|
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 ... |
53-157 |
1.18e-74 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 244.23 E-value: 1.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 53 DRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 132
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1207141782 133 RNDDIADGNPKLTLGLIWTIILHFQ 157
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
50-168 |
4.82e-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: 239.93 E-value: 4.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 50 DERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 129
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141782 130 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 168
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
170-275 |
2.34e-71 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 234.92 E-value: 2.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 170 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1207141782 250 PEDVDVPHPDEKSIITYVSSMYDVMP 275
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
49-166 |
2.59e-69 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 229.87 E-value: 2.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 128
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141782 129 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 166
Cdd:cd21236 91 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
171-275 |
7.18e-66 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.80 E-value: 7.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 250
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1207141782 251 EDVDVPHPDEKSIITYVSSMYDVMP 275
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
50-167 |
1.46e-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: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 50 DERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 129
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141782 130 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 167
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
171-275 |
9.36e-59 |
|
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: 198.67 E-value: 9.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 250
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1207141782 251 EDVDVPHPDEKSIITYVSSMYDVMP 275
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
169-275 |
6.31e-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: 6.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 169 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLL 248
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1207141782 249 DPEDVDVPHPDEKSIITYVSSMYDVMP 275
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
55-158 |
1.97e-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: 174.88 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 55 VQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 133
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1207141782 134 NDDIADGNPKLTLGLIWTIILHFQI 158
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 ... |
49-154 |
1.58e-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: 172.55 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQV 127
Cdd:cd21246 10 ADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRV 89
|
90 100
....*....|....*....|....*..
gi 1207141782 128 KLVNIRNDDIADGNPKLTLGLIWTIIL 154
Cdd:cd21246 90 HLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
171-271 |
7.45e-48 |
|
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: 167.59 E-value: 7.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 250
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1207141782 251 EDVDVPHPDEKSIITYVSSMY 271
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
171-271 |
6.66e-46 |
|
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: 161.79 E-value: 6.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 250
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141782 251 EDVDVPHPDEKSIITYVSSMY 271
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
51-158 |
2.82e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.54 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 51 ERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 126
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1207141782 127 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 158
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
49-154 |
5.86e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 156.69 E-value: 5.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLkHRQV 127
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 1207141782 128 KLVNIRNDDIADGNPKLTLGLIWTIIL 154
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
49-271 |
1.72e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 170.89 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHR 125
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 126 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGRL 204
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 205 FNAIIHKHRPNLIDINKVYRQTNLE--NLEQAFSIAERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 271
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
49-154 |
5.23e-43 |
|
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: 155.18 E-value: 5.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQV 127
Cdd:cd21318 32 ADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRV 111
|
90 100
....*....|....*....|....*..
gi 1207141782 128 KLVNIRNDDIADGNPKLTLGLIWTIIL 154
Cdd:cd21318 112 HLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
49-154 |
7.49e-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: 151.36 E-value: 7.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQV 127
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKV 104
|
90 100
....*....|....*....|....*..
gi 1207141782 128 KLVNIRNDDIADGNPKLTLGLIWTIIL 154
Cdd:cd21317 105 HLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
51-158 |
5.23e-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: 148.10 E-value: 5.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 51 ERDRVQKKTFTKWVNKHLVKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 126
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1207141782 127 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 158
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
158-271 |
6.94e-40 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 145.20 E-value: 6.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 158 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 237
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141782 238 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 271
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
170-275 |
7.75e-40 |
|
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: 144.77 E-value: 7.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 170 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1207141782 250 PEDVDVPHPDEKSIITYVSSMYDVMP 275
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
171-271 |
2.16e-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: 143.61 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 250
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1207141782 251 EDVDVPHPDEKSIITYVSSMY 271
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
917-994 |
1.95e-38 |
|
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: 139.66 E-value: 1.95e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 917 LSWQYLMRDITLINSWNFIMFKTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRS 994
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
55-156 |
2.35e-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: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 55 VQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 132
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1207141782 133 RNDDIADGNPKLTLGLIWTIILHF 156
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
53-154 |
3.37e-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: 139.83 E-value: 3.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 53 DRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 131
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1207141782 132 IRNDDIADGNPKLTLGLIWTIIL 154
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
170-271 |
3.91e-38 |
|
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: 140.00 E-value: 3.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 170 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1207141782 250 PEDVDVPHPDEKSIITYVSSMY 271
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
51-158 |
4.69e-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: 139.58 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 51 ERDRVQKKTFTKWVNKHLVKAQ--RHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 128
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1207141782 129 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 158
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
167-271 |
7.70e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.42 E-value: 7.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 167 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 246
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1207141782 247 LLDPEDVDVPHPDEKSIITYVSSMY 271
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
174-275 |
7.75e-37 |
|
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: 136.02 E-value: 7.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 174 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 252
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141782 253 VDVPHPDEKSIITYVSSMYDVMP 275
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
155-271 |
4.95e-36 |
|
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: 134.80 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 155 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQA 234
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141782 235 FSIAERDLGVTRLLDPEDVDVPHPDEKSIITYVSSMY 271
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
50-158 |
7.69e-36 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 133.51 E-value: 7.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 50 DERDRVQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 128
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1207141782 129 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 158
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1800-2645 |
2.54e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.91 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1800 QQKSKAEKETmsnTEKSKQLLESEAAKMRELAEEATKLRSV---AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 1876
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1877 TRLKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--------KIGQLKKSSDTELDRQKKIVEETL 1948
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1949 KQ----RKVVEEEIHILKLNFEKASSGKQELELELKKlkgiADETQKSKAkaeeeaekFRKLALEEEKKRKEAEAKVKQI 2024
Cdd:PTZ00121 1237 KDaeeaKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKADE--------LKKAEEKKKADEAKKAEEKKKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2025 QAAEEEAARQHKAAQeevgrLMKLAEEAKKQKEIAEKEAEkqvilvqEAAQKCSAAEQKAQnvlvqqnkdsmaqdKLKEE 2104
Cdd:PTZ00121 1305 DEAKKKAEEAKKADE-----AKKKAEEAKKKADAAKKKAE-------EAKKAAEAAKAEAE--------------AAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2105 FEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEasrraeaeaaalKLKQE 2184
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK------------------ADEAKKKAEED------------KKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2185 ADSEMAKYKKLAEKtLKQKSSVEEELVKVKVQLDETDKQKsvldvELKRLKQEVSDA--IKQKAQVEDELSKVKIQMEDL 2262
Cdd:PTZ00121 1409 ELKKAAAAKKKADE-AKKKAEEKKKADEAKKKAEEAKKAD-----EAKKKAEEAKKAeeAKKKAEEAKKADEAKKKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2263 LKLklkiekenQELMKKDKDNTKKlleeeAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2342
Cdd:PTZ00121 1483 KKA--------DEAKKKAEEAKKK-----ADEAKKAAEAKKK----ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2343 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQE--------TEGFQKSLEAERKRQLEITAEAEKLKVKVTQL 2414
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2415 SdaqsKAEEEAKK---FKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEkeklkkeAADL 2491
Cdd:PTZ00121 1626 K----KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-------AEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2492 QKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2571
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEK------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 2572 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEE 2645
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAniiEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
171-271 |
3.95e-35 |
|
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: 131.37 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 250
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141782 251 EDVDVPHPDEKSIITYVSSMY 271
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1639-2431 |
9.90e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 147.98 E-value: 9.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1639 EEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQ- 1717
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEi 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1718 -KEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEEELIKVRKEME 1796
Cdd:PTZ00121 1157 aRKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA--EAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1797 ILLQQKSKAEKETMSNTEKSKQLLESEAAKM--RELAEEATKLRSvAEEAKKQRQIAEEEAARQRAEAEKI--LKEKLTA 1872
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFarRQAAIKAEEARK-ADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1873 INEATRLKTEAEIALKEKEAendrLKRKAEEEGYQ---RKVLEDQAAQHKQAIEEKigqlKKSSDTELDRQKKIVEETLK 1949
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADA----AKKKAEEAKKAaeaAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1950 QRKVVEEEIHILKlnfeKASSGKQElelelkklkgiADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEE 2029
Cdd:PTZ00121 1386 KAEEKKKADEAKK----KAEEDKKK-----------ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2030 EAARQHKAAQEevgrLMKLAEEAKKQKEIAEKEAEKQVilVQEAAQKCSAAEQKAQNVlvqqnKDSMAQDKLKEEFEKAK 2109
Cdd:PTZ00121 1451 KKAEEAKKAEE----AKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEA-----KKAAEAKKKADEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2110 KlAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEM 2189
Cdd:PTZ00121 1520 E-AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2190 AKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVldvelKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKI 2269
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2270 EKENQELMKKDKDNTKK--LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKL 2347
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2348 KAEAEKLQKQKDQAQVEAQKLLEAKKE-MQQRLDQETE---------------GFQKSLEAERKRQLEITAEAEKLKVKV 2411
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEEDEkrrmevdkkikdifdNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
810 820
....*....|....*....|
gi 1207141782 2412 TQLSDAQSKAEEEAKKFKKQ 2431
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKH 1852
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
49-154 |
2.36e-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: 130.93 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQV 127
Cdd:cd21316 47 ADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRV 126
|
90 100
....*....|....*....|....*..
gi 1207141782 128 KLVNIRNDDIADGNPKLTLGLIWTIIL 154
Cdd:cd21316 127 HLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
54-159 |
9.70e-33 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 124.87 E-value: 9.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 54 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 130
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILHFQIS 159
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
158-271 |
1.88e-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: 123.79 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 158 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 237
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141782 238 AERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 271
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
170-268 |
2.05e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 123.30 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 170 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1207141782 250 PEDVDVPHPDEKSIITYVS 268
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
174-276 |
4.11e-32 |
|
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: 122.73 E-value: 4.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 174 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLDPE 251
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1207141782 252 DVDVPHPDEKSIITYVSSMYDVMPR 276
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
55-158 |
1.46e-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: 120.88 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 55 VQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 133
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1207141782 134 NDDIADGNPKLTLGLIWTIILHFQI 158
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1379-2255 |
1.61e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 137.58 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1379 QDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQE 1458
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1459 LKTLSEQEIKAKSQQVEEAllsrtRIEEEIHiirlqlettmkqkntaetELLQLRaKAVDADKLRNAaqEEAEKLRKqvA 1538
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAA-----RKAEEVR------------------KAEELR-KAEDARKAEAA--RKAEEERK--A 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1539 EETqkkRKAEEELKRKSEAEkdaakekkkaledLEKFKLQAEEAERHLKQAELEKQRQIQ--VVEEVAKKTAATQLESKQ 1616
Cdd:PTZ00121 1215 EEA---RKAEDAKKAEAVKK-------------AEEAKKDAEEAKKAEEERNNEEIRKFEeaRMAHFARRQAAIKAEEAR 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1617 VALTAR-LEESLKNEQVMVIQLQEEAEHLKKQQAEADKArEQAEKELETWRQKANEALRlrlqAEEEANKKtaaqeeaek 1695
Cdd:PTZ00121 1279 KADELKkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKK----KAEEAKKA--------- 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1696 qKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEEtAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVN 1775
Cdd:PTZ00121 1345 -AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEEDKKKA----DELKKAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1776 SAVKQKKELEEelikVRKEMEIllqqKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlrsvAEEAKKQRQIAEE-E 1854
Cdd:PTZ00121 1419 KADEAKKKAEE----KKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAKKKAEEAKKaD 1486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1855 AARQRAEAEKILKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--KIGQLKKS 1932
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADElkKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1933 SDTELDRQKKIVEETLKQ--------RKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKaeeeaekfR 2004
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--------K 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2005 KLALEEEKKRKEAEAKVKQIQAAEEE----AARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCS 2078
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2079 AAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEkaKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAE 2158
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2159 KLRKEAEKEASRRAEAEAAAlklkQEADSEMAKYKKLAEKTlkQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLK 2235
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDNFANI----IEGGKEGNLVINDSKEM--EDSAIKEVADSKNMQLEEADafeKHKFNKNNENGEDG 1864
|
890 900
....*....|....*....|
gi 1207141782 2236 QEVSDAIKQKAQVEDELSKV 2255
Cdd:PTZ00121 1865 NKEADFNKEKDLKEDDEEEI 1884
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
170-268 |
1.69e-31 |
|
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: 121.09 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 170 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1207141782 250 PEDVDVPHPDEKSIITYVS 268
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1348-1924 |
3.40e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.45 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1348 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANE 1426
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1427 LKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKsQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1506
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1507 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledLEKFKLQAEEAERHL 1586
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER------------------LEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1587 KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1666
Cdd:COG1196 434 EEEEEEEEEALE--EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1667 QKANEALR------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM----AEETA 1736
Cdd:COG1196 512 AALLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIraraALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1737 KQKLAAEQELIRLRADFEHAEQQRTVLDDEL---QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnT 1813
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----R 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1814 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1893
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
570 580 590
....*....|....*....|....*....|.
gi 1207141782 1894 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1924
Cdd:COG1196 748 LEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
55-158 |
5.41e-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: 119.31 E-value: 5.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 55 VQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 132
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1207141782 133 RNDDIADGNPKLTLGLIWTIILHFQI 158
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
174-275 |
7.24e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 118.91 E-value: 7.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 174 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 252
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141782 253 VDVPHPDEKSIITYVSSMYDVMP 275
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
176-271 |
1.74e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 117.83 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 176 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 254
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1207141782 255 VPHPDEKSIITYVSSMY 271
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
51-160 |
2.35e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.68 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 51 ERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 126
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1207141782 127 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 160
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
54-156 |
9.95e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 115.66 E-value: 9.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 54 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 130
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILHF 156
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1397-2599 |
2.22e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 129.95 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1397 AEMQAELEkqkqlAETHAKAIAKAEQEANEL-------KTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKA 1469
Cdd:NF041483 111 AEHQARLQ-----AELHTEAVQRRQQLDQELaerrqtvESHVNENVAWAEQLRARTESQA---RRLLDESRAEAEQALAA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1470 KSQQVEeallsrtRIEEEIHIiRLQLETtmkQKNTAETELLQLRAKAvDADKLRNAAQEEA-------EKLRKQVAEETQ 1542
Cdd:NF041483 183 ARAEAE-------RLAEEARQ-RLGSEA---ESARAEAEAILRRARK-DAERLLNAASTQAqeatdhaEQLRSSTAAESD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1543 KKRKAEEELKRKSEAekdaakekkkaledlekfklQAEEAERHLKQAELEKQRqiqVVEEvAKKTAATQLESKQVALTAR 1622
Cdd:NF041483 251 QARRQAAELSRAAEQ--------------------RMQEAEEALREARAEAEK---VVAE-AKEAAAKQLASAESANEQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1623 LEESLKNEQVMVIQLQEEAEHLKkqqAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKR 1702
Cdd:NF041483 307 TRTAKEEIARLVGEATKEAEALK---AEAEQALADARAEAEKLVAEAAEKAR-TVAAEDTAAQLAKAARTAEEVLTKASE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1703 EAKK--RAKAEEAALKQKEAaEMELGNQRKMAEETAKQ-KLAA--------------EQELIRLRADfehAEQQRTVLDD 1765
Cdd:NF041483 383 DAKAttRAAAEEAERIRREA-EAEADRLRGEAADQAEQlKGAAkddtkeyraktvelQEEARRLRGE---AEQLRAEAVA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1766 ELQRLKNDV-NSAVKQKKE----LEEELIKVRKEMEILLQQ-KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRS 1839
Cdd:NF041483 459 EGERIRGEArREAVQQIEEaartAEELLTKAKADADELRSTaTAESERVRTEAIERATTLRRQAEETLERTRAEAERLRA 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1840 VAEE-AKKQRQIAEEEAARQRAEAEK-ILKEKLTAINEATRLKTEAE-------IALKEKEAENDRLKRKAEEEGYQrkv 1910
Cdd:NF041483 539 EAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEerltaaeEALADARAEAERIRREAAEETER--- 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1911 LEDQAAqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHIlKLNFEKASSGKQelelelkklkgIADETQ 1990
Cdd:NF041483 616 LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAV-RLRSEAAAEAER-----------LKSEAQ 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1991 KSKAkaeeeaekfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE-----------EVGRLMKLAEE--AKKQKE 2057
Cdd:NF041483 677 ESAD---------RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraeadqERERAREQSEEllASARKR 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2058 IAEKEAEKQViLVQEAAQKC----SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAAllhk 2131
Cdd:NF041483 748 VEEAQAEAQR-LVEEADRRAtelvSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEAQ---- 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2132 kaEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELv 2211
Cdd:NF041483 815 --EEADRVRS--------------DAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL- 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2212 kvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKL 2287
Cdd:NF041483 868 ----RSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDE 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2288 LEEEAENMK-KLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEA 2365
Cdd:NF041483 944 ARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEA 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2366 QKLL-EAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEK 2444
Cdd:NF041483 1018 DRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAE 1089
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2445 HTSEKHTVVEK----------------------LEVQRLQSKQEADGLH-KAIADLEKEKEKLKKEAADLQKQSKEManv 2501
Cdd:NF041483 1090 ATVEGNSLVEKartdadellvgarrdatairerAEELRDRITGEIEELHeRARRESAEQMKSAGERCDALVKAAEEQ--- 1166
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2502 QQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKlqsAMDAAIKKQ 2581
Cdd:NF041483 1167 LAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTVEEGKR---ELDVLVRRR 1243
|
1290
....*....|....*...
gi 1207141782 2582 KEAEEEMNGKQKEMQDLE 2599
Cdd:NF041483 1244 EDINAEISRVQDVLEALE 1261
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1574-2166 |
8.90e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 8.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1574 KFKLQAEEAERHLKQA------------ELEKQR---QIQVveEVAKK--TAATQLESKQVALTA----RLEESLKNEQV 1632
Cdd:COG1196 169 KYKERKEEAERKLEATeenlerledilgELERQLeplERQA--EKAERyrELKEELKELEAELLLlklrELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1633 MVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE 1712
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1713 AALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR 1792
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1793 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 1872
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1873 INEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRK-----VLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEET 1947
Cdd:COG1196 487 AEAAARLLLLLE-AEADYEGFLEGVKAALLLAGLRGLagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1948 LKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIADEtqkskakaeEEAEKFRKLALEEEKKRKEAEAKVKQIQAA 2027
Cdd:COG1196 566 LKAAK--AGRATFLPLDKIRARAALAAALARGAIGAAVDLV---------ASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2028 EEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKLKEEFEK 2107
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 2108 AKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2166
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
174-273 |
1.02e-27 |
|
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: 110.07 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 174 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED- 252
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1207141782 253 VDVPHPDEKSIITYVSSMYDV 273
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
156-271 |
3.29e-27 |
|
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: 109.40 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 156 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAF 235
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141782 236 SIAERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 271
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
54-156 |
3.32e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 108.73 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 54 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 130
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILHF 156
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1372-1991 |
4.56e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 122.94 E-value: 4.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1372 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1451
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1452 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEeihiirlqlettmkQKNTAEtellQLRAKAVDADKLRNAAQEEAE 1531
Cdd:PTZ00121 1294 EAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEE--------------AKKKAD----AAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1532 KLRKQvAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER---HLKQAELEKQRQIQVVEEVAKKTA 1608
Cdd:PTZ00121 1354 AAADE-AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkadELKKAAAAKKKADEAKKKAEEKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1609 ATQLESKqvALTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRlrlqAEEEANKKTA 1688
Cdd:PTZ00121 1433 ADEAKKK--AEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKK----KAEEAKKKAD 1500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1689 aqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlddelq 1768
Cdd:PTZ00121 1501 --------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-------- 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1769 rlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 1848
Cdd:PTZ00121 1559 --KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1849 QIAEEEA--------ARQRAEAEKILKEKLTAINEATRLKTE-----------AEIALKEKEAEN---DRLKRKAEEEgy 1906
Cdd:PTZ00121 1637 QLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEeakkaeedekkAAEALKKEAEEAkkaEELKKKEAEE-- 1714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1907 QRKVLEDQAAQHKQAIeeKIGQLKKSSDTELDRQKKIVEETLKQRKV----VEEEIHILKLNFEKASSGKQELELELKKL 1982
Cdd:PTZ00121 1715 KKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlkKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
....*....
gi 1207141782 1983 KGIADETQK 1991
Cdd:PTZ00121 1793 RMEVDKKIK 1801
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
50-158 |
1.18e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 107.54 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 50 DERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHR- 125
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTKv 94
|
90 100 110
....*....|....*....|....*....|...
gi 1207141782 126 QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 158
Cdd:cd21247 95 PVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
54-159 |
1.28e-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: 107.42 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 54 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 130
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILHFQIS 159
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1372-1956 |
2.14e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 120.63 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1372 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1451
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1452 IQRELQELKTLSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQ---- 1527
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEA---KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkka 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1528 ---EEAEKLRK----QVAEETQKK----RKAEE------ELKRKSEAEKD----AAKEKKKALEDLEKFKLQAEEAERHL 1586
Cdd:PTZ00121 1287 eekKKADEAKKaeekKKADEAKKKaeeaKKADEakkkaeEAKKKADAAKKkaeeAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1587 KQAELEKQRQIQVVEEVAKKT----AATQLESKQVALTARLEESLKNEQVmviqlQEEAEHLKKQQAE---ADKAREQAE 1659
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAeekkKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEkkkADEAKKKAE 1441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1660 --KELETWRQKANEALR---LRLQAEE-----EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR 1729
Cdd:PTZ00121 1442 eaKKADEAKKKAEEAKKaeeAKKKAEEakkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1730 KMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQrlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET 1809
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKA--EELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1810 MSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKE 1889
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 1890 KEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE----KIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 1956
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1401-1966 |
2.45e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 119.66 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1401 AELEKQ-KQLAEthaKAiAKAEQeANELKTKMKDevsKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALL 1479
Cdd:COG1196 196 GELERQlEPLER---QA-EKAER-YRELKEELKE---LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1480 SRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEK 1559
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1560 DAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQE 1639
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLE----RLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1640 EAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1719
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1720 AAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1799
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1800 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEakkqRQIAEEEAARQRAEAEKILKEKLTAINEATRL 1879
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1880 KTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIH 1959
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
....*..
gi 1207141782 1960 ILKLNFE 1966
Cdd:COG1196 737 LLEELLE 743
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
158-271 |
8.08e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 105.17 E-value: 8.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 158 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 237
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141782 238 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 271
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
176-271 |
1.06e-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: 104.16 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 176 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 254
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1207141782 255 VPHPDEKSIITYVSSMY 271
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
158-271 |
2.60e-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: 104.04 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 158 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 237
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141782 238 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 271
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1702-2388 |
1.51e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.88 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1702 REAKK----RAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1777
Cdd:COG1196 207 RQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1778 VKQKKELEEELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 1857
Cdd:COG1196 287 QAEEYELLAELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1858 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLKKSSDTEL 1937
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA-------LLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1938 DRQKKIVEETLKQRKVVEEEIHILKLnfekassgkqelelelkklkgIADETQKskakaeeeaekfRKLALEEEKKRKEA 2017
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLEL---------------------LAELLEE------------AALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2018 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEkeaEKQVILVQEAAQKCSAAEQKAQNVLvqqnkdsma 2097
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---LIGVEAAYEAALEAALAAALQNIVV--------- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2098 qdklkeefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAA 2177
Cdd:COG1196 554 --------EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2178 ALklkQEADSEMAKYkkLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2257
Cdd:COG1196 626 TL---VAARLEAALR--RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2258 QMEDLLKLKLKIEKENQELmKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEK 2337
Cdd:COG1196 701 AEEEEERELAEAEEERLEE-ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2338 K----QAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA----KKEMQQRLdQET-----EGFQK 2388
Cdd:COG1196 780 GpvnlLAIEEYEELEERYDFLSEQREDLEEARETLEEAieeiDRETRERF-LETfdavnENFQE 842
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
172-271 |
1.85e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 100.71 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 172 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 251
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1207141782 252 D-VDVPHPDEKSIITYVSSMY 271
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1532-2436 |
1.88e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.61 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1532 KLRKqvaEETQKK-RKAEEELKRkseaekdAAKEKKKALEDLEKFKLQAEEAERH--LKQAELEKQRQIQVVEEVAKKTA 1608
Cdd:TIGR02168 171 KERR---KETERKlERTRENLDR-------LEDILNELERQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1609 ATQLESKQvaltARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEA-LRLRLQAEEEANkkt 1687
Cdd:TIGR02168 241 LEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLAN--- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1688 aaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDEL 1767
Cdd:TIGR02168 314 ------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1768 QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEketmsnTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQ 1847
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ------QEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1848 RQIAEEEAARQRAEaekilkekltaINEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKVLedQAAQHKQAIEEKI 1926
Cdd:TIGR02168 456 LERLEEALEELREE-----------LEEAEQALDAAERELAQLQARLDSLERLQENlEGFSEGVK--ALLKNQSGLSGIL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1927 GQLKKSSDTELDRQKKIV---EETLKQRKVVEEEIHILKLNF-EKASSGKQELELELKKLkgiADETQKSKAKAEEEAEK 2002
Cdd:TIGR02168 523 GVLSELISVDEGYEAAIEaalGGRLQAVVVENLNAAKKAIAFlKQNELGRVTFLPLDSIK---GTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2003 FRKLALEEEKKRKEAEAK----------VKQIQAAEEEAARQH---------------------KAAQEEVGRLMKLAEE 2051
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2052 AKKQKEIAekeaekqvilvqEAAQKCSAAEQKAQNVLVQqnkdsmaQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHK 2131
Cdd:TIGR02168 680 EELEEKIE------------ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2132 KAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2211
Cdd:TIGR02168 741 EVEQLEE--------------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2212 KVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkdkdntKKLLEEE 2291
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------------------AAEIEEL 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2292 AENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA 2371
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2372 KKEMQQRLDQETEGFQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2436
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
58-155 |
2.09e-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: 100.47 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 58 KTFTKWVNKHLVKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 133
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1207141782 134 NDDIADGnPKLTLGLIWTIILH 155
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
171-271 |
2.98e-24 |
|
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: 100.19 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 250
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1207141782 251 EDV---DVphPDEKSIITYVSSMY 271
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
158-271 |
4.40e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 100.15 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 158 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 237
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141782 238 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 271
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1160-1885 |
4.42e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 112.93 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1160 EASQTQLQKLRSEAEGKQATFD----RLEEELQRATEVNKRMSQLHSERDVELEHYRQlVGNLRERWQAVFAQ----IEL 1231
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKaedaRKAEEARKAEDARKAEEARKAEDAKRVEIARK-AEDARKAEEARKAEdakkAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1232 RQRELDLlnRQMQAYRESYDwlIRWIADAKQRQDKLHAVPIggSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKfakgyid 1311
Cdd:PTZ00121 1181 ARKAEEV--RKAEELRKAED--ARKAEAARKAEEERKAEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEE------- 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1312 aIKDYELQLVTYKALVEPIASPLKKAKMESAsddiiqeyvtlrtRYSELMTLSsqyikfiiETQRRLQDEEKAAEKLKEE 1391
Cdd:PTZ00121 1248 -ERNNEEIRKFEEARMAHFARRQAAIKAEEA-------------RKADELKKA--------EEKKKADEAKKAEEKKKAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1392 ERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANElkTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQ----EI 1467
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE--AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkadAA 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1468 KAKSQQVEEALLSRTRIEEEihiirLQLETTMKQKNTAETELLQLRAKAVD---ADKLRNAAQE--EAEKLRKQvAEETQ 1542
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEED-----KKKADELKKAAAAKKKADEAKKKAEEkkkADEAKKKAEEakKADEAKKK-AEEAK 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1543 K----KRKAEE-----ELKRKSEAEKDAAKEKKKAledlEKFKLQAEEAERhlKQAELEKQRQIQVVEEVAKKTAATQLE 1613
Cdd:PTZ00121 1458 KaeeaKKKAEEakkadEAKKKAEEAKKADEAKKKA----EEAKKKADEAKK--AAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1614 SKQVAltarlEESLKNEQVMVIQLQEEAEHLKKqqAEADKAREQAEKELE---TWRQKANEALRLRLQAEEEANKKTAAQ 1690
Cdd:PTZ00121 1532 EAKKA-----DEAKKAEEKKKADELKKAEELKK--AEEKKKAEEAKKAEEdknMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1691 EEAEKQKEEAKREAKKRA----KAEE-----AALKQKEAAEMELGNQRKMAEETAKQKlaAEQELIRLRADFEHAEQQRT 1761
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAeelkKAEEekkkvEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKK 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1762 VLDDELQRLKNDVNSAVKQKKelEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVA 1841
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKK--AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141782 1842 EEAKKQRQIAEEeaarQRAEAEKILKEKLTAINEATRLKTEAEI 1885
Cdd:PTZ00121 1761 HLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
816-882 |
6.09e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 97.72 E-value: 6.09e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 816 QLKPRNpaQPIKGKLPVQAVCDFKQMEITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSICFIVP 882
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
170-276 |
6.45e-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: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 170 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY--RQTNLENLEQAFSIAERDLGVTR 246
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1207141782 247 -LLDPEDVDvpHPDEKSIITYVSSMYDVMPR 276
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
55-158 |
7.76e-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: 98.90 E-value: 7.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 55 VQKKTFTKWVNKHLVKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 130
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILHFQI 158
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
171-275 |
1.50e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.94 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 250
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1207141782 251 EDVDVPHPDEKSIITYVSSMYDVMP 275
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1821-2705 |
5.91e-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: 108.91 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1821 ESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRK 1900
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1901 AEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 1980
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1981 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2060
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2061 KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQE-AEKAKDNAEKEAALLHKKAEEAERQ 2139
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2140 kkaaeaeaakqakaqedaEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDE 2219
Cdd:pfam02463 471 ------------------EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2220 tDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLA 2299
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2300 E-EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQR 2378
Cdd:pfam02463 612 TlEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2379 LDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEV 2458
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE---EEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2459 QRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQ--EKTILQQSFFAEKETLLKKEKAIEEEKK 2536
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEeeQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2537 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQsamdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNL 2616
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQK-------LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2617 REKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGvKKDVPLAFDGIREKVPASRLHEIGVLS 2696
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERL 1000
|
....*....
gi 1207141782 2697 KKEYDKLKK 2705
Cdd:pfam02463 1001 EEEKKKLIR 1009
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
174-274 |
6.62e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 96.00 E-value: 6.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 174 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPEDV 253
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1207141782 254 DVPHPDEKSIITYVSSMYDVM 274
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1652-2511 |
1.14e-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: 107.75 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1652 DKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1731
Cdd:pfam02463 168 KRKKKEALKKL---IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1732 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNdvnsavKQKKELEEELIKVRKEMEILLQQKSKAEKETmS 1811
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE------EELKLLAKEEEELKSELLKLERRKVDDEEKL-K 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1812 NTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 1891
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1892 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSG 1971
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1972 KQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGrlmKLAEE 2051
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV---IVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2052 AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAlLHK 2131
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK-DTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2132 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2211
Cdd:pfam02463 634 LTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2212 KVKVQLDETDKQKsvLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE 2291
Cdd:pfam02463 714 KLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2292 A-ENMKKLAEEAARLNIEAQEAA---RLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQK 2367
Cdd:pfam02463 792 KeEKLKAQEEELRALEEELKEEAellEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2368 LLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE-TEKHT 2446
Cdd:pfam02463 872 LLLKEEELEE-QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEaDEKEK 950
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2447 SEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2511
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEET 1015
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1756-2619 |
1.44e-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: 107.36 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1756 AEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS-----KAEKETMSNTEKSKQL--LESEAAKMR 1828
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkEQAKKALEYYQLKEKLelEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1829 ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI-LKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 1907
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1908 RKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIAD 1987
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1988 ETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQV 2067
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2068 ILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEfEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEA 2147
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS-GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2148 AKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKL-------AEKTLKQKSSVEEELVKVKVQLDET 2220
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpilnLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2221 DKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEkenQELMKKDKDNTKKLLEEEAENMKKLAE 2300
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ---ELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2301 EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ-KLLEAKKEMQQRL 2379
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKeKELAEEREKTEKL 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2380 DQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2459
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2460 RLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLE 2539
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI------EERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2540 KQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDA-AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2618
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLmAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
.
gi 1207141782 2619 K 2619
Cdd:pfam02463 1021 E 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2094-2672 |
2.39e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 107.15 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2094 DSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAallhKKAEEAERQKKAAEAEAAKQAkaqedAEKLRK-E----AEKEA 2168
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEA----RKAEEAKKKAEDARKAEEARK-----AEDARKaEearkAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2169 SRRAEAEAAALKLKQEA-DSEMAKYKKLAEKTLKQKSSVE----EELVKVKV--------QLDETDKQKSVLDVELKRLK 2235
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEArKAEDAKKAEAARKAEEVRKAEElrkaEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2236 QEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKEN----QELMKKDK----DNTKKLLEEEAENMKKLAEEAARLNI 2307
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADElkkaEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2308 EAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQrLDQETEGFQ 2387
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2388 KSLEAERKRQlEITAEAEKLKVKvtqlSDAQSKAEEEAKKF--KKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2465
Cdd:PTZ00121 1392 KADEAKKKAE-EDKKKADELKKA----AAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2466 EadglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE--QLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFE 2543
Cdd:PTZ00121 1467 E----EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2544 DEVKKAEALKAEQERQRKlmeEERKKLQSAmdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLReklqql 2623
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKA---EEKKKAEEA-----KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK------ 1608
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1207141782 2624 qsSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGVKKD 2672
Cdd:PTZ00121 1609 --AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1348-2138 |
2.87e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 106.68 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1348 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEkqkqlaeTHAKAIAKAEQEANE 1426
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1427 LKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1506
Cdd:TIGR02168 286 LQKELYALANEISRL----EQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1507 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledlekfklqaeeAERHL 1586
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------------------------LEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1587 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1666
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1667 QKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKAEEAALKQK 1718
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKKAIAFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1719 E---AAEMELGNQRKMAEETAKQKLAAEQELIRLRAD--FEHAEQQRTVLDDELQRLK--NDVNSAVKQKKELEEELIKV 1791
Cdd:TIGR02168 569 ElgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKdlVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1792 RKEMEILLQQKS---KAEKETMSNTEKSKQLLESEaAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 1868
Cdd:TIGR02168 649 TLDGDLVRPGGVitgGSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1869 KLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEdQAAQHKQAIEEKIGQLKKssdtELDRQKKIVEETL 1948
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEA----QIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1949 KQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAAE 2028
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA--------------EIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2029 EEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEF-EK 2107
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEE 948
|
810 820 830
....*....|....*....|....*....|.
gi 1207141782 2108 AKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2138
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
54-159 |
3.23e-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: 95.15 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 54 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 130
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILHFQIS 159
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
54-159 |
4.97e-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: 94.77 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 54 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 130
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILHFQIS 159
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
171-269 |
7.47e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 93.07 E-value: 7.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY-RQTNLENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1207141782 250 PEDVDVPHPDEKSIITYVSS 269
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1574-2464 |
9.04e-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: 104.75 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1574 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKktaatQLES--KQVALTARLEEslkneqvmviqLQEEAEHLKKQQAEA 1651
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELER-----QLKSleRQAEKAERYKE-----------LKAELRELELALLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1652 DKarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELgnqrkm 1731
Cdd:TIGR02168 233 RL--EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1732 aEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtms 1811
Cdd:TIGR02168 305 -QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ--- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1812 ntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIALKEK 1890
Cdd:TIGR02168 381 --------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1891 EAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLkkssdteldrqkkiveETLKQRKVVEEEihiLKLNFEKASS 1970
Cdd:TIGR02168 453 QEELERLEEALEE-------LREELEEAEQALDAAEREL----------------AQLQARLDSLER---LQENLEGFSE 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1971 GKQELELELKKLKGIADETQKSKAKAEEEaekfrKLALEEEKKRKEAEAKVKQIQAAEEEAARQhkaAQEEVGRLMKLAE 2050
Cdd:TIGR02168 507 GVKALLKNQSGLSGILGVLSELISVDEGY-----EAAIEAALGGRLQAVVVENLNAAKKAIAFL---KQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2051 EAKKQKEIAEKEAE--KQVILVQEAAQKCSAAEQKAQ--------NVLVQQNKDSmAQDKLKEEFEKAKKLAQEAEK--- 2117
Cdd:TIGR02168 579 DSIKGTEIQGNDREilKNIEGFLGVAKDLVKFDPKLRkalsyllgGVLVVDDLDN-ALELAKKLRPGYRIVTLDGDLvrp 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2118 ----AKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedaeklRKEAEKeasrraeaeaaalKLKQEADSEMAKYK 2193
Cdd:TIGR02168 658 ggviTGGSAKTNSSILERRRE--------------------------IEELEE-------------KIEELEEKIAELEK 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2194 KLAEkTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQME------DLLKLKL 2267
Cdd:TIGR02168 699 ALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEeleerlEEAEEEL 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2268 KIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKL 2347
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2348 KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ---ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2424
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1207141782 2425 AKKFKKQ-ADEIKIRLQETEKHTSEKHTVVEKLE--VQRLQSK 2464
Cdd:TIGR02168 938 IDNLQERlSEEYSLTLEEAEALENKIEDDEEEARrrLKRLENK 980
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1415-2293 |
1.73e-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: 103.90 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1415 KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrtRIEEEIHIIRLQ 1494
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK-----EEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1495 LETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEK 1574
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE-KEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1575 FKLQAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKqqaEADKA 1654
Cdd:pfam02463 354 EEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK---EEKKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1655 REQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEE 1734
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1735 TAKQKLAAEQELIRLRADFEHAEQQR---TVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL-QQKSKAEKETM 1810
Cdd:pfam02463 508 GLKVLLALIKDGVGGRIISAHGRLGDlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgARKLRLLIPKL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1811 SNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALKEK 1890
Cdd:pfam02463 588 KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES-GLRKGVSLEEGLAEKSEVKA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1891 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIgqlKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKass 1970
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIK---KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL--- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1971 gkqelelelkKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEvgrlmKLAE 2050
Cdd:pfam02463 741 ----------LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE-----ELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2051 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA-KDNAEKEAALL 2129
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2130 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKssVEEE 2209
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE--ERNK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2210 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE 2289
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELG 1043
|
....
gi 1207141782 2290 EEAE 2293
Cdd:pfam02463 1044 GSAE 1047
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
175-273 |
4.21e-21 |
|
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: 91.26 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 175 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 253
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141782 254 DVPHPDEKSIITYVSSMYDV 273
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1348-2185 |
4.24e-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: 102.74 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1348 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1427
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1428 KTKMKDEVSK---RQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNT 1504
Cdd:pfam02463 246 LRDEQEEIESskqEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1505 AETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1584
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1585 HlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ------LQEEAEHLKKQQAEADKAREQA 1658
Cdd:pfam02463 406 E-AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelkllkDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1659 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR-AKAEEAALKQKEAAEMELGNQRKMAEETAK 1737
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1738 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND--VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEK 1815
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1816 SKQLLESEAAkMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEK-EAE 1893
Cdd:pfam02463 645 ESGLRKGVSL-EEGLAEKSEVKASLSELTKELLEIQELqEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1894 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ---LKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 1970
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKkeeKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1971 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2050
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2051 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKaqNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2130
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKE--NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2131 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEA 2185
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1373-2455 |
6.34e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.21 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1373 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLA-ETHAKAIAKAEQeANELKTKMKdevskrqdvavdsekqKHN 1451
Cdd:NF041483 251 QARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAES-ANEQRTRTA----------------KEE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1452 IQRELQELKTLSEQeIKAKSQQVeealLSRTRIEEEihiiRLQLETTMKQKN-TAETELLQLRAKAVDADKLRNAAQEEA 1530
Cdd:NF041483 314 IARLVGEATKEAEA-LKAEAEQA----LADARAEAE----KLVAEAAEKARTvAAEDTAAQLAKAARTAEEVLTKASEDA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1531 EKLRKQVAEETQK-KRKAEEELKRKSEAEKDAAKEKKKALEDLEKfklqaeeaERHLKQAEL-EKQRQIqvveevakKTA 1608
Cdd:NF041483 385 KATTRAAAEEAERiRREAEAEADRLRGEAADQAEQLKGAAKDDTK--------EYRAKTVELqEEARRL--------RGE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1609 ATQLESKQVALTARLEESLKNEQVMviQLQEEA----EHLKKQQAEADKAREQAEKELETWRQKANE-ALRLRLQAEEEA 1683
Cdd:NF041483 449 AEQLRAEAVAEGERIRGEARREAVQ--QIEEAArtaeELLTKAKADADELRSTATAESERVRTEAIErATTLRRQAEETL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1684 NkktaaqeeaekqkeeakreaKKRAKAEEaalkqkeaaemelgnQRKMAEETA-KQKLAAEQELIRLRADFEHA-EQQRT 1761
Cdd:NF041483 527 E--------------------RTRAEAER---------------LRAEAEEQAeEVRAAAERAARELREETERAiAARQA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1762 VLDDELQRLKNDVNSAVKQKkelEEELIKVRKEMEILlqqkskaEKETMSNTEKskqlLESEAA-KMRELAEEATklrsv 1840
Cdd:NF041483 572 EAAEELTRLHTEAEERLTAA---EEALADARAEAERI-------RREAAEETER----LRTEAAeRIRTLQAQAE----- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1841 aEEAKKQRQIAEEEAARQRAEAEkilkekltaiNEATRLKTEAeialkekEAENDRLKRKAEEEGyQRKVLEDQAAQHKQ 1920
Cdd:NF041483 633 -QEAERLRTEAAADASAARAEGE----------NVAVRLRSEA-------AAEAERLKSEAQESA-DRVRAEAAAAAERV 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1921 AIEEkiGQLKKSSDTELDRQKKIVEETLkqrkvveeeihilklnfekassgkqelelelkklkgiadetqkskakaeeea 2000
Cdd:NF041483 694 GTEA--AEALAAAQEEAARRRREAEETL---------------------------------------------------- 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2001 ekfrklaleeekkrkeaeakvkqiQAAEEEAARQHKAAQEEVGRLMklaeeAKKQKEIAEKEAEKQViLVQEAAQKC--- 2077
Cdd:NF041483 720 ------------------------GSARAEADQERERAREQSEELL-----ASARKRVEEAQAEAQR-LVEEADRRAtel 769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2078 -SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAallhkkAEEAERqkkaaeaeaakqakAQ 2154
Cdd:NF041483 770 vSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEA------QEEADR--------------VR 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2155 EDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELvkvkvQLDETDKQKSVLDVELKRL 2234
Cdd:NF041483 822 SDAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL-----RSDASEYAQRVRTEASDTL 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2235 KQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMK-KLAEEAARLNIEA 2309
Cdd:NF041483 887 ASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEA 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2310 Q-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEAQKLL-EAKKEMQQRLDQETEGFQ 2387
Cdd:NF041483 967 TgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEADRTLdEARKDANKRRSEAAEQAD 1040
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2388 KSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEKHTSEKHTVVEK 2455
Cdd:NF041483 1041 TLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAEATVEGNSLVEK 1100
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1572-2505 |
6.83e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.21 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1572 LEKFKLQAEE----AERHLKQAELEKQRQIQvveEVAKKTAATQLESKQVALTARLE------------ESLKNEQVM-V 1634
Cdd:NF041483 78 LRNAQIQADQlradAERELRDARAQTQRILQ---EHAEHQARLQAELHTEAVQRRQQldqelaerrqtvESHVNENVAwA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1635 IQLQEEAEH-----LKKQQAEADK----AREQAEKELETWRQK-ANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1704
Cdd:NF041483 155 EQLRARTESqarrlLDESRAEAEQalaaARAEAERLAEEARQRlGSEAESARAEAEAILRRARKDAERLLNAASTQAQEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1705 KKRAK------AEEAALKQKEAAEMELGNQRKMAE-ETAKQKLAAEQELIRLRAD---------FEHAEQQRT-VLDDEL 1767
Cdd:NF041483 235 TDHAEqlrsstAAESDQARRQAAELSRAAEQRMQEaEEALREARAEAEKVVAEAKeaaakqlasAESANEQRTrTAKEEI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1768 QRLkndVNSAVKQ----KKELEEELIKVRKEMEILLQQ-----KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATklR 1838
Cdd:NF041483 315 ARL---VGEATKEaealKAEAEQALADARAEAEKLVAEaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKATT--R 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1839 SVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAI---------------NEATRLKTEAEIALKEKEAENDRLKRKAEE 1903
Cdd:NF041483 390 AAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAEAVAEGERIRGEARR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1904 EGYQR---------------KVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQkkiVEETLkQRKVVEEEihilKLNFEKA 1968
Cdd:NF041483 470 EAVQQieeaartaeelltkaKADADELRSTATAESERVRTEAIERATTLRRQ---AEETL-ERTRAEAE----RLRAEAE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1969 SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRL-MK 2047
Cdd:NF041483 542 EQAEEVRAAAERAARELREETERAIAARQAEAA--EELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrTE 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2048 LAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEF-EKAKKLAQEAEKAKDNAEKE 2125
Cdd:NF041483 620 AAERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAVRLRSEAAAEaERLKSEAqESADRVRAEAAAAAERVGTE 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2126 AA-LLHKKAEEAERQkkaaeaeaakqakaqedaeklRKEAEKEASRRaeaeaaalklKQEADSEMAKYKKLAEKTLKQ-K 2203
Cdd:NF041483 697 AAeALAAAQEEAARR---------------------RREAEETLGSA----------RAEADQERERAREQSEELLASaR 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2204 SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQ-KAQVEDELS-----------KVKIQMEDLLKLKLKIEK 2271
Cdd:NF041483 746 KRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGlQEQAEEEIAglrsaaehaaeRTRTEAQEEADRVRSDAY 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2272 ENQELMKKDKDNTKKLLEEEAENMKKLAE--------EAARLNIEAQE-AARLRQIAESDLAKQRELAEKMLEEkkqAIQ 2342
Cdd:NF041483 826 AERERASEDANRLRREAQEETEAAKALAErtvseaiaEAERLRSDASEyAQRVRTEASDTLASAEQDAARTRAD---ARE 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2343 EAAKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLE-----ITAEAEKLKVKVTQ-LS 2415
Cdd:NF041483 903 DANRIRSDaAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEqliaeATGEAERLRAEAAEtVG 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2416 DAQSKAE---EEAKKFKKQADEikirlqETEKHTSEKHTVVEKL--EVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2490
Cdd:NF041483 983 SAQQHAErirTEAERVKAEAAA------EAERLRTEAREEADRTldEARKDANKRRSEAAEQADTLITEAAAEADQLTAK 1056
|
1050
....*....|....*
gi 1207141782 2491 LQKQSKEMANVQQEQ 2505
Cdd:NF041483 1057 AQEEALRTTTEAEAQ 1071
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1170-1883 |
1.64e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1170 RSEAEGK-QATFDRLEEELQRATEVNKRMSQLHSERDVeLEHYRQLVGNLRERwqavfaQIELRQRELDLLNRQMQAyre 1248
Cdd:COG1196 174 KEEAERKlEATEENLERLEDILGELERQLEPLERQAEK-AERYRELKEELKEL------EAELLLLKLRELEAELEE--- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1249 sydwlirwiadakqrqdklhavpiggskgLQEQLTQEKKLLEEIEKNKDKVEDcqkfakgyidaikdyelqlvtykalve 1328
Cdd:COG1196 244 -----------------------------LEAELEELEAELEELEAELAELEA--------------------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1329 piasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEErkkmAEMQAELEKQKQ 1408
Cdd:COG1196 268 ------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1409 LAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEI 1488
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1489 HIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKA 1568
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1569 LEDLEKFKLQAEEA-ERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKneqvmviQLQEEAEHLKKQ 1647
Cdd:COG1196 497 LEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE-------VAAAAIEYLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1648 QA--------EADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1719
Cdd:COG1196 570 KAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1720 AAEMELGNQRKMAEETAKQKLAAEQELIRLRAdfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1799
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL--EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1800 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI-------AEEEAARQRAEAEKILKEK--- 1869
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQRedl 807
|
730 740
....*....|....*....|.
gi 1207141782 1870 -------LTAINEATRLKTEA 1883
Cdd:COG1196 808 eearetlEEAIEEIDRETRER 828
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
171-268 |
6.03e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 87.92 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 250
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90
....*....|....*....
gi 1207141782 251 ED-VDVPHPDEKSIITYVS 268
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLC 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2099-2647 |
1.07e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.09 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2099 DKLKEEFEKAKK---LAQEAEKAK--------DNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKE 2167
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2168 ASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ 2247
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2248 VEDELSKVKIQMEDLLKLKLKIEKENQELMkKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQR 2327
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEAL-RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2328 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDqetegfqksLEAERKRQLEITAEAEKL 2407
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---------LLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2408 KVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEAdglhKAIADLEKEKEKLKKE 2487
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG----RATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2488 AADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEER 2567
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2568 KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEEL 2647
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1155-1969 |
1.35e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 97.73 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1155 NEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQavfAQIELRQR 1234
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ---ELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1235 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1314
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1315 dyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDE-----------EK 1383
Cdd:pfam02463 332 --KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElelkseeekeaQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1384 AAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvavdSEKQKHNIQRELQELKTLS 1463
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-----ELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1464 EQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR-KQVAEETQ 1542
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAtADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1543 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTAR 1622
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1623 LEESLKNEQVMV---------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKktaaqEEA 1693
Cdd:pfam02463 645 ESGLRKGVSLEEglaeksevkASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLK-----LEA 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1694 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1773
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1774 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN-------------TEKSKQLLESEAAKMRELAEEATKLRSV 1840
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELalelkeeqkleklAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1841 AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaEEEGYQRKVLEDQAAQHKQ 1920
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE--ELLLEEADEKEKEENNKEE 957
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1207141782 1921 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 1969
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1373-2260 |
2.33e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.20 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1373 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK---------QKQLAETHAKAIAKAEQEANELKTKMKDEVSK------ 1437
Cdd:NF041483 313 EIARLVGEATKEAEALKAEAEQALADARAEAEKlvaeaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKAttraaa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1438 ------RQDVAVDSEK---QKHNIQRELQELKTLSEQEIKAKSQQV-EEALLSRTRIEE-------EIHIIRLQLETTMK 1500
Cdd:NF041483 393 eeaeriRREAEAEADRlrgEAADQAEQLKGAAKDDTKEYRAKTVELqEEARRLRGEAEQlraeavaEGERIRGEARREAV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1501 QK-----NTAEtELLQlRAKAvDADKLRNAAQEEAEKLRKQVAEE-TQKKRKAEEELKRKSEAEKDAAKEKKKALedlEK 1574
Cdd:NF041483 473 QQieeaaRTAE-ELLT-KAKA-DADELRSTATAESERVRTEAIERaTTLRRQAEETLERTRAEAERLRAEAEEQA---EE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1575 FKLQAEEAERHLKQaELEK---QRQIQVVEEVAKK--TAATQLESKQVALT-ARLE-ESLKNEQVmviqlqEEAEHLKKQ 1647
Cdd:NF041483 547 VRAAAERAARELRE-ETERaiaARQAEAAEELTRLhtEAEERLTAAEEALAdARAEaERIRREAA------EETERLRTE 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1648 QAEADKA-REQAEKELETWRQKA------------NEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR------- 1707
Cdd:NF041483 620 AAERIRTlQAQAEQEAERLRTEAaadasaaraegeNVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvgteaae 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1708 --AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELI---RLRADFEHAEQQRTVldDELQRLKNDVNSAVKQ-- 1780
Cdd:NF041483 700 alAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQRLV--EEADRRATELVSAAEQta 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1781 ----------KKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLESEAAKMRELA-EEATKLRSVA-EEAKKQR 1848
Cdd:NF041483 778 qqvrdsvaglQEQAEEEIAGLRSAAE-------HAAERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAK 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1849 QIAEEEAARQRAEAEKILKEkltAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGyqRKVLEDQAAQHKQAIEEKIGQ 1928
Cdd:NF041483 851 ALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDA--NRIRSDAAAQADRLIGEATSE 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1929 LKKSSDTELDRQKKIVEETLKQRKvveeeihilKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLAl 2008
Cdd:NF041483 926 AERLTAEARAEAERLRDEARAEAE---------RVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEA- 995
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2009 eeekkrkeaeakvKQIQA-AEEEAARQHKAAQEEVGRLMKLAEE--AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQ 2085
Cdd:NF041483 996 -------------ERVKAeAAAEAERLRTEAREEADRTLDEARKdaNKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2086 NVLV--QQNKDSMAQDKLKEefekAKKLAQEA--------EKAKDNAE-------KEAALLHKKAEEAeRQKKAAEAEAA 2148
Cdd:NF041483 1063 RTTTeaEAQADTMVGAARKE----AERIVAEAtvegnslvEKARTDADellvgarRDATAIRERAEEL-RDRITGEIEEL 1137
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2149 KQAKAQEDAEKLRKEAEK-------EASRRAEAEAAALKLKQEADSEMAKYK----KLAEKTLKQKSSVEEELVKvkvql 2217
Cdd:NF041483 1138 HERARRESAEQMKSAGERcdalvkaAEEQLAEAEAKAKELVSDANSEASKVRiaavKKAEGLLKEAEQKKAELVR----- 1212
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*..
gi 1207141782 2218 dETDKQKSVLDVELKRL----KQEVSDAIKQKAQVEDELSKVKIQME 2260
Cdd:NF041483 1213 -EAEKIKAEAEAEAKRTveegKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
171-271 |
2.59e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 85.86 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 250
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1207141782 251 EDVDV--PHPDEKSIITYVSSMY 271
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
56-156 |
3.58e-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: 85.71 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 56 QKKTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 131
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1207141782 132 IRNDDIADGNPKLTLGLIWTIILHF 156
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
171-267 |
3.99e-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: 85.67 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 250
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90
....*....|....*...
gi 1207141782 251 ED-VDVPHPDEKSIITYV 267
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYL 97
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
167-274 |
4.72e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 85.38 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 167 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 246
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1207141782 247 LLDPEDV-DVPHPDEKSIITYVSSMYDVM 274
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
174-270 |
5.24e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.06 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 174 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN----LENLEQAFSIAERDLGVTRLLD 249
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1207141782 250 PEDVDVPHPDEKSIITYVSSM 270
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1156-1801 |
1.43e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 94.35 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1156 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRE 1235
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1236 LDLLNRQMQAYRE----SYDWLIRWIADAKQRQDKLHAVPIggsKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYID 1311
Cdd:TIGR02168 395 IASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAEL---KELQAELEELEEELEELQEELERLEEALEELREELE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1312 ----AIKDYELQLVTYKALV--------------EPIASPLKKAKMESASDDIIQEYVTLRTRYS------------ELM 1361
Cdd:TIGR02168 472 eaeqALDAAERELAQLQARLdslerlqenlegfsEGVKALLKNQSGLSGILGVLSELISVDEGYEaaieaalggrlqAVV 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1362 TLSSQYIKFIIETQRRlQDEEKAA-----EKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAE--------------- 1421
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQ-NELGRVTflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdd 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1422 -QEANELKTKMK----------DEVSKRQDVAVDSEKQKHNIQ------RELQELKTLSEQEIKAKSQQVEEALLSRTRI 1484
Cdd:TIGR02168 631 lDNALELAKKLRpgyrivtldgDLVRPGGVITGGSAKTNSSILerrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1485 EEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE 1564
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1565 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT--------ARLEESLKNEQVMVIQ 1636
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelsediESLAAEIEELEELIEE 870
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1637 LQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTaaqeeaekQKEEAKREAKKRAKAEEAALK 1716
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR--------EKLAQLELRLEGLEVRIDNLQ 942
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1717 QK--EAAEMELGNQRKMAEETAKQKLAAEQELIRLR--------------ADFEHAEQQRtvldDELQRLKNDVNSAVKQ 1780
Cdd:TIGR02168 943 ERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEnkikelgpvnlaaiEEYEELKERY----DFLTAQKEDLTEAKET 1018
|
730 740
....*....|....*....|.
gi 1207141782 1781 kkeLEEELIKVRKEMEILLQQ 1801
Cdd:TIGR02168 1019 ---LEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1537-2411 |
1.74e-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: 93.98 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1537 VAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-QAELEKQRQIQVVEEvaKKTAATQLESK 1615
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAlLKEKREYEGYELLKE--KEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1616 QVALtARLEESLKneqvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRLRLQAEEEANKKTAAQEEAEK 1695
Cdd:TIGR02169 243 ERQL-ASLEEELE-------KLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1696 QKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1775
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1776 SAVKQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATklrSVAEEAKKQRQIAEEEA 1855
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEEL----ADLNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1856 ArQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ--------------AAQHKQA 1921
Cdd:TIGR02169 462 A-DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtvaqlgsvGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1922 IEEKIGQLKKS--SDTELDRQKKIveETLKQRKVveEEIHILKLNfEKASSGKQELELELKKLKGIA-------DETQKS 1992
Cdd:TIGR02169 541 IEVAAGNRLNNvvVEDDAVAKEAI--ELLKRRKA--GRATFLPLN-KMRDERRDLSILSEDGVIGFAvdlvefdPKYEPA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1993 KAKAEEEAEKFRKLALEEEKKRK-----------EAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEK 2061
Cdd:TIGR02169 616 FKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2062 EAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkk 2141
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE--- 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2142 aaeaeaakqakaqeDAEKLRKEAEKEASRraeaeaaalklkqEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETD 2221
Cdd:TIGR02169 773 --------------DLHKLEEALNDLEAR-------------LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2222 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnMKKLAEE 2301
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ-LRELERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2302 AARLNIEAQEA-ARLRQIAESDLAKQRELAEkmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-------LEAKK 2373
Cdd:TIGR02169 905 IEELEAQIEKKrKRLSELKAKLEALEEELSE--IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALepvnmlaIQEYE 982
|
890 900 910
....*....|....*....|....*....|....*...
gi 1207141782 2374 EMQQRLDqETEGFQKSLEAERKRQLEITAEAEKLKVKV 2411
Cdd:TIGR02169 983 EVLKRLD-ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
57-154 |
1.60e-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: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 57 KKTFTKWVNKHL-VKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 132
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1207141782 133 RNDDI-ADGNPKLTLGLIWTIIL 154
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
175-273 |
4.07e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.92 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 175 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 253
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141782 254 DVPHPDEKSIITYVSSMYDV 273
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1813-2476 |
4.48e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1813 TEKSKQL--LESEAAKmrelAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLtainEATRLKTEAEIALKEK 1890
Cdd:COG1196 196 GELERQLepLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1891 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKigqlkkssdtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 1970
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1971 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2050
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2051 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2130
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2131 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEEL 2210
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2211 vkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVkIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2290
Cdd:COG1196 578 -----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV-LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2291 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLE 2370
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2371 AKKEMQQRLDQETEGFqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSK-------AEEEAkkfkkqaDEIKIRLQEte 2443
Cdd:COG1196 732 AEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEY-------EELEERYDF-- 799
|
650 660 670
....*....|....*....|....*....|...
gi 1207141782 2444 khtsekhtvvekLEVQRLQSKQEADGLHKAIAD 2476
Cdd:COG1196 800 ------------LSEQREDLEEARETLEEAIEE 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1702-2622 |
5.02e-17 |
|
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: 89.35 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1702 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFEHAE-----QQRTVLDDELQRLKNDVNS 1776
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELElallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1777 AVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1856
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1857 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEgyqrkvleDQAAQHKQAIEEKIGQLKKssdtE 1936
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRS----K 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1937 LDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELElelkklkgiadetqkskakaeeeaekfRKLALEEEKKRKE 2016
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---------------------------KKLEEAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2017 AEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSM 2096
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2097 AQDKLKEEFEKAKKLAQEAEKA-----------KDNAEKEAALLHKKAEE-----------AERQKKAAEAEAAKQAKAQ 2154
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNELgrvtflpldsiKGTEIQGNDREILKNIEGF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2155 EDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKqkSSVEEELVKVK-VQLDETDKQKSVL---DVE 2230
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRI--VTLDGDLVRPGgVITGGSAKTNSSIlerRRE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2231 LKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ 2310
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2311 EAARLRQIAESDLAKQRElaekmleEKKQAIQEAAKLKAEAEKLQKQKDQ---AQVEAQKLLEAKKEMQQRLDQETEGFQ 2387
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEE-------ELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2388 KSLEAERKRQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQR 2460
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2461 LQSKQEADGLHKAIADlekekeklkkeaadlqkqskemANVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklek 2540
Cdd:TIGR02168 911 SELRRELEELREKLAQ----------------------LELRLEGLEVRIDNLQERLSEEYSLTLEE------------- 955
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2541 qFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2620
Cdd:TIGR02168 956 -AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
..
gi 1207141782 2621 QQ 2622
Cdd:TIGR02168 1035 KD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1344-2124 |
5.65e-17 |
|
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: 89.35 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1344 DDIIQEyvtLRTRYSELMTLSSQYIKFiietqRRLQDEEKAAE-----KLKEEERKKMAEMQAELEKQKQLAETHAKAIA 1418
Cdd:TIGR02168 192 EDILNE---LERQLKSLERQAEKAERY-----KELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1419 KAEQEANELKTKMKdEVSKRQDVavdsekqkhnIQRELQELKtlseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETT 1498
Cdd:TIGR02168 264 ELEEKLEELRLEVS-ELEEEIEE----------LQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1499 MKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKekkkaleDLEKFKLQ 1578
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL-------QIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1579 AEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1658
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1659 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKA 1710
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1711 EEAALKQKE---AAEMELGNQRKMAEETAKQKLAAEQELIRLRADF--EHAEQQRTVLDDELQRLK--NDVNSAVKQKKE 1783
Cdd:TIGR02168 561 AIAFLKQNElgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRKALSYLLGGVLvvDDLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1784 LEEE---------------------------LIKVRKEMEILLQQKSKAEketmSNTEKSKQLLESEAAKMRELAEEATK 1836
Cdd:TIGR02168 641 LRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELE----EKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1837 LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA 1916
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1917 QHKQAIEE----------------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 1980
Cdd:TIGR02168 797 ELKALREAldelraeltllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1981 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEA-ARQHKAAQEEVGRLMKLAEEAKKQKEIA 2059
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 2060 EKEAEKQVILVQEAAQKCSAAEQKAQNvLVQQNKDSMAQ-DKLKEEFEKAKKLAQEAEKAKDNAEK 2124
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKE-LGPVNLAAIEEyEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1141-1956 |
7.16e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.96 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1141 KYENQLREVnKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRE 1220
Cdd:TIGR02168 217 ELKAELREL-ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1221 RWQAVFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLhavpiggskglQEQLTQEKKLLEEIEKNkdkVE 1300
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDEL-----------AEELAELEEKLEELKEE---LE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1301 DCQKFAKGYIDAIKDYELQLVTykalvepiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQyIKFIIETQRRLQD 1380
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEE------------LEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1381 EEKAAEKLKEEERkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQELK 1460
Cdd:TIGR02168 422 EIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1461 TLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETeLLQLRAKAV-----DADKLRNAAQEEAEKLRK 1535
Cdd:TIGR02168 496 RL-QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA-ALGGRLQAVvvenlNAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1536 QVAEETQKKrkaEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA--------------ERHLKQAELEKQRQIQVVE 1601
Cdd:TIGR02168 574 TFLPLDSIK---GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddlDNALELAKKLRPGYRIVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1602 E---VAKKTAATQLESKQVALT-------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1671
Cdd:TIGR02168 651 DgdlVRPGGVITGGSAKTNSSIlerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1672 A----LRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE---AALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1744
Cdd:TIGR02168 731 LrkdlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1745 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA 1824
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1825 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALkeKEAENDRLKRKAEEE 1904
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--EEAEALENKIEDDEE 968
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 1905 GYQRKVledqaAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 1956
Cdd:TIGR02168 969 EARRRL-----KRLENKIKE-LGPVNLAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1709-2646 |
1.58e-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: 87.54 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1709 KAEEAALK-QKEAAEMELGNQRKMAEETAKQ-KLAAEQELirlradFEHAEQQRTVL---DDELQRLKNDVNSAVKQKKE 1783
Cdd:pfam01576 16 KVKERQQKaESELKELEKKHQQLCEEKNALQeQLQAETEL------CAEAEEMRARLaarKQELEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1784 LEEELIKVRKEMeillQQKSKAEKETMSNTEKSKQLLESEA----AKMRELAEEATKLRSVAEEAKKQRQIAEE---EAA 1856
Cdd:pfam01576 90 RSQQLQNEKKKM----QQHIQDLEEQLDEEEAARQKLQLEKvtteAKIKKLEEDILLLEDQNSKLSKERKLLEErisEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1857 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEA---ENDRLKRKAEEEGYQrkvLEDQAAQHKQAIEEKIGQLKKSS 1933
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTD---LQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1934 DTELDRQKKIVEETLK----QRKVVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQkskakaeeeaekfrklALE 2009
Cdd:pfam01576 243 EELQAALARLEEETAQknnaLKKIRELEAQISELQ-EDLESERAARNKAEKQRRDLGEELE----------------ALK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2010 eekkrkeaeakvkqiqaAEEEAARQHKAAQEEVgrlmklaeEAKKQKEIAEkeaekqvilvqeaAQKCSAAEQKAQNVLV 2089
Cdd:pfam01576 306 -----------------TELEDTLDTTAAQQEL--------RSKREQEVTE-------------LKKALEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2090 QQ--NKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK-------AEEAERQKKAAEAEAAKQAKAQEDAEKL 2160
Cdd:pfam01576 348 QEmrQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2161 RKEAEKEASRRAEAEAAALKLKQEADSEmakykklAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD 2240
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGK-------NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2241 AIKQ-------KAQVEDELSKVKIQMEDLLKLKLKIEKENQEL------MKKDKDNTKKLLEEEAENMKKLAEEAARLNI 2307
Cdd:pfam01576 501 LQEQleeeeeaKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkkrLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2308 EAQEAA----RLRQIAeSDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQV----EAQKLLEAKKEM---- 2375
Cdd:pfam01576 581 ELDDLLvdldHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALslarALEEALEAKEELertn 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2376 -QQRLD---------------QETEGFQKSLEA---ERKRQLE------ITAEAEKLKVKVT----------QLSDAQSK 2420
Cdd:pfam01576 660 kQLRAEmedlvsskddvgknvHELERSKRALEQqveEMKTQLEeledelQATEDAKLRLEVNmqalkaqferDLQARDEQ 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2421 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2500
Cdd:pfam01576 740 GEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2501 VQQEQLQQEKTILQQSFFAEKETL-----LKKEKAIEEEKKKLEKQFEDEVKKAEALK-AEQERQRKL------MEEERK 2568
Cdd:pfam01576 820 SRDEILAQSKESEKKLKNLEAELLqlqedLAASERARRQAQQERDELADEIASGASGKsALQDEKRRLeariaqLEEELE 899
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2569 KLQSAMDAAIKKQKEAEE-------EMNGKQKEMQDLEKKRIEQEKllaeENKNLREKLQQLQSSQKASYTKEIEIQTDK 2641
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLqveqlttELAAERSTSQKSESARQQLER----QNKELKAKLQEMEGTVKSKFKSSIAALEAK 975
|
....*
gi 1207141782 2642 VPEEE 2646
Cdd:pfam01576 976 IAQLE 980
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
173-271 |
3.70e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 77.34 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 173 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 252
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1207141782 253 -VDVPHPDEKSIITYVSSMY 271
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
53-152 |
7.74e-16 |
|
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: 76.42 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 53 DRVQKKTFTKWVNKHLVKAQ-RHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 127
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1207141782 128 KLVNIRNDDIADGNPKLTLGLIWTI 152
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
173-272 |
9.88e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.77 E-value: 9.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 173 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 252
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1207141782 253 VDV--PHPDEKSIITYVSSMYD 272
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
640-830 |
1.43e-15 |
|
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: 78.64 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 640 QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAF 719
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 720 TAALQTQWSWILQLCCCIETHLKENTAYFQFFSDVKEAEDRMKKMEDTMKKKYVCDrsiTVTRLEDLLQDAVEEKEQLNE 799
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1207141782 800 FKTHLEGLNRRAKTIIQLKPRNPAQPIKGKL 830
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
171-268 |
3.14e-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: 74.34 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1207141782 250 PEDVDVPHPDEKSIITYVS 268
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1638-2611 |
3.61e-15 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 83.34 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1638 QEEAEHLKKQQAEADKAREQAEK----------ELETWRQKANEALR------------LRLQAEEEANKKTAAQEEAEK 1695
Cdd:NF041483 11 RADDDHLSRFEAEMDRLKTEREKavqhaedlgyQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1696 QKEEAKREAKKRAK------AEEAALKQKE----------AAEMELGNQRKMAEETAKQKLA--------AEQELIRL-- 1749
Cdd:NF041483 91 DAERELRDARAQTQrilqehAEHQARLQAElhteavqrrqQLDQELAERRQTVESHVNENVAwaeqlrarTESQARRLld 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1750 --RADFEH------AEQQRtVLDDELQRLKNDVNSAvkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTE--KSKQL 1819
Cdd:NF041483 171 esRAEAEQalaaarAEAER-LAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDHAEqlRSSTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1820 LESEAAKMR----------ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE-------KILKEKLT-----AINEAT 1877
Cdd:NF041483 247 AESDQARRQaaelsraaeqRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1878 RLKTEAEIALKEKEAENDRLKRKAEEEGyQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEE 1957
Cdd:NF041483 327 ALKAEAEQALADARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1958 IHilKLNFEKASSGKQelelelkkLKGIA-DETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQA-AEEEAARQ- 2034
Cdd:NF041483 406 AD--RLRGEAADQAEQ--------LKGAAkDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGeARREAVQQi 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2035 HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLvqqnkdsmaqDKLKEEFEKAKKLAQE 2114
Cdd:NF041483 476 EEAARTAEELLTKAKADADELRSTATAESER---VRTEAIERATTLRRQAEETL----------ERTRAEAERLRAEAEE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2115 -AEKAKDNAEKEAALLHkkaEEAERqkkaaeAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAaalklkqEADSEMAKYK 2193
Cdd:NF041483 543 qAEEVRAAAERAARELR---EETER------AIAARQAEAAEELTRLHTEAEERLTAAEEALA-------DARAEAERIR 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2194 K-LAEKTLKQKSSVEEELVKVKVQLDEtdkqksvldvELKRLKQEVSdAIKQKAQVEDELSKVKIQMEdllklklkIEKE 2272
Cdd:NF041483 607 ReAAEETERLRTEAAERIRTLQAQAEQ----------EAERLRTEAA-ADASAARAEGENVAVRLRSE--------AAAE 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2273 NQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEkmlEEKKQAIQEAAKLKAEA 2351
Cdd:NF041483 668 AERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2352 eklQKQKDQAQVEAQKLLE------------AKKEMQQRLD----------QETEGFQKSLE--AERKRQlEITAEAEKL 2407
Cdd:NF041483 745 ---RKRVEEAQAEAQRLVEeadrratelvsaAEQTAQQVRDsvaglqeqaeEEIAGLRSAAEhaAERTRT-EAQEEADRV 820
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2408 KvkvtqlSDAQS---KAEEEAKKFKKQADEikirlqETE--KHTSEKhTVVEKL-EVQRLQSkQEADGLHKAIADLEKEK 2481
Cdd:NF041483 821 R------SDAYAereRASEDANRLRREAQE------ETEaaKALAER-TVSEAIaEAERLRS-DASEYAQRVRTEASDTL 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2482 EKLKKEAADLQKQSKEMANvqqeqlqqektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2561
Cdd:NF041483 887 ASAEQDAARTRADAREDAN------------RIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRAD 954
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2562 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQkemQDLEKKRIEQEKLLAE 2611
Cdd:NF041483 955 AAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2015-2575 |
4.16e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2015 KEAEAKVKQIQAAEEEAARQHKAAQEEVGRLmkLAEEAKKQKEIAEKEAEKQVilvqeaaqkcsaAEQKAQNVLVQQNKD 2094
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEA--QAEEYELLAELARLEQDIAR------------LEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2095 SMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEA 2174
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2175 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSK 2254
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2255 VKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKL------AEEAARLNIEAQEAARLRQIAESDLAKQRE 2328
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2329 LAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-----LEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAE 2403
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2404 AEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETekhtsekhtvvEKLEVQRLQSKQEADGLHKAIADLEKEKEK 2483
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE-----------LEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2484 LKKEAADLQKQSKEMANVQQEQLQQEKTILQQsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-------------- 2549
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELL----EEEELLEEEALEELPEPPDLEELERELERLereiealgpvnlla 786
|
570 580 590
....*....|....*....|....*....|...
gi 1207141782 2550 -EALKAEQER------QRKLMEEERKKLQSAMD 2575
Cdd:COG1196 787 iEEYEELEERydflseQREDLEEARETLEEAIE 819
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1135-1801 |
4.73e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1135 AEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkrmsqlhserdvELEHYRQL 1214
Cdd:COG1196 251 LEAELEELEAELAEL------EAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1215 VGNLRERwqavfaQIELRQRELDLLNRQMQAYREsydwLIRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK 1294
Cdd:COG1196 311 RRELEER------LEELEEELAELEEELEELEEE----LEELEEELEEAEEELEE--------AEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1295 NKDKVEdcqkfakgyidaikdyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRyselmtlssqyikfIIET 1374
Cdd:COG1196 373 ELAEAE----------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--------------LEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1375 QRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDvavdsEKQKHNIQR 1454
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----AAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1455 ELQELKTLSEQEIKAKSQQVEEALLSRTrieeeihiIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1534
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA--------VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1535 KQVAEEtqkkRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1614
Cdd:COG1196 570 KAGRAT----FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1615 KQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1694
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1695 KQKEEAKREAKKRAKAEEAALKQKEAAEMELgnQRKMAEETAKQKLA-AEQELIRL-----RADFEHAEQQRTVldDELQ 1768
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEEL--PEPPDLEELERELErLEREIEALgpvnlLAIEEYEELEERY--DFLS 801
|
650 660 670
....*....|....*....|....*....|...
gi 1207141782 1769 RLKNDVNSAvkqKKELEEELIKVRKEMEILLQQ 1801
Cdd:COG1196 802 EQREDLEEA---RETLEEAIEEIDRETRERFLE 831
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
173-276 |
6.56e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 73.54 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 173 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 252
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1207141782 253 VDV--PHPDEKSIITYVSSMYDVMPR 276
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4065-4103 |
8.00e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.82 E-value: 8.00e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 4065 LLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEMNGIL 4103
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1403-2338 |
8.76e-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: 82.02 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1403 LEKQKQLAETHAKAIAKAEQEANELKT------KMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSE--QEIKAKSQQV 1474
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQykekacEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKeiEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1475 EEALLSRTRIEEEIHIIRLQLETTMKQ--KNTAE--TELLQLRAKAV-DADKLRNAAQEEAEKLRKQVAEETQKKRKAEE 1549
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKvfQGTDEqlNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1550 ELKRKSEAEKDAAKEKKKALEDLEKFKLQAE--------EAERHLKQA-ELEKQRQIQVVEEVAKKTA--ATQLESKQVA 1618
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFhTLVIERQEDEAKTAAQLCAdlQSKERLKQEQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1619 LT------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEAdkarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEE 1692
Cdd:TIGR00606 428 ADeirdekKGLGRTIELKKEILEKKQEELKFVIKELQQL----EGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1693 AEKQKEEAKREAKKRAKAEEAALKQKEA---AEMELGNQRKMA--EETAKQKLAAEQELIRLRADFEHAEQqrtvLDDEL 1767
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQLNHHTttrTQMEMLTKDKMDkdEQIRKIKSRHSDELTSLLGYFPNKKQ----LEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1768 QRLKNDvnsavkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLES--EAAKMRELAEEATKLRSVAEEAK 1845
Cdd:TIGR00606 580 HSKSKE-------INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1846 KQRQIAEEEAARQRAEAEKILKEKLTAINEATR-LKTEAEIALKEKEAENDRLKRKAEEEGyqrkvLEDQAAQHKQAIEE 1924
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDLQSKLRLAPDKLKS-----TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1925 KIGqLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2004
Cdd:TIGR00606 728 MLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVER 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2005 KLA-LEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQK 2083
Cdd:TIGR00606 807 KIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE---LKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2084 AQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEaerqkkaaeaeaakqakaqedaeklRKE 2163
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS-------------------------NKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2164 AEKEASRRAEaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2243
Cdd:TIGR00606 939 AQDKVNDIKE------KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2244 QKAQVEDELSKVKIQMEdllklklkIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAArlNIEAQEAARLRQIAESDl 2323
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENE--------LKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID--LIKRNHVLALGRQKGYE- 1081
|
970
....*....|....*
gi 1207141782 2324 aKQRELAEKMLEEKK 2338
Cdd:TIGR00606 1082 -KEIKHFKKELREPQ 1095
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
173-271 |
8.78e-15 |
|
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: 73.58 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 173 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 252
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1207141782 253 -VDVPHPDEKSIITYVSSMY 271
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
176-271 |
1.06e-14 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 73.16 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 176 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDPED-VD 254
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1207141782 255 VPHPDEKSIITYVSSMY 271
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
56-156 |
1.07e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 72.72 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 56 QKKTFTKWVNKHLVK--AQRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 127
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1207141782 128 KLVNIRNDDIADGNPKLTLGLIWTIILHF 156
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2100-2635 |
1.99e-14 |
|
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: 80.54 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2100 KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaal 2179
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK--------------DLTFLLEESRDKAN---------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2180 KLKQEADSEMAKYKKLAEKtlkqKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQM 2259
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEK----KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2260 EDLLKLKLKIEKENQELMKKDKDNtkklLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQREL---AEKMLEE 2336
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQR----LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIlaeDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2337 KKQAIQEAAKLKAEAEKL-----QKQKDQAQVEAQklLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKV 2411
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllqAREKEIHDLEIQ--LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2412 TQLSDAQS-------KAEEEAKKFKKQADEIKIR---LQETEKH-TSEKHTVVEKLEVQRLQ-------SKQEADGLHKA 2473
Cdd:pfam05483 502 KELTQEASdmtlelkKHQEDIINCKKQEERMLKQienLEEKEMNlRDELESVREEFIQKGDEvkckldkSEENARSIEYE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2474 IADLEKEKEKLKKEAADLQKQSkEMANVQQEQLQQEKTILQQSFFAEKETLLK---KEKAIEEEKKKLEKQFEDEVKKAE 2550
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQI-ENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQ 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2551 ALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKN---LREKLQQLQSSQ 2627
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSA 740
|
....*...
gi 1207141782 2628 KASYTKEI 2635
Cdd:pfam05483 741 KAALEIEL 748
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1373-2468 |
2.46e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 80.60 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1373 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKaEQEANELKTKMKDEVSKRQDVAVDSEKQKHNI 1452
Cdd:pfam01576 23 KAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR-KQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1453 QRELQELKT-LSEQEIKAKSQQVEEALLSRT--RIEEEIHIIRLQLETTMKQKNTAE-------TELLQLRAKAVDADKL 1522
Cdd:pfam01576 102 QQHIQDLEEqLDEEEAARQKLQLEKVTTEAKikKLEEDILLLEDQNSKLSKERKLLEeriseftSNLAEEEEKAKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1523 RNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKkkaledLEKFKLQAEEAERHLKQAELEKQR-QIQVVE 1601
Cdd:pfam01576 182 KNKHEAMISDLEERLKKE-EKGRQELEKAKRKLEGESTDLQEQ------IAELQAQIAELRAQLAKKEEELQAaLARLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1602 EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-------LQEEAEHLKKQ----------QAEADKAREQAEKELEt 1664
Cdd:pfam01576 255 ETAQKNNALKKIRELEAQISELQEDLESERAARNKaekqrrdLGEELEALKTEledtldttaaQQELRSKREQEVTELK- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1665 wRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE--AAEMELGNQRKMAEETAKQKLaa 1742
Cdd:pfam01576 334 -KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAelQAELRTLQQAKQDSEHKRKKL-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1743 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLles 1822
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNL--- 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1823 eAAKMRELAEEATKLRSVAEEAKKQRQIAEEE---AARQRAEAEKILKEKLTAINEATRLKTEAEialKEKEAENDRLKR 1899
Cdd:pfam01576 488 -STRLRQLEDERNSLQEQLEEEEEAKRNVERQlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ---RELEALTQQLEE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1900 KAEEegYQRkvLEDQAAQHKQAIEEKIgqlkkssdTELDRQKKIVEETLKQRKVVEEeihilKLNFEKASSGKqelelel 1979
Cdd:pfam01576 564 KAAA--YDK--LEKTKNRLQQELDDLL--------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISAR------- 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1980 kklkgIADETQKSKAKAEEEAEKFRKLAleeekkrkeaeAKVKQIQAAEEEAARQHKAAQEEVGRLM-------KLAEEA 2052
Cdd:pfam01576 620 -----YAEERDRAEAEAREKETRALSLA-----------RALEEALEAKEELERTNKQLRAEMEDLVsskddvgKNVHEL 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2053 KKQKEIAEKEAEKQVILVQEAAQKCSAAEQ------------KAQNVLVQQNKDSMAQDKLKEEFEKAKKLaqEAEKAKD 2120
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATEDaklrlevnmqalKAQFERDLQARDEQGEEKRRQLVKQVREL--EAELEDE 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2121 NAEKEAALLHKKAEEAErqkkaaeaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTL 2200
Cdd:pfam01576 762 RKQRAQAVAAKKKLELD---------LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESE 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2201 KQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkd 2280
Cdd:pfam01576 833 KKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQL------------------ 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2281 kdntKKLLEEEAENMKKLAEEAARLNIEAqEAARLRQIAESDLAKQRELAEKMLEEKKQAIQeaAKLkAEAEKLQKQKDQ 2360
Cdd:pfam01576 895 ----EEELEEEQSNTELLNDRLRKSTLQV-EQLTTELAAERSTSQKSESARQQLERQNKELK--AKL-QEMEGTVKSKFK 966
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2361 AQVEAqklLEAK-KEMQQRLDQETEGFQKSLEAERKRQleitaeaEKLKVKVTQLSDAQSKAEEeakkFKKQADEIKIRL 2439
Cdd:pfam01576 967 SSIAA---LEAKiAQLEEQLEQESRERQAANKLVRRTE-------KKLKEVLLQVEDERRHADQ----YKDQAEKGNSRM 1032
|
1130 1140
....*....|....*....|....*....
gi 1207141782 2440 QETEKHTSEKHTVVEKLEVQRLQSKQEAD 2468
Cdd:pfam01576 1033 KQLKRQLEEAEEEASRANAARRKLQRELD 1061
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2290-2650 |
2.81e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2290 EEAEnmKKLaeEAARLNIEaqeaaRL--------RQIAEsdLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQK 2358
Cdd:COG1196 175 EEAE--RKL--EATEENLE-----RLedilgeleRQLEP--LERQAEKAERYRElkeELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2359 DQAQVEAQKLLEAKKEMQQRLDQETegfqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR 2438
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAE------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2439 LQETEKhtsekhtVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFF 2518
Cdd:COG1196 318 LEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2519 AEKETLlkkekaieeekkklekqfedevkKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDL 2598
Cdd:COG1196 391 ALRAAA-----------------------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2599 EKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQM 2650
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
173-268 |
6.69e-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: 70.49 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 173 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 251
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1207141782 252 DVDVPHPDEKSIITYVS 268
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3086-3124 |
7.19e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.12 E-value: 7.19e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 3086 LLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPELHEKL 3124
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1156-1924 |
1.51e-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: 77.91 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1156 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQR-ATEVNKRMSQLHSERDV--ELEHYRQLVGNLRERWQAVFAQIELR 1232
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQlCEEKNALQEQLQAETELcaEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1233 QRELDLLNRQMQAYRESydwLIRWIADAKQRQDKLHAvpigGSKGLQ-EQLTQE---KKLLEEIEKNKDKVEDCQKFAKG 1308
Cdd:pfam01576 84 LEEEEERSQQLQNEKKK---MQQHIQDLEEQLDEEEA----ARQKLQlEKVTTEakiKKLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1309 YIDAIKDYELQLvtykalvepiASPLKKAKMesasddiiqeyvtlrtryseLMTLSSQYIKFIIETQRRLQDEEK----- 1383
Cdd:pfam01576 157 LEERISEFTSNL----------AEEEEKAKS--------------------LSKLKNKHEAMISDLEERLKKEEKgrqel 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1384 -----AAEKLKEEERKKMAEMQAELEKQK-QLA---ETHAKAIAKAEQEAN-----------------ELKTKMKDEVSK 1437
Cdd:pfam01576 207 ekakrKLEGESTDLQEQIAELQAQIAELRaQLAkkeEELQAALARLEEETAqknnalkkireleaqisELQEDLESERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1438 RQdvavDSEKQKHNIQRELQELK---------TLSEQEIKAKSQQvEEALLSRTrIEEEIHIIRLQLEtTMKQKNTAETE 1508
Cdd:pfam01576 287 RN----KAEKQRRDLGEELEALKteledtldtTAAQQELRSKREQ-EVTELKKA-LEEETRSHEAQLQ-EMRQKHTQALE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1509 -----LLQLRAKAVDADKLRNAAQEEAEKLRKQV-------AEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1576
Cdd:pfam01576 360 elteqLEQAKRNKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1577 LQAEEAERHLKQAElekQRQIQVVEEVAkkTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKARE 1656
Cdd:pfam01576 440 SELESVSSLLNEAE---GKNIKLSKDVS--SLESQLQDTQELLQEETRQKLNLST-RLRQLEDERNSLQEQLEEEEEAKR 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1657 QAEKELETWRQ------KANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK-EAAEMELGNQR 1729
Cdd:pfam01576 514 NVERQLSTLQAqlsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElDDLLVDLDHQR 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1730 KMAEETAKQ-----KLAAEQELIRLRA--DFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1802
Cdd:pfam01576 594 QLVSNLEKKqkkfdQMLAEEKAISARYaeERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1803 SKAEKeTMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAK------------------KQRQIAEEEAARQRA---- 1860
Cdd:pfam01576 674 DDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqferdlQARDEQGEEKRRQLVkqvr 752
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 1861 EAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1924
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEE 816
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
49-155 |
1.65e-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: 69.62 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDrvqKKTFTKWVNKHLVKAQrhITDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALD 120
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVD 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141782 121 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 155
Cdd:cd21219 73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1114-1898 |
1.72e-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: 77.85 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1114 LSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVP-VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE 1192
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1193 VNKRmsQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYREsydwlirwiadakQRQDKLHAVpi 1272
Cdd:pfam15921 199 ASGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKS-------------ESQNKIELL-- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1273 ggskglqeqltqekklleeIEKNKDKVEDCqkfakgyidaIKDYELQLVtykALVEPIASPLKKAKMESASDDIIQEYVT 1352
Cdd:pfam15921 262 -------------------LQQHQDRIEQL----------ISEHEVEIT---GLTEKASSARSQANSIQSQLEIIQEQAR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1353 LRT-----RYSELMTLSSQYIKFIIETQRRLQDEEKaaeklkeeerkkmaemqaELEKQKQLAETHakaIAKAEQEANEL 1427
Cdd:pfam15921 310 NQNsmymrQLSDLESTVSQLRSELREAKRMYEDKIE------------------ELEKQLVLANSE---LTEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1428 KTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIkAKSQQVEEalLSRTRIEEEIHIIRLQ-LETTMKQKNTAE 1506
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDT-GNSITIDH--LRRELDDRNMEVQRLEaLLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1507 TEllqlraKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlekfKLQAEEAER-- 1584
Cdd:pfam15921 446 ME------RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK---------------------KMTLESSERtv 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1585 -HLKQAELEKQRQIQvveevAKKTAATQLESKqVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELE 1663
Cdd:pfam15921 499 sDLTASLQEKERAIE-----ATNAEITKLRSR-VDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1664 TWRQKANEALRL-------RLQAEEEANKKtaAQEEAEKQKEEAKREAKKRA-KAEEAALKQKEAAEMELGNQRKMAEET 1735
Cdd:pfam15921 573 NMTQLVGQHGRTagamqveKAQLEKEINDR--RLELQEFKILKDKKDAKIRElEARVSDLELEKVKLVNAGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1736 AKQKL--------AAEQELIRLRADFE--------HAEQQRTVLD----------DELQRLKNDVNS-------AVKQKK 1782
Cdd:pfam15921 651 IKQERdqllnevkTSRNELNSLSEDYEvlkrnfrnKSEEMETTTNklkmqlksaqSELEQTRNTLKSmegsdghAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1783 ELEEELIKVRKEMEIlLQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatKLRSVAEEakKQRQIAEEEAARQRaea 1862
Cdd:pfam15921 731 GMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ------ELSTVATE--KNKMAGELEVLRSQ--- 798
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1207141782 1863 EKILKEKLT----AINEATRLKTEAEIALKEKEAENDRLK 1898
Cdd:pfam15921 799 ERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
171-271 |
2.37e-13 |
|
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: 69.33 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 250
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1207141782 251 ED-VDVPHPDEKSIITYVSSMY 271
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3746-3784 |
3.89e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 3.89e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 3746 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEFHDKL 3784
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2759-2797 |
4.21e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.81 E-value: 4.21e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 2759 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPELHTKL 2797
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
74-153 |
4.36e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.39 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 74 HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 145
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1207141782 146 LGLIWTII 153
Cdd:cd21223 105 LALLWRII 112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1867-2665 |
4.60e-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: 76.25 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1867 KEKLTAINEA---TRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvLEDqaaqhkqAIEEKIGQLKKssdteLDRQKKI 1943
Cdd:TIGR02168 155 EERRAIFEEAagiSKYKERRKETERKLERTRENLDR-----------LED-------ILNELERQLKS-----LERQAEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1944 VEETLKQRKVVEE-EIHILKLNFEKASSGKQELELELKKLKGIADETQKskakaeeeaekfrklaleeekkrkeaeaKVK 2022
Cdd:TIGR02168 212 AERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTA----------------------------ELQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2023 QIQAAEEEAARQHKAAQEEVGRLMKLAEEAKkqKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmaqDKLK 2102
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALA--NEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-----DELA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2103 EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEK----LRKEAEKEASRRAEAEAAA 2178
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiasLNNEIERLEARLERLEDRR 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2179 LKLKQEADSEMAKYKKLAEKTLKQK-SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2257
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2258 QME--DLLKLKLKIEKENQELMKKDKDNTKKLLEEEA-----------ENMKKLA---EEAARLNIEAQEAARL--RQIA 2319
Cdd:TIGR02168 497 LQEnlEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaaieaalgGRLQAVVvenLNAAKKAIAFLKQNELgrVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2320 ESDLAKQRELAEKMLEEKK-------------------------------------QAIQEAAKL--------------- 2347
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggvlvvddldNALELAKKLrpgyrivtldgdlvr 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2348 -------------------KAEAEKLQKQKDQAQV---EAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAE 2405
Cdd:TIGR02168 657 pggvitggsaktnssilerRREIEELEEKIEELEEkiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2406 KLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEkekeklk 2485
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2486 keaADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEE 2565
Cdd:TIGR02168 810 ---AELTLLNEEAANLRERLESLERRI------AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2566 ERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEenknLREKLQQLQSsqkasytkEIEIQTDKVPEE 2645
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ----LELRLEGLEV--------RIDNLQERLSEE 948
|
890 900
....*....|....*....|
gi 1207141782 2646 ELVQMTMVETTKKVLNGSTE 2665
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEE 968
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1207-1905 |
4.89e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.16 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1207 ELEHYRQLVGNLRERWQAVFAQIELRQRELDLL----NRQMQAYRESYDWLIRWIADAKQRQDKLhavpiggsKGLQEQL 1282
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLtlctPCMPDTYHERKQVLEKELKHLREALQQT--------QQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1283 TQEKKLLEEIEKNkdkvedcQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDIIQ-------EYVTLRT 1355
Cdd:TIGR00618 246 TQKREAQEEQLKK-------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieqqaqrIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1356 RYSELMTLSSQYIKFI-----IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAEtHAKAIAKAEQEANELKTK 1430
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVkqqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1431 MKDEVSKRQDVAVDSEKQkHNIQRELQELKTLSEQEIKAksqQVEEALLSRTRIEEE--IHIIRLQLETTMKQKNTAETE 1508
Cdd:TIGR00618 398 LCKELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTaqCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1509 LLQlRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQ 1588
Cdd:TIGR00618 474 QLQ-TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1589 AELEkqrQIQVVEEvaKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEhlKKQQAEADKAREQAEKELETWRQK 1668
Cdd:TIGR00618 553 SERK---QRASLKE--QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1669 ANEALRLRLQ--AEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1746
Cdd:TIGR00618 626 DLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1747 IR-----LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLE 1821
Cdd:TIGR00618 706 LRelethIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1822 SEAAKMRELAEEATKLRSVAEEAKKQ-------RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEN 1894
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
730
....*....|.
gi 1207141782 1895 DRLKRKAEEEG 1905
Cdd:TIGR00618 866 QEQAKIIQLSD 876
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
58-159 |
8.89e-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: 67.65 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 58 KTFTKWVNKHLVKAqrHITDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 130
Cdd:cd21298 9 KTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILHFQIS 159
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
171-271 |
1.36e-12 |
|
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: 66.98 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 250
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1207141782 251 ED-VDVPHPDEKSIITYVSSMY 271
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1649-2436 |
1.66e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1649 AEADKAREQAEKELETWRQKANealRLRLQAEEEANKktaaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQ 1728
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIE---RLDLIIDEKRQQ--------------LERLRREREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1729 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRKEMEILLQQKSKAEK 1807
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1808 ETMSNTEKSKQLLESEA---AKMRELAEEATKL-RSVAEEAKKQRQIAEEEAARQ------RAEAEKILKEKLTAINEAT 1877
Cdd:TIGR02169 309 SIAEKERELEDAEERLAkleAEIDKLLAEIEELeREIEEERKRRDKLTEEYAELKeeledlRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1878 RLKTEAEIALKEKEAENDRLKRKAEEegyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKI------VEETLKQR 1951
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqewkLEQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1952 KVVEEEIHILKLNF---EKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-----------------LALEEE 2011
Cdd:TIGR02169 465 SKYEQELYDLKEEYdrvEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryaTAIEVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2012 KKRKEAEAKVKQIQAAEE--EAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLV 2089
Cdd:TIGR02169 545 AGNRLNNVVVEDDAVAKEaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-------DPKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2090 QQNKDSMaqdkLKEEFEKAKKLAQEAEKAKDNAEkeaalLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEAS 2169
Cdd:TIGR02169 618 YVFGDTL----VVEDIEAARRLMGKYRMVTLEGE-----LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2170 RRAEAEAAALKLKQEADSEMAKYKKLAEKT---LKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA 2246
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2247 QVEDELSKVKIQMEDllklklKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQ 2326
Cdd:TIGR02169 769 ELEEDLHKLEEALND------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2327 RELAEKMLEEKkqaiQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEK 2406
Cdd:TIGR02169 843 IDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830
....*....|....*....|....*....|
gi 1207141782 2407 LKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2436
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3162-3200 |
2.11e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 2.11e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 3162 LLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEMNQNL 3200
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
545-734 |
2.51e-12 |
|
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: 69.40 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 545 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 621
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIeegHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 622 LQYAKLLTSSKTRLRSLD---QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNV 698
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207141782 699 QMTGDKLLKDGHP-ARKTIEAFTAALQTQWSWILQLC 734
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1702-2354 |
5.76e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1702 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVNSAVKQK 1781
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1782 KELEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLEsEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 1861
Cdd:PRK03918 248 ESLEGSK----RKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1862 AEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegYQR-KVLEDQAAQHKqaieekigqlKKSSDTELDRQ 1940
Cdd:PRK03918 323 INGI-EERIKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEaKAKKEELERLK----------KRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1941 KKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-LALEEEKKRKEAEA 2019
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKIT---ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2020 KVKQIQAAEEEAarqhKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQD 2099
Cdd:PRK03918 467 ELKEIEEKERKL----RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2100 KLKEEFEKAKKLaqeaekakdnaEKEAALLHKKAEEAERQKkaaeaeaakqakaqedaEKLRKEAEKEASRRAEAEAAAL 2179
Cdd:PRK03918 543 SLKKELEKLEEL-----------KKKLAELEKKLDELEEEL-----------------AELLKELEELGFESVEELEERL 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2180 KLKQEADSEMAKYKKlAEKTLKQKssvEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVE-DELSKVKIQ 2258
Cdd:PRK03918 595 KELEPFYNEYLELKD-AEKELERE---EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLE 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2259 MEDLLKLKLKIEKENQELMKKDKDNTKKlLEEEAENMKKLAEEAARLNIEAQEAARLRQ--------IAESDLAKQRELA 2330
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEK-LKEELEEREKAKKELEKLEKALERVEELREkvkkykalLKERALSKVGEIA 749
|
650 660
....*....|....*....|....
gi 1207141782 2331 EKMLEEKKQAIQEAAKLKAEAEKL 2354
Cdd:PRK03918 750 SEIFEELTEGKYSGVRVKAEENKV 773
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2056-2636 |
6.76e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2056 KEIAEKEAEKQVILVQEA--AQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKD---NAEKEAALLH 2130
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2131 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAeaaaLKLKQEadseMAKYKKLAEKTLKQKSSVEEEL 2210
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY----IKLSEF----YEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2211 VKVKVQLDETDKQKSVLDvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2290
Cdd:PRK03918 324 NGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2291 EAENMKKLAEEAARLNIEAQEaaRLRQIAESDLAKQ------RELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQKDQ 2360
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKE--LKKAIEELKKAKGkcpvcgRELTEehrkELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2361 AQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITA-EAEKLKVKVTQLSDAQSKAEEEAKK---FKKQADE 2434
Cdd:PRK03918 481 ELRELEKVLKKESELikLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2435 IKIRLQETEKHTSEKHTvveKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlq 2514
Cdd:PRK03918 561 LEKKLDELEEELAELLK---ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL-- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2515 qsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME-EERKKLQSAMDAAIKKQKEAEEEMNGKQK 2593
Cdd:PRK03918 636 ----AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAElEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1207141782 2594 EMQDLEKKRieqekllaEENKNLREKLQQLQSSQKASYTKEIE 2636
Cdd:PRK03918 712 ELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVG 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1381-2138 |
6.96e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.41 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1381 EEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQ--------DVAVDSEKQKHNI 1452
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1453 QRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvdaDKLRNAAQEEAEK 1532
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE--------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL---EDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1533 LRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEKFKLQAEEAERHLKQAELEKQrqIQVVEEvAKKTAATQL 1612
Cdd:TIGR02169 380 FAETR-DELKDYREKLEKLKREINELKR------------ELDRLQEELQRLSEELADLNAA--IAGIEA-KINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1613 ESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAA 1689
Cdd:TIGR02169 444 EDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1690 QEEAEKQKEEAKREakkRAKAEEAA----------------------LKQKEAAEMELGNQRKMAEETAKQKLAAEQELI 1747
Cdd:TIGR02169 523 VHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavakeaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1748 RLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE-----LEEELIK---------VRKEMEILLQQKSKAEKE 1808
Cdd:TIGR02169 600 GFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKyrmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1809 TMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE----EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlK 1880
Cdd:TIGR02169 678 RLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkigEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---I 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1881 TEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHI 1960
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1961 LKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEKFRKLALEEEkkrkeaeakVKQIQAAEEEAARQHKAAQE 2040
Cdd:TIGR02169 827 EKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLNGKKEELEEE---------LEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2041 EVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL------------------VQQNKDSMAQD--- 2099
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledVQAELQRVEEEira 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1207141782 2100 ------KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2138
Cdd:TIGR02169 970 lepvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3413-3451 |
7.35e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.35e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 3413 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPEVHEKL 3451
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1397-1913 |
7.36e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1397 AEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQelktLSEQEIKAKSQQVEE 1476
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEAG----LDDADAEAVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1477 ALLSRTRIEEEIHIIRLQLETTmkqKNTAETellqLRAKAVDADKLRNAAQEEAEKLRKQV--AEETQKKRKAE-EELKR 1553
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAH---NEEAES----LREDADDLEERAEELREEAAELESELeeAREAVEDRREEiEELEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1554 KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEES-----LK 1628
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSphvetIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1629 NEQVMVIQLQEEAEHLKKQQAEADKAREQA------EKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakr 1702
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRETIE------------------ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1703 eakkrAKAEEAALKQKEAAEMELGNQRKmAEETAKQKLAAEQELIRLRAdfehAEQQRTVLDDELQRLkNDVNSAVKQKK 1782
Cdd:PRK02224 534 -----EKRERAEELRERAAELEAEAEEK-REAAAEAEEEAEEAREEVAE----LNSKLAELKERIESL-ERIRTLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1783 ELEEELIKVRKemeillQQKSKAEKEtmsntEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARqraea 1862
Cdd:PRK02224 603 DAEDEIERLRE------KREALAELN-----DERRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQ----- 664
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 1863 ekiLKEKLTAINEA-TRLKTE---AEIALKEKEAENDRLKRKAEEEGYQRKVLED 1913
Cdd:PRK02224 665 ---VEEKLDELREErDDLQAEigaVENELEELEELRERREALENRVEALEALYDE 716
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3989-4027 |
7.72e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.72e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 3989 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEFKDKL 4027
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4335-4373 |
1.11e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.11e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 4335 LLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMVDRI 4373
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
51-150 |
1.20e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 64.75 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 51 ERDRvQKKTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 122
Cdd:cd21300 4 EGER-EARVFTLWLNSLDVEPA--VNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1207141782 123 KHRQVKLVNIRNDDIADGNPKLTLGLIW 150
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1712-2618 |
1.28e-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: 71.64 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1712 EAALKQKEAAEMELGNQRKMAEETAKQklaaeqeLIRLRADFEHAEQQRTVLDD----ELQRLKNDVNSAVKQKKELEEE 1787
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1788 LIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEatklrsvaEEAKKQRQIAEEEAarQRAEAEKILK 1867
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1868 EKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQ---AIEEKIGQLKKSSDTELDRQKKIV 1944
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeleDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1945 EETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLaleeekkrkeaEAKVKQI 2024
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-----------EWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2025 QAAEEEAARQHKAAQEEVGRLMKlaEEAKKQKEIAEKEAEKQVIlvqEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKE 2103
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEK--ELSKLQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlGSVGE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2104 EFEKAKKLAQEAEKA----KDNAEKEAALLHKKAEEAERQKKAaeaeaakqakaqedaeKLRKEAEKEASRRAEAEAAAL 2179
Cdd:TIGR02169 536 RYATAIEVAAGNRLNnvvvEDDAVAKEAIELLKRRKAGRATFL----------------PLNKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2180 KLKQEADSEMAKYKKlAEKTLKQKSSVEEELVKVKVQLDETdkQKSVLDVEL-----------KRLKQEVSDAIKQKAQV 2248
Cdd:TIGR02169 600 GFAVDLVEFDPKYEP-AFKYVFGDTLVVEDIEAARRLMGKY--RMVTLEGELfeksgamtggsRAPRGGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2249 E---DELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnmkklaeeaarlnieaqeaarlRQIAESDLAK 2325
Cdd:TIGR02169 677 QrlrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE----------------------IEQLEQEEEK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2326 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLD----QETEGFQKSLEAERKRQLEIT 2401
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2402 AEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvqrlqskQEADGLHKAIADLEKEK 2481
Cdd:TIGR02169 815 REIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-------EELEELEAALRDLESRL 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2482 EKLKKEAADLQKQSKEMANVQQEQ-LQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERqr 2560
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELeAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR-- 962
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2561 klMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2618
Cdd:TIGR02169 963 --VEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
173-272 |
1.31e-11 |
|
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: 63.90 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 173 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN---LENLEQAFSIAER-DLGVTRLL 248
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1207141782 249 DPEDVdVPHPDEKSIITYVSSMYD 272
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1935-2649 |
1.44e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.15 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1935 TELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS-GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLA--LEEE 2011
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTqkREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2012 KKRKEAEAKVKQIQAAEEEAARQ---HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL--VQEAAQKCSAAEQKAQN 2086
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQeavLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHteLQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2087 VLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA---KDNAEKEAALLHK-KAEEAERQKKAAEAEAAKQAKAQEDAEKLRK 2162
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2163 EAEKEASRRAEAEAAALKLKQEADSEMAKYKKLA-EKTLKQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLKQEV 2238
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREqqlQTKEQIHLQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2239 SDAIKQKAQVEDELSKVKIQMEdLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQi 2318
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2319 AESDLAKQRElaekmleekkqaiqeaaKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrldqetegfqKSLEAERKRQL 2398
Cdd:TIGR00618 571 SFSILTQCDN-----------------RSKEDIPNLQNITVRLQDLTEKLSEAED--------------MLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2399 EITAEAEKLKVKVTQlsdaQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLE 2478
Cdd:TIGR00618 620 KLQPEQDLQDVRLHL----QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2479 KEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLlkkekaieEEKKKLEKQFEDEVKKAEALKAEQER 2558
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL--------NQSLKELMHQARTVLKARTEAHFNNN 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2559 QRKLMEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2637
Cdd:TIGR00618 768 EEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
730
....*....|..
gi 1207141782 2638 QTDKVPEEELVQ 2649
Cdd:TIGR00618 848 THQLLKYEECSK 859
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2040-2654 |
1.50e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.15 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2040 EEVGRLMKLAEEAKKQKEIAEKEAEKQV----ILVQEAAQKCSAAEQKAQnvlVQQNKDSMAQDKLKEEFEKAKKLAQEA 2115
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTlrsqLLTLCTPCMPDTYHERKQ---VLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2116 EKAKDNAEKEAALLHKKAEEAE-RQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkQEADSEMAKYKK 2194
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-QSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2195 LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQevsdaikqKAQVEDELSKVKIQMEDLLKLKLKIEKENQ 2274
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI--------SCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2275 ELMKKDKDNTKKLLEEEAENmkklAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQaIQEAAKLKAEAEKL 2354
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFR----DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2355 QKQKDQAQVEAQK--LLEAKKEMQQRLDQETEGFQKSLEAERKRQLEitaeAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2432
Cdd:TIGR00618 476 QTKEQIHLQETRKkaVVLARLLELQEEPCPLCGSCIHPNPARQDIDN----PGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2433 DEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTI 2512
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2513 LQQSFFAEKETLLKKEKAIEEEKKKLEKQFED--EVKKAEALKAEQeRQRKLMEEERKKLQSAMDAAIKKQK-----EAE 2585
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHalSIRVLPKELLAS-RQLALQKMQSEKEQLTYWKEMLAQCqtllrELE 710
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 2586 EEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVE 2654
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1636-2620 |
1.79e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.97 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1636 QLQEEAEHLKKQQAEADKArEQAEKELETWRQKANE---ALRLRLQAEEE----ANKKTAAQEEAEKQKEEAKREAKKRA 1708
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEeknALQEQLQAETElcaeAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1709 KAEE------AALKQKEAAEMELGNQRKMAEETAKQKL-----AAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1777
Cdd:pfam01576 85 EEEEersqqlQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1778 VKQKKELEEE---LIKVRKEMEIL---LQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatklrsvaEEAKKQRQIA 1851
Cdd:pfam01576 165 TSNLAEEEEKaksLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQE------------QIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1852 EEEAARQRAEAEkiLKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRkvleDQAAQHKQAIEEKIGQLKK 1931
Cdd:pfam01576 233 ELRAQLAKKEEE--LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1932 SSDTELDRQKkiVEETLKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIA-DETQKSKAKAEEEAEKFRKLALEE 2010
Cdd:pfam01576 307 ELEDTLDTTA--AQQELRSKR--EQEVTELKKALEEETRSHEAQLQEMRQKHTQAlEELTEQLEQAKRNKANLEKAKQAL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2011 EKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQK-EIAEK----------------EAEKQVILVQEA 2073
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRaELAEKlsklqselesvssllnEAEGKNIKLSKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2074 AQKCSAAEQKAQNVLVQQNKDSMAQD----KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEA----ERQKKAAEA 2145
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMkkklEEDAGTLEA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2146 EAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEAD-------------SEMAKYKKLAEKTLKQKSSVEEELVK 2212
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdllvdldhqrqlvSNLEKKQKKFDQMLAEEKAISARYAE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2213 VKVQLDETDKQKSVLDVELKRlkqEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKkdkdnTKKLLEEEA 2292
Cdd:pfam01576 623 ERDRAEAEAREKETRALSLAR---ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER-----SKRALEQQV 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2293 ENMKKLAEEA---------ARL----NIEAQEAARLRQIAESD---------LAKQ-RELAEKMLEEKKQAIQEAA---- 2345
Cdd:pfam01576 695 EEMKTQLEELedelqatedAKLrlevNMQALKAQFERDLQARDeqgeekrrqLVKQvRELEAELEDERKQRAQAVAakkk 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2346 ------KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-------------ETEGFQKSLEAERKRQLEITAEAEK 2406
Cdd:pfam01576 775 leldlkELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEarasrdeilaqskESEKKLKNLEAELLQLQEDLAASER 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2407 LKVKVTQLSDA-QSKAEEEAKKFKKQADE---IKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKE 2482
Cdd:pfam01576 855 ARRQAQQERDElADEIASGASGKSALQDEkrrLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQ 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2483 KLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSF------FAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQ 2556
Cdd:pfam01576 935 KSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIaaleakIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE 1014
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 2557 ERQRKLMEEERKKLQSAMDAAIKKQKEAEEE---MNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2620
Cdd:pfam01576 1015 RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEasrANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3489-3525 |
2.42e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.80 E-value: 2.42e-11
10 20 30
....*....|....*....|....*....|....*..
gi 1207141782 3489 LLDAQVATGGIIDPVNSHRLPNDVAIERGYFSKQLAK 3525
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1456-1769 |
2.75e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.15 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1456 LQELKTLSEQEIKAKSQQVEEallSRTRIEEEIHIIRLQLETTMKQKNTAETELLQlRAKAVDADKLRNAAQEEAEKLRK 1535
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ---ERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1536 QvaeetQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK-----LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1610
Cdd:pfam17380 354 R-----QEERKRELERIRQEEIAMEISRMRELERLQMERQQknervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1611 QLESKQVALTaRLEESLKNEQVMV----IQLQEEAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANK- 1685
Cdd:pfam17380 429 QEEARQREVR-RLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKILEKELEERKq 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1686 -------KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgnQRKMAEETAKqklaAEQELIRLRADFEHAEQ 1758
Cdd:pfam17380 507 amieeerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE-----RRRIQEQMRK----ATEERSRLEAMEREREM 577
|
330
....*....|.
gi 1207141782 1759 QRTVLDDELQR 1769
Cdd:pfam17380 578 MRQIVESEKAR 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1138-1929 |
3.17e-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: 70.10 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1138 ILNKYENQLREVNKVPVNEKEIEASQTQLQKLRSEAEgkqatfDRLEEELQRATEVNKRMSQLHSERDVElehyrqlvgn 1217
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE------KRLEEIEQLLEELNKKIKDLGEEEQLR---------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1218 LRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiADAKQRQDKLhavpiggskglqeqltQEKKLLEEIEKNKD 1297
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELED------------AEERLAKLEA----------------EIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1298 KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASddiiqeyvtLRTRYSELmtlsSQYIKFIIETQRR 1377
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------YREKLEKL----KREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1378 LQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEvskrqdvavdsEKQKHNIQRELQ 1457
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-----------EQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1458 ELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQ---LETTMKQKNTAETELLQLRAKAVDAdkLRNAAqeeAEKLR 1534
Cdd:TIGR02169 480 RV----EKELSKLQRELAEAEAQARASEERVRGGRAVeevLKASIQGVHGTVAQLGSVGERYATA--IEVAA---GNRLN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1535 KQVAEETQKKRKAEEELKRK-----------------SEAEKDAAKEKKKALEDLEKFKLQ-----------------AE 1580
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRkagratflplnkmrderRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvedIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1581 EAERHLKQAelekqRQIQVVEEVAKKT--------AATQLESKQVALTARLEESLKNEQVMVIQ---LQEEAEHLKKQQA 1649
Cdd:TIGR02169 631 AARRLMGKY-----RMVTLEGELFEKSgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1650 EADKAREQAEKELETWRQKANealrlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAE-EAALKQKEAAEMELgnq 1728
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIE-----QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKElEARIEELEEDLHKL--- 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1729 rKMAEETAKQKLaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSaVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1808
Cdd:TIGR02169 778 -EEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1809 TMSNTEKSKQLLESEAAK----MRELAEEATKLRSVAEEAKKQR---QIAEEEAARQRAEAEKILKEkltaineatrLKT 1881
Cdd:TIGR02169 855 EIENLNGKKEELEEELEEleaaLRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSE----------LKA 924
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1207141782 1882 EAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKIGQL 1929
Cdd:TIGR02169 925 KLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAE-LQRVEEEIRAL 970
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1397-1854 |
6.61e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1397 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAvDSEKQKHNIQRELQELKtlSEQEIKAKSQQVEE 1476
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELR--EELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1477 ALLSRTRIEEEIHIIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKse 1556
Cdd:COG4717 130 LYQELEALEAELAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1557 aEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQiQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVM--- 1633
Cdd:COG4717 201 -LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1634 ------VIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKkTAAQEEAEKQKEEAKREAKKR 1707
Cdd:COG4717 279 lflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-EELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1708 AKAEEAALKQKEAAEMELGNQRKMA-EETAKQKLAAEQELIRLRADFEHAEQQ----------------RTVLDDELQRL 1770
Cdd:COG4717 358 ELEEELQLEELEQEIAALLAEAGVEdEEELRAALEQAEEYQELKEELEELEEQleellgeleellealdEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1771 KNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI 1850
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1207141782 1851 AEEE 1854
Cdd:COG4717 509 YREE 512
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1423-1743 |
8.76e-11 |
|
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: 68.50 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1423 EANELKTKMKDEV-----SKRQDVAVDSEKQKH----NIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRL 1493
Cdd:NF033838 51 SGNESQKEHAKEVeshleKILSEIQKSLDKRKHtqnvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1494 QLETTMKQKNTAET----ELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakeKKKAL 1569
Cdd:NF033838 131 KKDTLEPGKKVAEAtkkvEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE----------EAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1570 EDLEKFKlqAEEAERHLKQAELEKQRQIQV----VEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1645
Cdd:NF033838 201 RDEEKIK--QAKAKVESKKAEATRLEKIKTdrekAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1646 KQQ-------------------------AEADKAREQAEKELETWRQK------ANEALRLRLQ-AEEEAN-KKTAAQEE 1692
Cdd:NF033838 279 KENdakssdssvgeetlpspslkpekkvAEAEKKVEEAKKKAKDQKEEdrrnypTNTYKTLELEiAESDVKvKEAELELV 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 1693 AEKQKEEAKREAKKRAKAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAE 1743
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVES-KKAEATRLEkIKTDRKKAEEEAKRKAAEE 409
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
173-271 |
8.85e-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: 61.60 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 173 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 252
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1207141782 253 VdVPHPDEKSIITYVSSMY 271
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2027-2384 |
1.15e-10 |
|
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: 67.61 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2027 AEEEAARQHKAAQEEVGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL----VQQNKDSMAQDKL 2101
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEArireLEEDIKTLTQRVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2102 KEEfekakklaQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKL 2181
Cdd:pfam07888 147 ERE--------TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2182 KQEADSEMAKYKKLaEKTLKQKSSVEEELvkvkvqldETDKQKSVLdvelkrLKQEVSDAIKQKAQVEDELSKVKI---Q 2258
Cdd:pfam07888 219 TQKLTTAHRKEAEN-EALLEELRSLQERL--------NASERKVEG------LGEELSSMAAQRDRTQAELHQARLqaaQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2259 MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKK 2338
Cdd:pfam07888 284 LTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESR 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1207141782 2339 QAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETE 2384
Cdd:pfam07888 364 RELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1252-1925 |
1.27e-10 |
|
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: 68.21 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1252 WLIRWIADAKQRQDKLH---AVPIGGSKGLQE-QLTQEK---KLLEEIEKNKDKV--------------EDCQKFAKGYI 1310
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIkennatrhlcnllkETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1311 DAIKDYELQLVTYKAL---VEPIASPLKKAKMEsASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRR-----LQDEE 1382
Cdd:pfam05483 173 KYEYEREETRQVYMDLnnnIEKMILAFEELRVQ-AENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQvslllIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1383 KAAEKLKEEERKKMAEMQA-ELEKQKQLAETHAKAIAKAE----QEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQ 1457
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKAnQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1458 ELKTLSEQEIKAKSQQ---VEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1534
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1535 KQVAE------ETQKKRKAEEELKRKSEAEKdaakekkkaledlekFKLQAEEAERHLKQAEL-----EKQRQIQVVEEV 1603
Cdd:pfam05483 412 KILAEdeklldEKKQFEKIAEELKGKEQELI---------------FLLQAREKEIHDLEIQLtaiktSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1604 akKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA 1683
Cdd:pfam05483 477 --KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1684 NKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVL 1763
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1764 DDELQRLKNDVNSAvkqKKELEEELIKVRKEMEIllqqKSKAEKETMSNTEKSKQlleseaakmreLAEEATKLRSVAEE 1843
Cdd:pfam05483 635 EIKVNKLELELASA---KQKFEEIIDNYQKEIED----KKISEEKLLEEVEKAKA-----------IADEAVKLQKEIDK 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1844 aKKQRQIAEEEA--ARQRAEAEKILKEKLTAI-------NEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ 1914
Cdd:pfam05483 697 -RCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
730
....*....|.
gi 1207141782 1915 AAQHKQAIEEK 1925
Cdd:pfam05483 776 AKENTAILKDK 786
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3822-3860 |
1.33e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.88 E-value: 1.33e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 3822 LLEAQVATGGLMDPEYYFRLPIDIAMQRGYMNKETSERI 3860
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
996-1783 |
1.88e-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: 67.79 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 996 EQEPALIQKDSTSGEQDESVCKSyitQIKDLRLRLEGCESRTVN----RLRQMVDKEPL-KACTQRATEQKKVQTELEGI 1070
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLER---SIAEKERELEDAEERLAKleaeIDKLLAEIEELeREIEEERKRRDKLTEEYAEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1071 KKDLDKVVEKSEAVLATSQQSSSAPV-LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ----GAEDILNKYENQ 1145
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1146 LREVN-KVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELqraTEVNKRMSQLHSERDV---ELEHYRQLVGNLRER 1221
Cdd:TIGR02169 443 KEDKAlEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL---SKLQRELAEAEAQARAseeRVRGGRAVEEVLKAS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1222 WQAVFAQIelrqreldllnRQMQAYRESYDWLIRWIADAKqrqdkLHAVPIGGSKGLQE--QLTQEKKL--LEEIEKNKD 1297
Cdd:TIGR02169 520 IQGVHGTV-----------AQLGSVGERYATAIEVAAGNR-----LNNVVVEDDAVAKEaiELLKRRKAgrATFLPLNKM 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1298 KVEDCQKfAKGYIDAIKDYELQLVTYKALVEPI-----ASPLKKAKMESASDDIIQ-EYVTLRTRYSE---LMTLSSQYI 1368
Cdd:TIGR02169 584 RDERRDL-SILSEDGVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAP 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1369 KFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQ 1448
Cdd:TIGR02169 663 RGGILFSRSEPAEL--------------QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1449 KHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdadklrnaaQE 1528
Cdd:TIGR02169 729 EQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---------QA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1529 EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhlKQAELEKQrqiqvveevaKKTA 1608
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK--EIENLNGK----------KEEL 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1609 ATQLESKQVALtARLEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANK--- 1685
Cdd:TIGR02169 867 EEELEELEAAL-RDLESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSE-LKAKLEALEEELSeie 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1686 KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMelgnqrkmaeetakqklAAEQELIRLRADFEHAEQQRTVLDD 1765
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM-----------------LAIQEYEEVLKRLDELKEKRAKLEE 1000
|
810
....*....|....*...
gi 1207141782 1766 ELQRLKNDVNSAVKQKKE 1783
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKRE 1018
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
48-156 |
1.97e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 61.06 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 48 CADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLK 123
Cdd:cd21222 9 EAPEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELME 88
|
90 100 110
....*....|....*....|....*....|...
gi 1207141782 124 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 156
Cdd:cd21222 89 DAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2354-2622 |
2.13e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.07 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2354 LQKQKDQAQVEAQKLLEakKEMQQRLDQETEgfQKSLEAERKRQLEitaEAEKLKvKVTQLSDAQSKAEEEAKKFKKQAD 2433
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE--KMEQERLRQEKE--EKAREVERRRKLE---EAEKAR-QAEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2434 EIKIRLQETEKHTS-----------EKHTVVEKLEVQRLQS----KQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEM 2498
Cdd:pfam17380 350 LERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKnervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2499 ANVQQEQLQQektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQ-------RKLMEEERKKLQ 2571
Cdd:pfam17380 430 EEARQREVRR----LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraeeqrRKILEKELEERK 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 2572 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2622
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1509-1939 |
2.89e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.28 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1509 LLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELK------RKSEAEKDAAKEKKKALEDLEKFKLQAEE- 1581
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlNLVQTALRQQEKIERYQEDLEELTERLEEq 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1582 ----AERHLKQAELEKQRQiQVVEEVakKTAATQLESKQVALTARLEESLKNEQVmvIQLQEEAEHLkkqQAEADKAREQ 1657
Cdd:COG3096 367 eevvEEAAEQLAEAEARLE-AAEEEV--DSLKSQLADYQQALDVQQTRAIQYQQA--VQALEKARAL---CGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1658 AEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEETAK 1737
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLS----------------VADAARRQFEKAYELVCKIAGEVE----RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1738 qklaaeqELIRLRADFEHAEQQRTVLDDELQRLkndvnsavkqkkeleEELIKVRKEMEILLQQKSKAEKETMSNTEKSK 1817
Cdd:COG3096 499 -------ELLRRYRSQQALAQRLQQLRAQLAEL---------------EQRLRQQQNAERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1818 QLLESEAAKMRELAEEAtklRSVAEEAKKQRQiAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 1897
Cdd:COG3096 557 ELLAELEAQLEELEEQA---AEAVEQRSELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAM 632
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1207141782 1898 KRKAEEEgYQRKVLEDQAAQHKQAIEEKIGQLKK---SSDTELDR 1939
Cdd:COG3096 633 QQLLERE-REATVERDELAARKQALESQIERLSQpggAEDPRLLA 676
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1368-2082 |
2.96e-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: 67.02 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1368 IKFIIETQRRLQDEE-------------------------KAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQ 1422
Cdd:TIGR02169 193 IDEKRQQLERLRRERekaeryqallkekreyegyellkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1423 EANELKTKMKDEVSKRQ--------DVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQ 1494
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAE--------IDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1495 LETTMKQKNTAETELLQLRAKavdADKLRNAAQEEAEKLRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEK 1574
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEE---LEDLRAELEEVDKEFAETR-DELKDYREKLEKLKREINELKR------------EL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1575 FKLQAEEAERHLKQAELEKqrQIQVVEEvAKKTAATQLESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1654
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNA--AIAGIEA-KINELEEEKEDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1655 REQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREakkRAKAEEAA----------------- 1714
Cdd:TIGR02169 485 LSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavak 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1715 -----LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE- 1783
Cdd:TIGR02169 562 eaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKy 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1784 ----LEEELIK---------VRKEMEILLQQKSKAEKETMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE---- 1842
Cdd:TIGR02169 640 rmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkig 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1843 EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAI 1922
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1923 EEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHILKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEK 2002
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTLEKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2003 FRKLALeeekkrkeaEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQ 2082
Cdd:TIGR02169 861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2082-2465 |
5.01e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.92 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2082 QKAQNVLVQQNK-DSMAQDKLKEEFEKakkLAQEAEKAKDNAEKEAAllhkKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2160
Cdd:pfam17380 281 QKAVSERQQQEKfEKMEQERLRQEKEE---KAREVERRRKLEEAEKA----RQAEMDRQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2161 RKEAEKEASRRAEaeaaalklKQEADSEMAKYKKLAektlkqkssveeelvkvKVQLDETDKQKsvldvelkRLKQEVSD 2240
Cdd:pfam17380 354 RQEERKRELERIR--------QEEIAMEISRMRELE-----------------RLQMERQQKNE--------RVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2241 AIKQKAQVEDELSKVKIQMEDllklklkiekenQELMKKDKDNTKKlleeeaENMKKLAEEAARlnieaqEAARLRQiae 2320
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVE------------MEQIRAEQEEARQ------REVRRLEEERAR------EMERVRL--- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2321 SDLAKQRElaekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEakKEMQQRLdqetegfQKSLEAERKRQLeI 2400
Cdd:pfam17380 454 EEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE--KELEERK-------QAMIEEERKRKL-L 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2401 TAEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2465
Cdd:pfam17380 519 EKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1526-1745 |
6.90e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.44 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1526 AQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledLEKFKLQA-EEAERHLKQAELEKQRQIQVVEEVA 1604
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQ-----------------LEKERLAAqEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1605 KKTAATQLESKQVAltARLEESLKneqvmviqlQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRlRLQAEEEA 1683
Cdd:PRK09510 140 KAAAAAKAKAEAEA--KRAAAAAK---------KAAAEAKKKAEAEAAkKAAAEAKKKAEAEAAAKAAAEA-KKKAEAEA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 1684 NKKTaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1745
Cdd:PRK09510 208 KKKA-------------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1573-1921 |
6.92e-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: 65.42 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1573 EKFKLQAEEAERHLK------QAELEKQRQIQVVE----------------EVAKKTAATQLESK-QVALTARLEESLKN 1629
Cdd:NF033838 54 ESQKEHAKEVESHLEkilseiQKSLDKRKHTQNVAlnkklsdikteylyelNVLKEKSEAELTSKtKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1630 eqvmVIQLQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRA 1708
Cdd:NF033838 134 ----TLEPGKKVAEATKKVEEAEkKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1709 KAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAEQE--LIRLRADFEHAEQQRTVLDDELQRL------KNDVNS--- 1776
Cdd:NF033838 210 KAKVES-KKAEATRLEkIKTDREKAEEEAKRRADAKLKeaVEKNVATSEQDKPKRRAKRGVLGEPatpdkkENDAKSsds 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1777 ----------AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSkqlLESEAAKMRELAEEAtKLRSVAEEAKK 1846
Cdd:NF033838 289 svgeetlpspSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKT---LELEIAESDVKVKEA-ELELVKEEAKE 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 1847 QRQIAEEEAARQRAEAEKIlkekltainEATRL-KTEAEIALKEKEAendrlKRKAEEEgyqRKVLEDQAAQHKQA 1921
Cdd:NF033838 365 PRNEEKIKQAKAKVESKKA---------EATRLeKIKTDRKKAEEEA-----KRKAAEE---DKVKEKPAEQPQPA 423
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1573-2347 |
7.54e-10 |
|
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: 65.63 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1573 EKFKLQAEEAERHLKQAELekqrqIQVVEEVAKKTAATQLESKQVaLTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAD 1652
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQA-----IAGIMKIRPEFTKLQQEFNTL-ESAELRLSHLHFGYKSDETLIASRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1653 KAREQAEKELEtWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA---KKRAKAEEAALKQKEAAEME----- 1724
Cdd:pfam12128 288 LNQLLRTLDDQ-WKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLDAdieTAAADQEQLPSWQSELENLEerlka 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1725 -LGNQRKMAEETAKQKLAAEQELIR--------LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKK---ELEEELIKVR 1792
Cdd:pfam12128 366 lTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELREQLEAGKlefNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1793 KEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 1872
Cdd:pfam12128 446 LGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1873 INEATRLKTEAEIALKEkeaendrlkrkaeeegyqrkVLEDQAAQHKQAIEEKIgqlkkssDTELDRQKKIVEETLKQRK 1952
Cdd:pfam12128 522 LDELELQLFPQAGTLLH--------------------FLRKEAPDWEQSIGKVI-------SPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1953 VVEEEIHILKLNFEKAS-----SGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAA 2027
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG--------------ELEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2028 EEEAARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcSAAEQKAQNVLVQQNKD----SMAQDKL 2101
Cdd:pfam12128 641 ETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQL-KQLDKKHQAWLEEQKEQkreaRTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2102 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER------------QKKAAEAEAAKQAKAQEDAEKLRKEA-EKEA 2168
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYkrdlaslgvdpdVIAKLKREIRTLERKIERIAVRRQEVlRYFD 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2169 SRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQK--- 2245
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKeda 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2246 --AQVEDELSKVKIQMED-LLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNieaqeAARLRQIAESD 2322
Cdd:pfam12128 880 nsEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQN-----DKGIRLLDYRK 954
|
810 820
....*....|....*....|....*.
gi 1207141782 2323 LAKQRE-LAEKMLEEKKQAIQEAAKL 2347
Cdd:pfam12128 955 LVPYLEqWFDVRVPQSIMVLREQVSI 980
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2194-2625 |
7.83e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2194 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkieken 2273
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2274 qelmkkdkdntkklLEEEAENMKKL-AEEAARLNIEAQEAARLRQIAEsdlaKQRELAEKMLEEKKQAIQEAAKLKAEAE 2352
Cdd:COG4717 141 --------------LAELPERLEELeERLEELRELEEELEELEAELAE----LQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2353 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQ-SKAEEEAKKFKKQ 2431
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLlSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2432 ADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2511
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2512 ILQQSFFAEKETLLKKEKAIEEEK-KKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ-KEAEEEMN 2589
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELE 442
|
410 420 430
....*....|....*....|....*....|....*...
gi 1207141782 2590 GKQKEMQDL--EKKRIEQEKLLAEENKNLREKLQQLQS 2625
Cdd:COG4717 443 ELEEELEELreELAELEAELEQLEEDGELAELLQELEE 480
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1525-1958 |
8.54e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1525 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1604
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1605 KKTAATQLESKQVALTARLEESLKNEqvmviqlQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEAN 1684
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEK-------AEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-IEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1685 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK--------QKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHA 1756
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAkkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1757 EQQRTVLDDELQRLKNDVNSAVKQKKELEE------------ELIKVRKEMEILLQQKSKAEKEtMSNTEKsKQLLESEA 1824
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTEehrkelleeytaELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1825 AKMRELAEEATKLRSV--------AEEAKKQRQIAEEEAARQRAEAeKILKEKLTAINEATRLKTEAEIALKEKEAENDR 1896
Cdd:PRK03918 496 IKLKELAEQLKELEEKlkkynleeLEKKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 1897 LKRKAEEEGYqrKVLEDqaaqhkqaIEEKIGQLKKSSD--TELDRQKKIVEETLKQRKVVEEEI 1958
Cdd:PRK03918 575 LLKELEELGF--ESVEE--------LEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEEL 628
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2277-2439 |
1.00e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.71 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2277 MKKDKDNTKKLLEEEAENMKK--LAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKL 2354
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKqrAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2355 QKQKDQAQveAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT--AEAEKLKVKVTQlsdAQSKAEEEAKKFKKQA 2432
Cdd:TIGR02794 142 RKAKEEAA--KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEakAKAEEAKAKAEA---AKAKAAAEAAAKAEAE 216
|
....*..
gi 1207141782 2433 DEIKIRL 2439
Cdd:TIGR02794 217 AAAAAAA 223
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
57-153 |
1.07e-09 |
|
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: 58.74 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 57 KKTFTKWVNKHLVKaQRHIT----------DLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 121
Cdd:cd21217 3 KEAFVEHINSLLAD-DPDLKhllpidpdgdDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 1207141782 122 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 153
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1128-1853 |
1.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1128 VIRSTQGAEDILNKYENqLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQatfDRLEEELQRATEVNKRMSQLHSERDvE 1207
Cdd:PRK03918 150 VVRQILGLDDYENAYKN-LGEV------IKEIKRRIERLEKFIKRTENIE---ELIKEKEKELEEVLREINEISSELP-E 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1208 LEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYdwlirwiadakqrqdklhavpiggsKGLQEQLTQEKK 1287
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-------------------------RELEERIEELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1288 LLEEIEKNKDKVEDCQKFAKGYIDAIKDYElqlvtykalvepiasplkkaKMESASDDIIQEYVTLRTRYSELmtlssqy 1367
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYE--------------------EYLDELREIEKRLSRLEEEINGI------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1368 ikfiietQRRLQDEEKaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKdevskrqdvavdsek 1447
Cdd:PRK03918 327 -------EERIKELEE------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE--------------- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1448 qkhNIQRELQELKTLSEQEIKAKSQQVEEAllsRTRIEEEIHII---RLQLETTMKQKNTAETELLQLRAKAV------- 1517
Cdd:PRK03918 373 ---ELERLKKRLTGLTPEKLEKELEELEKA---KEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPvcgrelt 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1518 --DADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1595
Cdd:PRK03918 447 eeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-----LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1596 qiqvveevAKKTAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL 1675
Cdd:PRK03918 522 --------KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1676 RLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEH 1755
Cdd:PRK03918 593 RLKELEPFYNEYL--------------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1756 AEQQRtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlqqksKAEKETMSNTEKSKQLLESEAAKMRELAEEAT 1835
Cdd:PRK03918 659 EEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKELEKLEKALERVEELREKVK 731
|
730 740
....*....|....*....|
gi 1207141782 1836 KLRSVAEEA--KKQRQIAEE 1853
Cdd:PRK03918 732 KYKALLKERalSKVGEIASE 751
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2835-2873 |
1.26e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 56.18 E-value: 1.26e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 2835 LLDCQYATGGIIDPVNSHHVPVQLACTQGQLDEDLSKIL 2873
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1636-1963 |
1.40e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.76 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1636 QLQEEAEHLKKQ---QAEADKAREQAEK----ELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREaKKRA 1708
Cdd:pfam17380 288 QQQEKFEKMEQErlrQEKEEKAREVERRrkleEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQEERKRE-LERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1709 KAEEAALKQKEAAEME-LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK--KELE 1785
Cdd:pfam17380 366 RQEEIAMEISRMRELErLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRleEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1786 EELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEeaaRQRAEAEKI 1865
Cdd:pfam17380 446 REMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE---RKRKLLEKE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1866 LKEKLTAINEATRLKTEAEIALKEKEAENDR----LKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 1941
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEERRriqeQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
330 340
....*....|....*....|..
gi 1207141782 1942 KIVEETLKQRKVVEEEIHILKL 1963
Cdd:pfam17380 602 PIYRPRISEYQPPDVESHMIRF 623
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
938-1746 |
1.74e-09 |
|
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: 64.61 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 938 KTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRSVEQEPALIQKDSTSGEQDESVCK 1017
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1018 SYITQIKDLRLRLEGCESRTVNRLRQMVDKEplkactqraTEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVL 1097
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKAE---------KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1098 RSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVpvNEKEIEASQTQLQKLRSEAEGKQ 1177
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK--EEKKEELEILEEEEESIELKQGK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1178 ATFDRLEEELQRATEVNKRMS------QLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAY----- 1246
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELElkksedLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggrii 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1247 RESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEE----------IEKNKDKVEDCQKFAKGYIDAIKDY 1316
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALtelplgarklRLLIPKLKLPLKSIAVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1317 EL---------QLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEK 1387
Cdd:pfam02463 606 AQldkatleadEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1388 LKEEERkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvAVDSEKQKHNIQRELQELKTLSEQEI 1467
Cdd:pfam02463 686 ESELAK---EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI--NEELKLLKQKIDEEEEEEEKSRLKKE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1468 KAKSQQVEEALLSRTRIEEEIHIIRLQLEttmKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKA 1547
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVE---EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1548 EEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESL 1627
Cdd:pfam02463 838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1628 KNEQVMV------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL------RLQAEEEANKKTAAQEEAEK 1695
Cdd:pfam02463 918 EIEERIKeeaeilLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEElgkvnlMAIEEFEEKEERYNKDELEK 997
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 1696 QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1746
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2183-2404 |
1.75e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2183 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2262
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2263 LKLKLKIEKENQElmkkDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2342
Cdd:COG4942 117 GRQPPLALLLSPE----DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2343 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegfqksLEAERKRQLEITAEA 2404
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR--------LEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1483-1838 |
1.79e-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: 64.32 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1483 RIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKL-------RNAAQEEAEKLRKQVAEETQKKRKAEEELKRKS 1555
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1556 EAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL-EKQRQIQVVEEVAkktaatqleSKQVALTARLEESLKNEQVMV 1634
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEV---------SRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1635 IQLQEEAEHLKKQQAEADKAREQAEKELetwrqkanEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAA 1714
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEI--------ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1715 LKQKEaaemelgNQRKMAEETAKQKLAaeqeliRLRADFEHAEQQRTVLDDELQRLKNDVNSA------VKQKKELEEEL 1788
Cdd:TIGR02169 901 LERKI-------EELEAQIEKKRKRLS------ELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvQAELQRVEEEI 967
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1789 IKVrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 1838
Cdd:TIGR02169 968 RAL-EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
171-268 |
2.10e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 58.16 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90
....*....|....*....
gi 1207141782 250 PEDVDVPHPDEKSIITYVS 268
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLS 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4411-4449 |
2.37e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.41 E-value: 2.37e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 4411 FLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTAQKL 4449
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
58-152 |
3.06e-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: 57.35 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 58 KTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 129
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1207141782 130 VNIRNDDIADGNPKLTLGLIWTI 152
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2099-2618 |
3.22e-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: 63.50 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2099 DKLKEEFEKAKKLAQEAEKAKD-------NAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRR 2171
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDkflteikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2172 AEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEE---ELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ- 2247
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQn 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2248 ------VEDELSKVKIQMEDLLKLKlkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQI--- 2318
Cdd:TIGR04523 280 nkkikeLEKQLNQLKSEISDLNNQK------EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltn 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2319 AESD-LAKQRELAEKmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQ 2397
Cdd:TIGR04523 354 SESEnSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQINDLE---SKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2398 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADL 2477
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2478 EKEKEklkkeaaDLQKQSKEMaNVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklekqfeDEVKKAEALKAE-Q 2556
Cdd:TIGR04523 509 EEKVK-------DLTKKISSL-KEKIEKLESEKKEKESKISDLEDELNKD----------------DFELKKENLEKEiD 564
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2557 ERQRKLmeeerKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2618
Cdd:TIGR04523 565 EKNKEI-----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1315-1962 |
3.44e-09 |
|
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: 63.20 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1315 DYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKE---E 1391
Cdd:pfam05483 38 DPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1392 ERKKMAEMQAELEKqkqlaethakaiakaeqeaneLKTKMKDEVSKRQDVAVDSEKQKHnIQRELQELKTLSEQEIKAKS 1471
Cdd:pfam05483 118 QRKAIQELQFENEK---------------------VSLKLEEEIQENKDLIKENNATRH-LCNLLKETCARSAEKTKKYE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1472 QQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETEL-LQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE 1550
Cdd:pfam05483 176 YEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1551 LKRKSEAEKDAAKEKKKALedlEKFKLQAEeaerHLKQAELEKQRQIQVVEEVAKKTaatqleSKQVALTARLEESLKNE 1630
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLE---EKTKLQDE----NLKELIEKKDHLTKELEDIKMSL------QRSMSTQKALEEDLQIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1631 QVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL---RLQAEEEANKKTAAQEEAEKQKEEAKREAKKR 1707
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1708 AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRL----RADFEHAEQQRTVLD-------DELQRLKNDVNS 1776
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKtseehylKEVEDLKTELEK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1777 AVKQKKELEEELIKVRKEMEILLQQKS------KAEKETMSNTEKSKQ--------LLESEAAKMRELAEEATKLRSVAE 1842
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASdmtlelKKHQEDIINCKKQEErmlkqienLEEKEMNLRDELESVREEFIQKGD 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1843 EAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKV-------LE 1912
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGSAENKQLNAyeikvnkLE 642
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1913 DQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 1962
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1495-1739 |
6.52e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.01 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1495 LETTMKQKNTAETELLQLRAKAVDADKlrnaAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlEK 1574
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAK----KEQERQKKLEQQAEEAEKQRAAEQARQKE------------------LE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1575 FKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNeqvmviqlQEEAEHLKKQQAEADKA 1654
Cdd:TIGR02794 96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--------QAEEEAKAKAAAEAKKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1655 REQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAalkQKEAAEMELGNQRKMAEE 1734
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA---ERKADEAELGDIFGLASG 243
|
....*
gi 1207141782 1735 TAKQK 1739
Cdd:TIGR02794 244 SNAEK 248
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1573-2240 |
6.83e-09 |
|
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: 62.43 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1573 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtaRLEESLKNEQVMVIQ----------LQE--- 1639
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSL--KLEEEIQENKDLIKEnnatrhlcnlLKEtca 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1640 -EAEHLKKQQAEADKARE-------------QAEKELETWRQKANEALRLRLQA--------EEEANKKTAAQEEAEKQK 1697
Cdd:pfam05483 166 rSAEKTKKYEYEREETRQvymdlnnniekmiLAFEELRVQAENARLEMHFKLKEdhekiqhlEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1698 EEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ----RTVLDDELQRLKND 1773
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1774 VNSAVKQKKELEEELIKVRKEMEIL----------LQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLrsvaee 1843
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAHSFVvtefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKF------ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1844 aKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIAL----KEKEAENDRLK---RKAEEEGYQRKVLEDQA 1915
Cdd:pfam05483 400 -KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFllqaREKEIHDLEIQltaIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1916 AQHKQAIE---------------EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELK 1980
Cdd:pfam05483 479 ELEKEKLKnieltahcdklllenKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1981 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2060
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2061 KEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAllHKKAEEAERQk 2140
Cdd:pfam05483 636 IKVNKLELELASAKQK---FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ--HKIAEMVALM- 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2141 kaaeaeaakqakaqedaEKLRKEAEkeasrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDET 2220
Cdd:pfam05483 710 -----------------EKHKHQYD--------------KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSL 758
|
730 740
....*....|....*....|
gi 1207141782 2221 DKQKSVLDVELKRLKQEVSD 2240
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKE 778
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1400-1941 |
6.96e-09 |
|
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: 62.55 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1400 QAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAL 1478
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1479 LsRTRIEEEIHIIRL-QLETTMKQKNTAETELLQLRAKavdaDKLRNAAQEEAEKLRKQVaeetqkkrkaeEELKRksea 1557
Cdd:pfam12128 433 L-EFNEEEYRLKSRLgELKLRLNQATATPELLLQLENF----DERIERAREEQEAANAEV-----------ERLQS---- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1558 ekdaakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQiqvveevakKTAATQLESKQVALTARLEESLKNEqvmviqL 1637
Cdd:pfam12128 493 -------------ELRQARKRRDQASEALRQASRRLEER---------QSALDELELQLFPQAGTLLHFLRKE------A 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1638 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEAL---RLRLQAEEeankktaaQEEAEKQKEEAKREAKKRAKAEEAA 1714
Cdd:pfam12128 545 PDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvKLDLKRID--------VPEWAASEEELRERLDKAEEALQSA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1715 LKQKEAAEMELGNQRKMAEEtakqklaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRK 1793
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEK-------ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1794 EMEIL---LQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklRSVAEEAKKQRQIAEEEAARQRAEA-EKILKEK 1869
Cdd:pfam12128 690 QLKQLdkkHQAWLEEQKEQKREARTEKQ------AYWQVVEGA----LDAQLALLKAAIAARRSGAKAELKAlETWYKRD 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1870 LTA--INEATRLKTEAEIALKEKEAENDRLKRKA---------EEEGYQRKVLEDQAAQHKQAIEEKIGQL-KKSSDTEL 1937
Cdd:pfam12128 760 LASlgVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKL 839
|
....
gi 1207141782 1938 DRQK 1941
Cdd:pfam12128 840 RRAK 843
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4333-4370 |
7.58e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 7.58e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1207141782 4333 QRLLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMV 4370
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2207-2434 |
8.65e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2207 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekeNQELmkkdkdntKK 2286
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----------QAEI--------AE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2287 LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES----DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQ 2362
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2363 VEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2434
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1022-1752 |
1.06e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1022 QIKDLRLRLEGCESR------TVNRLRQMVDKEPLKACTQRATEQKKVQTELEGIKKDLDKVvEKSEAVLATSQQSSSAP 1095
Cdd:TIGR02169 245 QLASLEEELEKLTEEiselekRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL-ERSIAEKERELEDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1096 V--LRSEIDITQKKMEhvyGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNK-VPVNEKEIEASQTQLQKLRSE 1172
Cdd:TIGR02169 324 LakLEAEIDKLLAEIE---ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKeFAETRDELKDYREKLEKLKRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1173 AEGKQATFDRLEEELQRATE-----------VNKRMSQLHSERDV-----------------ELEHYRQLVGNLRERWQA 1224
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEeladlnaaiagIEAKINELEEEKEDkaleikkqewkleqlaaDLSKYEQELYDLKEEYDR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1225 VFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLHAvPIGGSKGLQEQLTQ-EKKLLEEIE---------- 1293
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEER-------VRGGRAVEEVLKA-SIQGVHGTVAQLGSvGERYATAIEvaagnrlnnv 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1294 --KNKDKVEDCQKFAK------------------------GYIDAIKDYELQLVTYKALVEPI-----ASPLKKAKMESA 1342
Cdd:TIGR02169 553 vvEDDAVAKEAIELLKrrkagratflplnkmrderrdlsiLSEDGVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAA 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1343 SDDIIQ-EYVTLRTRYSE---LMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIA 1418
Cdd:TIGR02169 633 RRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRSEPAEL--------------QRLRERLEGLKRELSSLQSELR 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1419 KAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETT 1498
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1499 MKQKNTAETELLQLRAKAVdadklrnaaQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQ 1578
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEI---------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1579 AEEAERhlKQAELEKQrqiqvveevaKKTAATQLESKQVALtARLEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQA 1658
Cdd:TIGR02169 849 IKSIEK--EIENLNGK----------KEELEEELEELEAAL-RDLESRLGD-------LKKERDELEAQLRELERKIEEL 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1659 EKELETWRQKANEaLRLRLQAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1735
Cdd:TIGR02169 909 EAQIEKKRKRLSE-LKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKR 987
|
810 820
....*....|....*....|...
gi 1207141782 1736 ------AKQKLAAEQELIRLRAD 1752
Cdd:TIGR02169 988 ldelkeKRAKLEEERKAILERIE 1010
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
56-155 |
1.20e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 55.97 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 56 QKKTFTKWVNKhlVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLKHRQVKLV 130
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1207141782 131 NIRNDDIADGNPKLTLGLIWTIILH 155
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1694-1903 |
1.35e-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: 60.55 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1694 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKmaeetakqklAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1773
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----------ALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1774 VNSAVKQKKELEEELIKV---------RKEMEILLQQKSKAEKETMSNTEKS-KQLLESEAAKMRELAEEATKLRSVAEE 1843
Cdd:COG4942 92 IAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1844 AKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE 1903
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1047-1901 |
1.39e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1047 KEPLKACTQRATEQKKVQT---ELEGIKKDLDKVVEKSEAVLATSQQSSS--APVLRSEIDITQKKMEHVYGlssvyldk 1121
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASleeELEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKEKIGELEA-------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1122 lkTIDLVIRSTQGAEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ-RATEVNKRMSQL 1200
Cdd:TIGR02169 302 --EIASLERSIAEKERELEDAEERLAKL------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAeLKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1201 HSErDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQE 1280
Cdd:TIGR02169 374 EEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1281 QLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPI--ASPLKKAKMESASDDIIQEYVTLRtrys 1358
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeeRVRGGRAVEEVLKASIQGVHGTVA---- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1359 ELMTLSSQYIKFI-IETQRRLQ-----DEEKAAEKLkeeerkkmaemqaELEKQKQLAETHAKAIAKAEQEANELKTKMK 1432
Cdd:TIGR02169 529 QLGSVGERYATAIeVAAGNRLNnvvveDDAVAKEAI-------------ELLKRRKAGRATFLPLNKMRDERRDLSILSE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1433 DEVSKRQDVAVDSEKQKHNIQRE-------LQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKnta 1505
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFKYvfgdtlvVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSE--- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1506 ETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaaKEKKKALEDLEKFKLQAEEAERH 1585
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEED 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1586 LKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMviQLQEEAEHLKKQQAEADKAREQAEKELet 1664
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKL-- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1665 wrqkaNEALRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALkqkEAAEMELGNQRKMAEETAKQKLAAEQ 1744
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQEL-----------QEQRIDLKEQIKSIEKEI---ENLNGKKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1745 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELikvrkemEILLQQKSKAEKETMSNTEKSKQLLESE- 1823
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEEELSLEd 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 1824 -AAKMRELAEEATKLRSVAEEAKKQrqiAEEEAARQraeaeKILKEKLtaineaTRLKTEAEiALKEKEAENDRLKRKA 1901
Cdd:TIGR02169 956 vQAELQRVEEEIRALEPVNMLAIQE---YEEVLKRL-----DELKEKR------AKLEEERK-AILERIEEYEKKKREV 1019
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
171-268 |
1.80e-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: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 171 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 249
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1207141782 250 PEDVDVPHPDEKSIITYVS 268
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2183-2461 |
1.97e-08 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 60.50 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2183 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQldetdkqksvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2262
Cdd:pfam03528 14 EKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE-------------DLKRQNAVLQEAQVELDALQNQLALARAEMENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2263 LKLKLKIEKENQELMkkdkDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQ 2342
Cdd:pfam03528 81 KAVATVSENTKQEAI----DEVKSQWQEEVASLQAIMKETVR-EYEVQFHRRLEQ-ERAQWNQYRESAEREIADLRRRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2343 EAAklkaEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ------ETEGFQKSLEAERKRQLEITAEAEK-----LKVKV 2411
Cdd:pfam03528 155 EGQ----EEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAEKscrtdLEMYV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2412 TQLSDAQSKAEEEAKKFKKQADEIKIRL-QETEKHTSEKHTVVEK----LEVQRL 2461
Cdd:pfam03528 231 AVLNTQKSVLQEDAEKLRKELHEVCHLLeQERQQHNQLKHTWQKAndqfLESQRL 285
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1722-2465 |
2.04e-08 |
|
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: 60.90 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1722 EMELGNQRKMAEETAKQKLAaeqeliRLRADFEHAEQqrtvlddELQRLKNDVNSA-VKQKKELEEELIKVRKEMeillq 1800
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEHIE------RVLEEYSHQVK-------DLQRRLNESNELhEKQKFYLRQSVIDLQTKL----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1801 QKSKAEKETMSNTEKSkqllesEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK 1880
Cdd:pfam15921 120 QEMQMERDAMADIRRR------ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1881 TEAEIALKEKEAENDRL-----KRKAEEEGYQRKVLEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRk 1952
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISYLKGRIfpvEDQLEALKSESQNKIELLLQQHQDRIEQL- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1953 VVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQKskakaeEEAEKFRKLAleeekkrkEAEAKVKQIQAAEEEAA 2032
Cdd:pfam15921 273 ISEHEVEITGLT-EKASSARSQANSIQSQLEIIQEQARN------QNSMYMRQLS--------DLESTVSQLRSELREAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2033 RQHKAAQEEVGRLMKLAE----EAKKQKEIAEKEA-------EKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2101
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANseltEARTERDQFSQESgnlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2102 KEEFEKAKKLAQEAE--------KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKL--RKEAEKEASRR 2171
Cdd:pfam15921 418 RRELDDRNMEVQRLEallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtaKKMTLESSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2172 AEAEAAALKLKQEA----DSEMAKYK-----KLAE-KTLKQKS----SVEEELVKVKVQLDETDKQKSVLDVELKRLKQE 2237
Cdd:pfam15921 498 VSDLTASLQEKERAieatNAEITKLRsrvdlKLQElQHLKNEGdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2238 V------SDAIK-QKAQVEDELSKVKIQMEDLlklklkiekenqELMKKDKDNTKKLLEEEAENMkklaeEAARLNIEAQ 2310
Cdd:pfam15921 578 VgqhgrtAGAMQvEKAQLEKEINDRRLELQEF------------KILKDKKDAKIRELEARVSDL-----ELEKVKLVNA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2311 EAARLRqiAESDLAKQRElaeKMLEEKKQAIQEAAKLKAEAEKLQK----QKDQAQVEAQKLLEAKKEMQQRLDQeTEGF 2386
Cdd:pfam15921 641 GSERLR--AVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQ-TRNT 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2387 QKSLEAERKR--------QLEITA---EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEK 2455
Cdd:pfam15921 715 LKSMEGSDGHamkvamgmQKQITAkrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS---QELSTVATEKNKMAGE 791
|
810
....*....|
gi 1207141782 2456 LEVQRLQSKQ 2465
Cdd:pfam15921 792 LEVLRSQERR 801
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2122-2625 |
3.26e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2122 AEKEAALLHKKAEEAErqkkaaeaeaakQAKAQEDAEKLRKEAEKEASRRAeaeaaalklKQEADSEMAKYkklaEKTLK 2201
Cdd:PRK02224 197 EEKEEKDLHERLNGLE------------SELAELDEEIERYEEQREQARET---------RDEADEVLEEH----EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2202 QKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD-----------------AIKQKAQVEDELSKVKIQMEDLLK 2264
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaeaglddaDAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2265 LKLKIEKENQELMKKDKDNTKKlLEEEAenmKKLAEEAARLNIEAQEAARLRQIAESDLAK-----------------QR 2327
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADD-LEERA---EELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdapvDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2328 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2407
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2408 KVKVTQLSDAQSKAeEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvQRLQSKQEADGLHKAIADLEKEKEKLKKE 2487
Cdd:PRK02224 488 EEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKR-ERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2488 AADLQKQSKEMANVQQEQLQQEKTILqqsffAEKETLLKKEKAIEEEKKKLEKQFED----EVKKAEALKAEQERQRKL- 2562
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelNDERRERLAEKRERKRELe 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2563 --MEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKK------RIEQEKLLAEENKNLREKLQQLQS 2625
Cdd:PRK02224 641 aeFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavenELEELEELRERREALENRVEALEA 712
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1763-2516 |
3.35e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 60.37 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1763 LDDELQRLKNDVNSAVKQKKELEEELIKV--RKEMEILLQQKSKAEKETMSNT--------EKSKQLLESEAAK-MRELA 1831
Cdd:TIGR00618 83 LGTKIYRVHRTLRCTRSHRKTEQPEQLYLeqKKGRGRILAAKKSETEEVIHDLlkldyktfTRVVLLPQGEFAQfLKAKS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1832 EEATKLRSVAEEAKKQRQIAeeeaarqrAEAEKILKEkltaineatrLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVL 1911
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLA--------LMEFAKKKS----------LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1912 EDQAAQhkqaIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL-NFEKASSGKQELELELKKLKGIADETQ 1990
Cdd:TIGR00618 225 EKELKH----LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELrAQEAVLEETQERINRARKAAPLAAHIK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1991 ----------------KSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAA---QEEVGRLMKLAEE 2051
Cdd:TIGR00618 301 avtqieqqaqrihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQH 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2052 AKKQKEIAEKEAEKQVILVQE-----AAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEA 2126
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKEldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2127 ALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSV 2206
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2207 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK---------IQMEDLLKLKLKIEKENQELM 2277
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrlqdlTEKLSEAEDMLACEQHALLRK 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2278 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEA--------QEAARLRQIAESDLAKQRELAEKMLEEKKQAI-------- 2341
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQltltqervREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemla 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2342 QEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgFQKSLEAERKRQLEITAEAEKLK----VKVTQLSDA 2417
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFNNneevTAALQTGAE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2418 QSKAEEEAKKFKKQADEIKIRLQETE-KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKeaadLQKQSK 2496
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEaEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH----QLLKYE 855
|
810 820
....*....|....*....|
gi 1207141782 2497 EMANVQQEQLQQEKTILQQS 2516
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLS 875
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1712-2399 |
3.36e-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: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1712 EAALKQKEAAEMELGNQRKmaEETAKQKLAAEQELIRLRADFEHAEQQRTvLDDELQRLKNDVNSavkQKKELEEELIKV 1791
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHF--GYKSDETLIASRQEERQETSAELNQLLRT-LDDQWKEKRDELNG---ELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1792 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEE----ATKLRSVAEEAKKQRQIAEEEAARQRAEaekiLK 1867
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERlkalTGKHQDVTAKYNRRRSKIKEQNNRDIAG----IK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1868 EKLTAINEA-TRLKTEAEIALKEKEA----ENDRLKRKAEEEGYQrkvledqaaqhkqaIEEKIGQLKKSSDteldrQKK 1942
Cdd:pfam12128 397 DKLAKIREArDRQLAVAEDDLQALESelreQLEAGKLEFNEEEYR--------------LKSRLGELKLRLN-----QAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1943 IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQkskakaeeeaekfRKLALeeekkrkeAEAKVK 2022
Cdd:pfam12128 458 ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS-------------EALRQ--------ASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2023 QIQAAEEEAARQHKAAQeevGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL---------VQQN 2092
Cdd:pfam12128 517 ERQSALDELELQLFPQA---GTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvkldlkrIDVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2093 KDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEkeasrra 2172
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR--------------EETFARTALKNAR------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2173 eaeaaaLKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDEL 2252
Cdd:pfam12128 653 ------LDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2253 SKVKI-QMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES---------- 2321
Cdd:pfam12128 727 LDAQLaLLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwl 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2322 ----DLAKQRELAEKMLEEKKQ---AIQEAAKLK-AEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL-----DQETEGFQK 2388
Cdd:pfam12128 807 qrrpRLATQLSNIERAISELQQqlaRLIADTKLRrAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkeDANSEQAQG 886
|
730
....*....|.
gi 1207141782 2389 SLeAERKRQLE 2399
Cdd:pfam12128 887 SI-GERLAQLE 896
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
166-268 |
3.41e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 54.33 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 166 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGV 244
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....
gi 1207141782 245 TRLLDPEDVDVPHPDEKSIITYVS 268
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLS 103
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2543-2727 |
3.41e-08 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 60.23 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2543 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ--------KEAEEEMNGKQKEMQDLEKKRIEQ--EKLLAEE 2612
Cdd:PRK00409 533 EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAHELIEA 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2613 NKNLREKLQQLQSSQKASYTKEIEIQT-DKVPEEELVQMTMVETTKKvlngstevdgvKKDVPLAFDGIREKVPASRLHE 2691
Cdd:PRK00409 613 RKRLNKANEKKEKKKKKQKEKQEELKVgDEVKYLSLGQKGEVLSIPD-----------DKEAIVQAGIMKMKVPLSDLEK 681
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207141782 2692 IGVLSKKEydklKKGKTTVQELSKNDKVKMCLKGKD 2727
Cdd:PRK00409 682 IQKPKKKK----KKKPKTVKPKPRTVSLELDLRGMR 713
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2022-2166 |
4.40e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2022 KQIQAAEEE---AARQHKAAQEEvgrlMKLAEEAKKQKEIAEKEAEKQviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ 2098
Cdd:TIGR02794 81 EKQRAAEQArqkELEQRAAAEKA----AKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEE 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2099 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2166
Cdd:TIGR02794 155 EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAA 222
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2286-2636 |
4.89e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2286 KLLEEEAENMKKLAEEAARLnieaqeaarlrqiaeSDLAKQRELAEKMLEEKKQAIQE----AAKLKAEAEKLQKQKDQA 2361
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGI---------------SKYKERRKETERKLERTRENLDRlediLNELERQLKSLERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2362 QvEAQKLLEAKKEMQ--------QRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2433
Cdd:TIGR02168 213 E-RYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2434 EIKIRLQETEKhtsekhtvveklEVQRLQSKQEADglhkaiadlekekeklkkeaadlqKQSKEMANVQQEQLQQEKTIL 2513
Cdd:TIGR02168 292 ALANEISRLEQ------------QKQILRERLANL------------------------ERQLEELEAQLEELESKLDEL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2514 QQSFfAEKETLLKKEKAIEEekkklekQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQK 2593
Cdd:TIGR02168 336 AEEL-AELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1207141782 2594 EMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIE 2636
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1451-1972 |
6.14e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 58.89 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1451 NIQRELQELKTLSEQEIKAKSQQVEEaLLSRTRIEEEIhiiRLQLETTMKQKNTA--ETELLQLRAKAVD---ADKLRNA 1525
Cdd:pfam05701 46 KVQEEIPEYKKQSEAAEAAKAQVLEE-LESTKRLIEEL---KLNLERAQTEEAQAkqDSELAKLRVEEMEqgiADEASVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1526 AQE--EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKAledlekfklQAEEAERHLKQAElekqrqiQVVEEV 1603
Cdd:pfam05701 122 AKAqlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIK---------RAEEAVSASKEIE-------KTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1604 AKKTAATQlESKQVALTARLEeslKNEQVMVIQLQEEAEHLKKQqaeadKAREQAEKELETWRQK------------ANE 1671
Cdd:pfam05701 186 TIELIATK-ESLESAHAAHLE---AEEHRIGAALAREQDKLNWE-----KELKQAEEELQRLNQQllsakdlkskleTAS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1672 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKaeeAALKQKEAAEMElGNQRKMAEETAKQKLAAEQelirLRA 1751
Cdd:pfam05701 257 ALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAA---LASAKKELEEVK-ANIEKAKDEVNCLRVAAAS----LRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1752 DFehaEQQRTVLdDELQRLKNDVNSAVKQkkeLEEELIKVRKEMEiLLQQKSKAEKETMSNTEKskqlleseaaKMRELA 1831
Cdd:pfam05701 329 EL---EKEKAEL-ASLRQREGMASIAVSS---LEAELNRTKSEIA-LVQAKEKEAREKMVELPK----------QLQQAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1832 EEATKLRSVAEEAKKQRQIAEEEAARQRAEA-------EKILKEKLtAINEATRLKTEAEIALKEKEAEndrlKRKAEEE 1904
Cdd:pfam05701 391 QEAEEAKSLAQAAREELRKAKEEAEQAKAAAstvesrlEAVLKEIE-AAKASEKLALAAIKALQESESS----AESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1905 GYQRKV---LEDQAAQHKQA----------IEEKIGQLKKSSDTELDRQKKI--VEETLKQRKvveEEIHILKLNFEKAS 1969
Cdd:pfam05701 466 DSPRGVtlsLEEYYELSKRAheaeelankrVAEAVSQIEEAKESELRSLEKLeeVNREMEERK---EALKIALEKAEKAK 542
|
...
gi 1207141782 1970 SGK 1972
Cdd:pfam05701 543 EGK 545
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1705-2441 |
6.38e-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: 59.35 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1705 KKRAKAEEAALKQKEAaemELGNQRKM--AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR-----LKNDVNSA 1777
Cdd:pfam05483 91 KKWKVSIEAELKQKEN---KLQENRKIieAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1778 VKQKKELEEELIKVRkemEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 1857
Cdd:pfam05483 168 AEKTKKYEYEREETR---QVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1858 ---QRAEAEKILKEkLTAINEATRLKTEAeiaLKEK-EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIeekigqlkkSS 1933
Cdd:pfam05483 245 lliQITEKENKMKD-LTFLLEESRDKANQ---LEEKtKLQDENLKELIEKKDHLTKELEDIKMSLQRSM---------ST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1934 DTELDRQKKIVEETLKQRkVVEEEIHILKLNfeKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKK 2013
Cdd:pfam05483 312 QKALEEDLQIATKTICQL-TEEKEAQMEELN--KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2014 RKEAEAKVKQIQAAEEEAARQHKAAqeeVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQNK 2093
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKI---LAEDEKLLDEKKQFEKIAEELKGKE----QELIFLLQAREKEIHDLEIQLTA 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2094 DSMAQDKLKEEFEKAKKlaqEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAE 2173
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKT---ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2174 AEAAALKLKQEADSemakykklAEKTLKQKSSveeelvKVKVQLDETDKQKsvldvelKRLKQEVSDAIKQKAQVEDELS 2253
Cdd:pfam05483 539 LEEKEMNLRDELES--------VREEFIQKGD------EVKCKLDKSEENA-------RSIEYEVLKKEKQMKILENKCN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2254 KVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAE-NMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEk 2332
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE- 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2333 mLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLDQETE---GFQKSLEAERKR-QLEITAEAEKLK 2408
Cdd:pfam05483 677 -VEKAKAIADEAVKLQKEIDKRCQHK---IAEMVALMEKHKHQYDKIIEERDselGLYKNKEQEQSSaKAALEIELSNIK 752
|
730 740 750
....*....|....*....|....*....|...
gi 1207141782 2409 VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE 2441
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1348-1950 |
7.26e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1348 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1427
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-------------LEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1428 KTKMKDevskrqdvavdsekqkhNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTmkqkntaET 1507
Cdd:COG4913 329 EAQIRG-----------------NGGDRLEQL----EREIERLERELEERERRRARLEALLAALGLPLPAS-------AE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1508 ELLQLRAKAVDadkLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA----- 1582
Cdd:COG4913 381 EFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1583 -------------------------------------ERHLKQA-------ELEKQRQIQVVEEVAKKTAATQLESKQVA 1618
Cdd:COG4913 458 aelpfvgelievrpeeerwrgaiervlggfaltllvpPEHYAAAlrwvnrlHLRGRLVYERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1619 ---------LTARLEESLkNEQVMVIQLqEEAEHLKKqqaeADKA----------REQAEKELETWRQKA------NEAL 1673
Cdd:COG4913 538 gkldfkphpFRAWLEAEL-GRRFDYVCV-DSPEELRR----HPRAitragqvkgnGTRHEKDDRRRIRSRyvlgfdNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1674 RLRLQAEEEAnkktaaqeeaEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR---KMAEETAKQKLAAEQELIRLR 1750
Cdd:COG4913 612 LAALEAELAE----------LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1751 ADFEHAEQqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMREL 1830
Cdd:COG4913 682 ASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1831 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE-KLTAINEATRLKTEAEiALKEKEAENDRLkrkaEEEGyqrk 1909
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRL----EEDG---- 828
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1207141782 1910 vLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 1950
Cdd:COG4913 829 -LPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
51-158 |
7.57e-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: 54.24 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 51 ERDRVQKKTFTKWVNKHLVKAqrHITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 121
Cdd:cd21331 18 EGETREERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141782 122 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 158
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1100-1956 |
8.60e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.90 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1100 EIDITQKKMEHVYGLSSVYLDKLKTIDLVIRST--------QGAEDILNKYENQLREVNKvpvNEKEIEASQTQLQKLRS 1171
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYENELDPLKN---RLKEIEHNLSKIMKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1172 EAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFaqielrQRELDLLNRQMQAYRESYD 1251
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDC------QRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1252 WLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKklLEEIEKNKDKVEDCQKFAKGYIDAIKDyelqlvtykalvepia 1331
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIKNFHTLVIERQED---------------- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1332 splkKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQR-RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLA 1410
Cdd:TIGR00606 406 ----EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKeILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1411 ETHAKaIAKAEQEANeLKTKMKDEVSkRQDVAVDSEKQKHNIQRELQELKTLSEQEikaksQQVEEALLSRTRIEEEIHI 1490
Cdd:TIGR00606 482 KAERE-LSKAEKNSL-TETLKKEVKS-LQNEKADLDRKLRKLDQEMEQLNHHTTTR-----TQMEMLTKDKMDKDEQIRK 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1491 IRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE------ 1564
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcg 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1565 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMVIQLQEEAEH 1643
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTeAELQEFISDLQSKLRLAPDKLKS 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1644 LKKQQAEADKAREQAEKELETwrqKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1723
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPG---RQSI-IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1724 ELGNQRKMAEETAK-----QKLAAEQELIRLRADFEHAEQQRTVLDDELQRlkndvnsaVKQKKELEEELIKVRKEMEIL 1798
Cdd:TIGR00606 790 DVTIMERFQMELKDverkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDT--------VVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1799 LQQKS---KAEKETMS-NTEKSKQLLESEAAKMRELAEEATKLRSVAEE------AKKQRQIAEEEAARQRAEAEKILKE 1868
Cdd:TIGR00606 862 LKSKTnelKSEKLQIGtNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLEKDQQEKEELISSKETSNKKAQD 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1869 KLTAINEATRLKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTElDRQKKIVEET 1947
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ-KIQERWLQDN 1020
|
....*....
gi 1207141782 1948 LKQRKVVEE 1956
Cdd:TIGR00606 1021 LTLRKRENE 1029
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2021-2225 |
1.06e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.55 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2021 VKQIQAAEEEAArqhKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDsmAQDK 2100
Cdd:TIGR02794 52 ANRIQQQKKPAA---KKEQERQKKLEQQAEEAEKQRA-AEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA--EEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2101 LKEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAL 2179
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAErKAKEEAAKQAEEEAKAKAAAEAKKKAEE--AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141782 2180 KLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKS 2225
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1580-2138 |
1.17e-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: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1580 EEAERHLKQAElEKQRQIQVVEEVAKK-TAATQLESKQVALTARLEesLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1658
Cdd:COG4913 238 ERAHEALEDAR-EQIELLEPIRELAERyAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1659 EKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKq 1738
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDR-----------------LEQLEREIERLERELEERERRRARLEALLAALGLPLP- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1739 klAAEQELIRLRADfehAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSkaeketmsntekskq 1818
Cdd:COG4913 377 --ASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS--------------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1819 LLESEAAKMRELAEEATK-----LRSVAEEAkkqrQIAEEEAARQRAeAEKIL--------------KEKLTAINE---A 1876
Cdd:COG4913 437 NIPARLLALRDALAEALGldeaeLPFVGELI----EVRPEEERWRGA-IERVLggfaltllvppehyAAALRWVNRlhlR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1877 TRLKTEaeialKEKEAENDRLKRKAEEEGYQRKVL-------------------------EDQAAQHKQAIEEKiGQLKK 1931
Cdd:COG4913 512 GRLVYE-----RVRTGLPDPERPRLDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdsPEELRRHPRAITRA-GQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1932 SSDT-ELDRQKKIVEE------TLKQRKVVEEEIHILKLNFEKASSgkqelelELKKLKGIADETQKskakaeeeaekfR 2004
Cdd:COG4913 586 NGTRhEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEE-------RLEALEAELDALQE------------R 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2005 KLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKA 2084
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQA 725
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2085 QNVL--VQQNKDSMAQDKLKEEFEKAKKLAQEA------EKAKDNAEKEAALLHKKAEEAER 2138
Cdd:COG4913 726 EEELdeLQDRLEAAEDLARLELRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEE 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2021-2602 |
1.20e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2021 VKQIQAAEEEAARQHKAAQEEVGRLMKLAE---EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQnVLVQQNKDSMA 2097
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2098 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAA 2177
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK--------------ELEEKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2178 ALKLKQEADS-EMAKYKKLAEKTLKQKSSvEEELVKVKVQLDETDKQKSVLDVELKRLKQEvsdaikqKAQVEDELSKVK 2256
Cdd:PRK03918 354 LEELEERHELyEEAKAKKEELERLKKRLT-GLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2257 IQMEDLLKLKLKIEKENQELmkkDKDNTKKLLEEEAENMKKLAEEAARL-NIEAQEAARLRQI-----AESDLAKQRELA 2330
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGREL---TEEHRKELLEEYTAELKRIEKELKEIeEKERKLRKELRELekvlkKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2331 EKMLE-EKKQAIQEAAKLKAEAEKLQKQKdqaqveaQKLLEAKKEmqqrldqetegfQKSLEAERKRQLEITAEAEKLKV 2409
Cdd:PRK03918 503 EQLKElEEKLKKYNLEELEKKAEEYEKLK-------EKLIKLKGE------------IKSLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2410 KVTQLSDAQSKAEEEAKKFK-KQADEIKIRLQETEKHTSEKHTVVE-KLEVQRLQSKQE--ADGLHKAIADLEKEKEKLK 2485
Cdd:PRK03918 564 KLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDaEKELEREEKELKklEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2486 KEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKkklekqfedevKKAEALKAEQERqrklMEE 2565
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK-----------KTLEKLKEELEE----REK 708
|
570 580 590
....*....|....*....|....*....|....*..
gi 1207141782 2566 ERKKLQSamdaaIKKQKEAEEEMNGKQKEMQDLEKKR 2602
Cdd:PRK03918 709 AKKELEK-----LEKALERVEELREKVKKYKALLKER 740
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2285-2608 |
1.21e-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: 57.24 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2285 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQrELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2364
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ-ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2365 AQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA--DEIKIRLQET 2442
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNE-EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEekEREIARLRAQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2443 EKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffAEKE 2522
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREE--------EEFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2523 TLLkkekaieeekkklekqfEDEVKKAEALKAEQERQRKLMEEERKKLQSAMD---AAIKKQKEAEEEMNGKQKEMQDLE 2599
Cdd:pfam13868 265 RML-----------------RKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEereEQRAAEREEELEEGERLREEEAER 327
|
....*....
gi 1207141782 2600 KKRIEQEKL 2608
Cdd:pfam13868 328 RERIEEERQ 336
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1452-1959 |
1.32e-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: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1452 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE-----TELLQLRAKAVDADKLRNAA 1526
Cdd:COG4913 244 LEDAREQIELL--EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEleelrAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1527 QEEAEKLRKQVAE-ETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK 1605
Cdd:COG4913 322 REELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1606 K--TAATQLESKQVALTARLEEslkneqvmviqLQEEAEHLKKQQ----AEADKAREQAEKEL----------------- 1662
Cdd:COG4913 402 AleEALAEAEAALRDLRRELRE-----------LEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgelievr 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1663 ---ETWRQKANEAL---RLRL----QAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK---------EA 1720
Cdd:COG4913 471 peeERWRGAIERVLggfALTLlvppEHYAAALRwvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrAW 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1721 AEMELGNQRKMAeetakqKLAAEQELIRL-RA----------------DFEHAEQQRTVLddelqrlkndVNSAVKQKKE 1783
Cdd:COG4913 551 LEAELGRRFDYV------CVDSPEELRRHpRAitragqvkgngtrhekDDRRRIRSRYVL----------GFDNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1784 LEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEE-AKKQRQIAE--------EE 1854
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAE-LDALQERREALQ----RLAEYSWDEIDVASAEREiAELEAELERldassddlAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1855 AARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkVLEDQAAQHKQAIEEKIGQLKKSsd 1934
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA------AEDLARLELRALLEERFAAALGD-- 761
|
570 580
....*....|....*....|....*
gi 1207141782 1935 telDRQKKIVEETLKQRKVVEEEIH 1959
Cdd:COG4913 762 ---AVERELRENLEERIDALRARLN 783
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2185-2426 |
1.41e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2185 ADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlk 2264
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2265 lklkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLN-IEAQEAARLRQIAEsdlakQRELAEKMLEEKKQAIQE 2343
Cdd:COG3883 92 --------ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkIADADADLLEELKA-----DKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2344 AAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEE 2423
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
...
gi 1207141782 2424 EAK 2426
Cdd:COG3883 239 AAA 241
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2309-2444 |
1.53e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.78 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2309 AQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQK 2388
Cdd:TIGR02794 49 AQQANRIQQ-QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 2389 SlEAERKRQLEitAEAEKlkvkvTQLSDAQSKAEEEAKKfkKQADEIKIRLQETEK 2444
Cdd:TIGR02794 128 Q-AAEAKAKAE--AEAER-----KAKEEAAKQAEEEAKA--KAAAEAKKKAEEAKK 173
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1469-2069 |
1.66e-07 |
|
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: 57.84 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1469 AKSQQVEeaLLSRT-----RIEEEIHIIRlqlETTMKQKNTAETELLQLRAKAVdADKlrnAAQEEAEKLRKQVAEETQK 1543
Cdd:pfam07111 60 ALSQQAE--LISRQlqelrRLEEEVRLLR---ETSLQQKMRLEAQAMELDALAV-AEK---AGQAEAEGLRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1544 KRKAEEELKR-----KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAA--TQLESKQ 1616
Cdd:pfam07111 131 RKNLEEGSQReleeiQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELlrKQLSKTQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1617 VALTAR--LEESLKN---EQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETWR-QKANEALRLRlqaEEEAN 1684
Cdd:pfam07111 211 EELEAQvtLVESLRKyvgEQVPPEVHSQTWELERQelldtmQHLQEDRADLQATVELLQVRvQSLTHMLALQ---EEELT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1685 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK-QKEAAEMELGNQRKmaeeTAKQKLAAEQELIRLRAdfehaeQQRTVL 1763
Cdd:pfam07111 288 RKIQPSDSLEPEFPKKCRSLLNRWREKVFALMvQLKAQDLEHRDSVK----QLRGQVAELQEQVTSQS------QEQAIL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1764 DDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE---TMSNTEKSKQLLESEAAKMRELAEEATKLRSV 1840
Cdd:pfam07111 358 QRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQlkfVVNAMSSTQIWLETTMTRVEQAVARIPSLSNR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1841 AEEAKKQRQIAEEEAARQRAEAEkILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvlEDQAAQHkq 1920
Cdd:pfam07111 438 LSYAVRKVHTIKGLMARKVALAQ-LRQESCPPPPPAPPVDADLSLELEQLREERNRLDA------------ELQLSAH-- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1921 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEea 2000
Cdd:pfam07111 503 LIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQ-- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2001 ekfRKLALEEEKKRKEAEAKVKQIQAAEEEAAR--------QHKAAQEE--VGRLMKLAEEAKKQ------KEIAEKEAE 2064
Cdd:pfam07111 581 ---EKVAEVETRLREQLSDTKRRLNEARREQAKavvslrqiQHRATQEKerNQELRRLQDEARKEegqrlaRRVQELERD 657
|
....*
gi 1207141782 2065 KQVIL 2069
Cdd:pfam07111 658 KNLML 662
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4063-4099 |
1.67e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.17 E-value: 1.67e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1207141782 4063 IRLLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEM 4099
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1757-1953 |
1.81e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 57.53 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1757 EQQRTVLDDELQRLKNDVNSAVKQKKELEEElikvRKEMEILLQQkskAEKETMSNTEKSKQLLESEAAKMRELAEEATK 1836
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQK----AEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1837 LRSVAEEAKKQ--RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE---NDRLK-RKAEEEGYQRKV 1910
Cdd:PRK00409 578 AIKEAKKEADEiiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkvGDEVKyLSLGQKGEVLSI 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141782 1911 LEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRKV 1953
Cdd:PRK00409 658 PDDKEAIVQAGImkmKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTV 703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1625-1864 |
2.06e-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: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1625 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakREA 1704
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-----------AEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1705 KKRAKAEEAALKQKEA--AEMELGNQRKMAEETAKQKLAAE--QELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQ 1780
Cdd:COG4942 89 EKEIAELRAELEAQKEelAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1781 KKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRA 1860
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1207141782 1861 EAEK 1864
Cdd:COG4942 249 AALK 252
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
175-268 |
2.12e-07 |
|
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: 53.07 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 175 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-------------------------- 227
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141782 228 -----LENLEQAFSIAE---RDLG-VTRLLDPEDVDVPHPDEKSIITYVS 268
Cdd:cd21224 82 lsselLANEKRNFKLVQqavAELGgVPALLRASDMSNTIPDEKVVILFLS 131
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1061-1595 |
2.23e-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: 57.44 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1061 KKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVyLDKLKTIDLVIRSTQGAEDILn 1140
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQSQLEII- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1141 kyENQLREVNKVPVNE-KEIEASQTQLqklRSE-AEGKQATFDRLEEELQRATEVNKRMSQLHSERDveleHYRQLVGNL 1218
Cdd:pfam15921 305 --QEQARNQNSMYMRQlSDLESTVSQL---RSElREAKRMYEDKIEELEKQLVLANSELTEARTERD----QFSQESGNL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1219 RERWQAVFAQIELRQRELDLLNRQMQAYRE-------SYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQE------ 1285
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqg 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1286 -KKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAkmESASDDIIQEYVTLRTRYsELMTLS 1364
Cdd:pfam15921 456 kNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNAEITKLRSRV-DLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1365 SQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVD 1444
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1445 SEKQKHNIQR--------ELQELKTLSE--------QEIKA-KSQQVEEALLSRTRIE---EEIHIIRL-------QLET 1497
Cdd:pfam15921 613 KDKKDAKIRElearvsdlELEKVKLVNAgserlravKDIKQeRDQLLNEVKTSRNELNslsEDYEVLKRnfrnkseEMET 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1498 TMK----QKNTAETELLQLR-------------------------AKAVDADKLRNAAQ-----------------EEAE 1531
Cdd:pfam15921 693 TTNklkmQLKSAQSELEQTRntlksmegsdghamkvamgmqkqitAKRGQIDALQSKIQfleeamtnankekhflkEEKN 772
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 1532 KLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1595
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1636-1892 |
3.12e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.99 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1636 QLQEEAEHLkkqQAEADKAREQAEkELETWRQKANEALRL------RLQAEEEANKKTaaqeeaekqkeeakreakkrAK 1709
Cdd:PRK10929 117 QLLEKSRQA---QQEQDRAREISD-SLSQLPQQQTEARRQlneierRLQTLGTPNTPL--------------------AQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1710 AEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFehAEQQRTVLDDELQRLKNDVNSAVKQK-------- 1781
Cdd:PRK10929 173 AQLTALQAESAALKALVDELELAQLSANNR----QELARLRSEL--AKKRSQQLDAYLQALRNQLNSQRQREaeralest 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1782 ---------------------KELEEELIKVRKEMEILLQQKSKAEKETM------------------SNT--------- 1813
Cdd:PRK10929 247 ellaeqsgdlpksivaqfkinRELSQALNQQAQRMDLIASQQRQAASQTLqvrqalntlreqsqwlgvSNAlgealraqv 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1814 ----EKSK-QLLESEAAKMR-------ELAEEATKLRSVAEE-----AKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 1876
Cdd:PRK10929 327 arlpEMPKpQQLDTEMAQLRvqrlryeDLLNKQPQLRQIRQAdgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILEL 406
|
330 340
....*....|....*....|
gi 1207141782 1877 TRLK---TEAEIALKE-KEA 1892
Cdd:PRK10929 407 TKLKvanSQLEDALKEvNEA 426
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1705-1905 |
3.23e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.71 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1705 KKRAKAEEAALKQKEAAEMElgnqrkmAEETAKQK-LAAEQELIRLRADFEhaeqqrtvlddelqrlkndvnsavKQKKE 1783
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-------AEAIKKEAlLEAKEEIHKLRNEFE------------------------KELRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1784 LEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA-KKQRQIAEEEAARQRAEA 1862
Cdd:PRK12704 80 RRNEL----QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207141782 1863 EKILKEKLTAineatrlKTEAEIALKEKEAENdrlkrKAEEEG 1905
Cdd:PRK12704 156 KEILLEKVEE-------EARHEAAVLIKEIEE-----EAKEEA 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1721-1925 |
3.58e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1721 AEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM----- 1795
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1796 ------------EILLQQKSKAEkeTMSNTEKSKQLLESEAAKMRELAEEATKLrsvaEEAKKQRQIAEEEAARQRAEAE 1863
Cdd:COG3883 94 alyrsggsvsylDVLLGSESFSD--FLDRLSALSKIADADADLLEELKADKAEL----EAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 1864 KILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEK 1925
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2274-2436 |
3.69e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 56.76 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2274 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAE 2352
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAiKEAKKEAD 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2353 KLQK------QKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS------------------------LEAERKRQLEITA 2402
Cdd:PRK00409 588 EIIKelrqlqKGGYASVKAHELIEARKRLNKANEKKEKKKKKQkekqeelkvgdevkylslgqkgevLSIPDDKEAIVQA 667
|
170 180 190
....*....|....*....|....*....|....
gi 1207141782 2403 EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2436
Cdd:PRK00409 668 GIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1166-1895 |
3.74e-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: 56.77 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1166 LQKLRSEAEGKQATFDRLEEELQRATEVNK-------RMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELR------ 1232
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFgyksdetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaada 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1233 -----QRELDLLNRQMQAYR----ESY----DWLIRWIADAKQRQDKLHAVPigGSKGLQEQLTQEKKLLEEiEKNKDKV 1299
Cdd:pfam12128 316 avakdRSELEALEDQHGAFLdadiETAaadqEQLPSWQSELENLEERLKALT--GKHQDVTAKYNRRRSKIK-EQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1300 EDCQKfakgYIDAIKD-YELQLVTYKALVEPIASPLKKaKMESASDDIIQEYVTLRTRYSELMTL--SSQYIKFIIETQR 1376
Cdd:pfam12128 393 AGIKD----KLAKIREaRDRQLAVAEDDLQALESELRE-QLEAGKLEFNEEEYRLKSRLGELKLRlnQATATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1377 RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMkDEVSKRQDvavdseKQKHNIQREL 1456
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAL-DELELQLF------PQAGTLLHFL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1457 QELKTLSEQEIkakSQQVEEALLSRTRIEEEIhiirlqLETTMKQKNTAETelLQLRAKAVDADK---LRNAAQEEAEKL 1533
Cdd:pfam12128 541 RKEAPDWEQSI---GKVISPELLHRTDLDPEV------WDGSVGGELNLYG--VKLDLKRIDVPEwaaSEEELRERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1534 RKQVAEETQKKRKAEEELKRKSEAekdaakekkkaledLEKFKLQAEEAERHLKQAElEKQRQIQVVEEVAKKTAATQLE 1613
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGE--------------LEKASREETFARTALKNAR-LDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1614 SKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeea 1693
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG---------- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1694 ekqkeeakreakkrAKAEEAALKQKEAAEMElgnqRKMAEETAKQKLAAE-QELIRLRADFEHAEQQRTVLDDELQrlkn 1772
Cdd:pfam12128 745 --------------AKAELKALETWYKRDLA----SLGVDPDVIAKLKREiRTLERKIERIAVRRQEVLRYFDWYQ---- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1773 dvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET-MSNTEKSKQLLESEAAKMReLAEEATKLRSVaeeakkQRQIA 1851
Cdd:pfam12128 803 --ETWLQRRPRLATQLSNIERAISELQQQLARLIADTkLRRAKLEMERKASEKQQVR-LSENLRGLRCE------MSKLA 873
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141782 1852 EEEAARQRAEAEKILKEKLTAINEaTRLKTEAEIALKEKEAEND 1895
Cdd:pfam12128 874 TLKEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHF 916
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2066-2641 |
3.89e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2066 QVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEkAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEA 2145
Cdd:pfam15921 239 RIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE-ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2146 EAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkqeADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKS 2225
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2226 VLDVELKRL--------------KQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLlEEE 2291
Cdd:pfam15921 395 LEKEQNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL-EST 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2292 AENMKKLAEE--AARLNIEAQEaarlRQIaeSDLAKQRELAEKMLEEKKQAI-----------QEAAKLKAEAEKLQKQk 2358
Cdd:pfam15921 474 KEMLRKVVEEltAKKMTLESSE----RTV--SDLTASLQEKERAIEATNAEItklrsrvdlklQELQHLKNEGDHLRNV- 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2359 dQAQVEAQKLLEAKKemqqrlDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR 2438
Cdd:pfam15921 547 -QTECEALKLQMAEK------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2439 LQETEKHTSEKHtvVEKLEV-----QRLQS----KQEADGLHKAI----ADLEKEKEKLKKEAADLQKQSKEM---ANVQ 2502
Cdd:pfam15921 620 IRELEARVSDLE--LEKVKLvnagsERLRAvkdiKQERDQLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMettTNKL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2503 QEQLQQEKTILQQSffaeKETLLKKekaieeekkklekqfedEVKKAEALKAEQERQRKLMEEerkklQSAMDAAIKKQK 2582
Cdd:pfam15921 698 KMQLKSAQSELEQT----RNTLKSM-----------------EGSDGHAMKVAMGMQKQITAK-----RGQIDALQSKIQ 751
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2583 EAEEEMNGKQKEMQDL--EKKRIEQE-KLLAEENKNLREKLQQLQSSQKASYTK--EIEIQTDK 2641
Cdd:pfam15921 752 FLEEAMTNANKEKHFLkeEKNKLSQElSTVATEKNKMAGELEVLRSQERRLKEKvaNMEVALDK 815
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2278-2491 |
4.08e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2278 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAE--SDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2355
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2356 KQKDQAQVEAqkllEAKKemqqrldQETEGFQKSLEAERKRQleitAEAEklkvkvtqlsdAQSKAEEEAKKFKKQADEI 2435
Cdd:PRK09510 156 AAAAAKKAAA----EAKK-------KAEAEAAKKAAAEAKKK----AEAE-----------AAAKAAAEAKKKAEAEAKK 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 2436 KIRLQETEKHTSEKHTVVEKLEVqrlQSKQEADGLHKAIADLEKEKEKLKKEAADL 2491
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1573-1893 |
4.35e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1573 EKFKLQAEEAERhlKQAELEKQRqiqvveevakktaatqLESKQvaltARLEEslkneqvmviqlqEEAEHLKKQQAEAD 1652
Cdd:PRK05035 434 AKAEIRAIEQEK--KKAEEAKAR----------------FEARQ----ARLER-------------EKAAREARHKKAAE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1653 KAREQAEKELetwrQKANEALRLRlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRK-- 1730
Cdd:PRK05035 479 ARAAKDKDAV----AAALARVKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA----DPKKaa 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1731 --MAEETAKQKLAAEQElirlradfEHAEQQRTVlDDELQRLKNDVNSAVKQKKELEEElikvrkemeillqQKSKAEKE 1808
Cdd:PRK05035 550 vaAAIARAKAKKAAQQA--------ANAEAEEEV-DPKKAAVAAAIARAKAKKAAQQAA-------------SAEPEEQV 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1809 TMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKqrqiAEEEAARQRAEAEKILKEKLTAINEAT----RLKTEAE 1884
Cdd:PRK05035 608 AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRK----AAVAAAIARAKARKAAQQQANAEPEEAedpkKAAVAAA 683
|
330
....*....|
gi 1207141782 1885 IA-LKEKEAE 1893
Cdd:PRK05035 684 IArAKAKKAA 693
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1578-1787 |
4.78e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.24 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1578 QAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLEskqvalTARLEESLKneqvmviqlQEEAEHLKKQQAEADKAREQ 1657
Cdd:TIGR02794 76 QAEEAE---KQRAAEQARQKELEQRAAAEKAAKQAE------QAAKQAEEK---------QKQAEEAKAKQAAEAKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1658 AEKEletwRQKANEALRlrlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAK 1737
Cdd:TIGR02794 138 AEAE----RKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1738 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1787
Cdd:TIGR02794 211 AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1158-1686 |
4.83e-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: 56.29 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1158 EIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELE-HYRQLVGNLRERWQAVFAQIELRQREL 1236
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1237 DLLNRQMQAYRESYDWL-------------IRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQ 1303
Cdd:pfam05557 83 KYLEALNKKLNEKESQLadarevisclkneLSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1304 KFAKGYIDAIKD--YELQLVTYKALVepiaspLKKAKMESAS-DDIIQEYVTLRTRYSELMTLSSQyiKFIIETQ----- 1375
Cdd:pfam05557 163 SSLAEAEQRIKEleFEIQSQEQDSEI------VKNSKSELARiPELEKELERLREHNKHLNENIEN--KLLLKEEvedlk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1376 RRLQDEEKaAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSE-KQKHNIQ 1453
Cdd:pfam05557 235 RKLEREEK-YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1454 RELQE-----LKTLSEQEIKAKSQQVEEALLSRTRI--EEEIHIIRLQL-----ETTMKQKNTAETELLQLRAKAVDADK 1521
Cdd:pfam05557 314 RELEQelaqyLKKIEDLNKKLKRHKALVRRLQRRVLllTKERDGYRAILesydkELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1522 LRNA--------AQEEAE--KLRKQVAEETQKKRKAEEELKRKSeaekDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL 1591
Cdd:pfam05557 394 AHNEemeaqlsvAEEELGgyKQQAQTLERELQALRQQESLADPS----YSKEEVDSLRRKLETLELERQRLREQKNELEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1592 EKQRQIQVVEEVAKKTAATQLESKQvalTARLEESLKNeqvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN- 1670
Cdd:pfam05557 470 ELERRCLQGDYDPKKTKVLHLSMNP---AAEAYQQRKN---QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFk 543
|
570
....*....|....*.
gi 1207141782 1671 EALRLRLQAeEEANKK 1686
Cdd:pfam05557 544 EVLDLRKEL-ESAELK 558
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1439-1661 |
5.26e-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: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1439 QDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvd 1518
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1519 aDKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-----QAELEK 1593
Cdd:COG4942 93 -AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAelaalRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 1594 QRQIQVV---EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKE 1661
Cdd:COG4942 172 ERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1729-1868 |
6.05e-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: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1729 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR---------KEMEILL 1799
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 1800 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 1868
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1261-1596 |
6.34e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1261 KQRQDKLHavpiggsKGLQEQLTQEKK-LLEEIEKNKdKVEDCQKFAKGYID---AI-KDYELQLVTYKALVEPIASPLK 1335
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDrqaAIyAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1336 KAKMESASDDIIQEYVTlRTRYSELMTLSSQyikfiiETQRRLQDEEKAAEKLKEEERkkmaEMQAELEKQKQLAEThak 1415
Cdd:pfam17380 359 KRELERIRQEEIAMEIS-RMRELERLQMERQ------QKNERVRQELEAARKVKILEE----ERQRKIQQQKVEMEQ--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1416 aIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHniQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEihiirlql 1495
Cdd:pfam17380 425 -IRAEQEEARQREVRRLEEERAREMERVRLEEQER--QQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQ-------- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1496 ettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF 1575
Cdd:pfam17380 493 -----RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340
....*....|....*....|...
gi 1207141782 1576 KLQAEEAERHLKQ--AELEKQRQ 1596
Cdd:pfam17380 567 RLEAMEREREMMRqiVESEKARA 589
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2022-2164 |
6.42e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2022 KQIQAAEEEAARQHKAAQEEVgrlmklAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKL 2101
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQA------EEAAAKAAAAAKAKAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKK 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2102 KEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEA 2164
Cdd:PRK09510 186 KAEAEAAAKAAAEAKkKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1402-1884 |
6.72e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1402 ELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIqRELQELKTLSEQ---------EIKAKSQ 1472
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEyiklsefyeEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1473 QVEEALlsrTRIEEEIHIIRLQL----------ETTMKQKNTAETELLQLRAKAVDADKLRnAAQEEAEKLRKQVAEETQ 1542
Cdd:PRK03918 311 EIEKRL---SRLEEEINGIEERIkeleekeerlEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1543 KKRKAE-EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQA---------ELEKQRQIQVVEEVAKKTAATql 1612
Cdd:PRK03918 387 EKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEYTAELKRI-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1613 eSKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANK-KTAAQE 1691
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1692 EAEKQKEEAKREAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR 1769
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELlkELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1770 LKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQ 1849
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
490 500 510
....*....|....*....|....*....|....*...
gi 1207141782 1850 IAEEEAARQRAEAEKILK--EKLTAINEATR-LKTEAE 1884
Cdd:PRK03918 701 EELEEREKAKKELEKLEKalERVEELREKVKkYKALLK 738
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4166-4194 |
7.14e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 7.14e-07
10 20
....*....|....*....|....*....
gi 1207141782 4166 IVDPETGKEMSVYEAYRKGLIDHQTYIEL 4194
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1522-1963 |
9.30e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1522 LRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVE 1601
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1602 EVAKKTAATQLESKQVALTARLEEsLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA--------EKELETWRQKANEAL 1673
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1674 RLRLQAEEEANKKTAAQEEAEKQKEEAkrEAKKRAKAEEAALKQKE------AAEMELGNQRKMAEETAKQKLAAEQELI 1747
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1748 RLRAD-FEHAEQQRTVLDDELQRLkndvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAK 1826
Cdd:COG4717 284 GLLALlFLLLAREKASLGKEAEEL----QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1827 MRELAEEAtkLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEND--RLKRKAEEE 1904
Cdd:COG4717 360 EEELQLEE--LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1905 GYQRKVLEDQAAQHKQAIEEKIGQLKK-SSDTELDRQKKIVEETLKQRKVVEEEIHILKL 1963
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1737-2444 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1737 KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKeTMSNTEKS 1816
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK-NIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1817 KQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE---EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1893
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKdniEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1894 NDRLKRKAEEegyqrkvLEDQAAQHKQAIE----EKIGQLKKSSDTELDRQKKIVEETlkQRKVVEEEIHILKLNfekas 1969
Cdd:TIGR04523 276 LEQNNKKIKE-------LEKQLNQLKSEISdlnnQKEQDWNKELKSELKNQEKKLEEI--QNQISQNNKIISQLN----- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1970 sgkqelelelkklkgiadetqkskakaeeeaekfrklaleeekkrkeaeakvKQIQAAEEEaarqhkaaqeevgRLMKLA 2049
Cdd:TIGR04523 342 ----------------------------------------------------EQISQLKKE-------------LTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2050 EEAKKQKEIAEKEAEKQVILVQEAAQKcsaaeQKAQNVLVQQNkdsmaqdKLKEEFEKAKKLAQEAEKAKDNAEKEAALL 2129
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYK-----QEIKNLESQIN-------DLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2130 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLaEKTLKQKssvEEE 2209
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE----------SLETQLKVLSRSINKI-KQNLEQK---QKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2210 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDllklklkiekENQELMKKDKDNTKKLLE 2289
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD----------LEDELNKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2290 EEAENMKKLAEEaarlnieaqeaarLRQIAESDLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2366
Cdd:TIGR04523 561 KEIDEKNKEIEE-------------LKQTQKSLKKKQEEKQELIDQkekEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2367 KLLEAKK---EMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2443
Cdd:TIGR04523 628 KLSSIIKnikSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLP 707
|
.
gi 1207141782 2444 K 2444
Cdd:TIGR04523 708 K 708
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2022-2207 |
1.28e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2022 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmAQDKL 2101
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---AEAKK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2102 KEEFEKAKKLAQEA-EKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALK 2180
Cdd:PRK09510 170 KAEAEAAKKAAAEAkKKAEAEAAAKAAAEAKKKAEAEA------------------KKKAAAEAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*..
gi 1207141782 2181 LKQEADSEMAKYKKLAEKTLKQKSSVE 2207
Cdd:PRK09510 232 AEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2392-2614 |
1.37e-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: 54.00 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2392 AERKRQLEitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLH 2471
Cdd:COG4942 19 ADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2472 KAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQ--QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2549
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2550 EALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENK 2614
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1751-2490 |
1.49e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 54.73 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1751 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKsKAEKETMSNTEKSKQLLESEAAKMREL 1830
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQR-KAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1831 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIAlkEKEAENDRLKrkaeeegYQRKV 1910
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAENARLE-------MHFKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1911 LEDQaaqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAssgkQELELELKKLKGIADETQ 1990
Cdd:pfam05483 218 KEDH---------EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES----RDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1991 KskakaeeeaekfrklalEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEV----GRLMKLAEEAKKQKEIAEKEAEKQ 2066
Cdd:pfam05483 285 K-----------------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiatKTICQLTEEKEAQMEELNKAKAAH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2067 VILVQE-AAQKCSAAEQ-KAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAE 2144
Cdd:pfam05483 348 SFVVTEfEATTCSLEELlRTEQQRLEKNEDQLKI--ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2145 AeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQK 2224
Cdd:pfam05483 426 Q-----------FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2225 SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ----------MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEN 2294
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQeermlkqienLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2295 MKKLAEEAarlnIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKE 2374
Cdd:pfam05483 575 ARSIEYEV----LKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKALKKKGSAE--NKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2375 MQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK-----------KFKKQADEIkIRLQETE 2443
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmeKHKHQYDKI-IEERDSE 726
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2444 -----KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2490
Cdd:pfam05483 727 lglykNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
53-152 |
1.49e-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: 49.96 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 53 DRVQKKTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLKHRQVK 128
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1207141782 129 LVNIRNDDIADGNPKLTLGLIWTI 152
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1421-1765 |
1.50e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1421 EQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSeqeikAKSQQVEEALLSRTRIEEEIHIIRLQlETTMK 1500
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERRQKRLQ-EALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1501 QKNTAETellQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE--LKRKSEAEKDAAKEKKKALEDLEKFKLQ 1578
Cdd:pfam02029 86 QKEFDPT---IADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1579 AEEAERHLKQAEL-EKQRQIQVVEEVAKKTAATQLESKQVALTarlEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQ 1657
Cdd:pfam02029 163 SEEAEEVPTENFAkEEVKDEKIKKEKKVKYESKVFLDQKRGHP---EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1658 AEKELETwrQKANEALRLRLQA--EEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEET 1735
Cdd:pfam02029 240 AEVFLEA--EQKLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE----RKLREEE 313
|
330 340 350
....*....|....*....|....*....|
gi 1207141782 1736 AKQKLaaEQELIRLRAdfEHAEQQRTVLDD 1765
Cdd:pfam02029 314 EKRRM--KEEIERRRA--EAAEKRQKLPED 339
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1756-1926 |
1.53e-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: 52.62 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1756 AEQQRTVLDdeLQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLESEAAKMRELAEEAT 1835
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1836 KLrsvAEEAKKQRQIA-----EEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKV 1910
Cdd:COG1579 80 EQ---LGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1207141782 1911 LEDQAAQHKQAIEEKI 1926
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2415-2630 |
1.62e-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: 54.00 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2415 SDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQ 2494
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2495 SKEmanvQQEQLQQEKTILQQSFFAEKETLL------KKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERK 2568
Cdd:COG4942 99 LEA----QKEELAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2569 KLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKAS 2630
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1738-1933 |
1.80e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1738 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSK 1817
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1818 Q-----------LLESEAAKmrELAEEATKLRSVAEEAKK---QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 1883
Cdd:COG3883 96 YrsggsvsyldvLLGSESFS--DFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1884 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSS 1933
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1779-1926 |
1.83e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.72 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1779 KQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSV---------AEEAKKQRQ 1849
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEAnaerevqrqLEIAERERE 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 1850 IAEEEAARQRAEAEKILKEKLTAinEATRLKTEAEialKEKEAENDRLKRKAEEEGYQRKVlEDQAAQHKQAIEEKI 1926
Cdd:COG2268 292 IELQEKEAEREEAELEADVRKPA--EAEKQAAEAE---AEAEAEAIRAKGLAEAEGKRALA-EAWNKLGDAAILLML 362
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1762-1962 |
1.88e-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: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1762 VLDDelQRLKNDVNSAVKQKKEL---EEELIKVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAA--KMRELA 1831
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDLeraHEALEDAREQIELLepireLAERYAAARERLAELEYLRAALRLWFAqrRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1832 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA----INEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 1907
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 1908 ----RKVLEDQAAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 1962
Cdd:COG4913 375 lpasAEEFAALRAEAAALLEA-LEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
642-734 |
1.99e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 642 HAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTA 721
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1207141782 722 ALQTQWSWILQLC 734
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2291-2433 |
2.41e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.34 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2291 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQkDQAQVEA- 2365
Cdd:COG2268 187 DALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAEleqeREIETARIAEAEAELAKKKAEERREA-ETARAEAe 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2366 QKLLEAKKEMQQRLDQETEgfqkslEAERKRQLEItAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2433
Cdd:COG2268 266 AAYEIAEANAEREVQRQLE------IAEREREIEL-QEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2310-2587 |
3.69e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.41 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2310 QEAARLRQIAE----SDLAKQR-ELAEKMLEEKKQAiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrlDQETE 2384
Cdd:PRK05035 433 QAKAEIRAIEQekkkAEEAKARfEARQARLEREKAA--REARHKKAAEARAAKDKDAVAAALARVKAKK------AAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2385 GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA----DEIKIRLQETEKHTSEKHTVVEKLEVQR 2460
Cdd:PRK05035 505 PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiarAKAKKAAQQAANAEAEEEVDPKKAAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2461 LQSKQEAdglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQ---QEQLQQEKTILQQSFFAEKETLlkkekaieeekkk 2537
Cdd:PRK05035 585 AIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARakaKKAEQQANAEPEEPVDPRKAAV------------- 648
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2538 lekqfEDEVKKAEALKAEQER--QRKLMEEERKKLQSAMDAAIKKQKEAEEE 2587
Cdd:PRK05035 649 -----AAAIARAKARKAAQQQanAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1777-2646 |
3.85e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1777 AVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlRSVAEEAKKQRQIAEEEAA 1856
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITS-KEAQLESSREIVKSYENEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1857 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE-------------EGYQRKVLEDQaaQHKQAIE 1923
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyHNHQRTVREKE--RELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1924 EKIGQLKKSSdTELDRQKK--IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKA-KAEEEA 2000
Cdd:TIGR00606 326 RELEKLNKER-RLLNQEKTelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTlVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2001 EKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAK-KQKEIAEKEAEKQVILVQEAAQKCSA 2079
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKfVIKELQQLEGSSDRILELDQELRKAE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2080 AEqkaqnvLVQQNKDSMAQDKLKEEF----EKA---KKLAQEAEK-AKDNAEKEA-----ALLHKKAEEAERQKKAAEAE 2146
Cdd:TIGR00606 485 RE------LSKAEKNSLTETLKKEVKslqnEKAdldRKLRKLDQEmEQLNHHTTTrtqmeMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2147 AAKQAKAQEDAEKlRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSv 2226
Cdd:TIGR00606 559 SDELTSLLGYFPN-KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD- 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2227 LDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD------NTKKLLEEEAENMKKLAE 2300
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAElqefisDLQSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2301 EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKD--QAQVEAQKLLEAKKEMQQR 2378
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtiMPEEESAKVCLTDVTIMER 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2379 LDQETEGFQKSLEAERKR------QLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTV 2452
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKlqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2453 VE------KLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN-------VQQEQLQQEKTILQQSFFA 2519
Cdd:TIGR00606 877 GTnlqrrqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISsketsnkKAQDKVNDIKEKVKNIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2520 EKETllkkEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ----------------KE 2583
Cdd:TIGR00606 957 MKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqdnltlrkrenelKE 1032
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141782 2584 AEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEE 2646
Cdd:TIGR00606 1033 VEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2280-2476 |
4.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2280 DKDNTKKLLEEEAENMKKL--AEEAARlnIEAQEAARLRQI---------AESDLAKQREL--------AEKMLEEKKQA 2340
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLerAHEALE--DAREQIELLEPIrelaeryaaARERLAELEYLraalrlwfAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2341 I----QEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKvkvTQLSD 2416
Cdd:COG4913 297 LeelrAELARLEAELERLEARLDALR---EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2417 AQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAD 2476
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1414-1654 |
4.05e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1414 AKAIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEallsrtrIEEEIHIIRL 1493
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1494 QLETTMKQKNTAETELLQLR---AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALE 1570
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1571 DLEKfKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQEEAEHLKKQQAE 1650
Cdd:COG4942 164 ALRA-ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAA 238
|
....
gi 1207141782 1651 ADKA 1654
Cdd:COG4942 239 AAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1469-1718 |
4.95e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1469 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1548
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1549 EELK-RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE----LEKQRQIQVVEEVAKKTAATQLESKQVALTARL 1623
Cdd:COG4942 97 AELEaQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkyLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1624 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKRE 1703
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA-----------------AAA 239
|
250
....*....|....*
gi 1207141782 1704 AKKRAKAEEAALKQK 1718
Cdd:COG4942 240 AERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1673-2091 |
5.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1673 LRLRLQAE-EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE------ETAKQKLAAEQE 1745
Cdd:COG4717 47 LLERLEKEaDELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEaeleelREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1746 LIRLRADFEHAEQQRTVLDDELQRLKN---DVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT--------- 1813
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaeeleelqq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1814 --EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAArQRAEAEKILKEKLTAINEATRLKTEAEIAL---- 1887
Cdd:COG4717 207 rlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1888 ------------KEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDT-----ELDRQKKIVEETLkQ 1950
Cdd:COG4717 286 lallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELEEEL-Q 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1951 RKVVEEEIHILkLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEE 2030
Cdd:COG4717 365 LEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 2031 AARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQ 2091
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELE----ELKAELRELAEEWAALKLALE 500
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2156-2629 |
5.17e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2156 DAEKLRKEAEKEASRRAEAEAAALKLK---------QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqlDETDKQKSV 2226
Cdd:pfam12128 235 GIMKIRPEFTKLQQEFNTLESAELRLShlhfgyksdETLIASRQEERQETSAELNQLLRTLDDQWKEKR--DELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2227 LDVELKRLKQEVSDAIKQKAQVEDE-LSKVKIQMEDLLKLKLKIEKENQELmkkdkdntkKLLEEEAENMKKlAEEAARL 2305
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---------KALTGKHQDVTA-KYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2306 NIEAQEAARLRQIaESDLAKQRELAEKMLEEKKQAIQeaaKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET- 2383
Cdd:pfam12128 383 KIKEQNNRDIAGI-KDKLAKIREARDRQLAVAEDDLQ---ALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2384 --------EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEK-HTVVE 2454
Cdd:pfam12128 459 tpelllqlENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQaGTLLH 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2455 KLevqRLQSKQEADGLHKAIADLEKEKeklkkeaADLQKQSKEMANVQQEQLQQEKTILQQ----SFFAEKETLlkkeka 2530
Cdd:pfam12128 539 FL---RKEAPDWEQSIGKVISPELLHR-------TDLDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEEL------ 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2531 ieeekKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLA 2610
Cdd:pfam12128 603 -----RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK---NKALA 674
|
490
....*....|....*....
gi 1207141782 2611 EENKNLREKLQQLQSSQKA 2629
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQ 693
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1523-1738 |
5.21e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1523 RNAAQEEAEKLRKQVAE----ETQKKRKAEEELKRkseAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQaELEKQRQIQ 1598
Cdd:pfam15709 328 REQEKASRDRLRAERAEmrrlEVERKRREQEEQRR---LQQEQLERAEKMREELELEQQRRFEEIRLRKQ-RLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1599 VVEEvakKTAATQLESKQVALTARLEESLKNEQvmviQLQEeaehlKKQQAEADKAREQAEKELETWRQKANEALRLRLQ 1678
Cdd:pfam15709 404 EEEE---RKQRLQLQAAQERARQQQEEFRRKLQ----ELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1679 AEEEankktaaqeEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQ 1738
Cdd:pfam15709 472 AEEE---------RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2221-2436 |
5.46e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2221 DKQKSVLDVELKRLKQEvsdaikqkAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE--AENMKKL 2298
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE--------QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2299 AEEAARLNIEAQeaarlrQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQr 2378
Cdd:PRK09510 141 AAAAAKAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA- 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2379 ldqetegfqkslEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2436
Cdd:PRK09510 214 ------------EAKKK------AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2289-2425 |
5.51e-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: 52.70 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2289 EEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA------------KLKAEAEKLQK 2356
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtsspkedkqvaeNQKREIEKAQI 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 2357 QKDQAQVEAQKLLEAKKE--MQQRLDQETEGFQKSLEAERKRqLEITAEAEKLKVKVtqlsDAQSKAEEEA 2425
Cdd:pfam05262 289 EIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQV----EAQPTSLNED 354
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2027-2571 |
5.66e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.80 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2027 AEEEAARQHKAAQEEVGRLMKLAEEAkkQKEIAEKEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQ-------- 2098
Cdd:pfam05483 206 AENARLEMHFKLKEDHEKIQHLEEEY--KKEINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQleektklq 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2099 -DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE---KEASRRAEA 2174
Cdd:pfam05483 281 dENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2175 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVK----VQLDE-------------TDKQKSVLDVELKRLKQE 2237
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkeVELEElkkilaedeklldEKKQFEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2238 VSDAIKQKaqvEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQ 2317
Cdd:pfam05483 441 LIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVED-LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2318 IAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2397
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2398 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQ--ADEIKIRLQETEKHTSEK------HTVVEKLEVQRLQSKQEADG 2469
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQlnAYEIKVNKLELELASAKQkfeeiiDNYQKEIEDKKISEEKLLEE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2470 LHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2549
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
570 580
....*....|....*....|..
gi 1207141782 2550 EALKAEQERQRKLMEEERKKLQ 2571
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEKLK 773
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
160-268 |
5.82e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 48.26 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 160 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIA 238
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|
gi 1207141782 239 ERDLGVTRLLDPEDVDVPHPDEKSIITYVS 268
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLS 107
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1702-2137 |
5.94e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1702 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1781
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1782 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 1861
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1862 AEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 1941
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1942 KIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKV 2021
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2022 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2101
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1207141782 2102 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAE 2137
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAAL 517
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1636-1925 |
6.25e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1636 QLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLR-----LQ---AEEEANKKTAAQEEAEKQKEEAKREAKKR 1707
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREELAEEVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1708 AKAEEAAL----------------KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLK 1771
Cdd:PRK02224 297 DLLAEAGLddadaeavearreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1772 NDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnteksKQLLESEAAKMRE-LAEEATKLRSVAEEAKKQRQI 1850
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF--------LEELREERDELRErEAELEATLRTARERVEEAEAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1851 AEE-----------------EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEnDRLKRKAEeegyQRKVLED 1913
Cdd:PRK02224 449 LEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE----RREDLEE 523
|
330
....*....|..
gi 1207141782 1914 QAAQHKQAIEEK 1925
Cdd:PRK02224 524 LIAERRETIEEK 535
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1588-1808 |
6.97e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1588 QAELEKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvmviQLQEEaehlKKQQAEADKAREQAEKELETWRQ 1667
Cdd:PRK09510 74 AKRAEEQRKKKE------QQQAEELQQKQAAEQERLKQLEKERL----AAQEQ----KKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1668 KANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEli 1747
Cdd:PRK09510 140 KAAAAAKAKAEAEAKR-----------------AAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK-- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 1748 rlradfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1808
Cdd:PRK09510 201 ------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
51-159 |
7.02e-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: 48.06 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 51 ERDRVQKKTFTKWVNKhlVKAQRHITDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 121
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141782 122 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 159
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2207-2636 |
7.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2207 EEELVKVKVQLDETDKQKSvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKK 2286
Cdd:PRK02224 212 ESELAELDEEIERYEEQRE----QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2287 LLEEEAENMKKLAE-EAARLNIEAQEAARlrqiaeSDLAKQRELAEKMLEEKKQAIQEAAKlkaEAEKLQKQKDQAQVEA 2365
Cdd:PRK02224 288 LEELEEERDDLLAEaGLDDADAEAVEARR------EELEDRDEELRDRLEECRVAAQAHNE---EAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2366 QKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKH 2445
Cdd:PRK02224 359 EELREEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2446 TSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLqkqSKEMANVQQEQLQQEKTILQQSFFAEketll 2525
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEEL---EAELEDLEEEVEEVEERLERAEDLVE----- 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2526 kkekaieeekkkLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQ 2605
Cdd:PRK02224 507 ------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
410 420 430
....*....|....*....|....*....|....*
gi 1207141782 2606 EKLLAE--ENKNLREKLQQLQSSQK--ASYTKEIE 2636
Cdd:PRK02224 575 AELNSKlaELKERIESLERIRTLLAaiADAEDEIE 609
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1135-1795 |
7.30e-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: 52.74 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1135 AEDILNKYENQLREVNKVPVNEKEI-EASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQ 1213
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1214 L------------VGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYD----------WLIRWIADAKQRQDKLHAVP 1271
Cdd:TIGR00606 504 KslqnekadldrkLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiksrhsdeltSLLGYFPNKKQLEDWLHSKS 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1272 iGGSKGLQEQLTQEKKLLEEIEKNKD--------KVEDCQKFAKGYIDAIKDYELQlVTYKALVEPIASPLKKAKMESAS 1343
Cdd:TIGR00606 584 -KEINQTRDRLAKLNKELASLEQNKNhinnelesKEEQLSSYEDKLFDVCGSQDEE-SDLERLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1344 DDIIQEYVTLRTRYSE----LMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAK 1419
Cdd:TIGR00606 662 TAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1420 AEQEANELKTKMkdevskrQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTM 1499
Cdd:TIGR00606 742 KEKEIPELRNKL-------QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1500 KQKNTAETELLQLRAKAVDAD-KLRNAAQ--EEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1576
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQhELDTVVSkiELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1577 LQAEEAERHLKQAElekqrqiqvVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHL--------KKQQ 1648
Cdd:TIGR00606 895 TEVQSLIREIKDAK---------EQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdieNKIQ 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1649 AEADKAREQAEKELETWRQKANEALRLRLQAEEEankktaaqeeaekqkEEAKREAKKRAKAEEAALkQKEAAEMELGNQ 1728
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLEECEKHQEKINED---------------MRLMRQDIDTQKIQERWL-QDNLTLRKRENE 1029
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 1729 RKMAEETAKQKLAAEQELIRLRADFEHAEqqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1795
Cdd:TIGR00606 1030 LKEVEEELKQHLKEMGQMQVLQMKQEHQK-----LEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1336-1912 |
8.03e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1336 KAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELE----KQKQLAE 1411
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1412 THAKAIAK--AEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEqEIKAKSQQVEEALLS-----RTRI 1484
Cdd:pfam05557 88 LNKKLNEKesQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNlekqqSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1485 EEEIHIIRLQLETTMKQKNTAETELLQLR-AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAeEELKRKSEAEKDAAK 1563
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIENKLLLKEEV-EDLKRKLEREEKYRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1564 EKKKALEDLEKFKLQAEEAERhlkqaeLEKQRQIQVVEEVAKKTAATQLESKQVALTAR---LEESLKNEQVMVIQLQEE 1640
Cdd:pfam05557 246 EAATLELEKEKLEQELQSWVK------LAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEnssLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1641 AEHLKKQQAEADKAREQAEKELETWRQKANEALRLR--LQAEEEANKKTAAQEEAEKQKEEAKREAKK---RAKAEEAAL 1715
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgYRAILESYDKELTMSNYSPQLLERIEEAEDmtqKMQAHNEEM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1716 K-QKEAAEMELGNQRKMAEetakqklAAEQELIRLRADFEHAEQQRTvlddelqrlKNDVNSAVKQKKELEEELIKVRKE 1794
Cdd:pfam05557 400 EaQLSVAEEELGGYKQQAQ-------TLERELQALRQQESLADPSYS---------KEEVDSLRRKLETLELERQRLREQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1795 MEILLQQKSKAEKETMSNTEKSK--QLLESEAAKMRE-LAEEATKLRsvaeeakkqrqiAEEEAARQRAEAEKILKEKLT 1871
Cdd:pfam05557 464 KNELEMELERRCLQGDYDPKKTKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVL 531
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1207141782 1872 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLE 1912
Cdd:pfam05557 532 RLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2189-2397 |
8.10e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.38 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2189 MAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAikQKAQVEDELSKVKIQMEdllklklk 2268
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE--KAAKQAEQAAKQAEEKQ-------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2269 iekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARL-----NIEAQEAARLRQ-----IAESDLAKQRELAEKMLEEKK 2338
Cdd:TIGR02794 119 ----KQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQaeeeaKAKAAAEAKKKAeeakkKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 2339 QAIQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2397
Cdd:TIGR02794 195 KAKAEAAKAKAAAE--AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
48-156 |
8.18e-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: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 48 CADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLK 123
Cdd:cd21306 9 HAPDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQ 88
|
90 100 110
....*....|....*....|....*....|...
gi 1207141782 124 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 156
Cdd:cd21306 89 DAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1425-1972 |
8.30e-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: 52.33 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1425 NELKTKmKDEVSKRQDVAVDSEKQKHNIQRELQELKTlSEQEIKAKSQQVEEALlsrTRIEEEIHIIRLQLETTMKQKNT 1504
Cdd:TIGR04523 47 NELKNK-EKELKNLDKNLNKDEEKINNSNNKIKILEQ-QIKDLNDKLKKNKDKI---NKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1505 AETELLQLRAKAvdadklrnaaqEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1584
Cdd:TIGR04523 122 LEVELNKLEKQK-----------KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1585 HLKQAELEKQRQIQVVEEvakktaatqLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAeKELET 1664
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKK---------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL-NQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1665 WRQKANEALRLRLQAEEEANKKTAAQEEAEkqkeeakreakKRAKAEEAALKQKEAAEMelgnQRKMAEETAKQklaaEQ 1744
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQL-----------NQLKSEISDLNNQKEQDW----NKELKSELKNQ----EK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1745 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKaEKETMSNTEKSKQLLESea 1824
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-YKQEIKNLESQINDLES-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1825 aKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEkltaINEATRLKTEAEIALKEKEAENDRLKRKAEEE 1904
Cdd:TIGR04523 399 -KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 1905 GYQRKVLEDQAAQHKQAIEEKIGQLKKssdteLDRQKKIVEETLkqrKVVEEEIHILKLNFEKASSGK 1972
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKK-----LNEEKKELEEKV---KDLTKKISSLKEKIEKLESEK 533
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
56-163 |
8.67e-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: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 56 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 122
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141782 123 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 163
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2492-2658 |
8.78e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2492 QKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2571
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2572 SAMDaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKnlREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT 2651
Cdd:pfam15709 434 ELQR---KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE--EERLEYQRQKQEAEEKARLEAEERRQKEEEAARLA 508
|
....*..
gi 1207141782 2652 MVETTKK 2658
Cdd:pfam15709 509 LEEAMKQ 515
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2275-2449 |
8.86e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2275 ELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEA--E 2352
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2353 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQEtegfqksLEAERKRQLEItAEAEKLKVKvTQLSDAQSKAEEEAKKFKKQA 2432
Cdd:pfam15709 431 KLQELQRKKQQEEAERAEAEKQRQKELEMQ-------LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEERRQKE 501
|
170
....*....|....*...
gi 1207141782 2433 DE-IKIRLQETEKHTSEK 2449
Cdd:pfam15709 502 EEaARLALEEAMKQAQEQ 519
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1619-1957 |
8.86e-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: 51.82 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1619 LTARLEESLKnEQVMVIQLQEEAehlkKQQAEADKAREQAEKEleTWRQKANEaLRLRLQAEEEANKKTaaqeeaekqke 1698
Cdd:pfam07888 32 LQNRLEECLQ-ERAELLQAQEAA----NRQREKEKERYKRDRE--QWERQRRE-LESRVAELKEELRQS----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1699 eakreakkRAKAEEAALKQKEAAEMelgnQRKMAEETA---KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1775
Cdd:pfam07888 93 --------REKHEELEEKYKELSAS----SEELSEEKDallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1776 SAVKQKKELEEElikvRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAkkQRQIAEEEA 1855
Cdd:pfam07888 161 KAGAQRKEEEAE----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA--HRKEAENEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1856 ARQRAEAekiLKEKLTAINEATR-LKTEaeiaLKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ------ 1928
Cdd:pfam07888 235 LLEELRS---LQERLNASERKVEgLGEE----LSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARwaqere 307
|
330 340 350
....*....|....*....|....*....|
gi 1207141782 1929 -LKKSSDTELDRQKKIVEETLKQRKVVEEE 1957
Cdd:pfam07888 308 tLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2274-2641 |
9.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2274 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES--DLAKQRELAEKMLEEKKQAIQ------EAA 2345
Cdd:COG4717 56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQllplyqELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2346 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2425
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2426 KKFKKQADEIKIRLQETEKhTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA--------------DL 2491
Cdd:COG4717 216 EEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallfllLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2492 QKQSKEMANVQQEQLQQEKTILQQsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-----EALKAEQERQRKLMEEE 2566
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEE---EELEELLAALGLPPDLSPEELLELLDRIEELqellrEAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2567 RKKLQSAMDA-----------AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENknLREKLQQLQSSQKASYTKEI 2635
Cdd:COG4717 372 IAALLAEAGVedeeelraaleQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELE 449
|
....*.
gi 1207141782 2636 EIQTDK 2641
Cdd:COG4717 450 ELREEL 455
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1424-1884 |
9.15e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1424 ANELKTKMKDEVSKRQDVA-----VDSEKQKHN-IQRELQELK---TLSEQEIKAKS---QQVEEALLSRTRIE---EEI 1488
Cdd:PRK04863 278 ANERRVHLEEALELRRELYtsrrqLAAEQYRLVeMARELAELNeaeSDLEQDYQAASdhlNLVQTALRQQEKIEryqADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1489 HIIRLQLETTMKQKNTAETELLQLRAKAvdadklrNAAQEEAEKLRKQVAEETQkkrkAEEELKRKSeaekdaakekkka 1568
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARA-------EAAEEEVDELKSQLADYQQ----ALDVQQTRA------------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1569 ledlekfkLQAEEAerhlKQAeLEKQRQIQVVEEVAKKTAATQLEskqvALTARLEEslkneqvmviqLQEEAEHLKKQQ 1648
Cdd:PRK04863 414 --------IQYQQA----VQA-LERAKQLCGLPDLTADNAEDWLE----EFQAKEQE-----------ATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1649 AEADKAREQAEKELETWRQKANEALRLrlQAEEEAnkktaaqeeaekqkeeakREAKKRAKAEEAALKQKEAAEMELGnq 1728
Cdd:PRK04863 466 SVAQAAHSQFEQAYQLVRKIAGEVSRS--EAWDVA------------------RELLRRLREQRHLAEQLQQLRMRLS-- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1729 rkmaeeTAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEillQQKSKAEKE 1808
Cdd:PRK04863 524 ------ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALR---QQLEQLQAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1809 TMSNTEKSKQLLESEAA--KMRELAEEATK--------LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR 1878
Cdd:PRK04863 595 IQRLAARAPAWLAAQDAlaRLREQSGEEFEdsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPR 674
|
....*.
gi 1207141782 1879 LKTEAE 1884
Cdd:PRK04863 675 LNALAE 680
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1795-2127 |
9.96e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1795 MEILLQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklrsVAEEAKKQRQIAEEEAARQRAeaekiLKEKLTAIN 1874
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQ------ERLRQEKEE------KAREVERRRKLEEAEKARQAE-----MDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1875 EATRLKTEAE-----IALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQlkkssDTELDRQKKIVEETlK 1949
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ-----ELEAARKVKILEEE-R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1950 QRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLalEEEKKRKEAEAKVKQIQAAEE 2029
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ--EEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2030 EAARQHKAAQEEVGRLMKLAEEAKKQKeIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEFEKA 2108
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRK-LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQmRKATEERSRL 568
|
330
....*....|....*....
gi 1207141782 2109 KKLAQEAEKAKDNAEKEAA 2127
Cdd:pfam17380 569 EAMEREREMMRQIVESEKA 587
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1601-1823 |
9.98e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1601 EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQA- 1679
Cdd:pfam15709 317 EEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRl 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1680 ------EEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEEtaKQKLAAEQELIRLRADF 1753
Cdd:pfam15709 397 eeerqrQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKEL--EMQLAEEQKRLMEMAEE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1754 EHAEQQRtvlddelqrlkndvnsavkQKKELEEeliKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESE 1823
Cdd:pfam15709 475 ERLEYQR-------------------QKQEAEE---KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2158-2430 |
1.16e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2158 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKV---KVQLDETDKQKSVLDVELKRL 2234
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2235 KQEVSDAIKQKAQVeDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAAR 2314
Cdd:COG1340 98 RKELAELNKAGGSI-DKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2315 LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAER 2394
Cdd:COG1340 175 EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELKKLR 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207141782 2395 KRQLEITAEAEKlkvkvtqlSDAQSKAEEEAKKFKK 2430
Cdd:COG1340 251 KKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1405-1796 |
1.16e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1405 KQKQLAEThAKAIAKAEQEANELKTKMKDevsKRQDVavdSEKQKHniqreLQELKTLSEQEIKAKSQQVEEALL----- 1479
Cdd:PRK10246 438 QQKRLAQL-QVAIQNVTQEQTQRNAALNE---MRQRY---KEKTQQ-----LADVKTICEQEARIKDLEAQRAQLqagqp 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1480 -------SRTRIEE----EIHIIRLQLETTMKQKNTAETELLQLRAKaVDAdklrnaaqeeaekLRKQV---AEETQKKR 1545
Cdd:PRK10246 506 cplcgstSHPAVEAyqalEPGVNQSRLDALEKEVKKLGEEGAALRGQ-LDA-------------LTKQLqrdESEAQSLR 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1546 KAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT-QLESKQVALTARLE 1624
Cdd:PRK10246 572 QEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1625 E-SLK-----NEQVMVIQLQEEAEHLKKQQAEADKAREQ---------------------AEKELETWRQKANEALRLR- 1676
Cdd:PRK10246 652 GyALTlpqedEEASWLATRQQEAQSWQQRQNELTALQNRiqqltplletlpqsddlphseETVALDNWRQVHEQCLSLHs 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1677 ---------LQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE---ETAKQKLAAEQ 1744
Cdd:PRK10246 732 qlqtlqqqdVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQtlvTQTAQALAQHQ 811
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 1745 ----ELIRLRADFEHAEQQRTVLDDEL-----------QRLKNDVNSAvKQKKELEEELIKVRKEME 1796
Cdd:PRK10246 812 qhrpDGLDLTVTVEQIQQELAQLAQQLrenttrqgeirQQLKQDADNR-QQQQALMQQIAQATQQVE 877
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1741-1940 |
1.26e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1741 AAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLL 1820
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQA----EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1821 ESEA--AKMRELAEEATKLRSVAEEAKKQRQI-----AEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAE 1893
Cdd:TIGR02794 123 EAKAkqAAEAKAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141782 1894 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQ 1940
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2197-2601 |
1.28e-05 |
|
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: 51.56 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2197 EKTLKQKSSVEEELVKVKVQLDETDKQK-----SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEK 2271
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2272 ENQELMKKDKDNTKKLLEEEAEN------MKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA 2345
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2346 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2425
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV----LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2426 KKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQE--ADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQ 2503
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2504 EQLQQEKTILQQsfFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKE 2583
Cdd:TIGR04523 593 QKEKEKKDLIKE--IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
410
....*....|....*...
gi 1207141782 2584 AEEEMNGKQKEMQDLEKK 2601
Cdd:TIGR04523 671 SKTKIDDIIELMKDWLKE 688
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1417-1683 |
1.42e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1417 IAKAEQEaNELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQElktlsEQEIKAKsQQVEEALLSRTRIEEEIhiirlqle 1496
Cdd:pfam15709 325 LEKREQE-KASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ-----EQLERAE-KMREELELEQQRRFEEI-------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1497 ttmkqkntaetellQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtqKKRKAEEELKRKSEAEKDaakekkkaledlekfK 1576
Cdd:pfam15709 390 --------------RLRKQRLEEERQRQEEEERKQRLQLQAAQE--RARQQQEEFRRKLQELQR---------------K 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1577 LQAEEAERhlkqAELEKQRQIQvveevakktaatqleskqvaltarLEESLKNEQVMVIQLQEEA--EHLKKQQAEADKA 1654
Cdd:pfam15709 439 KQQEEAER----AEAEKQRQKE------------------------LEMQLAEEQKRLMEMAEEErlEYQRQKQEAEEKA 490
|
250 260 270
....*....|....*....|....*....|....
gi 1207141782 1655 REQAEKEletwRQKANEALRLRL-----QAEEEA 1683
Cdd:pfam15709 491 RLEAEER----RQKEEEAARLALeeamkQAQEQA 520
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2182-2377 |
1.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2182 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMED 2261
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2262 LLKLKLKIEK-----------ENQELMKKDKDNTKKLLEE------EAENMK-KLAEEAARLNIEAQEAARLRQIAESDL 2323
Cdd:COG3883 98 SGGSVSYLDVllgsesfsdflDRLSALSKIADADADLLEElkadkaELEAKKaELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2324 AKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQ 2377
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1642-1928 |
1.54e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.75 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1642 EHLKKQQAEadKAREQAEKELetwrqKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAAL-KQKEA 1720
Cdd:PRK07735 8 EDLKKEAAR--RAKEEARKRL-----VAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALaKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1721 A-----EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1795
Cdd:PRK07735 81 GteevtEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1796 EILLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKKqrqiaeeeAARQRAEAEKILKEKLTAIN- 1874
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQ----KAAEAGEGTEEVTEEEKAKAKAKA--------AAAAKAKAAALAKQKASQGNg 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141782 1875 --EATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA-------QHKQAIEEKIGQ 1928
Cdd:PRK07735 229 dsGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEEPSvnqpylnKYVEVIKEKLGE 291
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1573-1875 |
1.58e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1573 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLK-NEQVMVIQLQEEAEHLKKQQAEA 1651
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1652 DKaREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1731
Cdd:pfam13868 123 EK-QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1732 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMS 1811
Cdd:pfam13868 202 ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 1812 NTEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINE 1875
Cdd:pfam13868 280 EAEKRRMKRLEHRRELEKQIEEREEQR--AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1587-1743 |
1.59e-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: 50.61 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1587 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1666
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1667 QKANEALRLRLQAE------EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKL 1740
Cdd:TIGR02794 126 AKQAAEAKAKAEAEaerkakEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
...
gi 1207141782 1741 AAE 1743
Cdd:TIGR02794 206 AAE 208
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1136-1942 |
1.62e-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: 51.33 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1136 EDILNKYENQLREVNKVPVN-EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkRMSQLHSERDVELEHYRQL 1214
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKlEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLEEETAQKNNALKKIREL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1215 VGNLRE------RWQAVFAQIELRQREldlLNRQMQAYR-ESYDWLirwiaDAKQRQDKLHavpiggSKGLQEqLTQEKK 1287
Cdd:pfam01576 270 EAQISElqedleSERAARNKAEKQRRD---LGEELEALKtELEDTL-----DTTAAQQELR------SKREQE-VTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1288 LLEEIEKNKD-KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQ 1366
Cdd:pfam01576 335 ALEEETRSHEaQLQEMRQKHTQALEELTEQLEQAKRNKANLEK-----AKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1367 YIKFIIETQRRLQDEEKAaeklKEEERKKMAEMQAELEK---------------QKQLA---------------ETHAK- 1415
Cdd:pfam01576 410 LEGQLQELQARLSESERQ----RAELAEKLSKLQSELESvssllneaegkniklSKDVSslesqlqdtqellqeETRQKl 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1416 ----AIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELKTLSEQEikakSQQVEEALLSRTRIEEEIHII 1491
Cdd:pfam01576 486 nlstRLRQLEDERNSLQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEED----AGTLEALEEGKKRLQRELEAL 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1492 RLQLETTM-------KQKNTAETELLQLrakAVDADKLR---NAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDA 1561
Cdd:pfam01576 558 TQQLEEKAaaydkleKTKNRLQQELDDL---LVDLDHQRqlvSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1562 AKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKtaATQLESKQVALTARLEEslkneqvMVIQLQEEA 1641
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKN--VHELERSKRALEQQVEE-------MKTQLEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1642 EHLkkqqaeadKAREQAEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakrEAKKRakaeeAALKQKEAA 1721
Cdd:pfam01576 706 DEL--------QATEDAKLRLEVNMQALKAQFERDLQARDEQG------------------EEKRR-----QLVKQVREL 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1722 EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlDDELQRLKNdvnsAVKQKKELEEELIKVRKEM-EILLQ 1800
Cdd:pfam01576 755 EAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGR---EEAVKQLKK----LQAQMKDLQRELEEARASRdEILAQ 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1801 QKskaeketmsNTEKSKQLLESEAAKMRELAeeatklrSVAEEAKKQRQIAEEEAARQRAEAekiLKEKLTAINEATRLk 1880
Cdd:pfam01576 828 SK---------ESEKKLKNLEAELLQLQEDL-------AASERARRQAQQERDELADEIASG---ASGKSALQDEKRRL- 887
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 1881 tEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKK 1942
Cdd:pfam01576 888 -EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNK 948
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
193-269 |
1.70e-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: 46.53 E-value: 1.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 193 DNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSiAERDLGVTRLLDPEDVDVPHPDEKSIITYVSS 269
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQ 95
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1446-1925 |
1.79e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1446 EKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNA 1525
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1526 AQ--EEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfklQAEEAERHLKQAELEKQRQIqvveev 1603
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEELEERLEELR----------------------ELEEELEELEAELAELQEEL------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1604 akktaATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEK-ELETWRQKANEALR-------- 1674
Cdd:COG4717 180 -----EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKearlllli 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1675 ----------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1744
Cdd:COG4717 255 aaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1745 ELIRLRADFEHAEQQRTvLDDELQRLKNDVNSAVkQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQL---LE 1821
Cdd:COG4717 335 SPEELLELLDRIEELQE-LLREAEELEEELQLEE-LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELeeqLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1822 SEAAKMRELAEEATKlrsvaEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKA 1901
Cdd:COG4717 413 ELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
490 500
....*....|....*....|....*
gi 1207141782 1902 EEEGYQRKVLEDQA-AQHKQAIEEK 1925
Cdd:COG4717 488 LAEEWAALKLALELlEEAREEYREE 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1157-1846 |
1.80e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1157 KEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE-VNKRMSQL-HSERdveLEHYRQLVGNLRERWQAVFAQIELRQR 1234
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhLNLVQTALrQQEK---IERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1235 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQeQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1314
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1315 DYELQLVTY------------KA--LVEPIASPLKKAKMESASDDIIQEY----------VTLRTRYSELMTLSSQYikf 1370
Cdd:COG3096 455 EEVLELEQKlsvadaarrqfeKAyeLVCKIAGEVERSQAWQTARELLRRYrsqqalaqrlQQLRAQLAELEQRLRQQ--- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1371 iiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQK-QLAETHAKAIAKA---EQEANELKTKMKdEVSKRqdvavdsE 1446
Cdd:COG3096 532 --QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLeELEEQAAEAVEQRselRQQLEQLRARIK-ELAAR-------A 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1447 KQKHNIQRELQELKTLSE------QEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTA----ETELLQLR--- 1513
Cdd:COG3096 602 PAWLAAQDALERLREQSGealadsQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPggaeDPRLLALAerl 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1514 -----AKAVDADKLRNAAQEEA--------------EKLRKQVAE-------------------------ETQKKR---K 1546
Cdd:COG3096 682 ggvllSEIYDDVTLEDAPYFSAlygparhaivvpdlSAVKEQLAGledcpedlyliegdpdsfddsvfdaEELEDAvvvK 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1547 AEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEE-AERHLKQA-ELEK-QR-----------QIQVVEEVAKKTAATQL 1612
Cdd:COG3096 762 LSDRQWRYSRFPEVPLFGRAAREKRLEELRAERDElAEQYAKASfDVQKlQRlhqafsqfvggHLAVAFAPDPEAELAAL 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1613 ESKQVALTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA------NKK 1686
Cdd:COG3096 842 RQRRSELERELAQHRAQEQ----QLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGK 917
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1687 TAAQEEAEK-------QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRK-MAEETAKQKLAAEQELI-RLRADFEHAE 1757
Cdd:COG3096 918 ALAQLEPLVavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAE 997
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1758 QQRTVLDDELQRLKNDVNSA------------VKQK--KELEEEL----IKVRKEMEIL-------LQQKSKAEKETMSN 1812
Cdd:COG3096 998 EARREAREQLRQAQAQYSQYnqvlaslkssrdAKQQtlQELEQELeelgVQADAEAEERarirrdeLHEELSQNRSRRSQ 1077
|
810 820 830
....*....|....*....|....*....|....*...
gi 1207141782 1813 TEKSKQLLESEAA----KMRELAEEATKLRSVAEEAKK 1846
Cdd:COG3096 1078 LEKQLTRCEAEMDslqkRLRKAERDYKQEREQVVQAKA 1115
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1577-2444 |
1.80e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1577 LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvALTARlEESLKNEQVMVIQLQEEAEHLKKQQAEADKARE 1656
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRD-QITSK-EAQLESSREIVKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1657 ---QAEKELETWRQKANEALRLRLQAEEEAnKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEaaeMELGNQRKMAE 1733
Cdd:TIGR00606 263 kimKLDNEIKALKSRKKQMEKDNSELELKM-EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1734 ETAKQKLAAEQELIRLRADFEH-------AEQQRTVLDDELQRLKND------VNSAVKQKKELEEELIKVRKEMEILLQ 1800
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQehirardSLIQSLATRLELDGFERGpfserqIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1801 QKSKAEKETMSNTE-KSKQLLESEAAKMRELAEEATKLRSVAEEAKK----QRQIAEEEAARQRAEAEKILKEKltaiNE 1875
Cdd:TIGR00606 419 SKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQELRKAERELSKAEK----NS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1876 ATRLKTEAEIALKEKEAENDRLKRKAEEEGYQR------KVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQ------KKI 1943
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnKKQ 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1944 VEETL----KQRKVVEEEIHILKLNFEKASSGKQELELelkklkgiaDETQKSKAKAEEEAEKFRklaleeekkrkeaea 2019
Cdd:TIGR00606 575 LEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINN---------ELESKEEQLSSYEDKLFD--------------- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2020 kvkqiqaaeeeaARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSA----------AEQKAQNVLV 2089
Cdd:TIGR00606 631 ------------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAELQEFIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2090 Q-QNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEkea 2168
Cdd:TIGR00606 699 DlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG--- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2169 srraeAEAAALKLKQEADSEMAKYKKLAEKTlkqkSSVEEELVKVKVQLDETDKQKSVLDV-ELKRLKQEVSDAIKQKAQ 2247
Cdd:TIGR00606 776 -----TIMPEEESAKVCLTDVTIMERFQMEL----KDVERKIAQQAAKLQGSDLDRTVQQVnQEKQEKQHELDTVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2248 VEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQR 2327
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2328 ELAEKMLEEKKQAIQEAAKLKAEAE--------------------KLQKQKDQAQVEAQklLEAKKEMQQRLDQETEGFQ 2387
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVKnihgymkdienkiqdgkddyLKQKETELNTVNAQ--LEECEKHQEKINEDMRLMR 1004
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2388 KSLEAERKR------QLEITAEAEKLK---------------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEK 2444
Cdd:TIGR00606 1005 QDIDTQKIQerwlqdNLTLRKRENELKeveeelkqhlkemgqMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4159-4187 |
1.81e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.81e-05
10 20
....*....|....*....|....*....
gi 1207141782 4159 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4187
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1154-1324 |
1.94e-05 |
|
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: 48.98 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1154 VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ----RATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQI 1229
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAaheeRVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1230 ELRQRELDLLNRQMQAYRESYDwLIRWIADAKQRQDKLhaVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGY 1309
Cdd:cd00176 96 EERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEEL 172
|
170
....*....|....*
gi 1207141782 1310 IDAIKDYELQLVTYK 1324
Cdd:cd00176 173 LEEGHPDADEEIEEK 187
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1618-1924 |
2.00e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1618 ALTARLE-----ESLKNEQVMVIQLQEEAEhlkkQQAEADKAREQAEKELETWRQKANEALRLRLQ---AEEEANKKTaa 1689
Cdd:PRK04863 288 ALELRRElytsrRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAASDHLNLVQTALRQQEKierYQADLEELE-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1690 qeeaekqkeeakreakkrAKAEEAALKQKEAAEmelgnQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD 1764
Cdd:PRK04863 362 ------------------ERLEEQNEVVEEADE-----QQEENEA---RAEAAEEEVDELKsqlADYQQAldVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1765 --------DELQRLKNDVNSAVKQKKELEEELikVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAAKM---- 1827
Cdd:PRK04863 416 yqqavqalERAKQLCGLPDLTADNAEDWLEEF--QAKEQEATeellsLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrse 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1828 -----RELAEEATKLRSVAEEAK---------KQRQIAEEEAARQRAEAEKILKEKLTAINEATRLkteaeiaLKEKEAE 1893
Cdd:PRK04863 494 awdvaRELLRRLREQRHLAEQLQqlrmrlselEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-------QEELEAR 566
|
330 340 350
....*....|....*....|....*....|.
gi 1207141782 1894 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1924
Cdd:PRK04863 567 LESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1670-1902 |
2.06e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1670 NEALRLRLQAEEEANKKTAaqeeaEKQKEEAKREAKKRAKAEEAALKQkeaaEMELGNQRKMAEETAKQKLAAEQeliRL 1749
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ----EREIETARIAEAEAELAKKKAEE---RR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1750 RADFEHAEQQRTVlddELQRlkndvnsaVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqllESEAAKMRE 1829
Cdd:COG2268 256 EAETARAEAEAAY---EIAE--------ANAEREVQRQLEIAEREREIELQEKEAEREE------------AELEADVRK 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141782 1830 LAeeatklrsvaeEAKKQRQIAEEEaarqrAEAEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 1902
Cdd:COG2268 313 PA-----------EAEKQAAEAEAE-----AEAEAI-RAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE 368
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1396-1551 |
2.11e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1396 MAEMQAELEKQKQLAETHA-KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKAKSQQV 1474
Cdd:COG2268 194 IAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAK---KKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1475 EEALLSRTrIEEEIHIIRLQLETTMKQKNtAETELLQLRA---KAVDADKLRNAAQEEAE------KLRKQvAEETQKKR 1545
Cdd:COG2268 271 AEANAERE-VQRQLEIAEREREIELQEKE-AEREEAELEAdvrKPAEAEKQAAEAEAEAEaeairaKGLAE-AEGKRALA 347
|
....*.
gi 1207141782 1546 KAEEEL 1551
Cdd:COG2268 348 EAWNKL 353
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2022-2428 |
2.16e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.21 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2022 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEK--QVI-----LVQEAAQKCSAAEQKAQNVLVQQNKD 2094
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqQVIdnfpkLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2095 SMAQDKLK---EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedAEKLRKEAEKEasrr 2171
Cdd:PRK10929 106 ALEQEILQvssQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE----------------------ARRQLNEIERR---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2172 aeaeaaaLKLKQEADS--EMAKYKKLAEKTLKQKSSVEE-ELVkvkvQLDETDKQksvldvELKRLKQEVsdAIKQKAQV 2248
Cdd:PRK10929 160 -------LQTLGTPNTplAQAQLTALQAESAALKALVDElELA----QLSANNRQ------ELARLRSEL--AKKRSQQL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2249 EDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLeeeAENMKKLAEEAARLNIEAQE----AARLRQIAESDLa 2324
Cdd:PRK10929 221 DAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSI---VAQFKINRELSQALNQQAQRmdliASQQRQAASQTL- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2325 kQRELAEKMLEEKKQ------AIQEAakLKAEAEKL-------QKQKDQAQVEAQKL-LEAKKEMQQRLDQE-------- 2382
Cdd:PRK10929 297 -QVRQALNTLREQSQwlgvsnALGEA--LRAQVARLpempkpqQLDTEMAQLRVQRLrYEDLLNKQPQLRQIrqadgqpl 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 2383 TEGFQKSLEAERKRQ---------------LEITaeaeKLKVKVTQLSDAQSKAEEEAKKF 2428
Cdd:PRK10929 374 TAEQNRILDAQLRTQrellnsllsggdtliLELT----KLKVANSQLEDALKEVNEATHRY 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2296-2447 |
2.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2296 KKLAEEAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-----AKLKAEAEKLQKQKDQAQVEAQKLLE 2370
Cdd:COG4913 288 RRLELLEAELEELRAELARLEA-ELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 2371 AKKEMQQRLDQETEGFQksleaerKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTS 2447
Cdd:COG4913 367 LLAALGLPLPASAEEFA-------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1034-1616 |
2.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1034 ESRTVNRLRQMVDKEPLKACTQRATEQKKVqtelEGIKKDLDKVVEKSEAVLATSQQSS-SAPVLRSEIDITQKKMEHVY 1112
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKKADAAKKKAEEAKkAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1113 GLSSVylDKLKTIDlvirSTQGAEDILNKYEnqlrEVNKVPVNEKEIEASQTQLQKLRSEAEGKQATfdrleEELQRATE 1192
Cdd:PTZ00121 1364 EKAEA--AEKKKEE----AKKKADAAKKKAE----EKKKADEAKKKAEEDKKKADELKKAAAAKKKA-----DEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1193 VNKRMSQLHSERDvELEHYRQLVGNLRERWQAVFAQIELRQ-RELDLLNRQMQAYRESyDWLIRWIADAKQRQDKLHAVP 1271
Cdd:PTZ00121 1429 EKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1272 IGGSKGLQEQLTQEKKLLEEIEK--NKDKVEDCQKF--AKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDII 1347
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1348 QEyvTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEerkkmaemqaelEKQKQLAETHAKAIAKAEQEANEL 1427
Cdd:PTZ00121 1587 KK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA------------EEEKKKVEQLKKKEAEEKKKAEEL 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1428 KTKMKDEVSKRQDVAVDSEKQKhniqRELQELKTLSEQEIKAKSQQVEEALLSRtRIEEeihiirlqlettMKQKNTAET 1507
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDK----KKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEE------------LKKKEAEEK 1715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1508 EllqlrakavDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlEKFKLQAEEAERHLK 1587
Cdd:PTZ00121 1716 K---------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE-----------------EKKKIAHLKKEEEKK 1769
|
570 580
....*....|....*....|....*....
gi 1207141782 1588 QAELEKQRQIQVVEEVAKKTAATQLESKQ 1616
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1397-1623 |
2.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1397 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEE 1476
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1477 AllsRTRIEEEIHIIRLQLETTMKQKNTAETELL------------------QLRAKAVDADKLRnAAQEEAEKLRKQVA 1538
Cdd:COG4942 95 L---RAELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqylkyLAPARREQAEELR-ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1539 EETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVA 1618
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1207141782 1619 LTARL 1623
Cdd:COG4942 251 LKGKL 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2281-2515 |
2.49e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2281 KDNTKKLLEEEAENMKKLAEEAARLNIEAQEAAR----LRQ-IAESDLAKQR-----ELAEKMLEE--KKQAIQEAAKLK 2348
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEevleLEQkLSVADAARRQfekayELVCKIAGEveRSQAWQTARELL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2349 AEAEKLQKQKDQAQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2426
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2427 KFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQeadglhkAIADLEKEKEKLKKEAADL--QKQSKEMANVQQE 2504
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGE-------ALADSQEVTAAMQQLLEREreATVERDELAARKQ 654
|
250
....*....|.
gi 1207141782 2505 QLQQEKTILQQ 2515
Cdd:COG3096 655 ALESQIERLSQ 665
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2048-2466 |
2.74e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2048 LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNA---EK 2124
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddlEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2125 EAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYK-KLAEKTLKQK 2203
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELReREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2204 SsVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLklklkiekenqelmkkdkdn 2283
Cdd:PRK02224 437 T-ARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVE-------------------- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2284 tKKLleEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEekkqaiqEAAKLKAEAEKLQKQKDQAQV 2363
Cdd:PRK02224 496 -ERL--ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE-------RAAELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2364 EAQKLLEAKKEMQQRLdqetegfqksleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2443
Cdd:PRK02224 566 EAEEAREEVAELNSKL------------AELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
410 420
....*....|....*....|...
gi 1207141782 2444 KHTSEKHTVVEKLEVQRLQSKQE 2466
Cdd:PRK02224 634 ERKRELEAEFDEARIEEAREDKE 656
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1758-2414 |
2.74e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.52 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1758 QQRTVLDDELQRLKndvnsavkqkkELEEElikVRKEMEILLQQKSKAEKETMSntekskqlLESEAAKMRELAEEATKL 1837
Cdd:pfam07111 63 QQAELISRQLQELR-----------RLEEE---VRLLRETSLQQKMRLEAQAME--------LDALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1838 RSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEAtrlkteAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQ 1917
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQA------HEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1918 HKQAIEEKIGQLKKSSDtELDRQKKIVEETlkqRKVVEE----EIHILKLNFEKassgKQELELELKKLKGIADETQKSK 1993
Cdd:pfam07111 195 AQKEAELLRKQLSKTQE-ELEAQVTLVESL---RKYVGEqvppEVHSQTWELER----QELLDTMQHLQEDRADLQATVE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1994 AKAEEEAEKFRKLALEEEKKRKEaeakVKQIQAAEEEAARQHKAA----QEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL 2069
Cdd:pfam07111 267 LLQVRVQSLTHMLALQEEELTRK----IQPSDSLEPEFPKKCRSLlnrwREKVFALMVQLKAQDLEHRDSVKQLRGQVAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2070 VQEAAqkcsAAEQKAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEaallHKKAEEAERQKKAAEAEAAK 2149
Cdd:pfam07111 343 LQEQV----TSQSQEQAILQRALQDKAAE--VEVERMSAKGLQMELSRAQEARRRQ----QQQTASAEEQLKFVVNAMSS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2150 QAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKykKLAEKTLKQKSSVEEELV-----KVKVQLDETDKQK 2224
Cdd:pfam07111 413 TQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMAR--KVALAQLRQESCPPPPPAppvdaDLSLELEQLREER 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2225 SVLDVELKR----LKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkiekenQELMKKdkdntkkllEEEAENMKKLAE 2300
Cdd:pfam07111 491 NRLDAELQLsahlIQQEVGRAREQGEAERQQLSEVAQQLE-------------QELQRA---------QESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2301 EAARLNIEA-QEAARLRQiaesDLAKQRELAEKMLEEKKQAIQeaAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2379
Cdd:pfam07111 549 VARQGQQEStEEAASLRQ----ELTQQQEIYGQALQEKVAEVE--TRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRA 622
|
650 660 670
....*....|....*....|....*....|....*
gi 1207141782 2380 DQETEgfqKSLEAERKRQLEITAEAEKLKVKVTQL 2414
Cdd:pfam07111 623 TQEKE---RNQELRRLQDEARKEEGQRLARRVQEL 654
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2215-2382 |
2.76e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2215 VQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE----E 2290
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2291 EAENMKKlAEEAARLNIEAQEAARLrqiaesDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQAQVEAQKLL 2369
Cdd:COG1579 90 EYEALQK-EIESLKRRISDLEDEIL------ELMERIEELEEELAELEAELAELeAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|...
gi 1207141782 2370 EAKKEMQQRLDQE 2382
Cdd:COG1579 163 AEREELAAKIPPE 175
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3084-3119 |
2.79e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.79e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1207141782 3084 LNLLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPE 3119
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1534-1742 |
2.93e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1534 RKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQVVEeVAKKTAATQLE 1613
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERET--------------------EIAIAQANREAEEAELEQEREIETAR-IAEAEAELAKK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1614 skqvaltarleeslkneqvmviqlQEEAEhlkkqqAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEA 1693
Cdd:COG2268 250 ------------------------KAEER------REAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEA 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207141782 1694 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1742
Cdd:COG2268 300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
832-877 |
2.97e-05 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 2.97e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1207141782 832 VQAVCDFKQME---ITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSI 877
Cdd:cd11768 2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPSN 50
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2025-2203 |
2.99e-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: 49.84 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2025 QAAEEEAARQHK--AAQEEVGRLMKLAEEAKKQkeiAEKEAEKQvilVQEAAQKcSAAEQKAQnvlvqqnkdSMAQDKLK 2102
Cdd:TIGR02794 119 KQAEEAKAKQAAeaKAKAEAEAERKAKEEAAKQ---AEEEAKAK---AAAEAKK-KAEEAKKK---------AEAEAKAK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2103 EEFE---KAKKLAQEAEKAKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEaeaaal 2179
Cdd:TIGR02794 183 AEAEakaKAEEAKAKAEAAKAKAAAEAA---AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR------ 253
|
170 180
....*....|....*....|....
gi 1207141782 2180 klKQEADSEMAKYKKLAEKTLKQK 2203
Cdd:TIGR02794 254 --GAAAGSEVDKYAAIIQQAIQQN 275
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1624-1789 |
3.22e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1624 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAE-EEANKKTAAQEEAEKQKEEAKR 1702
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1703 EAKKRAkaeEAALKQKEAAEMELGNQRKMAEETAKQKLaaeqelirlradfEHAEQQRTVLDDELQRLKNDVNSavkQKK 1782
Cdd:pfam05262 289 EIKKND---EEALKAKDHKAFDLKQESKASEKEAEDKE-------------LEAQKKREPVAEDLQKTKPQVEA---QPT 349
|
....*..
gi 1207141782 1783 ELEEELI 1789
Cdd:pfam05262 350 SLNEDAI 356
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2299-2504 |
3.27e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2299 AEEAARLNIEAQEAARLRQIAESDLAKQ-RELAEKMLEEKkQAIQEAAKLKAEAEKLQKQKDQAqveAQKLLEAKKEMQQ 2377
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQaEELQQKQAAEQ-ERLKQLEKERLAAQEQKKQAEEA---AKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2378 RLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQlSDAQSKAEEEAKkfKKQADEIKIRLQETEKHTSEKhtvvEKLE 2457
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAE-AEAAKKAAAEAK--KKAEAEAAAKAAAEAKKKAEA----EAKK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141782 2458 VQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE 2504
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2421-2637 |
3.46e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2421 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2500
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2501 VQQEQLQQEKTIlqqsffaekETLLKKEkaieeekkklekQFEDEVKKAEALKAEQERQRKLMEE---ERKKLQSAMDAA 2577
Cdd:COG3883 94 ALYRSGGSVSYL---------DVLLGSE------------SFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2578 IKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2637
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1151-1625 |
3.53e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1151 KVPVNEKEIEASQTQLQklrsEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGN--LRERWQAVFAQ 1228
Cdd:COG4717 65 KPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1229 IELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKG 1308
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1309 YIDAIKDyELQLVTYKALVEPIASPLKKAKMESASDDIIqeyVTLRTRYSELMTLSSQYIKFIIetqrrlqdeekAAEKL 1388
Cdd:COG4717 221 ELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLF-----------LVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1389 KEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIK 1468
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1469 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1548
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 1549 EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQ-IQVVEEVAKKTAATQLESKQVALTARLEE 1625
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAaLKLALELLEEAREEYREERLPPVLERASE 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1376-1584 |
3.66e-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: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1376 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRE 1455
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1456 LQELKTLSEQ---EIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNtaetELLQLRAKAVDADKLRNAAQEEAEK 1532
Cdd:COG4942 110 LRALYRLGRQpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 1533 LRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF--KLQAEEAER 1584
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAA 239
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
62-152 |
3.88e-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: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 62 KWVNKHLVKAQR---HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 134
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1207141782 135 DDIADGNPKLTLGLIWTI 152
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2022-2430 |
4.18e-05 |
|
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: 49.76 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2022 KQIQAAEEEAARQHKAAQEEVgrlmKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAaeqKAQNVLVQQNKDSMAQDKl 2101
Cdd:pfam09731 89 VKIPRQSGVSSEVAEEEKEAT----KDAAEAKAQLPKSEQEKEKALEEVLKEAISKAE---SATAVAKEAKDDAIQAVK- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2102 keefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAerqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKL 2181
Cdd:pfam09731 161 ----AHTDSLKEASDTAEISREKATDSALQKAEAL--------------------AEKLKEVINLAKQSEEEAAPPLLDA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2182 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqLDETDKQksVLDVELKRLKQEVSDAIKQK-AQVEDELSKVkiqME 2260
Cdd:pfam09731 217 APETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKE-LVASERI--VFQQELVSIFPDIIPVLKEDnLLSNDDLNSL---IA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2261 DLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQIAESdlakqrelaekmLEEKKQA 2340
Cdd:pfam09731 291 HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSA-RLEEVRAADEAQLRLE------------FEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2341 IQEAAKLKAEAEklqkQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS-LEAERKRQLEITAEAeKLKVK-VTQLSDAQ 2418
Cdd:pfam09731 358 IRESYEEKLRTE----LERQAEAHEEHLKDVLVEQEIELQREFLQDIKEkVEEERAGRLLKLNEL-LANLKgLEKATSSH 432
|
410
....*....|..
gi 1207141782 2419 SKAEEEAKKFKK 2430
Cdd:pfam09731 433 SEVEDENRKAQQ 444
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2315-2761 |
4.38e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2315 LRQIAES-DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQK----------QKDQAQVEAQKLLEAKKEMQQRLDQET 2383
Cdd:pfam05483 50 LEQVANSgDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkQKENKLQENRKIIEAQRKAIQELQFEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2384 EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQS 2463
Cdd:pfam05483 130 EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2464 KQEadgLHKAIADLEKEKEKlkkeaadLQKQSKEMANVQQEQLQqekTILQQSffAEKETLLKKEKAIEEEKKKLEKQFE 2543
Cdd:pfam05483 210 RLE---MHFKLKEDHEKIQH-------LEEEYKKEINDKEKQVS---LLLIQI--TEKENKMKDLTFLLEESRDKANQLE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2544 DEVK-KAEALKAEQERQRKLMEEeRKKLQSAMDAAIKKQKEAEEEMN-----------GKQKEMQDLEKKRIEQEKLLAE 2611
Cdd:pfam05483 275 EKTKlQDENLKELIEKKDHLTKE-LEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNKAKAAHSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2612 ENKN-------LREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT-----MVETTKKVLNGSTEVDGVKKDvplaFDG 2679
Cdd:pfam05483 354 FEATtcsleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkevELEELKKILAEDEKLLDEKKQ----FEK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2680 IREKVPASRLHEIGVLSKKEYD------KLKKGKTTVQELSKNDKVKMCLKGKDCIGGVIVEPNQKMsiyQALKDKMITQ 2753
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREKEihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK---LLLENKELTQ 506
|
....*...
gi 1207141782 2754 STAIMLLE 2761
Cdd:pfam05483 507 EASDMTLE 514
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1276-1934 |
4.83e-05 |
|
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: 49.63 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1276 KGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKAlvepiasplKKAKMESASDDIIQEYVTLRT 1355
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK---------EKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1356 RYSELMTLssqyikfiIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQlaethakAIAKAEQEANELK---TKMK 1432
Cdd:TIGR04523 202 LLSNLKKK--------IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT-------EISNTQTQLNQLKdeqNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1433 DEVSKRQDVAVDSEKQKHNIQRELQELKTlseqEIKAKSQQVEEALLSRtrieeeihiIRLQLETTMKQKNTAETELLQl 1512
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKS----EISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQISQ- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1513 rakavdADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHL-KQAEL 1591
Cdd:TIGR04523 333 ------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1592 EKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1671
Cdd:TIGR04523 407 NQQKDEQI------KKLQQEKELLEKEIERLKETIIKNNS-EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1672 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKrAKAEEAALKQKEaaemelgnqrkmaEETAKQKLAAEQELIRLRA 1751
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD-LTKKISSLKEKI-------------EKLESEKKEKESKISDLED 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1752 DFEHAEQQRTvlDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELA 1831
Cdd:TIGR04523 546 ELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1832 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAE--IALKEKEAENDRLKRKAEEEGYQRK 1909
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiIELMKDWLKELSLHYKKYITRMIRI 703
|
650 660
....*....|....*....|....*
gi 1207141782 1910 VLEDQAAQHKQAIEEKIGQLKKSSD 1934
Cdd:TIGR04523 704 KDLPKLEEKYKEIEKELKKLDEFSK 728
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1466-1744 |
5.07e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1466 EIKAKSQQVEEALLSRTRIEEEIhiIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKR 1545
Cdd:PRK05035 437 EIRAIEQEKKKAEEAKARFEARQ--ARLEREK-------AAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1546 KAEEELKRKSEAEKDAakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvalTARLEE 1625
Cdd:PRK05035 508 IKAGARPDNSAVIAAR---------EARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANA---EAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1626 SLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAK 1705
Cdd:PRK05035 576 DPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP---KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141782 1706 KRAKAEEAALKQKEAAEMELGNQRKMAEETA----KQKLAAEQ 1744
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1399-1554 |
5.10e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1399 MQAELEKQKQLAETHAKaIAKAEQEANELK---TKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVE 1475
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKELPaelAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1476 --EALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKR 1553
Cdd:COG1579 77 kyEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
.
gi 1207141782 1554 K 1554
Cdd:COG1579 157 E 157
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
56-164 |
5.30e-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: 46.20 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 56 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 122
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141782 123 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 164
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
2228-2462 |
5.56e-05 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 47.86 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2228 DVELKRLK------QEVSDAIKQKAQVEDELSKVKIQMEDLLKLklkiekenqelmkKDKDNTkklLEEEAENMKKLAEE 2301
Cdd:cd07647 8 DTLLQRLKegkkmcKELEDFLKQRAKAEEDYGKALLKLSKSAGP-------------GDEIGT---LKSSWDSLRKETEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2302 AARLNIEaqeaarlrqiaesdLAKQ-RELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLd 2380
Cdd:cd07647 72 VANAHIQ--------------LAQSlREEAEKLEEFREKQKEERKKTEDIMKRSQKNK---KELYKKTMKAKKSYEQKC- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2381 QETEGFQKSleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEVQR 2460
Cdd:cd07647 134 REKDKAEQA--YEKSSSGAQPKEAEKLKKKAAQCKTSAEEADSAYKSSIGCLEDAR---VEWESEHATACQVFQNMEEER 208
|
..
gi 1207141782 2461 LQ 2462
Cdd:cd07647 209 IK 210
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2280-2441 |
6.11e-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: 49.23 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2280 DKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmleekkqAIQEAAKLKAEAEKLQKQKD 2359
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2360 QAQVEAQKLLEAKKEMQQRLDQETEGFQKSlEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRL 2439
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKR-EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
..
gi 1207141782 2440 QE 2441
Cdd:pfam05262 331 EP 332
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1404-1838 |
6.22e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1404 EKQKQLaethakaiakaeQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQelkTLSEQeIKAKSQQVEEAllsRTR 1483
Cdd:pfam10174 363 KKTKQL------------QDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE---NLQEQ-LRDKDKQLAGL---KER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1484 IEEeihiirLQLETTmkqknTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAK 1563
Cdd:pfam10174 424 VKS------LQTDSS-----NTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1564 EKKKALEDL-EKFKLQAEEA---ERHLKQAELEkqrqIQVVEEVAKKTAATQLESKQVALTARLEESLKNE-QVMVIQLQ 1638
Cdd:pfam10174 493 EKESSLIDLkEHASSLASSGlkkDSKLKSLEIA----VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQEVA 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1639 EEAEHLKKQQAEADK---AREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakreakkraKAEEAAL 1715
Cdd:pfam10174 569 RYKEESGKAQAEVERllgILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI------------------KHGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1716 KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLradfehaEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1795
Cdd:pfam10174 631 KKKGAQLLEEARRREDNLADNSQQLQLEELMGAL-------EKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL 703
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1207141782 1796 EILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 1838
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1618-2050 |
6.33e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1618 ALTARLE-----ESLKNEQVMVIQLQEEAEHLkkqqaeadkarEQAEKELETWRQKANEALRLRLQAEEEANKKtaaqee 1692
Cdd:COG3096 287 ALELRRElfgarRQLAEEQYRLVEMARELEEL-----------SARESDLEQDYQAASDHLNLVQTALRQQEKI------ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1693 aekqkeeakreAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD- 1764
Cdd:COG3096 350 -----------ERYQEDLEELTERLEEQEEVveEAAEQLAEAEA---RLEAAEEEVDSLKsqlADYQQAldVQQTRAIQy 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1765 -DELQRLKN----------DVNSAVKQKKELEEELIKVRKEMeILLQQKSKAEKETMSNTEKSKQLLESEAA-------- 1825
Cdd:COG3096 416 qQAVQALEKaralcglpdlTPENAEDYLAAFRAKEQQATEEV-LELEQKLSVADAARRQFEKAYELVCKIAGeversqaw 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1826 -KMRELAEEATKLRSVAEEAKK-QRQIAE-EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 1902
Cdd:COG3096 495 qTARELLRRYRSQQALAQRLQQlRAQLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1903 EEGYQRKVLEdqaaQHKQAIEEKIGQLKKS------SDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKqele 1976
Cdd:COG3096 575 EAVEQRSELR----QQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVER---- 646
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 1977 lelkklkgiaDETQkskakaeeeaekFRKLALeeekkrkeaeakvkqiqaaEEEAARQHKAAQEEVGRLMKLAE 2050
Cdd:COG3096 647 ----------DELA------------ARKQAL-------------------ESQIERLSQPGGAEDPRLLALAE 679
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1703-1951 |
6.56e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1703 EAKKRAKAEEAALKQKEAAEMELGNQrkmAEETAKQKLAAEQELIRLRADFEHAEQQRTVlddELQRLKndvnsAVKQKK 1782
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQ---AEEAEKQRAAEQARQKELEQRAAAEKAAKQA---EQAAKQ-----AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1783 ELEEELIKVRKEmeillqQKSKAEKEtmsntekSKQLLESEAAKMRElaEEATKlrSVAEEAKKQRQIAE---EEAARQR 1859
Cdd:TIGR02794 120 QAEEAKAKQAAE------AKAKAEAE-------AERKAKEEAAKQAE--EEAKA--KAAAEAKKKAEEAKkkaEAEAKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1860 AEAE-KILKEKLTAINEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ-LKKSSDTEL 1937
Cdd:TIGR02794 183 AEAEaKAKAEEAKAKAEAAKAKAAAE-AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGaRGAAAGSEV 261
|
250
....*....|....
gi 1207141782 1938 DRQKKIVEETLKQR 1951
Cdd:TIGR02794 262 DKYAAIIQQAIQQN 275
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1638-1866 |
6.64e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1638 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEalRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAK-AEEAALK 1716
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLE--KERLAAQEQKKQA-----------EEAAKQAALKQKqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1717 QKEAAemelgnqrkmaeetakqKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEElikVRKEME 1796
Cdd:PRK09510 141 AAAAA-----------------KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKK----AAAEAKKKAEAE---AAAKAA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1797 ILLQQKSKAEKETMSNTEkSKQLLESEAAKMRELAEEATKlrSVAEEAKKQRQIAEEEAARQRAEAEKIL 1866
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAE-AKKKAAAEAKAAAAKAAAEAK--AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1743-1903 |
7.14e-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: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1743 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLles 1822
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEY--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1823 eAAKMRELaEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEatrLKTEAEIALKEKEAENDRLKRKAE 1902
Cdd:COG1579 92 -EALQKEI-ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
.
gi 1207141782 1903 E 1903
Cdd:COG1579 167 E 167
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2022-2160 |
8.25e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2022 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQkeiAEKEAEKQVilvQEAAQKCSAAEQKAQNVLVQQNKdSMAQDKL 2101
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKKA---EAEAAKKAAAEAKKKAEAEAAAK-AAAEAKK 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2102 KEEFEKAKKLAQEAEK-----AKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2160
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKkaaaeAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2324-2591 |
8.87e-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: 48.22 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2324 AKQRELAEKMLEEKKQAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLdQETEGFQKSLEAErkrqleitae 2403
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAE---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2404 aeklkvkvtqLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVeklevqrLQSKQEADGLHKAIADLEKEKEK 2483
Cdd:COG4942 85 ----------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL-------LLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2484 LKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLM 2563
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|....*...
gi 1207141782 2564 EEERKKLQSAMDAAIKKQKEAEEEMNGK 2591
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1354-1770 |
9.20e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.75 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1354 RTRYSELMTLSSQYIKF---IIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTK 1430
Cdd:COG5278 106 QARLDELEALIDQWLAEleqVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1431 MKDEVSKRQDVAVDSEKQKHNIQRELQELkTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELL 1510
Cdd:COG5278 186 LALAELLLLALARALAALLLLLLLEAELA-AAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1511 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1590
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1591 LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN 1670
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1671 EALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLR 1750
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410 420
....*....|....*....|
gi 1207141782 1751 ADFEHAEQQRTVLDDELQRL 1770
Cdd:COG5278 505 LAALLLAAAEAALAAALAAA 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1451-1790 |
9.42e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1451 NIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEA 1530
Cdd:COG4372 32 QLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1531 EKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1610
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1611 QLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQ 1690
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1691 EEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRL 1770
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1207141782 1771 KNDVNSAVKQKKELEEELIK 1790
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2288-2499 |
9.93e-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: 48.41 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2288 LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdlAKQRELAekmLEEKKQAIQEAAKLKAEA-EKLQKQKDQAQVEAQ 2366
Cdd:pfam15709 309 MESEEERSEEDPSKALLEKREQEKASRDRLRAER--AEMRRLE---VERKRREQEEQRRLQQEQlERAEKMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2367 KLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAEAEK-------LKVKVTQLS-DAQSKAEEEAKKFKKQADEIKIR 2438
Cdd:pfam15709 384 RRFEEIRLRKQRLEEER---QRQEEEERKQRLQLQAAQERarqqqeeFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQ 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 2439 LQETEKHTSEKhTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMA 2499
Cdd:pfam15709 461 LAEEQKRLMEM-AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2515-2637 |
9.95e-05 |
|
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: 47.67 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2515 QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRklmeEERKKLQSAMDAAIKKQKEAEEEMngKQKE 2594
Cdd:pfam02841 179 QEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLR----EKQKEEEQMMEAQERSYQEHVKQL--IEKM 252
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141782 2595 MQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2637
Cdd:pfam02841 253 EAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQD 295
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3744-3780 |
1.13e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.13e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1207141782 3744 IDLLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEF 3780
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2543-2635 |
1.16e-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: 47.84 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2543 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2622
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90
....*....|...
gi 1207141782 2623 LQSSQKASYTKEI 2635
Cdd:COG4942 113 LYRLGRQPPLALL 125
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2293-2514 |
1.19e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2293 ENMKKLAEE-AARLNIEAQEAARLRQIAESDLAKQREL--AEKMLEEKKQAIQEAAKLKAEAEKLQkQKDQAQVEAQKLL 2369
Cdd:PRK10929 75 DNFPKLSAElRQQLNNERDEPRSVPPNMSTDALEQEILqvSSQLLEKSRQAQQEQDRAREISDSLS-QLPQQQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2370 eakKEMQQRLdqETEGFQKSLEAERKRQLeITAEAEKLKVKVTQLSDAQSKAEE-------EAKKFKKQADEIKIRLQET 2442
Cdd:PRK10929 154 ---NEIERRL--QTLGTPNTPLAQAQLTA-LQAESAALKALVDELELAQLSANNrqelarlRSELAKKRSQQLDAYLQAL 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2443 EKH-TSEKHTVVEK-LEVQRLQSKQEADgLHKAIADLEKEKEKLkkeAADLQKQSKEMANVQQEQLQQEKTILQ 2514
Cdd:PRK10929 228 RNQlNSQRQREAERaLESTELLAEQSGD-LPKSIVAQFKINREL---SQALNQQAQRMDLIASQQRQAASQTLQ 297
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1751-2124 |
1.22e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1751 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKetmsntekskqllESEAAKMR-E 1829
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ-------------DYQAASDHlN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1830 LAEEAtklrsVAEEAKKQRQIAEEEAARQRAEAEKILKEkltainEATRLKTEAEIALKEKEAENDRLkrKAEEEGYQRK 1909
Cdd:PRK04863 339 LVQTA-----LRQQEKIERYQADLEELEERLEEQNEVVE------EADEQQEENEARAEAAEEEVDEL--KSQLADYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1910 --VLEDQAAQHKQAIE--EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGI 1985
Cdd:PRK04863 406 ldVQQTRAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1986 ADETQKSkakaeEEAEKFRKLaLEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQeevgRLMKLAEEAKKQKEIAEKEAEK 2065
Cdd:PRK04863 486 AGEVSRS-----EAWDVAREL-LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 2066 QVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEK 2124
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1494-1917 |
1.23e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1494 QLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLE 1573
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1574 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADK 1653
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1654 AREQAEKELETWRQKANEALRLRLQAEEEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE 1733
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALA-----ELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1734 ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT 1813
Cdd:COG5278 346 LLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1814 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1893
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1207141782 1894 NDRLKRKAEEEGYQRKVLEDQAAQ 1917
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2037-2250 |
1.25e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2037 AAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVilvQEAAQKCSAAEQKAQnvlvQQNKDSMAQDKLKEEFEKAKKLAQEAE 2116
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQA---EELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2117 KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAlKLKQEADSEM-AKYKKL 2195
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAeAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2196 AEKTLKQKSSVEEELVKVKvqldETDKQKSVLDVELKRLKQEVSDAIKQKAQVED 2250
Cdd:PRK09510 211 AAAEAKKKAAAEAKAAAAK----AAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1625-1909 |
1.27e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1625 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1704
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE-LNAQVKELREEAQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1705 KKRAKAEEAALKQKEAaemELGNQRKMAEETAKQKLAAEQELIRLRAdfehaEQQRTVLD--------DELQRLKNDVNs 1776
Cdd:COG1340 80 RDELNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEW-----RQQTEVLSpeeekelvEKIKELEKELE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1777 AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1856
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHE----EMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1207141782 1857 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRK 1909
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKG 279
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1571-1871 |
1.34e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1571 DLEKFKLQAEEAERHLKQAELEKQRQIQvveevakktAATQLEsKQVALTARLEEslkneQVMVIQ---LQEEAEHLKKQ 1647
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRS---------QLEQAK-EGLSALNRLLP-----RLNLLAdetLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1648 QAEADKAR----------EQAEKELETWRQKANEALRLRLQAEEeankktaaqeeaekqkeeakreakkrAKAEEAALKQ 1717
Cdd:PRK04863 903 LDEAEEAKrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDYQQ--------------------------AQQTQRDAKQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1718 KEAAEMELgNQRK--MAEETAKQKLAAEQEL-IRLRADFEHAEQQRTVLDDEL--------------QRLKNDVNSAVKQ 1780
Cdd:PRK04863 957 QAFALTEV-VQRRahFSYEDAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQM 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1781 KKELEEEL--IKVR--KEMEILLQQKSKAEKETMSNT-------EKSKQLLESE----AAKMRELAEEATKLRSVAEEAK 1845
Cdd:PRK04863 1036 LQELKQELqdLGVPadSGAEERARARRDELHARLSANrsrrnqlEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAK 1115
|
330 340
....*....|....*....|....*.
gi 1207141782 1846 KqRQIAEEEAARQRAEAEKILKEKLT 1871
Cdd:PRK04863 1116 A-GWCAVLRLVKDNGVERRLHRRELA 1140
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1592-1909 |
1.48e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 47.72 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1592 EKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETW 1665
Cdd:pfam15558 4 ERDRKIAALMLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQsqeqwqAEKEQRKARLGREERRRAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1666 RQKANEAL---RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALkQKEAAEMELGNQRKMAE--------- 1733
Cdd:pfam15558 84 RREKQVIEkesRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL-QALREQNSLQLQERLEEachkrqlke 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1734 --------ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKA 1805
Cdd:pfam15558 163 reeqkkvqENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1806 EKETMSNTEKSKQLLESEAAKMRelaeeatKLRSVAEEAKKQR--QIAEEEAARQRaeAEKILKEKLTAINEATRLKTEA 1883
Cdd:pfam15558 243 EEKEEERQEHKEALAELADRKIQ-------QARQVAHKTVQDKaqRARELNLEREK--NHHILKLKVEKEEKCHREGIKE 313
|
330 340
....*....|....*....|....*.
gi 1207141782 1884 EIALKEKEAENDRLKRKAEEEGYQRK 1909
Cdd:pfam15558 314 AIKKKEQRSEQISREKEATLEEARKT 339
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4409-4446 |
1.51e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.51e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141782 4409 QRFLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTA 4446
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2033-2622 |
1.52e-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: 48.30 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2033 RQHKAA-QEEVGRLMKLAEEAKkQKEIAE------KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ--DKLKE 2103
Cdd:pfam12128 230 IQAIAGiMKIRPEFTKLQQEFN-TLESAElrlshlHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEkrDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2104 EfekakKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAaalkLKQ 2183
Cdd:pfam12128 309 E-----LSAADAAVAKDRSELEALEDQHGAFLDA------------------DIETAAADQEQLPSWQSELEN----LEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2184 EADSEMAKYKKLAEKTLKQKSSVEEELV-KVKVQLDETDKQKSVLDvelkrlkqevsdaiKQKAQVEDELSKVKIQMEDL 2262
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGIKDKLAKIREARD--------------RQLAVAEDDLQALESELREQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2263 LklklkiekenqELMKKDKDNTKKLLEEEAENMKklaeeaARLNIEAQEAARLRQIAESDlakqrELAEKMLEEKKQAIQ 2342
Cdd:pfam12128 428 L-----------EAGKLEFNEEEYRLKSRLGELK------LRLNQATATPELLLQLENFD-----ERIERAREEQEAANA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2343 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-ETEGFQKS------LEAE----RKRQLEITAEAEKLKVKV 2411
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElELQLFPQAgtllhfLRKEapdwEQSIGKVISPELLHRTDL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2412 TQLSDAQSKAEE-------------EAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLE 2478
Cdd:pfam12128 566 DPEVWDGSVGGElnlygvkldlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2479 KEKEKLKKeaaDLQKQSKEManvQQEQLQQEKTILQQSFFAEKEtlLKKEKAIEEEKKKLEKQFEDEVKKaEALKAEQER 2558
Cdd:pfam12128 646 TALKNARL---DLRRLFDEK---QSEKDKKNKALAERKDSANER--LNSLEAQLKQLDKKHQAWLEEQKE-QKREARTEK 716
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2559 Q--RKLMEEERKKLQSAMDAAI-KKQKEAEEEMNGKQKEM-QDLEKKRIEQEKL--LAEENKNLREKLQQ 2622
Cdd:pfam12128 717 QayWQVVEGALDAQLALLKAAIaARRSGAKAELKALETWYkRDLASLGVDPDVIakLKREIRTLERKIER 786
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2300-2593 |
1.60e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.94 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2300 EEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2379
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2380 DQETEGFQKSLEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEE-----AKKFKKQADEIKIRLQETEKHTSEKHTVVE 2454
Cdd:pfam02029 140 YQENKWSTEVRQAEEE------GEEEEDKSEEAEEVPTENFAKEEvkdekIKKEKKVKYESKVFLDQKRGHPEVKSQNGE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2455 KlEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA----DLQKQSKEMANVQQEQLQQEktilQQSFFAEKETLLKKEKA 2530
Cdd:pfam02029 214 E-EVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqkleELRRRRQEKESEEFEKLRQK----QQEAELELEELKKKREE 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2531 IEEEKKKLEKQFEDEvkKAEALKAEQERQRKLMEE-ERKKlqsaMDAAIKKQKEAEEEMNGKQK 2593
Cdd:pfam02029 289 RRKLLEEEEQRRKQE--EAERKLREEEEKRRMKEEiERRR----AEAAEKRQKLPEDSSSEGKK 346
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1795-2252 |
1.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1795 MEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEE-AKKQRQIAEEEAARQRAEAEKILKEKLTAI 1873
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1874 NEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKV--LEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 1950
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1951 RKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAeee 2030
Cdd:COG4717 208 LAELEEELEEAQ---EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL--- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2031 aarqhkaaqeEVGRLMKLAEEAKKQKEIAEKEAEKqvilVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKK 2110
Cdd:COG4717 282 ----------VLGLLALLFLLLAREKASLGKEAEE----LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2111 LAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEaeaaalkLKQEADSEMA 2190
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ-------LEELLGELEE 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2191 KYKKLAEKTLKQK-SSVEEELVKVKVQLDETDKQKSVLDVELKRLK--QEVSDAIKQKAQVEDEL 2252
Cdd:COG4717 421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAEL 485
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
57-122 |
1.71e-04 |
|
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: 43.80 E-value: 1.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 57 KKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 122
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
56-163 |
1.71e-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: 45.00 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 56 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 122
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141782 123 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 163
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2226-2596 |
1.73e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2226 VLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARL 2305
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2306 NIEAQEAARLRQIAESDLAKQRELAE--KMLEEKKQAIQ-EAAKLKAEAEKLQKQKDQAQVEaQKLLEAKKEMQQrldQE 2382
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEdiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE-RKQLQAKLQQTE---EE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2383 TEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKA---EEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2459
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2460 RLQSKQEadgLHKAiadlekekeklKKEAADLQKQSKEMANVQQE---QLQQEKTILQQSFFAEKETLLKKEKAIEEEKK 2536
Cdd:pfam07888 267 RDRTQAE---LHQA-----------RLQAAQLTLQLADASLALREgraRWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2537 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQ 2596
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2301-2437 |
1.77e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2301 EAARLNIeAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQEAAKLKaeaEKLQKQKDQAQ-VEAQKLLEAKKEMQQRL 2379
Cdd:PRK00409 505 EEAKKLI-GEDKEKLNELIASLEELERELEQK-AEEAEALLKEAEKLK---EELEEKKEKLQeEEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 2380 DQETEgfqkslEAERK-RQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKI 2437
Cdd:PRK00409 580 KEAKK------EADEIiKELRQLQKGGYASVKAHELIEARKrlnkaneKKEKKKKKQKEKQEELKV 639
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1716-1921 |
1.89e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1716 KQKEAAEMElgNQRKMAEETAKQKLAAEQElirlradfehAEQQRtVLDDELQRLKndvnsAVKQKKELEEElikvrkEM 1795
Cdd:PRK09510 70 QQKSAKRAE--EQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERLA-----AQEQKKQAEEA------AK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1796 EILLQQKsKAEKETMSNTEKSKqlLESEAAKMReLAEEATKlrsvAEEAKKQRQIAE-----EEAARQRAEAEKILKEKL 1870
Cdd:PRK09510 126 QAALKQK-QAEEAAAKAAAAAK--AKAEAEAKR-AAAAAKK----AAAEAKKKAEAEaakkaAAEAKKKAEAEAAAKAAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 1871 TAINEATRLKTEAEIALKEKEAENDRlKRKAEEEGYQRKVLEDQAAQHKQA 1921
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAEA-KAAAAKAAAEAKAAAEKAAAAKAA 247
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2548-2649 |
1.90e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2548 KAEALKAEQERQRKLMEEER-------KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2620
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKeaeaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100
....*....|....*....|....*....
gi 1207141782 2621 QQLQSSQKASYTKEIEIQTDKVPEEELVQ 2649
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1767-1936 |
2.14e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1767 LQRLKNDVNSAVKQKKELEEElikvrKEMEilLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKK 1846
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ-----QAEE--LQQKQAAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1847 QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENdrlKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 1926
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKKKAA 212
|
170
....*....|
gi 1207141782 1927 GQLKKSSDTE 1936
Cdd:PRK09510 213 AEAKKKAAAE 222
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1455-1788 |
2.32e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1455 ELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKavdadklRNAAQEEAEKLR 1534
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1535 KQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1614
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1615 KQVALTARLEESLKNEQVmVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1694
Cdd:COG4372 167 AALEQELQALSEAEAEQA-LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1695 KQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDV 1774
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 1207141782 1775 NSAVKQKKELEEEL 1788
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1580-1956 |
2.36e-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: 47.44 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1580 EEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESlkneqvmviqlqeeaEHLKKQQAEADKAREQAE 1659
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVS---------------SEVAEEEKEATKDAAEAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1660 KELETWRQKANEALRLRLQ-AEEEANKKTAAQEEAekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMaEETAKQ 1738
Cdd:pfam09731 117 AQLPKSEQEKEKALEEVLKeAISKAESATAVAKEA---------KDDAIQAVKAHTDSLKEASDTAEISREKA-TDSALQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1739 KLAAEQELIRLRADFEHAEQQrTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ 1818
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1819 LLESEAAKMREL-AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 1897
Cdd:pfam09731 266 IFPDIIPVLKEDnLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEA 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 1898 KRKAEeegYQRKVLEDQaaqhkQAIEEKIgqlkkssDTELDRQKKIVEETLKQRKVVEE 1956
Cdd:pfam09731 346 QLRLE---FEREREEIR-----ESYEEKL-------RTELERQAEAHEEHLKDVLVEQE 389
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1000-1973 |
2.43e-04 |
|
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: 47.74 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1000 ALIQKDSTSGEQDESVCKSYITQIKDLRLRLEGCESRTVNRLRQMVDKEPLKACTQRATEQKKVQTElegIKKDLDKVVE 1079
Cdd:TIGR01612 682 SIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGE---INKDLNKILE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1080 KSEAvlATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLkTIDlvirsTQGAEDILNKYENQLREVNKVPVNEKEI 1159
Cdd:TIGR01612 759 DFKN--KEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQI-NID-----NIKDEDAKQNYDKSKEYIKTISIKEDEI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1160 EASQTQLQKLRSEAEGKQATFDRLE---------EELQRATEVNKRMSQLHSERdveLEHYRQLVGNLRERWQAVFAQIE 1230
Cdd:TIGR01612 831 FKIINEMKFMKDDFLNKVDKFINFEnnckekidsEHEQFAELTNKIKAEISDDK---LNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1231 LRQRELDLLNRqmqayresYDWLIRWIADAKQRQDKLHavpiggskglqeqlTQEKKLLEEIEKNKDKVEDCQKFAKGYI 1310
Cdd:TIGR01612 908 EEYQNINTLKK--------VDEYIKICENTKESIEKFH--------------NKQNILKEILNKNIDTIKESNLIEKSYK 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1311 DaikDYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRY--SELMTLSSQYI---KFIIETQRRLQDEEKAA 1385
Cdd:TIGR01612 966 D---KFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLgkNKENMLYHQFDekeKATNDIEQKIEDANKNI 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1386 EKLKEEERKKMAEMQAELEKQ--KQLAETHAKAIAKAEQEA---NELKTKMK----------------DEVSK-RQDVAV 1443
Cdd:TIGR01612 1043 PNIEIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINItnfNEIKEKLKhynfddfgkeenikyaDEINKiKDDIKN 1122
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1444 DSEKQKHNIqRELQELKTLSEQ---EIKAKSQQVEEaLLSRTRIEEEIHIIRLQLETTM----KQKNTAE------TELL 1510
Cdd:TIGR01612 1123 LDQKIDHHI-KALEEIKKKSENyidEIKAQINDLED-VADKAISNDDPEEIEKKIENIVtkidKKKNIYDeikkllNEIA 1200
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1511 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEE--------------ELKRKSEAEKDAAKEKKKALEDLEKFK 1576
Cdd:TIGR01612 1201 EIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmikameayiedldEIKEKSPEIENEMGIEMDIKAEMETFN 1280
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1577 LQAEE-------AERHLKQAELEKQRQIQVVEEVAKKTAATQLESKqvaLTARLEESLKNEQVMVIQLQEEAE-----HL 1644
Cdd:TIGR01612 1281 ISHDDdkdhhiiSKKHDENISDIREKSLKIIEDFSEESDINDIKKE---LQKNLLDAQKHNSDINLYLNEIANiynilKL 1357
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1645 KKQQAEADKAREQAeKELETWRQKANEAL----RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAK-------AEEA 1713
Cdd:TIGR01612 1358 NKIKKIIDEVKEYT-KEIEENNKNIKDELdkseKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKelknhilSEES 1436
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1714 ALKQ--KEAAEME-----LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEE 1786
Cdd:TIGR01612 1437 NIDTyfKNADENNenvllLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHI--DKSKGCKDEADKNAKAIEKNKE 1514
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1787 ELIKVRKEMEILLQQKSKAE-KETMSNTEK-SKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEK 1864
Cdd:TIGR01612 1515 LFEQYKKDVTELLNKYSALAiKNKFAKTKKdSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKA 1594
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1865 ILKEKLTAINEATRL------KTEAEIALKEKEA------------ENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKi 1926
Cdd:TIGR01612 1595 AIDIQLSLENFENKFlkisdiKKKINDCLKETESiekkissfsidsQDTELKENGDNLNSLQEFLESLKDQ-KKNIEDK- 1672
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 1207141782 1927 gqlKKSSDtELDRQKKIVEETLKQRK------VVEEEIHILKLNFEKASSGKQ 1973
Cdd:TIGR01612 1673 ---KKELD-ELDSEIEKIEIDVDQHKknyeigIIEKIKEIAIANKEEIESIKE 1721
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2325-2638 |
2.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2325 KQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL---LEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT 2401
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLeeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2402 AEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAdlEKEK 2481
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2482 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2561
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 2562 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQ 2638
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
989-1354 |
2.68e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 989 DNLLRSVEQEPALIQKDSTSGEQDESVCKSYITQIKDLRLRLEGCESRTVNRLRQMVDKepLKACTQRATEQKKVQTELE 1068
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED--LSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1069 GIKKDLDKVVEKSEAVLATSQQSSSapvlRSEIDITQKKMEHVYglssvylDKLKTIDLVIRSTQG-----------AED 1137
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLS----HSRIPEIQAELSKLE-------EEVSRIEARLREIEQklnrltlekeyLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1138 ILNKYENQLREV-NKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELqratevnkrmSQLHSERDVELEHYRQlvg 1216
Cdd:TIGR02169 834 EIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----------GDLKKERDELEAQLRE--- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1217 nLRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiadAKQRQDKlhavpIGGSKGLQEQLTQEKKLLEEIEKNK 1296
Cdd:TIGR02169 901 -LERKIEELEAQIEKKRKRLSELKAKLEA--------------LEEELSE-----IEDPKGEDEEIPEEELSLEDVQAEL 960
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 1297 DKVE-DCQKFAKGYIDAIKDYELQLVTYKALVEpiasplKKAKMESASDDI---IQEYVTLR 1354
Cdd:TIGR02169 961 QRVEeEIRALEPVNMLAIQEYEEVLKRLDELKE------KRAKLEEERKAIlerIEEYEKKK 1016
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2795-2832 |
2.78e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.78e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141782 2795 TKLLSAERAVTGFKDPFTGDTISVFEAMKKGLITEDQA 2832
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2315-2474 |
2.79e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2315 LRQIAESDLAKQRELAEKMLEE--------KKQAIQEA----AKLKAEAEKLQKQKDQaqvEAQKLLEAKKEMQQRLDQE 2382
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEakkeaeaiKKEALLEAkeeiHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2383 TEGFQK---SLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFkkQADEIK-IRLQETEKHTSEK--HTVVEKL 2456
Cdd:PRK12704 102 LELLEKreeELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKeILLEKVEEEARHEaaVLIKEIE 179
|
170
....*....|....*...
gi 1207141782 2457 EvqrlQSKQEADGLHKAI 2474
Cdd:PRK12704 180 E----EAKEEADKKAKEI 193
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3161-3196 |
3.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.22e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1207141782 3161 RLLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEM 3196
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2183-2416 |
3.23e-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: 46.94 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2183 QEADSEMAKYKKLAEKTLKQKSsvEEELVKVKVQLDETDKQKSVLDVELKRLKQEVsdaikqkAQVEDELSKVKIQMEdl 2262
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQR--EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2263 lklklkIEKENQELMKKdkdnTKKLLEEEAENMKKL----AEEAARL-NIEAQ-EAARlrqiaESDLAKQRELAEKMLEE 2336
Cdd:pfam05667 381 ------ELEKQYKVKKK----TLDLLPDAEENIAKLqalvDASAQRLvELAGQwEKHR-----VPLIEEYRALKEAKSNK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2337 KKqaiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSleAERKRQLEITAEAEKLKVKVTQ-LS 2415
Cdd:pfam05667 446 ED----ESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRS--AYTRRILEIVKNIKKQKEEITKiLS 519
|
.
gi 1207141782 2416 D 2416
Cdd:pfam05667 520 D 520
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2312-2516 |
3.47e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2312 AARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLE 2391
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2392 AERKRQ-----LEITAEAEKLK------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKL--EV 2458
Cdd:COG3883 94 ALYRSGgsvsyLDVLLGSESFSdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2459 QRLQSKQEADgLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQS 2516
Cdd:COG3883 174 EAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4299-4332 |
3.59e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.59e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141782 4299 EETGPVAGILDTDTLEKVSVTEAMHRNLVDNITG 4332
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1657-1969 |
3.89e-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: 46.82 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1657 QAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQ--RKMAEE 1734
Cdd:pfam15964 321 SSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKemKKEREE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1735 TAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQrlkndvnSAVKQKKELEEELIKVRKEMEILLQQkSKAEKEtmsntE 1814
Cdd:pfam15964 401 LGATMLALSQNVAQLEAQVEKVTREKNSLVSQLE-------EAQKQLASQEMDVTKVCGEMRYQLNQ-TKMKKD-----E 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1815 KSKQLLESEAAKMRELA---EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKIlkekltaineaTRLKTEAEIALKEKE 1891
Cdd:pfam15964 468 AEKEHREYRTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQDAARAREECLKL-----------TELLGESEHQLHLTR 536
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 1892 AENDRLKRKAEEEGyqrKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 1969
Cdd:pfam15964 537 LEKESIQQSFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT 611
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1511-1672 |
3.98e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1511 QLRAKAVDADKLRN--AAQEEAEKLRKQVAE-----ETQKKRKAEEELKRKSEAEKDAAKEKKKALED-----LEKFKLQ 1578
Cdd:PRK09510 69 QQQKSAKRAEEQRKkkEQQQAEELQQKQAAEqerlkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEaaakaAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1579 AEEAERHL----KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1654
Cdd:PRK09510 149 AEAEAKRAaaaaKKAAAEAKKKAE--AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170
....*....|....*...
gi 1207141782 1655 REQAEKELETWRQKANEA 1672
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAA 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2222-2473 |
3.99e-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: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2222 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLkiekenqelmkkdkdntkklLEEEAENMKKLAEE 2301
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE--------------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2302 AARLNieaQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ 2381
Cdd:COG4913 670 IAELE---AELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2382 ETEgfqKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKL-EVQR 2460
Cdd:COG4913 746 ELR---ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN---REWPAETADLDADLESLpEYLA 819
|
250
....*....|...
gi 1207141782 2461 LQSKQEADGLHKA 2473
Cdd:COG4913 820 LLDRLEEDGLPEY 832
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2194-2471 |
4.02e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2194 KLAEKTLKQKSSVEEelvkVKVQLDETDKQKSVLDVELKRLKQEVSD-----------AIkQKAQVEDELSKVKIQMEDL 2262
Cdd:PRK04863 359 ELEERLEEQNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtrAI-QYQQAVQALERAKQLCGLP 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2263 LKLKLKIEKENQELMKKDKDNTKKLLEEE-----AENMKKLAEEAARL------NIEAQEAARLRQIAESDLAKQRELAE 2331
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAE 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2332 KM---------LEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITA 2402
Cdd:PRK04863 514 QLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141782 2403 EAEKLKVKVTQLSDAQSKAEE------EAKKFKKQADEIKIRLQETEKHTSEkhtVVEKLEVQRLQSKQEADGLH 2471
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALARlreqsgEEFEDSQDVTEYMQQLLERERELTV---ERDELAARKQALDEEIERLS 665
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1463-1714 |
4.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1463 SEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELlqlrakavdadklrNAAQEEAEKLRKQVAEETQ 1542
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------------EALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1543 KKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQ---RQIQVVEEVakKTAATQLESKQval 1619
Cdd:COG3883 80 EIEERREELGE-----RARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKiadADADLLEEL--KADKAELEAKK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1620 tARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEE 1699
Cdd:COG3883 150 -AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*
gi 1207141782 1700 AKREAKKRAKAEEAA 1714
Cdd:COG3883 229 AAAAAAAAAAAAAAA 243
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1752-2636 |
4.17e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1752 DFEHAEQQRTVLDDELQRLKNDVNSAVK-QKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ-LLESEAAKMRE 1829
Cdd:TIGR00606 55 DFPPGTKGNTFVHDPKVAQETDVRAQIRlQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHgEKVSLSSKCAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1830 LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR----LKTEAEIAL------KEKEAENDRLKR 1899
Cdd:TIGR00606 135 IDREMISHLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRyikaLETLRQVRQtqgqkvQEHQMELKYLKQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1900 KAEEEGYQRKVLEDQAAQhkQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekasSGKQELELEL 1979
Cdd:TIGR00606 215 YKEKACEIRDQITSKEAQ--LESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK-------SRKKQMEKDN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1980 KKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeakvKQIQAAEEEAARQHKaaqeEVGRLMKLAEEAKKQKeiA 2059
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQ----------------RTVREKERELVDCQR----ELEKLNKERRLLNQEK--T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2060 EKEAEKQVILVQEAAQKCsaaEQKAQNVLVQQNKDSMAQDKLKE------EFEKAKKLAQE--AEKAKDNAEKEAALLHK 2131
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQE---HIRARDSLIQSLATRLELDGFERgpfserQIKNFHTLVIErqEDEAKTAAQLCADLQSK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2132 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2211
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2212 KVKVQLDEtdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD--NTKKL-- 2287
Cdd:TIGR00606 501 KEVKSLQN---EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpNKKQLed 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2288 -LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLaKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2366
Cdd:TIGR00606 578 wLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-ESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2367 KLLEAKKEMQQRLDQETEGFQKSL---EAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEI----KIRL 2439
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglaPGRQ 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2440 QETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAiADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFA 2519
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2520 EKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALK---------------------------AEQERQRKLMEEERKKLQS 2572
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktnelkseklqiGTNLQRRQQFEEQLVELST 895
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 2573 AMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSS--QKASYTKEIE 2636
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkNIHGYMKDIE 961
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1579-1904 |
4.71e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1579 AEEAERHLKQAELEKQRQIQVVEEVAK------KTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAd 1652
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGqvtesvEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1653 karEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKeeakreaKKRAKAEEAALKQKEAAEMELGNQRKMA 1732
Cdd:pfam02029 83 ---LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR-------LGRYKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1733 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN 1812
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1813 T----EKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQiaeEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALK 1888
Cdd:pfam02029 233 SqereEEAEVFLEAEQ-KLEELRRRRQEKESEEFEKLRQKQ---QEAELELEELKKKREER-RKLLEEEEQRRKQEEAER 307
|
330
....*....|....*.
gi 1207141782 1889 EKEAENDRLKRKAEEE 1904
Cdd:pfam02029 308 KLREEEEKRRMKEEIE 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1097-1301 |
4.81e-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: 45.91 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1097 LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAediLNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGK 1176
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAAL------EAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1177 QATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRW 1256
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207141782 1257 IADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVED 1301
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2033-2357 |
5.00e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2033 RQHKAAQEEVGRLMKLAEEAK-----KQ----KEIAEKEAEKqvilvQEAAQKCSAAEQKAqnvlVQQNKDSMAQDKLKE 2103
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeaRQarleREKAAREARH-----KKAAEARAAKDKDA----VAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2104 EFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqaKAQEDAEKLRKEAekeasrraeaeaaalklkQ 2183
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAE--------------KQAAAAADPKKAA------------------V 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2184 EADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqldetdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLL 2263
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAV-------AAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIAR 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2264 KLKLKIEKENQElmkkdkdntkklLEEEAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRElaekmLEEKKQAIqE 2343
Cdd:PRK05035 624 AKAKKAEQQANA------------EPEEPVDPRKAAVAAAI----ARAKARKAAQQQANAEPEEA-----EDPKKAAV-A 681
|
330
....*....|....
gi 1207141782 2344 AAKLKAEAEKLQKQ 2357
Cdd:PRK05035 682 AAIARAKAKKAAQQ 695
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2295-2434 |
5.96e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2295 MKKLAEEAARLNIEAQEAARlRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL--LEAK 2372
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAE-EKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLdnLENQ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2373 KEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2434
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE 168
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2547-2636 |
6.00e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2547 KKAEALKAEQ-ERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMngKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQS 2625
Cdd:cd16269 200 IEAERAKAEAaEQERKLLEEQQRELEQKLEDQERSYEEHLRQL--KEKMEEERENLLKEQERALESKLKEQEALLEEGFK 277
|
90
....*....|.
gi 1207141782 2626 SQKASYTKEIE 2636
Cdd:cd16269 278 EQAELLQEEIR 288
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2306-2585 |
6.51e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2306 NIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiqEAAKLKAEAEKlQKQKDqAQVEAQKLLEAKKemQQRLDQETEG 2385
Cdd:NF012221 1533 NVVATSESSQQADAVSKHAKQDDAAQNALADKERA--EADRQRLEQEK-QQQLA-AISGSQSQLESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2386 FQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQ-ADEIKIRLQEteKHTSEKHTVVEKLEVQRLQSK 2464
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQE--QLDDAKKISGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2465 QEADGLHKAIADLEkekeklkkeaADLQKQSKEMANVQQEqLQQEKTilqQSFFAEKETLLKKEKAIEEEkkklekqfed 2544
Cdd:NF012221 1682 DNQQKVKDAVAKSE----------AGVAQGEQNQANAEQD-IDDAKA---DAEKRKDDALAKQNEAQQAE---------- 1737
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141782 2545 evKKAEAL--KAEQERQRKLMEEERKKLQSAMDAAIKKQKEAE 2585
Cdd:NF012221 1738 --SDANAAanDAQSRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2214-2456 |
6.86e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2214 KVQLDETDKQKSVLDVELKRLKQEVsdAIKQKAQVE-DELSKVKIQ----MEDLLKLKLKIEKENQELMKKDKDNTKKLL 2288
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQI--KTYNKNIEEqRKKNGENIArkqnKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2289 EEEAENMKKLAEEAARLNIEAQEAARLrqiaesdlakqrelaEKMLEEK------KQAIQEAAKLkaeAEKLQKQKDQAQ 2362
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKV---------------IKMYEKGgvcptcTQQISEGPDR---ITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2363 VEAQKLLEAKKEMQQRLDQETE------GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2436
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEqskkllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|
gi 1207141782 2437 IRLQETEKHTSEKHTVVEKL 2456
Cdd:PHA02562 393 KTKSELVKEKYHRGIVTDLL 412
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2090-2436 |
6.93e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.77 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2090 QQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKA----EEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE 2165
Cdd:NF033838 112 EAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAkdqkEEDRRNYPTNTYKTLELEIAESDVEVKKAELE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2166 --KEASRRAEAEAAALKLKQEADSEMAKYKKLaEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2243
Cdd:NF033838 192 lvKEEAKEPRDEEKIKQAKAKVESKKAEATRL-EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2244 QKAQVEDElSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAARLR-QIAESD 2322
Cdd:NF033838 271 GEPATPDK-KENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKV--EEAKKKAKDQKEEDRRNYPTNTYKTLElEIAESD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2323 LAKQRELAEKMLEEKKQAIQEAAKLKAEAEklqkqkdqaqveaqklLEAKKEMQQRLDQ-ETEGFQKSLEAERKrqleiT 2401
Cdd:NF033838 348 VKVKEAELELVKEEAKEPRNEEKIKQAKAK----------------VESKKAEATRLEKiKTDRKKAEEEAKRK-----A 406
|
330 340 350
....*....|....*....|....*....|....*..
gi 1207141782 2402 AEAEKLKVKVTQLSDAQS--KAEEEAKKFKKQADEIK 2436
Cdd:NF033838 407 AEEDKVKEKPAEQPQPAPapQPEKPAPKPEKPAEQPK 443
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2183-2387 |
7.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2183 QEADSEMAKYKK---------LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA--QVEDE 2251
Cdd:COG3206 192 EEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2252 LSKVKIQMedllklklkiekenQELMKKDKDNT---KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQre 2328
Cdd:COG3206 272 LAELEAEL--------------AELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ-- 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 2329 laekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQ 2387
Cdd:COG3206 336 -----LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| DUF2968 |
pfam11180 |
Protein of unknown function (DUF2968); This family of proteins has no known function. |
2292-2368 |
7.57e-04 |
|
Protein of unknown function (DUF2968); This family of proteins has no known function.
Pssm-ID: 431707 [Multi-domain] Cd Length: 180 Bit Score: 43.52 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2292 AENMKKLAE-EAARLNIEAQEAARLRQIAES---------DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2361
Cdd:pfam11180 88 ARQTAQLADvEIRRAQLEAQKAQTERQIAASearaarlqaDLQVARQQEQQVASRQKQTRQEAAALEAQRQAAQAQLRAL 167
|
....*..
gi 1207141782 2362 QVEAQKL 2368
Cdd:pfam11180 168 QRQIRQL 174
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
545-639 |
7.78e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 545 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 621
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIeegHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1207141782 622 LQYAKLLTSSKTRLRSLD 639
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3413-3446 |
7.88e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.88e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141782 3413 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPE 3446
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2759-2792 |
8.19e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 8.19e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141782 2759 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPE 2792
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1504-1736 |
8.46e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1504 TAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaLEDLEKFKLQAEEAe 1583
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL--------------QAEIDKLQAEIAEA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1584 rhlkQAELEKQRqiqvvEEVAKKTAATQLESKQVALTARLEES----------------LKNEQVMVIQLQEEAEHLKKQ 1647
Cdd:COG3883 78 ----EAEIEERR-----EELGERARALYRSGGSVSYLDVLLGSesfsdfldrlsalskiADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1648 QAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGN 1727
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
....*....
gi 1207141782 1728 QRKMAEETA 1736
Cdd:COG3883 229 AAAAAAAAA 237
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
56-153 |
8.63e-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: 42.65 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 56 QKKTFTKWVN---------KHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 122
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1207141782 123 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 153
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1712-1955 |
8.90e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1712 EAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKV 1791
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1792 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLT 1871
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1872 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQR 1951
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
....
gi 1207141782 1952 KVVE 1955
Cdd:COG4372 288 LEEA 291
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1765-2438 |
9.84e-04 |
|
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: 45.81 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1765 DELQRLKNDVNSaVKQK-----KELEEELIKVRKEMEILLQQKSKAEK---ETMSN-----TEKSKQLLESEAAKMRELA 1831
Cdd:TIGR01612 1111 DEINKIKDDIKN-LDQKidhhiKALEEIKKKSENYIDEIKAQINDLEDvadKAISNddpeeIEKKIENIVTKIDKKKNIY 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1832 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKV 1910
Cdd:TIGR01612 1190 DEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKK-KSEHMIKAMEAYIEDlDEIKEKSPEIENEMGI 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1911 LEDQAAQ--------------------HKQAI----------------EEKIGQLKKSSDTELDRQKKIVEETLKQRKVV 1954
Cdd:TIGR01612 1269 EMDIKAEmetfnishdddkdhhiiskkHDENIsdirekslkiiedfseESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1955 EEEIHILKLNFEKA--SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfrKLALEEEKKRKEAEAKVKQIqaaeEEAA 2032
Cdd:TIGR01612 1349 ANIYNILKLNKIKKiiDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD---DINLEECKSKIESTLDDKDI----DECI 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2033 RQHKAAQEEVgrlmkLAEEAKKQKEIAE-KEAEKQVILVqeaAQKCSAAEQKAQNVLVQQnKDSMAQD------KLKEEF 2105
Cdd:TIGR01612 1422 KKIKELKNHI-----LSEESNIDTYFKNaDENNENVLLL---FKNIEMADNKSQHILKIK-KDNATNDhdfninELKEHI 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2106 EKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER--QKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQ 2183
Cdd:TIGR01612 1493 DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKTKKDSEIIIKEIKDAHK----------KFIL 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2184 EADSEMAKYKKLAektlKQKSSVEEELVKV-KVQLDETDKQKSVLDVELKRLK-----QEVSDAIKQKAQVEDELSKVKI 2257
Cdd:TIGR01612 1563 EAEKSEQKIKEIK----KEKFRIEDDAAKNdKSNKAAIDIQLSLENFENKFLKisdikKKINDCLKETESIEKKISSFSI 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2258 QMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEK-MLEE 2336
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKeEIES 1718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2337 KKQAIQEAAKLKAEA------------EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAEA 2404
Cdd:TIGR01612 1719 IKELIEPTIENLISSfntndlegidpnEKLEEYNTEIGDIYEEFIELYNIIAGCLETVS---KEPITYDEIKNTRINAQN 1795
|
730 740 750
....*....|....*....|....*....|....
gi 1207141782 2405 EKLKVKvtqlsdaqskaeEEAKKFKKQADEIKIR 2438
Cdd:TIGR01612 1796 EFLKII------------EIEKKSKSYLDDIEAK 1817
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1752-1921 |
1.10e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 45.31 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1752 DFEHAEQQRTVLDDELQRL---------KNDVNSAVKQKKELEEELIkvrkemeillqQKSKAEKetmsnTEKSKQLLES 1822
Cdd:pfam04147 126 DDDSEEEEDGQLDLKRVRRahfgggeddEEEEPERKKSKKEVMEEVI-----------AKSKLHK-----YERQKAKEED 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1823 EAakMRE-----LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE--KILKEkLTAINEAT---RLKTEAEIALKEKE- 1891
Cdd:pfam04147 190 EE--LREeldkeLKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLVRE-LAFDKRAKpsdRTKTEEELAEEEKEr 266
|
170 180 190
....*....|....*....|....*....|....
gi 1207141782 1892 ---AENDRLKR-KAEEEGYQRKvlEDQAAQHKQA 1921
Cdd:pfam04147 267 lekLEEERLRRmRGEEDEEEED--GKKKKKHKSA 298
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2286-2516 |
1.17e-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: 44.04 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2286 KLLEEEAENMKKLAEEaarlniEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ-KQKDQAQVE 2364
Cdd:pfam17045 38 DIREEELLSARNTLER------KHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQrKQLKEAREE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2365 AQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITaeaeklkvKVTQLsDAQSKA-EEEAKKFKKQADEIKI--RLQE 2441
Cdd:pfam17045 112 AKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQ--------QVASL-EAQRKAlAEQSSLIQSAAYQVQLegRKQC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2442 TEKHTSEKHTVVEKLEVQR---LQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKeMANVQQEQLQQEKTILQQS 2516
Cdd:pfam17045 183 LEASQSEIQRLRSKLERAQdslCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELR-MSQRQLQVLQNELMELKAT 259
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2216-2449 |
1.21e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2216 QLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKL------LE 2289
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkeeRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2290 EEAENMKKLAEEAARLNIEAQEAARLR-----------------QIAESDLAKQRELAEKM------LEEKKQAIQEAAK 2346
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGgsidklrkeierlewrqQTEVLSPEEEKELVEKIkelekeLEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2347 LKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2426
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE-ADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|...
gi 1207141782 2427 KFKKQADEIKIRLQETEKHTSEK 2449
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKE 263
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2192-2407 |
1.21e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2192 YKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiek 2271
Cdd:PRK09510 64 YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA--------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2272 enQELMKKDKDNTKKLLEEEAenmKKLAEEAARlnieAQEAARLRQIAESDlAKQRELAEKMLEEKKQAiQEAAKLKAEA 2351
Cdd:PRK09510 135 --EEAAAKAAAAAKAKAEAEA---KRAAAAAKK----AAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAA-KAAAEAKKKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 2352 EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2407
Cdd:PRK09510 204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1630-1796 |
1.24e-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: 43.76 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1630 EQVMVIQLQE---EAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKtaaqeeAEKQKEEAKREAKK 1706
Cdd:COG1579 5 DLRALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1707 RAKAEEAA-LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELE 1785
Cdd:COG1579 79 EEQLGNVRnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|.
gi 1207141782 1786 EELIKVRKEME 1796
Cdd:COG1579 159 EELEAEREELA 169
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3450-3486 |
1.26e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141782 3450 KLLSAEKAVTGYKDPYTGNKISLLQAMQKQLVLREHA 3486
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
51-159 |
1.33e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.90 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 51 ERDRVQKKTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 121
Cdd:cd21330 9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141782 122 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 159
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1527-1742 |
1.38e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1527 QEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhLKQAELEKQRQIQVVE----- 1601
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAK-AKAAALAKQKREGTEEvteee 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1602 -EVAKKTAATQLESKQVALTArleeslkneqvmviQLQEEAEHLKKQQAEADKAREQAEKeletwRQKANEALRLRLQAE 1680
Cdd:PRK07735 90 kAKAKAKAAAAAKAKAAALAK--------------QKREGTEEVTEEEKAAAKAKAAAAA-----KAKAAALAKQKREGT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 1681 EEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1742
Cdd:PRK07735 151 EEV-----TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKA 207
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1332-1682 |
1.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1332 SPLKKA--KMESASD------DIIQEYVTLRTRYSELMTLSSQYIK---FIIETQRRLQDEEK--------AAEKLKEEE 1392
Cdd:PRK04863 226 SGVRKAfqDMEAALRenrmtlEAIRVTQSDRDLFKHLITESTNYVAadyMRHANERRVHLEEAlelrrelyTSRRQLAAE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1393 RKKMAEMQAELEKQK--------------------QLAETHAKAIAKAEQEANELKTKMKD--EVSKRQDVAVD-SEKQK 1449
Cdd:PRK04863 306 QYRLVEMARELAELNeaesdleqdyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEqnEVVEEADEQQEeNEARA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1450 HNIQRELQELKT--------LSEQEIKA-KSQQVEEAL-----------LSRTRIEEEIHIIRLQLEttmkqknTAETEL 1509
Cdd:PRK04863 386 EAAEEEVDELKSqladyqqaLDVQQTRAiQYQQAVQALerakqlcglpdLTADNAEDWLEEFQAKEQ-------EATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1510 LQLRAKAVDADKLRNAAQEEAEKLRKQVAE--ETQKKRKAEEELK--RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERH 1585
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVRKIAGEvsRSEAWDVARELLRrlREQRHLAEQLQQLRMRLSELEQRLRQQQRAERL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1586 LKQAElekQRQIQVVEevakktAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHlkkQQAEADKAREQAEKELETW 1665
Cdd:PRK04863 539 LAEFC---KRLGKNLD------DEDELEQLQEELEARL-ESLSESVSEARERRMALRQ---QLEQLQARIQRLAARAPAW 605
|
410
....*....|....*...
gi 1207141782 1666 RQkANEAL-RLRLQAEEE 1682
Cdd:PRK04863 606 LA-AQDALaRLREQSGEE 622
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
109-153 |
1.46e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1207141782 109 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 153
Cdd:cd21294 78 FQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
49-157 |
1.46e-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: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 124
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 1207141782 125 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 157
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1525-1854 |
1.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1525 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1604
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1605 KktAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAN 1684
Cdd:COG4372 122 K--ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1685 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLD 1764
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1765 DELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA 1844
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
330
....*....|
gi 1207141782 1845 KKQRQIAEEE 1854
Cdd:COG4372 360 SKGAEAGVAD 369
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
58-150 |
1.58e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.55 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 58 KTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLKHRQV 127
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 1207141782 128 KLVNIRNDDIADGNpKLTLGLIW 150
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
1702-1912 |
1.63e-03 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.09 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1702 REAKKRAKAEEAALkQKEAAemelgNQRKMAEETAKQKLAAEQE---------LIRLRADFEHAEQQRTVLD-------- 1764
Cdd:NF033875 66 SETPKTAVSEEATV-QKDTT-----SQPTKVEEVASEKNGAEQSsatpndttnAQQPTVGAEKSAQEQPVVSpettnepl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1765 ---DELQRLKNDVNSAVKQKKELE-----EELIKVRKEMEILLQQKSKaekETMSNTEkSKQLleseAAKMRElaeeatk 1836
Cdd:NF033875 140 gqpTEVAPAENEANKSTSIPKEFEtpdvdKAVDEAKKDPNITVVEKPA---EDLGNVS-SKDL----AAKEKE------- 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 1837 lrsVAEEAKKQRQIAEEEAARQRAEAEKILKEKltaineatrlkteAEIALKEkeaendrlkrKAEEEGYQRKVLE 1912
Cdd:NF033875 205 ---VDQLQKEQAKKIAQQAAELKAKNEKIAKEN-------------AEIAAKN----------KAEKERYEKEVAE 254
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1644-1963 |
1.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1644 LKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1723
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1724 ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS 1803
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1804 KAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 1883
Cdd:COG4372 168 ALEQE---LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1884 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL 1963
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1511-1802 |
1.77e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1511 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1590
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1591 LEKQRQIQVVEEVAKKTAATQLESKQVALTAR----LEESLKNEQVMVIQLQ----EEAEHLKKQQAEADKAREQ----A 1658
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekEEEREEDERILEYLKEkaerEEEREAEREEIEEEKEREIarlrA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1659 EKELETWRQKANEALRLRLQAEE---EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1735
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEqerKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 1736 AKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1802
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1178-1773 |
1.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1178 ATFDRLEEELQRATE---VNKRMSQLHSERDVELEHYRQLVGnLRERWQAVFAQielrqRELDLLNRQMQAYRESYDWLI 1254
Cdd:COG4913 235 DDLERAHEALEDAREqieLLEPIRELAERYAAARERLAELEY-LRAALRLWFAQ-----RRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1255 RWIADAKQRQDKLHAVpiggSKGLQEQLTQ-----EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVT----YKA 1325
Cdd:COG4913 309 AELERLEARLDALREE----LDELEAQIRGnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1326 LVEPIASplKKAKMESASDDIIQEYVTLRTRYSELMtlssqyikfiiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK 1405
Cdd:COG4913 385 LRAEAAA--LLEALEEELEALEEALAEAEAALRDLR-----------RELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1406 QKQLAETHAKAIA-----KAEQEA---------NELKTKM------KDEVSKrqdvAVDSEKQKHNIQ-------RELQE 1458
Cdd:COG4913 452 ALGLDEAELPFVGelievRPEEERwrgaiervlGGFALTLlvppehYAAALR----WVNRLHLRGRLVyervrtgLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1459 LKTLSEQ----EIKAKSQQVEEALlsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAV-----DADKLR------ 1523
Cdd:COG4913 528 RPRLDPDslagKLDFKPHPFRAWL--EAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGNGTrhekdDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1524 --NAAQEEAekLRKQVAEETQKKRKAEEELKrkseaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQvVE 1601
Cdd:COG4913 606 fdNRAKLAA--LEAELAELEEELAEAEERLE-----------------------ALEAELDALQERREALQRLAEYS-WD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1602 EVAKKTAATQLESKQVALtarleESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEE 1681
Cdd:COG4913 660 EIDVASAEREIAELEAEL-----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1682 EANKKTAAQEEAEKQkeeakrEAKKRAKAEEAALKQKEAAEmELGNQRKMAEETAKQklaAEQELIRLRADF------EH 1755
Cdd:COG4913 735 RLEAAEDLARLELRA------LLEERFAAALGDAVERELRE-NLEERIDALRARLNR---AEEELERAMRAFnrewpaET 804
|
650 660
....*....|....*....|...
gi 1207141782 1756 AEQQRTVLD-----DELQRLKND 1773
Cdd:COG4913 805 ADLDADLESlpeylALLDRLEED 827
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1702-1958 |
1.84e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1702 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1781
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1782 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA---AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQ 1858
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdleQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1859 RAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELD 1938
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260
....*....|....*....|
gi 1207141782 1939 RQKKIVEETLKQRKVVEEEI 1958
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEE 262
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1641-1865 |
2.03e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1641 AEHLKKQQAEADKAREQAEKELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEeAALKQKEA 1720
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR-AELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1721 AEMELGNQRKMAEETAKQkLAAEQELIRLRADFEHAEQQRTVL-------DDELQRLKNDVNSAVKQ-KKELEEELIKVR 1792
Cdd:COG3206 241 RLAALRAQLGSGPDALPE-LLQSPVIQQLRAQLAELEAELAELsarytpnHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141782 1793 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI 1865
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4026-4057 |
2.11e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.11e-03
10 20 30
....*....|....*....|....*....|..
gi 1207141782 4026 KLLSAERAVTGYKDPYSGKVISLFQAMKKGLI 4057
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1733-1863 |
2.27e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1733 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsN 1812
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE---R 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141782 1813 TEKSKQLLEsEAAKMRELAEEAT------KLRSVAEEAKKQR----QIAEEEAARQRAEAE 1863
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETrilidqQLRKAGWEADSKTlrfsKGARPEKGRNLAIAE 274
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1385-1621 |
2.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1385 AEKLKEEERKKMAEMQAELEK-QKQLAETHAKaIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKT-L 1462
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAaQAELDALQAE-LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1463 SEQEIKAKSQQVEEALLSRTRIEEEIHiiRLQLETTMKQKNTAETELLQLRAKAVDADKlrNAAQEEAEKLRKQVAEETQ 1542
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLD--RLSALSKIADADADLLEELKADKAELEAKK--AELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 1543 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTA 1621
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
56-153 |
2.39e-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: 40.97 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 56 QKKTFTKWVNKHLVK---------AQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 121
Cdd:cd21293 2 EKGSYVDHINRYLGDdpflkqflpIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1207141782 122 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 153
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3123-3159 |
2.46e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141782 3123 KLLSAERAVCGYKDPYTGKTVSLFEAMQKDLIKKEQG 3159
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1820-1950 |
2.58e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.31 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1820 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAarqRAEAEKILKEkltAINEATRLKTEaeiALKEKEAENDRLKR 1899
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 1900 KAEEEGYQ-----RKVLEDQAAQHKQAIEEKIgqLKKSSDTelDRQKKIVEETLKQ 1950
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKI--LGKELDA--AAQAALVDRFIAE 151
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3951-3989 |
2.62e-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: 2.62e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 3951 YLEGISSIAGVFVEATKDRLSVYQAMKKTMIRPGTAFEL 3989
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2204-2444 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2204 SSVEEELVKVKVQLDETDKQKSVLDVEL-KRLKQEVSDAIKQKAQVEDELSKVkiqMEDLLKLKLKIEKENQELMKKdkd 2282
Cdd:COG5185 206 SIKESETGNLGSESTLLEKAKEIINIEEaLKGFQDPESELEDLAQTSDKLEKL---VEQNTDLRLEKLGENAESSKR--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2283 ntkklLEEEAENMKKLAEEAARLNIEAQEAARLRQ-IAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2360
Cdd:COG5185 280 -----LNENANNLIKQFENTKEKIAEYTKSIDIKKaTESLEEQLAAAEAEQELEESKRETETGiQNLTAEIEQGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2361 AQVEAQKLLEAKKEMQQ--RLDQETEGFQKSLEAERKRQLEITAEAEK-LKVKVTQLSDAQSKAEEEAKKFKKQADEIKI 2437
Cdd:COG5185 355 NLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGyAQEILATLEDTLKAADRQIEELQRQIEQATS 434
|
....*..
gi 1207141782 2438 RLQETEK 2444
Cdd:COG5185 435 SNEEVSK 441
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2285-2432 |
2.70e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2285 KKLLEEEAENMKKLAEEAARLNIEAQEAAR---LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2361
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2362 QVEAQKLLEAKKEMQQRLDQETEGFQK--SLEAERKRQ-----LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2432
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKlllklLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1745-1893 |
2.74e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.90 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1745 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAE----KETMSNTEKSKQLL 1820
Cdd:pfam05911 682 ENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAEtqlkCMAESYEDLETRLT 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1821 ESEaAKMRELAEEATKLRSVAEEakkQRQIAEEEAAR--------QRAEAEKILKEklTAINEATRLKTEAEI-ALKEKE 1891
Cdd:pfam05911 762 ELE-AELNELRQKFEALEVELEE---EKNCHEELEAKclelqeqlERNEKKESSNC--DADQEDKKLQQEKEItAASEKL 835
|
..
gi 1207141782 1892 AE 1893
Cdd:pfam05911 836 AE 837
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
2354-2436 |
2.92e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 42.60 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2354 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgfQKSLEAERKRQLeiTAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2433
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDD--EKQELLAEYRAL--KAELESLEVYNRQLERLVASQEQEIASLERQIE 86
|
...
gi 1207141782 2434 EIK 2436
Cdd:pfam11932 87 EIE 89
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2205-2443 |
3.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2205 SVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklKIEKENQELMKKDKDnt 2284
Cdd:PRK01156 194 SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-------MKNRYESEIKTAESD-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2285 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2364
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141782 2365 AQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2443
Cdd:PRK01156 345 KSRYDDLNNQILE-LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1702-2138 |
3.42e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1702 REAKKRAKAEEAALKQKEAAEMElgnQRKMAEETAKQKLAAEQELIRLRADFEHAEQQrtvlddelqrlkndvnsAVKQK 1781
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEE-----------------AREAK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1782 KELEEELIKVRKEMEillQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE----EEAAR 1857
Cdd:COG3064 62 AEAEQRAAELAAEAA---KKLAEAEKAA----AEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAkrkaEEEAK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1858 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTEL 1937
Cdd:COG3064 135 RKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1938 DRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEA 2017
Cdd:COG3064 215 ALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2018 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMA 2097
Cdd:COG3064 295 LVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGA 374
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1207141782 2098 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2138
Cdd:COG3064 375 LLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAA 415
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2196-2513 |
3.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2196 AEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenQE 2275
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA-----------QE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2276 LMKKDKDNTKKLLEEeaenMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2355
Cdd:COG4372 102 ELESLQEEAEELQEE----LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2356 KQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEI 2435
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2436 KIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2513
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1159-1685 |
3.51e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1159 IEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLrERWQAVFAQIELRQRELDL 1238
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNL-EKKQKKFDQMLAEEKAISA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1239 lnrqmqAYRESYDwliRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK-NKDKVEDCQKFAKGYIDAIKDYE 1317
Cdd:pfam01576 619 ------RYAEERD---RAEAEAREKETRALS--------LARALEEALEAKEELERtNKQLRAEMEDLVSSKDDVGKNVH 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1318 lQLVTYKALVEPIASPLkKAKMESASDDI-IQEYVTLRTRYSeLMTLSSQYikfiietQRRLQDEEKAAEKLKEEERKKM 1396
Cdd:pfam01576 682 -ELERSKRALEQQVEEM-KTQLEELEDELqATEDAKLRLEVN-MQALKAQF-------ERDLQARDEQGEEKRRQLVKQV 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1397 AEMQAELE---KQKQLAETHAKaiaKAEQEANELKTKMkDEVSKRQDVAVDSEK----QKHNIQRELQELKtLSEQEIKA 1469
Cdd:pfam01576 752 RELEAELEderKQRAQAVAAKK---KLELDLKELEAQI-DAANKGREEAVKQLKklqaQMKDLQRELEEAR-ASRDEILA 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1470 KSQQVEEALLSrtrIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVA---EETQKKRK 1546
Cdd:pfam01576 827 QSKESEKKLKN---LEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAqleEELEEEQS 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1547 AEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK---KTAATQLESKQVALTARL 1623
Cdd:pfam01576 904 NTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKskfKSSIAALEAKIAQLEEQL 983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1624 EESLKNEQVMVIQLQEEAEHLKK-------QQAEADKAREQAEKELETWRQkaneaLRLRL-QAEEEANK 1685
Cdd:pfam01576 984 EQESRERQAANKLVRRTEKKLKEvllqvedERRHADQYKDQAEKGNSRMKQ-----LKRQLeEAEEEASR 1048
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4305-4335 |
3.55e-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: 3.55e-03
10 20 30
....*....|....*....|....*....|.
gi 1207141782 4305 AGILDTDTLEKVSVTEAMHRNLVDNITGQRL 4335
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1774-2311 |
3.57e-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: 43.41 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1774 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA---KKQRQI 1850
Cdd:COG5185 3 QRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQndvKKSESS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1851 AEEEAARQRA-EAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 1926
Cdd:COG5185 83 VKARKFLKEKkLDTKILQEYVNSLIKLPNYEWSADILislLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1927 GQLKKSSDTELDRQKK--IVEETLKQRKVVEEEihiLKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2004
Cdd:COG5185 163 DIFGKLTQELNQNLKKleIFGLTLGLLKGISEL---KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2005 KLALEEEKKRKEA---EAKVKQIQAAEEEAARQH----KAAQEEVGRLMKLAEEAKKQkeIAEKEAEKQVILVQEAAQKC 2077
Cdd:COG5185 240 DPESELEDLAQTSdklEKLVEQNTDLRLEKLGENaessKRLNENANNLIKQFENTKEK--IAEYTKSIDIKKATESLEEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2078 SAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedA 2157
Cdd:COG5185 318 LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEE------------------L 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2158 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEK-------TLKQKSSVEEELVKVKVQLDE--TDKQKSVLD 2228
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRqieelqrQIEQATSSNEEVSKLLNELISelNKVMREADE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2229 VELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIE 2308
Cdd:COG5185 460 ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
...
gi 1207141782 2309 AQE 2311
Cdd:COG5185 540 ALE 542
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2288-2434 |
3.84e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2288 LEEEAENMKKLAEEAARLNIEAQE--AARLRQIAESDLAKQ-RELAEKMLEEKKQAIQ----EAAKLKAEAEKLQKQKDQ 2360
Cdd:PRK07735 37 LEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAALAKQkREGTEEVTEEEKAKAKakaaAAAKAKAAALAKQKREGT 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2361 AQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2434
Cdd:PRK07735 117 EEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGE 190
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2285-2434 |
3.90e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2285 KKLLEEEAENMKKLAE---EAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2360
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLE-AKEEIHKLRNEFEKELRERRNELQKLeKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141782 2361 AQVEAQKLLEAKKEMQQRLDQ--ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2434
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQEleKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1825-1968 |
4.23e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1825 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEE 1904
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1905 GYQRKVLEDQAAQHKQAIEE------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKA 1968
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2099-2407 |
4.23e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2099 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAA 2178
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2179 LKLKQEADSEMAKYKKLAEKTLKQKSSVEEelvkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ 2258
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDE-------FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2259 MEDLLKLKLKIEKENQELMKKDKDN-----TKKLLEEEAENMKKLAEEAARLNIEAQEA---ARLRQIAESDLAKQRElA 2330
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAErdelrAKLYQEEQERKERQKEREEAEKKARQRQElqqAREEQIELKERRLAEE-A 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2331 EKMLEEKKQAIQEAAKL----KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET-EGFQKSLEAERKRQLEITAEAE 2405
Cdd:pfam13868 257 EREEEEFERMLRKQAEDeeieQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEElEEGERLREEEAERRERIEEERQ 336
|
..
gi 1207141782 2406 KL 2407
Cdd:pfam13868 337 KK 338
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
2286-2408 |
4.51e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.17 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2286 KLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdLAKQrelAEKMLEEKKQAIQEAAKLKAEA-----EKLQKQKDQ 2360
Cdd:PRK00290 499 GLSDEEIERMVKDAEANAEEDKKRKELVEARNQADS-LIYQ---TEKTLKELGDKVPADEKEKIEAaikelKEALKGEDK 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2361 AQVEA--QKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLK 2408
Cdd:PRK00290 575 EAIKAktEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDDVVDAEFEEVK 624
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2402-2611 |
4.59e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2402 AEAEKLKVKVtqlsdAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEK 2481
Cdd:PRK09510 75 KRAEEQRKKK-----EQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2482 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKEtllkkekaieeekkkLEKQFEDEVKKaealKAEQERQRK 2561
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAE---------------AAAKAAAEAKK----KAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2562 LMEEERKKlqSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE 2611
Cdd:PRK09510 211 AAAEAKKK--AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2288-2623 |
4.87e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2288 LEEEAENMKKLAEE----AARLNIeAQEAARLR-QI--AESDLAkqrELAEKmLEEKKQAIQEAAKLKAEAEKlqkQKDQ 2360
Cdd:PRK04863 316 LAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER-LEEQNEVVEEADEQQEENEA---RAEA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2361 AQveaQKLLEAKKEM---QQRLD-QETEG--FQKSLEA-ERKRQL----------------EITAEAEKLKVKV----TQ 2413
Cdd:PRK04863 388 AE---EEVDELKSQLadyQQALDvQQTRAiqYQQAVQAlERAKQLcglpdltadnaedwleEFQAKEQEATEELlsleQK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2414 LSDAQSKAEEEAKKFK---KQADEI-KIRLQETEKHTSEKHTVvEKLEVQRLQSKQEAdglHKAIADLEKEKEKLKKEAA 2489
Cdd:PRK04863 465 LSVAQAAHSQFEQAYQlvrKIAGEVsRSEAWDVARELLRRLRE-QRHLAEQLQQLRMR---LSELEQRLRQQQRAERLLA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2490 DLQKQSKEMANVQQ--EQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME--- 2564
Cdd:PRK04863 541 EFCKRLGKNLDDEDelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsg 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 2565 ---EERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLAEENKNLrEKLQQL 2623
Cdd:PRK04863 621 eefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI---ERLSQPGGSED-PRLNAL 678
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2194-2524 |
5.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2194 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkieken 2273
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2274 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEK 2353
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2354 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2433
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2434 EIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2513
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
330
....*....|.
gi 1207141782 2514 QQSFFAEKETL 2524
Cdd:COG4372 312 ALEDALLAALL 322
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1444-1655 |
5.06e-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: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1444 DSEKQKHNIQRElqelktlSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdADKlr 1523
Cdd:COG2268 200 DARIAEAEAERE-------TEIAIAQANREAEEA---ELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEA-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1524 nAAQEEAEKLRKQVAEETQKKRKAEE-ELKRKseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQRQIQVVE- 1601
Cdd:COG2268 267 -AYEIAEANAEREVQRQLEIAEREREiELQEK------------------EAEREEAELEADVRKPAEAEKQAAEAEAEa 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141782 1602 --EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-LQEEAEHLKKQQAEADKAR 1655
Cdd:COG2268 328 eaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEkLPEIAEAAAKPLEKIDKIT 384
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1777-1903 |
5.18e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.90 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1777 AVKQKKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1856
Cdd:pfam20492 4 AEREKQELEERLKQYEEETK-------KAQEELEESEETAEELEE----ERRQAEEEAERLEQKRQEAEEEKERLEESAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141782 1857 RQRAEAEKILKEKLTAINEATRLKTEAEialkEKEAENDRLKRKAEE 1903
Cdd:pfam20492 73 MEAEEKEQLEAELAEAQEEIARLEEEVE----RKEEEARRLQEELEE 115
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1054-1477 |
5.34e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1054 TQRATEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ 1133
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1134 GAE-DILNKYENQLREVNKVPVNEKEIEASQ----TQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVEL 1208
Cdd:pfam05483 436 GKEqELIFLLQAREKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1209 EHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESY----DWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQ 1284
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1285 EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMEsasddiIQEYVTLRTRYSELMTLS 1364
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK------FEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1365 SQYIKFIIETQRRLQDEE-KAAEKLKEEERKKMAEMQAELEKQKQlaeTHAKAIAKAEQEANELKTKMKDEVSKRqdvaV 1443
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAvKLQKEIDKRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAK----A 742
|
410 420 430
....*....|....*....|....*....|....
gi 1207141782 1444 DSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEA 1477
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1521-1686 |
5.34e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1521 KLRNAAQEEAEKLRKQVAEETQK-----KRKAEEELKrkseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQR 1595
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKeaeaiKKEALLEAK--------------------EEIHKLRNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1596 Q----IQVVEEVAKKTAAtqLESKQVALTARlEESLKNEQVMVIQLQEEAEHLKKQQAE---------ADKAR----EQA 1658
Cdd:PRK12704 87 LekrlLQKEENLDRKLEL--LEKREEELEKK-EKELEQKQQELEKKEEELEELIEEQLQelerisgltAEEAKeillEKV 163
|
170 180
....*....|....*....|....*...
gi 1207141782 1659 EKELETwrQKANEALRLRLQAEEEANKK 1686
Cdd:PRK12704 164 EEEARH--EAAVLIKEIEEEAKEEADKK 189
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1588-1905 |
5.51e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1588 QAELEKQRQiQVVEevAKKTAATQLESKQVALTARLEESLKNE---QVMVIQLQEEAEHLKKQQAEADKAREQAEKELET 1664
Cdd:PLN03229 435 EGEVEKLKE-QILK--AKESSSKPSELALNEMIEKLKKEIDLEyteAVIAMGLQERLENLREEFSKANSQDQLMHPVLME 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1665 WRQKANEALRLRL-QAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR-KMA---EETAKQK 1739
Cdd:PLN03229 512 KIEKLKDEFNKRLsRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKeKMEalkAEVASSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1740 LAAEQELirlradfehaeqqrtvlDDELqrlkndVNSAVKQKKELEEELIKVRKEME---ILLQQKSKAEKETMSNTEKS 1816
Cdd:PLN03229 592 ASSGDEL-----------------DDDL------KEKVEKMKKEIELELAGVLKSMGlevIGVTKKNKDTAEQTPPPNLQ 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1817 KQL--LESEAAKMRELAEEATKLRSVAEEAKKqrQIAEEEAARQRAEAEKI------LKEKLTAINEATRLKT-----EA 1883
Cdd:PLN03229 649 EKIesLNEEINKKIERVIRSSDLKSKIELLKL--EVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSELKEkfeelEA 726
|
330 340
....*....|....*....|....
gi 1207141782 1884 EIALKEK--EAENDRLKRKAEEEG 1905
Cdd:PLN03229 727 ELAAAREtaAESNGSLKNDDDKEE 750
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2033-2137 |
5.51e-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: 39.93 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2033 RQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLA 2112
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREA-------QQNYERELVLHAEDIKALQALREELNELKAEI 73
|
90 100
....*....|....*....|....*
gi 1207141782 2113 QEAEKAKDNAEKEAALLHKKAEEAE 2137
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQK 98
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1749-2136 |
5.60e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1749 LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMR 1828
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1829 ELAEEATKLrSVAEEAKKQRqIAEEEAARQRAEAEKILKEkltaiNEATRLKTEAEIA---LKEKEAENDRLKRKAEEEG 1905
Cdd:pfam07888 112 ELSEEKDAL-LAQRAAHEAR-IRELEEDIKTLTQRVLERE-----TELERMKERAKKAgaqRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1906 YQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIveeTLKQRKVVEEEIHILKLNF--EKASSGKQELELELKKLK 1983
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL---TTAHRKEAENEALLEELRSlqERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1984 GIAdeTQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE---------EVGRLMKLAEEAKK 2054
Cdd:pfam07888 262 SMA--AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrieklsaELQRLEERLQEERM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2055 QKEIAEKE--AEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKlKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK 2132
Cdd:pfam07888 340 EREKLEVElgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK-QELLEYIRQLEQRLETVADAKWSEAALTSTE 418
|
....
gi 1207141782 2133 AEEA 2136
Cdd:pfam07888 419 RPDS 422
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1512-1670 |
5.62e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1512 LRAKAVDADKLRNAAQEEAEK------LRKQVAEETQK---KRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA 1582
Cdd:pfam13904 61 LAAKQRQRQKELQAQKEEREKeeqeaeLRKRLAKEKYQewlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1583 ERHLKQAELEKQRQIQvveevAKKtaatqleskqvaltarleeslkneqvmviqlQEEAEHLKKQQAEADKAREQAEKEL 1662
Cdd:pfam13904 141 KEVLQEWERKKLEQQQ-----RKR-------------------------------EEEQREQLKKEEEEQERKQLAEKAW 184
|
....*...
gi 1207141782 1663 ETWRQKAN 1670
Cdd:pfam13904 185 QKWMKNVK 192
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2299-2443 |
6.02e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2299 AEEAARLNIEAQEAARLRQIAESDLAKQRELAEKML--EEKKQAIQEAAKLKAEAEKL-QKQKDQAQVEAQKLLEAKKEM 2375
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLEKEEEERLRkeELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEER 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141782 2376 QQRLDQETEGFQKSLEAERKRQLEitaEAEKLKVKVTQLsdaQSKAEEEAKKFKKQADEIKIRLQETE 2443
Cdd:pfam05672 89 EQREQEEQERLQKQKEEAEAKARE---EAERQRQEREKI---MQQEEQERLERKKRIEEIMKRTRKSD 150
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1400-1660 |
6.51e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1400 QAELEKQKQlaethAKAiAKAEQEANELKTKMKDEVSKrqdvAVDSEKQKHNIQRELQELKTLSEQEIKA-KSQQVEEAL 1478
Cdd:PRK05035 459 QARLEREKA-----ARE-ARHKKAAEARAAKDKDAVAA----ALARVKAKKAAATQPIVIKAGARPDNSAvIAAREARKA 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1479 LSRTRIEEEihiirlqlettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKlrKQVAEETQKKRKAEEEL---KRKS 1555
Cdd:PRK05035 529 QARARQAEK-------------QAAAAADPKKAAVAAAIARAKAKKAAQQAANA--EAEEEVDPKKAAVAAAIaraKAKK 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1556 EAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAtqleskqVALTARLEESLKNEQVMVI 1635
Cdd:PRK05035 594 AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-------VAAAIARAKARKAAQQQAN 666
|
250 260
....*....|....*....|....*
gi 1207141782 1636 QLQEEAEHLKKQQAEADKAREQAEK 1660
Cdd:PRK05035 667 AEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1820-2062 |
6.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1820 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTeAEIALKEKEAENDRLK 1898
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1899 RKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekassgkqelele 1978
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---------------- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1979 lkklkgiadetqkskakaeeeaEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEI 2058
Cdd:COG4913 366 ----------------------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
....
gi 1207141782 2059 AEKE 2062
Cdd:COG4913 424 LEAE 427
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1376-1686 |
6.64e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1376 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEAN---ELKTKMKDEVSKRQDVAVDSEKQKHNI 1452
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrqELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1453 QRELQELKTLSEQEIKAKSQQVEEALlsrtriEEEIHIIRLQLEttMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEK 1532
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLR------EEIDEFNEEQAE--WKELEKEEEREEDERILEYLKEKAEREEEREAER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1533 LRKQVAEETQKKRKAEEELKRKseaekdaakeKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQL 1612
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQ----------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 1613 ESKQVALTARLEESlKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKK 1686
Cdd:pfam13868 246 ELKERRLAEEAERE-EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGE 318
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1571-1787 |
6.65e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1571 DLEKFKLQAEEAERHLKQAE-----LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1645
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKkeekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1646 KQQAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAkaeEAALKQKEAAEMEL 1725
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAEL---EAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141782 1726 GNQRKmaeETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1787
Cdd:COG4942 184 EEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2278-2424 |
6.66e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2278 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQ---EAAKLKAEAEKL 2354
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141782 2355 QKQKDQA---QVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2424
Cdd:COG1579 102 KRRISDLedeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2543-2625 |
7.00e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.67 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2543 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEE----MNGKQKEM--QDLEK--KRIEQeklLAEEN- 2613
Cdd:pfam13779 495 QERLSEALERGASDEEIAKLMQELREALDDYMQALAEQAQQNPQDlqqpDDPNAQEMtqQDLQRmlDRIEE---LARSGr 571
|
90
....*....|...
gi 1207141782 2614 -KNLREKLQQLQS 2625
Cdd:pfam13779 572 rAEAQQMLSQLQQ 584
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3989-4023 |
7.14e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 7.14e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141782 3989 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEF 4023
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
654-734 |
7.37e-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: 39.22 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 654 WLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTAALQTQWSWILQL 733
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 1207141782 734 C 734
Cdd:pfam00435 96 A 96
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
2274-2381 |
7.39e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 40.06 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2274 QELMKKDKDNTKKLLEEEAEnmkkLAEEAARLNIEAQEAARlrQIAESDLAKQRELAEKMLEEKKQAIqeAAKLKAEAEK 2353
Cdd:PRK08476 40 NASIKNDLEKVKTNSSDVSE----IEHEIETILKNAREEAN--KIRQKAIAKAKEEAEKKIEAKKAEL--ESKYEAFAKQ 111
|
90 100
....*....|....*....|....*....
gi 1207141782 2354 LQKQKDQAQVEAQ-KLLEAKKEMQQRLDQ 2381
Cdd:PRK08476 112 LANQKQELKEQLLsQMPEFKEALNAKLSK 140
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1817-1931 |
7.45e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1817 KQLLESEAAKMRELA----EEATKlrsVAEEAKKQRQI-AEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 1891
Cdd:PRK12704 26 KKIAEAKIKEAEEEAkrilEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141782 1892 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKK 1931
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
842-876 |
7.61e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 37.63 E-value: 7.61e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141782 842 EITVHKGDECALVNNSQPYkWKVRDSSGNEAVVPS 876
Cdd:cd11764 15 ELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1769-1886 |
7.75e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1769 RLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 1848
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141782 1849 qiaeEEAARQRAEAEKILKEKLTAINEATRLK----TEAEIA 1886
Cdd:COG0542 481 ----EQRYGKIPELEKELAELEEELAELAPLLreevTEEDIA 518
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1587-1926 |
7.85e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1587 KQAELEKQRQIQVVEEVAKKTAATQLESKQV-ALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETW 1665
Cdd:COG5022 822 LQKTIKREKKLRETEEVEFSLKAEVLIQKFGrSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVN 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1666 RQKANEALRLRLQAEEEANKKTAaqeeaekqkeeakreakkrakaeeaaLKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1745
Cdd:COG5022 902 LELESEIIELKKSLSSDLIENLE--------------------------FKTELIARLKKLLNNIDLEEGPSIEYVKLPE 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1746 LIRLRadfehaeQQRTVLDDELQRLKNdvnsAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESE-- 1823
Cdd:COG5022 956 LNKLH-------EVESKLKETSEEYED----LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPve 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1824 ----AAKMRELAEEATKLRSVAEEaKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKR 1899
Cdd:COG5022 1025 vaelQSASKIISSESTELSILKPL-QKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340
....*....|....*....|....*..
gi 1207141782 1900 KAEEEGYQRKVLEDQAAQHKQAIEEKI 1926
Cdd:COG5022 1104 TNRNLVKPANVLQFIVAQMIKLNLLQE 1130
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
2326-2442 |
7.96e-03 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 40.33 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 2326 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKR-QLEITAEA 2404
Cdd:pfam16535 37 QQQKGLELSDEFQTALSEAEEATDAYEKAINKLKNAKSKAKAAEKKIDQAQTRLQSLAPDSPGKAKLEAAEqQAGIKKDA 116
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141782 2405 EKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQET 2442
Cdd:pfam16535 117 LQADRTLDKALDAASKLTTKAMAKEKEADDFSAKFQGT 154
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2541-2612 |
8.72e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 8.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2541 QFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMN--GKQKEMQDLEKKRIEQEKLLAEE 2612
Cdd:pfam20492 17 QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKErlEESAEMEAEEKEQLEAELAEAQE 90
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1645-1798 |
8.74e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1645 KKQQAEADK---AREQAEK-ELEtwRQK-----ANEALR---LRLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEE 1712
Cdd:PTZ00491 662 KSQEAAARHqaeLLEQEARgRLE--RQKmhdkaKAEEQRtklLELQAESAAVESSG--------------QSRAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1713 AALKQKEAAEMELGNQRkmaeeTAKQKLAAEQELIRLRadfehaeqQRTVLDDELQRLKNDVnsAVKQKKELEE-ELIKV 1791
Cdd:PTZ00491 726 EARLIEAEAEVEQAELR-----AKALRIEAEAELEKLR--------KRQELELEYEQAQNEL--EIAKAKELADiEATKF 790
|
....*..
gi 1207141782 1792 RKEMEIL 1798
Cdd:PTZ00491 791 ERIVEAL 797
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1525-1760 |
9.16e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1525 AAQEEAEKLRKQVaEETQKKRKAEEELKRKseaekdAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1604
Cdd:COG4942 17 AQADAAAEAEAEL-EQLQQEIAELEKELAA------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1605 KKTAA--TQLESKQVALTARLEESLKNEQ---VMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQA 1679
Cdd:COG4942 90 KEIAElrAELEAQKEELAELLRALYRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1680 EEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ 1759
Cdd:COG4942 170 EAERAEL-----------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 1207141782 1760 R 1760
Cdd:COG4942 239 A 239
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
49-160 |
9.28e-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: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 49 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 124
Cdd:cd21338 15 APDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQD 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 1207141782 125 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 160
Cdd:cd21338 95 GGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
2285-2356 |
9.51e-03 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 40.81 E-value: 9.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141782 2285 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESD--LAKQRELAEKMLEEKKQAiqeAAKLKAEAEKLQK 2356
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQdrRAEELEELKHLLEERKEA---LEKLRAEAREEAE 71
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3375-3413 |
9.51e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.51e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141782 3375 YLQGSDCIAGVFFQKTKEKLSIYQAMKQKLLTSDTGMSL 3413
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1645-1742 |
9.69e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 39.76 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141782 1645 KKQQAEADKAREQAEKELETWRQKANEalrLRLQAEEEANKKtaaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEME 1724
Cdd:PRK05759 48 ERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQI----------------IEEAKAEAEAEAARIKAQAQAE 108
|
90
....*....|....*...
gi 1207141782 1725 LGNQRKMAEETAKQKLAA 1742
Cdd:PRK05759 109 IEQERKRAREELRKQVAD 126
|
|
| |
