1247
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQ--------------QIENMTQLVGQHGR----------------TAGAMQVEK 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1248 IQavpisdsraLREQLTDEKKLLGEIEKNKDKIDDCHKNAKAyidSVKDYEFQILTYKALQDPIASPLKKPKMEcaSDDI 1327
Cdd:pfam15921 593 AQ---------LEKEINDRRLELQEFKILKDKKDAKIRELEA---RVSDLELEKVKLVNAGSERLRAVKDIKQE--RDQL 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1328 IQEYVNLRtrySELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQM--AEAHAKSVAKAEQ-- 1403
Cdd:pfam15921 659 LNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMegSDGHAMKVAMGMQkq 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1404 --------EALELKMKMKEEAskrqdvAADAEKQKQNIQQELQHLkslsdqeikskNQQLEDALVSRRKIEEEIHIIRIQ 1475
Cdd:pfam15921 736 itakrgqiDALQSKIQFLEEA------MTNANKEKHFLKEEKNKL-----------SQELSTVATEKNKMAGELEVLRSQ 798
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1389908282 1476 LEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQ 1517
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4010-4041 |
5.45e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.45e-03
10 20 30
....*....|....*....|....*....|..
gi 1389908282 4010 KLVSAERAVTGYKDPYSGKVISLFQAMKKGLI 4041
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1078-1555 |
5.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1078 LRSELDLTLKKMEQVYGLSSVYLDKLKTVDVVIRNTADAEETLKNYEARLRDV-SKVPSEQKEVEKHRS-QMKSMRSEAE 1155
Cdd:PRK01156 209 DEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAeSDLSMELEKNNYYKElEERHMKIIND 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1156 ADQVMFDRLQDDLRKATTVHDKmTRIHSERDADLEHYRQLVNGL---------LERWQAVFAQIELRLRELDLLGRHMNS 1226
Cdd:PRK01156 289 PVYKNRNYINDYFKYKNDIENK-KQILSNIDAEINKYHAIIKKLsvlqkdyndYIKKKSRYDDLNNQILELEGYEMDYNS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1227 YRDSYEWLIRWLTEARQRQEKIQAvPISDSRALREQLTDE-KKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYK 1305
Cdd:PRK01156 368 YLKSIESLKKKIEEYSKNIERMSA-FISEILKIQEIDPDAiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNM 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1306 A-LQDPIASPLKKPKM-ECASDDIIQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEK--ASEKLKE--EERRKMAE 1379
Cdd:PRK01156 447 EmLNGQSVCPVCGTTLgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEylESEEINKsiNEYNKIES 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1380 IQAEL----DKQKQMAEAHAKSVAKAEQ------EALELK-------------------MKMKEEASKRQDvaaDAEKQK 1430
Cdd:PRK01156 527 ARADLedikIKINELKDKHDKYEEIKNRykslklEDLDSKrtswlnalavislidietnRSRSNEIKKQLN---DLESRL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1431 QNIQQELQHLKSLSDQEIKSKNQQLeDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEA---------- 1500
Cdd:PRK01156 604 QEIEIGFPDDKSYIDKSIREIENEA-NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEItsrindiedn 682
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908282 1501 -EKLRKAAQD-EAERLRKQVAEETQRKKNAEDElKRKSDAEK--EAAKQKQRALDDLQK 1555
Cdd:PRK01156 683 lKKSRKALDDaKANRARLESTIEILRTRINELS-DRINDINEtlESMKKIKKAIGDLKR 740
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1628-1757 |
6.16e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.71 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1628 LKKQQKEANTAREEAEQELeiwrQKANEALrlrlqaEEEAQKKSHAQEEAEKQKLEAERDAK-------KRGKAEEAALK 1700
Cdd:PRK07352 48 LEERREAILQALKEAEERL----RQAAQAL------AEAQQKLAQAQQEAERIRADAKARAEairaeieKQAIEDMARLK 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908282 1701 QKENAEKELDKQRKFAE---QIAQQKLS-AEQEcirLKADFEHAEQQRgLLDNELQRLKNE 1757
Cdd:PRK07352 118 QTAAADLSAEQERVIAQlrrEAAELAIAkAESQ---LPGRLDEDAQQR-LIDRSIANLGGN 174
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2510-2577 |
6.20e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 6.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908282 2510 EKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKK----LQAIMDEAVRKQKEAEEEMKNKQREM 2577
Cdd:pfam03938 21 QAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEkeqeLQKKEQELQQLQQKAQQELQKKQQEL 92
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2242-2345 |
6.41e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 41.90 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2242 QMEElVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQI--AESNLAEQRALAE---- 2315
Cdd:cd03406 170 AMEA-EKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEieDEMHLAREKARADaeyy 248
|
90 100 110
....*....|....*....|....*....|
gi 1389908282 2316 KILKEKmqaiqEATKLKAEAEKLQKQKDQA 2345
Cdd:cd03406 249 RALREA-----EANKLKLTPEYLELKKYQA 273
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1589-1721 |
6.91e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1589 AATQLQTKAMSFSEQTTKLEESLKKeqgnvlkLQEEADKLKKQQKEANTAR-EEAEQELEIWRQKANEalrlrLQAEEEA 1667
Cdd:COG0542 398 AAARVRMEIDSKPEELDELERRLEQ-------LEIEKEALKKEQDEASFERlAELRDELAELEEELEA-----LKARWEA 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1389908282 1668 QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1721
Cdd:COG0542 466 EKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAE 519
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1762-1914 |
7.04e-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: 42.30 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1762 EKQRKQLEDELNKVRSEMD-SLLQMKINAEKASMVNTEKSKQLLESEALKMK-QLADEAA-RMRSVAEEAKKQRQIAEEE 1838
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDlKERESQEDAKRAQQLKEELDKKQIDADKAQQKaDFAQDNAdKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1839 AARQRSEAEKILKEKLAAINEATRLKTE--AEMALKAKEAENERLKRQAEEeayQRKLLEDQAAQHKQDIEEKITQLQ 1914
Cdd:pfam05262 264 ADTSSPKEDKQVAENQKREIEKAQIEIKknDEEALKAKDHKAFDLKQESKA---SEKEAEDKELEAQKKREPVAEDLQ 338
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1376-1555 |
7.32e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1376 KMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmkmkEEASKRQDVAADAEKQKQNIQQELQHLKSLsdqeIKSKNQQL 1455
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALE----ARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1456 EDALVSRrkieeeihiIRIQLEKttahkakseaELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRK 1535
Cdd:COG1579 83 GNVRNNK---------EYEALQK----------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
170 180
....*....|....*....|
gi 1389908282 1536 SDAEKEAAKQKQRALDDLQK 1555
Cdd:COG1579 144 KAELDEELAELEAELEELEA 163
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2211-2443 |
7.92e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2211 LDQELQRVKGEVNDAFKQKSQVEVELARVRIQ-----MEELVKLkLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEE 2285
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEELDLDEAEEKNEeiqerIDQLYDI-LEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2286 AGRLS----VEAEETARQRQIaESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQI-- 2359
Cdd:PRK04778 333 IDRVKqsytLNESELESVRQL-EKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLrk 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 2360 -QQRLDKETEGFQKSLEaERKRQLEASA-----EAEKLKLRVKELSLAQTKAEDEAKKF-----KKQADEVKAQLQRTEK 2428
Cdd:PRK04778 412 dELEAREKLERYRNKLH-EIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEELEEKPInmeavNRLLEEATEDVETLEE 490
|
250
....*....|....*
gi 1389908282 2429 HTTEIVVQKLETQRL 2443
Cdd:PRK04778 491 ETEELVENATLTEQL 505
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
1845-1984 |
8.12e-03 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 42.35 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1845 EAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKrqaeeeayqrkllEDQAAQHKQDIEEKITQLQTSSDSELGRQ 1924
Cdd:TIGR00422 721 EAEKAFELLKEIIVSIRNLKAESNIPPNAPLKVLLIYT-------------EAETAERLKLNAVDIKGAINFSEVEVVIE 787
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1925 KNIVEETLkQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGiadETQKSKLKAEEEA 1984
Cdd:TIGR00422 788 KPEVTEAV-VELVPGFEIIIPVKGLINKAKELARLQKQLDKEKK---EVIRIEGKLENEG 843
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1627-1891 |
8.38e-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: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1627 KLKKQQKEANTAREEAEQEL----EIWRQKANEALRLRLQAE--EEAQKKSHA-----QEEAEKQKLEAERDAKKRGKAE 1695
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLrknlTVEPVKGSNVIEISYTSPdpELAAAVANAlaeayLEQNLELRREEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1696 EAALKQK-ENAEKELDKQRK---------FAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1765
Cdd:COG3206 184 LPELRKElEEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1766 --KQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLEsealkmKQLADEAARmrsVAEEAKKQRQIAEEEAARQR 1843
Cdd:COG3206 264 viQQLRAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALR------AQLQQEAQR---ILASLEAELEALQAREASLQ 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1844 SEAEKiLKEKLAAINEatrlkteaemalkaKEAENERLKRQAE--EEAYQ 1891
Cdd:COG3206 334 AQLAQ-LEARLAELPE--------------LEAELRRLEREVEvaRELYE 368
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1410-1892 |
8.92e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1410 MKMKEEASKRqdvAADAEKQKQNIQQE----LQHLKSLSDQEIKSKNQQLEDALVSRRkieeeIHIIRIQLEKTTAHKAK 1485
Cdd:pfam05622 6 QEEKDELAQR---CHELDQQVSLLQEEknslQQENKKLQERLDQLESGDDSGTPGGKK-----YLLLQKQLEQLQEENFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1486 SEAELQELRDRAAEAEKLRKAAQDEAERLRKqVAEETQRKKNAEDELKRKSDAekeaakqkqralddLQKYKMQAEEAER 1565
Cdd:pfam05622 78 LETARDDYRIKCEELEKEVLELQHRNEELTS-LAEEAQALKDEMDILRESSDK--------------VKKLEATVETYKK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1566 RMKQAEEEKiRQIRVVEEvaqksaatqlqtKAMSFSEQTTKLEESLKKeqGNVLKLQEEAdkLKKQQKEANTAREEAEQE 1645
Cdd:pfam05622 143 KLEDLGDLR-RQVKLLEE------------RNAEYMQRTLQLEEELKK--ANALRGQLET--YKRQVQELHGKLSEESKK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1646 LEIWRQKANealrlRLQAEEEAQKKshaqeeaEKQKLEAERDAKKRGKAE----EAALKQKENAEKELDKQRKFAEQIAQ 1721
Cdd:pfam05622 206 ADKLEFEYK-----KLEEKLEALQK-------EKERLIIERDTLRETNEElrcaQLQQAELSQADALLSPSSDPGDNLAA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1722 QKLSAE--QECIRLKADFEH-AEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTE 1798
Cdd:pfam05622 274 EIMPAEirEKLIRLQHENKMlRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGS 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1799 KSkqllESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKIlkeklaaineatrlkTEAEMALKAKEAE 1877
Cdd:pfam05622 354 KA----EDSSLLKQKLEEHLEKLHEAQSElQKKKEQIEELEPKQDSNLAQKI---------------DELQEALRKKDED 414
|
490
....*....|....*
gi 1389908282 1878 NerlkrQAEEEAYQR 1892
Cdd:pfam05622 415 M-----KAMEERYKK 424
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4431-4468 |
9.01e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 9.01e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1389908282 4431 QKLRDVSAYSKYLTCPKTKLKISYKDAMERSMTEEGTG 4468
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1475-1555 |
9.20e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.60 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1475 QLEKTTAHKAKSEAELQELRdraAEAEKLRKAAQDEAERLRKQVAEETQRKKNAedelkRKSDAEKEAAKQKQRALDDLQ 1554
Cdd:PRK07353 51 RLAEAEKLEAQYEQQLASAR---KQAQAVIAEAEAEADKLAAEALAEAQAEAQA-----SKEKARREIEQQKQAALAQLE 122
|
.
gi 1389908282 1555 K 1555
Cdd:PRK07353 123 Q 123
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
40-145 |
9.61e-03 |
|
second calponin homology (CH) domain found in beta-parvin; 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. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-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: 409187 Cd Length: 130 Bit Score: 39.57 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 40 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKHRQVKLV 115
Cdd:cd21338 21 VVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQDGGLKKP 100
|
90 100 110
....*....|....*....|....*....|
gi 1389908282 116 NIRNDDIADGNPKLTLGLIWTIILHFQISD 145
Cdd:cd21338 101 KARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1681-1916 |
9.80e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1681 KLEAERDAKKRGKAEEAALKQkenaekeLDKQRKFAEQIAQQKLSAEQEcirlkadfEHAEQQRGLLDNELQRLKNEVns 1760
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRR-------LEVERKRREQEEQRRLQQEQL--------ERAEKMREELELEQQRRFEEI-- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1761 teKQRKQ-LEDElnkvrsemdsllqmkinaekasmvntekskQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEA 1839
Cdd:pfam15709 390 --RLRKQrLEEE------------------------------RQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQR 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1840 ARQRSEAEKILKEKLAAINEATRLKTE----AEMAlKAKEAENERLKRQAEE----EAYQRKLLEDQAAQHKQDIEEKIT 1911
Cdd:pfam15709 438 KKQQEEAERAEAEKQRQKELEMQLAEEqkrlMEMA-EEERLEYQRQKQEAEEkarlEAEERRQKEEEAARLALEEAMKQA 516
|
....*
gi 1389908282 1912 QLQTS 1916
Cdd:pfam15709 517 QEQAR 521
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1629-1908 |
9.96e-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: 41.72 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1629 KKQQKEANTAREEAEQELEIwrqkanealrLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQ---KENA 1705
Cdd:pfam15905 63 KKSQKNLKESKDQKELEKEI----------RALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAsleKQLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1706 E----KELDKQrKFAEQIAQQKLSAeqecirlkadfehaeqqrglLDNELQRLKNEVNSTEK----QRKQLEDELNKVRS 1777
Cdd:pfam15905 133 EltrvNELLKA-KFSEDGTQKKMSS--------------------LSMELMKLRNKLEAKMKevmaKQEGMEGKLQVTQK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908282 1778 EMDSlLQMKINAEKASMVNTEKSKQlleSEALKMKQLADEAARMRSVAEEAKKQR---QIAEEEAARQRSEAEKILKEKL 1854
Cdd:pfam15905 192 NLEH-SKGKVAQLEEKLVSTEKEKI---EEKSETEKLLEYITELSCVSEQVEKYKldiAQLEELLKEKNDEIESLKQSLE 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908282 1855 AAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRK----LLEDQAAQHKQDIEE 1908
Cdd:pfam15905 268 EKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNaeleELKEKLTLEEQEHQK 325
|
|
| |
