|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
187-292 |
2.77e-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: 234.53 E-value: 2.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 187 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1207141751 267 PEDVDVPHPDEKSIITYVSSMYDVMP 292
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
53-174 |
5.21e-70 |
|
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: 230.75 E-value: 5.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 53 DRVQKKTFTKWVNKHLVKHWkaeaqRHITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlprekGRMRFHKLQNV 132
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKAR-----RRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNV 63
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141751 133 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 174
Cdd:cd21188 64 QTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
50-185 |
1.21e-67 |
|
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: 224.52 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 50 DERDRVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlpreKGRMRFHKL 129
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 130 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 185
Cdd:cd21235 64 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
188-292 |
8.09e-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: 8.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 267
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1207141751 268 EDVDVPHPDEKSIITYVSSMYDVMP 292
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
49-183 |
4.81e-64 |
|
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: 214.85 E-value: 4.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 49 ADERDRVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlpreKGRMRFHK 128
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRFHR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 183
Cdd:cd21236 74 LQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
188-292 |
9.39e-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: 9.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 267
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1207141751 268 EDVDVPHPDEKSIITYVSSMYDVMP 292
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
50-184 |
8.62e-57 |
|
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: 193.71 E-value: 8.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 50 DERDRVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGetlprerdvvrnSRLPREKGRMRFHKL 129
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 130 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 184
Cdd:cd21237 64 QNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
186-292 |
6.40e-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: 6.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 186 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLL 265
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1207141751 266 DPEDVDVPHPDEKSIITYVSSMYDVMP 292
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
188-288 |
7.48e-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: 7.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 267
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1207141751 268 EDVDVPHPDEKSIITYVSSMY 288
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
49-171 |
5.67e-46 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 162.54 E-value: 5.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 49 ADERDRVQKKTFTKWVNKHLVKHwkaeaQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHK 128
Cdd:cd21246 10 ADEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKMRIHC 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 171
Cdd:cd21246 74 LENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
188-288 |
6.68e-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: 6.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 267
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141751 268 EDVDVPHPDEKSIITYVSSMY 288
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
55-175 |
1.14e-45 |
|
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: 161.40 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 55 VQKKTFTKWVNKHLVKHWKAeaqrHITDLYEDLRDGHNLISLLEVLSGEtlprerdvvrnsRLPREKGRMRFHKLQNVQI 134
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKP----PIKDLFEDLRDGTRLLALLEVLTGK------------KLKPEKGRMRVHHLNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141751 135 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21186 66 ALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
49-288 |
6.87e-42 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 165.88 E-value: 6.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 49 ADERDRVQKKTFTKWVNKHLVKhwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLprerdvVRNSRLPRekgrMRFHK 128
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GL 207
Cdd:COG5069 69 MENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 208 RCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLE--NLEQAFSIAERDLGVTRLLDPEDV-DVPHPDEKSIITYV 284
Cdd:COG5069 146 DTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
|
....
gi 1207141751 285 SSMY 288
Cdd:COG5069 226 SWYI 229
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
51-175 |
7.05e-42 |
|
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: 150.60 E-value: 7.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 51 ERDRVQKKTFTKWVNKHLVKHwkaEAQRHITDLYEDLRDGHNLISLLEVLSGEtlprerdvvrnsRLPREKGRM--RFHK 128
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHF 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21241 66 LSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
49-171 |
2.83e-40 |
|
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: 146.29 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 49 ADERDRVQKKTFTKWVNKHLVKHwkaeaQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHK 128
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRLRVQK 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 129 LQNVQIALDFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 171
Cdd:cd21193 74 IENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
175-288 |
7.03e-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: 7.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 175 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 254
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141751 255 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 288
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
187-292 |
8.01e-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: 8.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 187 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1207141751 267 PEDVDVPHPDEKSIITYVSSMYDVMP 292
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
49-171 |
2.14e-39 |
|
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: 144.78 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 49 ADERDRVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHK 128
Cdd:cd21318 32 ADEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGRMRIHS 95
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 171
Cdd:cd21318 96 LENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
188-288 |
2.17e-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: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 267
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1207141751 268 EDVDVPHPDEKSIITYVSSMY 288
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
51-175 |
8.07e-39 |
|
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: 141.94 E-value: 8.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 51 ERDRVQKKTFTKWVNKHLVKHWKAEAqrhITDLYEDLRDGHNLISLLEVLSGETLPRERDVVRNsrlprekgrmRFHKLQ 130
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQ----------RAHKLS 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207141751 131 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21190 68 NIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
49-171 |
1.91e-38 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 141.73 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 49 ADERDRVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHK 128
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMRIHC 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 171
Cdd:cd21317 89 LENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
934-1011 |
1.96e-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: 1.96e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 934 LSWQYLMRDITLINSWNFIMFKTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRS 1011
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
187-288 |
3.93e-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: 3.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 187 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1207141751 267 PEDVDVPHPDEKSIITYVSSMY 288
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
184-288 |
7.73e-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: 7.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 184 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 263
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1207141751 264 LLDPEDVDVPHPDEKSIITYVSSMY 288
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
191-292 |
8.01e-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: 8.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 191 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 269
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141751 270 VDVPHPDEKSIITYVSSMYDVMP 292
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
51-175 |
1.86e-36 |
|
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: 134.96 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 51 ERDRVQKKTFTKWVNKHLVKHWKAEAqrhITDLYEDLRDGHNLISLLEVLSGEtlprerdvvrnsRLPREKGRMRFHKLQ 130
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207141751 131 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21242 66 NIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
172-288 |
4.97e-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: 4.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 172 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQA 251
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141751 252 FSIAERDLGVTRLLDPEDVDVPHPDEKSIITYVSSMY 288
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1817-2662 |
3.54e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.52 E-value: 3.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1817 QQKSKAEKETmsnTEKSKQLLESEAAKMRELAEEATKLRSV---AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 1893
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1894 TRLKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--------KIGQLKKSSDTELDRQKKIVEETL 1965
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1966 KQ----RKVVEEEIHILKLNFEKASSGKQELELELKKlkgiADETQKSKAkaeeeaekFRKLALEEEKKRKEAEAKVKQI 2041
Cdd:PTZ00121 1237 KDaeeaKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKADE--------LKKAEEKKKADEAKKAEEKKKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2042 QAAEEEAARQHKAAQeevgrLMKLAEEAKKQKEIAEKEAEkqvilvqEAAQKCSAAEQKAQnvlvqqnkdsmaqdKLKEE 2121
Cdd:PTZ00121 1305 DEAKKKAEEAKKADE-----AKKKAEEAKKKADAAKKKAE-------EAKKAAEAAKAEAE--------------AAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2122 FEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEasrraeaeaaalKLKQE 2201
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK------------------ADEAKKKAEED------------KKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2202 ADSEMAKYKKLAEKtLKQKSSVEEELVKVKVQLDETDKQKsvldvELKRLKQEVSDA--IKQKAQVEDELSKVKIQMEDL 2279
Cdd:PTZ00121 1409 ELKKAAAAKKKADE-AKKKAEEKKKADEAKKKAEEAKKAD-----EAKKKAEEAKKAeeAKKKAEEAKKADEAKKKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2280 LKLklkiekenQELMKKDKDNTKKlleeeAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2359
Cdd:PTZ00121 1483 KKA--------DEAKKKAEEAKKK-----ADEAKKAAEAKKK----ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2360 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQE--------TEGFQKSLEAERKRQLEITAEAEKLKVKVTQL 2431
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2432 SdaqsKAEEEAKK---FKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEkeklkkeAADL 2508
Cdd:PTZ00121 1626 K----KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-------AEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2509 QKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2588
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEK------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 2589 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEE 2662
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAniiEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
188-288 |
3.96e-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: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 267
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141751 268 EDVDVPHPDEKSIITYVSSMY 288
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
53-171 |
6.63e-35 |
|
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: 130.59 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 53 DRVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdvvrnsrlPREKGRMRFHKLQNV 132
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANV 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141751 133 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 171
Cdd:cd21214 67 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1656-2448 |
1.37e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 147.59 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1656 EEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQ- 1734
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEi 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1735 -KEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEEELIKVRKEME 1813
Cdd:PTZ00121 1157 aRKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA--EAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1814 ILLQQKSKAEKETMSNTEKSKQLLESEAAKM--RELAEEATKLRSvAEEAKKQRQIAEEEAARQRAEAEKI--LKEKLTA 1889
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFarRQAAIKAEEARK-ADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1890 INEATRLKTEAEIALKEKEAendrLKRKAEEEGYQ---RKVLEDQAAQHKQAIEEKigqlKKSSDTELDRQKKIVEETLK 1966
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADA----AKKKAEEAKKAaeaAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1967 QRKVVEEEIHILKlnfeKASSGKQElelelkklkgiADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEE 2046
Cdd:PTZ00121 1386 KAEEKKKADEAKK----KAEEDKKK-----------ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2047 EAARQHKAAQEevgrLMKLAEEAKKQKEIAEKEAEKQVilVQEAAQKCSAAEQKAQNVlvqqnKDSMAQDKLKEEFEKAK 2126
Cdd:PTZ00121 1451 KKAEEAKKAEE----AKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEA-----KKAAEAKKKADEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2127 KlAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEM 2206
Cdd:PTZ00121 1520 E-AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2207 AKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVldvelKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKI 2286
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2287 EKENQELMKKDKDNTKK--LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKL 2364
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2365 KAEAEKLQKQKDQAQVEAQKLLEAKKE-MQQRLDQETE---------------GFQKSLEAERKRQLEITAEAEKLKVKV 2428
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEEDEkrrmevdkkikdifdNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
810 820
....*....|....*....|
gi 1207141751 2429 TQLSDAQSKAEEEAKKFKKQ 2448
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKH 1852
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
55-173 |
2.12e-34 |
|
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: 129.06 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 55 VQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlprEKGRMRFHKLQNVQI 134
Cdd:cd21215 4 VQKKTFTKWLNTKLSS-----RGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNK 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141751 135 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 173
Cdd:cd21215 69 ALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
175-288 |
1.97e-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: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 175 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 254
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141751 255 AERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 288
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
187-285 |
2.08e-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: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 187 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1207141751 267 PEDVDVPHPDEKSIITYVS 285
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
50-175 |
2.76e-32 |
|
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: 123.11 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 50 DERDRVQKKTFTKWVNKHLVKHWKaeaqRHITDLYEDLRDGHNLISLLEVLSGEtlprerdvvrnsRLPREKGRMRFHKL 129
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHAL 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207141751 130 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21231 65 NNVNKALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
191-293 |
4.38e-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: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 191 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLDPE 268
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1207141751 269 DVDVPHPDEKSIITYVSSMYDVMPR 293
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
187-285 |
1.68e-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: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 187 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1207141751 267 PEDVDVPHPDEKSIITYVS 285
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1396-2272 |
2.22e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 137.19 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1396 QDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQE 1475
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1476 LKTLSEQEIKAKSQQVEEAllsrtRIEEEIHiirlqlettmkqkntaetELLQLRaKAVDADKLRNAaqEEAEKLRKqvA 1555
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAA-----RKAEEVR------------------KAEELR-KAEDARKAEAA--RKAEEERK--A 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1556 EETqkkRKAEEELKRKSEAEkdaakekkkaledLEKFKLQAEEAERHLKQAELEKQRQIQ--VVEEVAKKTAATQLESKQ 1633
Cdd:PTZ00121 1215 EEA---RKAEDAKKAEAVKK-------------AEEAKKDAEEAKKAEEERNNEEIRKFEeaRMAHFARRQAAIKAEEAR 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1634 VALTAR-LEESLKNEQVMVIQLQEEAEHLKKQQAEADKArEQAEKELETWRQKANEALRlrlqAEEEANKKtaaqeeaek 1712
Cdd:PTZ00121 1279 KADELKkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKK----KAEEAKKA--------- 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1713 qKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEEtAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVN 1792
Cdd:PTZ00121 1345 -AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEEDKKKA----DELKKAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1793 SAVKQKKELEEelikVRKEMEIllqqKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlrsvAEEAKKQRQIAEE-E 1871
Cdd:PTZ00121 1419 KADEAKKKAEE----KKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAKKKAEEAKKaD 1486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1872 AARQRAEAEKILKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--KIGQLKKS 1949
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADElkKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1950 SDTELDRQKKIVEETLKQ--------RKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKaeeeaekfR 2021
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--------K 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2022 KLALEEEKKRKEAEAKVKQIQAAEEE----AARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCS 2095
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2096 AAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEkaKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAE 2175
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2176 KLRKEAEKEASRRAEAEAAAlklkQEADSEMAKYKKLAEKTlkQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLK 2252
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDNFANI----IEGGKEGNLVINDSKEM--EDSAIKEVADSKNMQLEEADafeKHKFNKNNENGEDG 1864
|
890 900
....*....|....*....|
gi 1207141751 2253 QEVSDAIKQKAQVEDELSKV 2272
Cdd:PTZ00121 1865 NKEADFNKEKDLKEDDEEEI 1884
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1365-1941 |
3.50e-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: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1365 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANE 1443
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1444 LKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKsQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1523
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1524 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledLEKFKLQAEEAERHL 1603
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER------------------LEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1604 KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1683
Cdd:COG1196 434 EEEEEEEEEALE--EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1684 QKANEALR------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM----AEETA 1753
Cdd:COG1196 512 AALLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIraraALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1754 KQKLAAEQELIRLRADFEHAEQQRTVLDDEL---QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnT 1830
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----R 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1831 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1910
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
570 580 590
....*....|....*....|....*....|.
gi 1207141751 1911 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1941
Cdd:COG1196 748 LEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
49-171 |
6.57e-31 |
|
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: 120.92 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 49 ADERDRVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHK 128
Cdd:cd21316 47 ADEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMRIHC 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 171
Cdd:cd21316 111 LENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
191-292 |
7.41e-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: 7.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 191 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 269
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141751 270 VDVPHPDEKSIITYVSSMYDVMP 292
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
193-288 |
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 1207141751 193 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 271
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1207141751 272 VPHPDEKSIITYVSSMY 288
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1414-2616 |
2.60e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 129.95 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1414 AEMQAELEkqkqlAETHAKAIAKAEQEANEL-------KTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKA 1486
Cdd:NF041483 111 AEHQARLQ-----AELHTEAVQRRQQLDQELaerrqtvESHVNENVAWAEQLRARTESQA---RRLLDESRAEAEQALAA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1487 KSQQVEeallsrtRIEEEIHIiRLQLETtmkQKNTAETELLQLRAKAvDADKLRNAAQEEA-------EKLRKQVAEETQ 1559
Cdd:NF041483 183 ARAEAE-------RLAEEARQ-RLGSEA---ESARAEAEAILRRARK-DAERLLNAASTQAqeatdhaEQLRSSTAAESD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1560 KKRKAEEELKRKSEAekdaakekkkaledlekfklQAEEAERHLKQAELEKQRqiqVVEEvAKKTAATQLESKQVALTAR 1639
Cdd:NF041483 251 QARRQAAELSRAAEQ--------------------RMQEAEEALREARAEAEK---VVAE-AKEAAAKQLASAESANEQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1640 LEESLKNEQVMVIQLQEEAEHLKkqqAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKR 1719
Cdd:NF041483 307 TRTAKEEIARLVGEATKEAEALK---AEAEQALADARAEAEKLVAEAAEKAR-TVAAEDTAAQLAKAARTAEEVLTKASE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1720 EAKK--RAKAEEAALKQKEAaEMELGNQRKMAEETAKQ-KLAA--------------EQELIRLRADfehAEQQRTVLDD 1782
Cdd:NF041483 383 DAKAttRAAAEEAERIRREA-EAEADRLRGEAADQAEQlKGAAkddtkeyraktvelQEEARRLRGE---AEQLRAEAVA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1783 ELQRLKNDV-NSAVKQKKE----LEEELIKVRKEMEILLQQ-KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRS 1856
Cdd:NF041483 459 EGERIRGEArREAVQQIEEaartAEELLTKAKADADELRSTaTAESERVRTEAIERATTLRRQAEETLERTRAEAERLRA 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1857 VAEE-AKKQRQIAEEEAARQRAEAEK-ILKEKLTAINEATRLKTEAE-------IALKEKEAENDRLKRKAEEEGYQrkv 1927
Cdd:NF041483 539 EAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEerltaaeEALADARAEAERIRREAAEETER--- 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1928 LEDQAAqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHIlKLNFEKASSGKQelelelkklkgIADETQ 2007
Cdd:NF041483 616 LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAV-RLRSEAAAEAER-----------LKSEAQ 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2008 KSKAkaeeeaekfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE-----------EVGRLMKLAEE--AKKQKE 2074
Cdd:NF041483 677 ESAD---------RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraeadqERERAREQSEEllASARKR 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2075 IAEKEAEKQViLVQEAAQKC----SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAAllhk 2148
Cdd:NF041483 748 VEEAQAEAQR-LVEEADRRAtelvSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEAQ---- 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2149 kaEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELv 2228
Cdd:NF041483 815 --EEADRVRS--------------DAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL- 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2229 kvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKL 2304
Cdd:NF041483 868 ----RSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDE 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2305 LEEEAENMK-KLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEA 2382
Cdd:NF041483 944 ARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEA 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2383 QKLL-EAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEK 2461
Cdd:NF041483 1018 DRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAE 1089
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2462 HTSEKHTVVEK----------------------LEVQRLQSKQEADGLH-KAIADLEKEKEKLKKEAADLQKQSKEManv 2518
Cdd:NF041483 1090 ATVEGNSLVEKartdadellvgarrdatairerAEELRDRITGEIEELHeRARRESAEQMKSAGERCDALVKAAEEQ--- 1166
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2519 QQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKlqsAMDAAIKKQ 2598
Cdd:NF041483 1167 LAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTVEEGKR---ELDVLVRRR 1243
|
1290
....*....|....*...
gi 1207141751 2599 KEAEEEMNGKQKEMQDLE 2616
Cdd:NF041483 1244 EDINAEISRVQDVLEALE 1261
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
51-177 |
4.50e-29 |
|
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: 114.21 E-value: 4.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 51 ERDRVQKKTFTKWVNKHLVKhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDVVRNsrlprekgrmRFHKLQ 130
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSH----------RIFRLN 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141751 131 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 177
Cdd:cd21191 68 NIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
54-176 |
9.23e-29 |
|
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: 113.70 E-value: 9.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 54 RVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlprEKGRMRFHKLQNVQ 133
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFN----------KRPTFRSQKLENVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207141751 134 IALDFLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 176
Cdd:cd21311 79 VALKFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
55-175 |
1.22e-28 |
|
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: 112.80 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 55 VQKKTFTKWVNKHLVKHWKAEaqrhITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlprekGRMRFHKLQNVQI 134
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKPP----IKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141751 135 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21232 66 VLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
55-175 |
1.77e-28 |
|
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: 112.38 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 55 VQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRerdVVRNSRlprekgrMRFHKLQNVQI 134
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIKKPL-------NQHQKLENVTL 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141751 135 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21227 69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1591-2183 |
8.94e-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: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1591 KFKLQAEEAERHLKQA------------ELEKQR---QIQVveEVAKK--TAATQLESKQVALTA----RLEESLKNEQV 1649
Cdd:COG1196 169 KYKERKEEAERKLEATeenlerledilgELERQLeplERQA--EKAERyrELKEELKELEAELLLlklrELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1650 MVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE 1729
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1730 AALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR 1809
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1810 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 1889
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1890 INEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRK-----VLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEET 1964
Cdd:COG1196 487 AEAAARLLLLLE-AEADYEGFLEGVKAALLLAGLRGLagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1965 LKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIADEtqkskakaeEEAEKFRKLALEEEKKRKEAEAKVKQIQAA 2044
Cdd:COG1196 566 LKAAK--AGRATFLPLDKIRARAALAAALARGAIGAAVDLV---------ASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2045 EEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKLKEEFEK 2124
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 2125 AKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2183
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 ... |
191-290 |
1.03e-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: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 191 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED- 269
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1207141751 270 VDVPHPDEKSIITYVSSMYDV 290
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
54-173 |
3.32e-27 |
|
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: 108.72 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 54 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDvvrnsrlprEKGRMRFHKLQNVQ 133
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141751 134 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 173
Cdd:cd21183 69 TALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
173-288 |
3.34e-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: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 173 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAF 252
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141751 253 SIAERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 288
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1389-2008 |
5.94e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 122.56 E-value: 5.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1389 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1468
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1469 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEeihiirlqlettmkQKNTAEtellQLRAKAVDADKLRNAAQEEAE 1548
Cdd:PTZ00121 1294 EAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEE--------------AKKKAD----AAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1549 KLRKQvAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER---HLKQAELEKQRQIQVVEEVAKKTA 1625
Cdd:PTZ00121 1354 AAADE-AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkadELKKAAAAKKKADEAKKKAEEKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1626 ATQLESKqvALTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRlrlqAEEEANKKTA 1705
Cdd:PTZ00121 1433 ADEAKKK--AEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKK----KAEEAKKKAD 1500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1706 aqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlddelq 1785
Cdd:PTZ00121 1501 --------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-------- 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1786 rlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 1865
Cdd:PTZ00121 1559 --KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1866 QIAEEEA--------ARQRAEAEKILKEKLTAINEATRLKTE-----------AEIALKEKEAEN---DRLKRKAEEEgy 1923
Cdd:PTZ00121 1637 QLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEeakkaeedekkAAEALKKEAEEAkkaEELKKKEAEE-- 1714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1924 QRKVLEDQAAQHKQAIeeKIGQLKKSSDTELDRQKKIVEETLKQRKV----VEEEIHILKLNFEKASSGKQELELELKKL 1999
Cdd:PTZ00121 1715 KKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlkKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
....*....
gi 1207141751 2000 KGIADETQK 2008
Cdd:PTZ00121 1793 RMEVDKKIK 1801
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1418-1983 |
2.48e-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: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1418 AELEKQ-KQLAEthaKAiAKAEQeANELKTKMKDevsKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALL 1496
Cdd:COG1196 196 GELERQlEPLER---QA-EKAER-YRELKEELKE---LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1497 SRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEK 1576
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1577 DAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQE 1656
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLE----RLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1657 EAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1736
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1737 AAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1816
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1817 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEakkqRQIAEEEAARQRAEAEKILKEKLTAINEATRL 1896
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1897 KTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIH 1976
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
....*..
gi 1207141751 1977 ILKLNFE 1983
Cdd:COG1196 737 LLEELLE 743
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1389-1973 |
2.67e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 120.25 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1389 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1468
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1469 IQRELQELKTLSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQ---- 1544
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEA---KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkka 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1545 ---EEAEKLRK----QVAEETQKK----RKAEE------ELKRKSEAEKD----AAKEKKKALEDLEKFKLQAEEAERHL 1603
Cdd:PTZ00121 1287 eekKKADEAKKaeekKKADEAKKKaeeaKKADEakkkaeEAKKKADAAKKkaeeAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1604 KQAELEKQRQIQVVEEVAKKT----AATQLESKQVALTARLEESLKNEQVmviqlQEEAEHLKKQQAE---ADKAREQAE 1676
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAeekkKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEkkkADEAKKKAE 1441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1677 --KELETWRQKANEALR---LRLQAEE-----EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR 1746
Cdd:PTZ00121 1442 eaKKADEAKKKAEEAKKaeeAKKKAEEakkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1747 KMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQrlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET 1826
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKA--EELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1827 MSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKE 1906
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 1907 KEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE----KIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 1973
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
175-288 |
8.11e-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: 8.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 175 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 254
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141751 255 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 288
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
193-288 |
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 1207141751 193 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 271
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1207141751 272 VPHPDEKSIITYVSSMY 288
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
175-288 |
2.61e-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: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 175 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 254
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141751 255 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 288
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
50-175 |
1.41e-24 |
|
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: 101.76 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 50 DERDRVQKKTFTKWVNKHLVKHwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHKL 129
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRVHFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141751 130 QNVQIALDFLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21247 81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1719-2405 |
1.59e-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: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1719 REAKK----RAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1794
Cdd:COG1196 207 RQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1795 VKQKKELEEELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 1874
Cdd:COG1196 287 QAEEYELLAELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1875 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLKKSSDTEL 1954
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA-------LLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1955 DRQKKIVEETLKQRKVVEEEIHILKLnfekassgkqelelelkklkgIADETQKskakaeeeaekfRKLALEEEKKRKEA 2034
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLEL---------------------LAELLEE------------AALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2035 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEkeaEKQVILVQEAAQKCSAAEQKAQNVLvqqnkdsma 2114
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---LIGVEAAYEAALEAALAAALQNIVV--------- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2115 qdklkeefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAA 2194
Cdd:COG1196 554 --------EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2195 ALklkQEADSEMAKYkkLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2274
Cdd:COG1196 626 TL---VAARLEAALR--RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2275 QMEDLLKLKLKIEKENQELmKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEK 2354
Cdd:COG1196 701 AEEEEERELAEAEEERLEE-ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2355 K----QAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA----KKEMQQRLdQET-----EGFQK 2405
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), ... |
189-288 |
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 1207141751 189 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 268
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1207141751 269 D-VDVPHPDEKSIITYVSSMY 288
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1549-2453 |
1.86e-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: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1549 KLRKqvaEETQKK-RKAEEELKRkseaekdAAKEKKKALEDLEKFKLQAEEAERH--LKQAELEKQRQIQVVEEVAKKTA 1625
Cdd:TIGR02168 171 KERR---KETERKlERTRENLDR-------LEDILNELERQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1626 ATQLESKQvaltARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEA-LRLRLQAEEEANkkt 1704
Cdd:TIGR02168 241 LEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLAN--- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1705 aaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDEL 1784
Cdd:TIGR02168 314 ------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1785 QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEketmsnTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQ 1864
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ------QEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1865 RQIAEEEAARQRAEaekilkekltaINEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKVLedQAAQHKQAIEEKI 1943
Cdd:TIGR02168 456 LERLEEALEELREE-----------LEEAEQALDAAERELAQLQARLDSLERLQENlEGFSEGVK--ALLKNQSGLSGIL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1944 GQLKKSSDTELDRQKKIV---EETLKQRKVVEEEIHILKLNF-EKASSGKQELELELKKLkgiADETQKSKAKAEEEAEK 2019
Cdd:TIGR02168 523 GVLSELISVDEGYEAAIEaalGGRLQAVVVENLNAAKKAIAFlKQNELGRVTFLPLDSIK---GTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2020 FRKLALEEEKKRKEAEAK----------VKQIQAAEEEAARQH---------------------KAAQEEVGRLMKLAEE 2068
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2069 AKKQKEIAekeaekqvilvqEAAQKCSAAEQKAQNVLVQqnkdsmaQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHK 2148
Cdd:TIGR02168 680 EELEEKIE------------ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2149 KAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2228
Cdd:TIGR02168 741 EVEQLEE--------------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2229 KVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkdkdntKKLLEEE 2308
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------------------AAEIEEL 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2309 AENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA 2388
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2389 KKEMQQRLDQETEGFQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2453
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
188-288 |
3.00e-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: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 267
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1207141751 268 EDV---DVphPDEKSIITYVSSMY 288
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 ... |
175-288 |
4.37e-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: 100.53 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 175 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 254
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141751 255 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 288
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
54-173 |
4.37e-24 |
|
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: 99.87 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 54 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDvvrnsrlprEKGRMRFHKLQNVQ 133
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141751 134 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 173
Cdd:cd21228 69 VALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1177-1902 |
5.57e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 112.54 E-value: 5.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1177 EASQTQLQKLRSEAEGKQATFD----RLEEELQRATEVNKRMSQLHSERDVELEHYRQlVGNLRERWQAVFAQ----IEL 1248
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKaedaRKAEEARKAEDARKAEEARKAEDAKRVEIARK-AEDARKAEEARKAEdakkAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1249 RQRELDLlnRQMQAYRESYDwlIRWIADAKQRQDKLHAVPIggSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKfakgyid 1328
Cdd:PTZ00121 1181 ARKAEEV--RKAEELRKAED--ARKAEAARKAEEERKAEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEE------- 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1329 aIKDYELQLVTYKALVEPIASPLKKAKMESAsddiiqeyvtlrtRYSELMTLSsqyikfiiETQRRLQDEEKAAEKLKEE 1408
Cdd:PTZ00121 1248 -ERNNEEIRKFEEARMAHFARRQAAIKAEEA-------------RKADELKKA--------EEKKKADEAKKAEEKKKAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1409 ERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANElkTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQ----EI 1484
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE--AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkadAA 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1485 KAKSQQVEEALLSRTRIEEEihiirLQLETTMKQKNTAETELLQLRAKAVD---ADKLRNAAQE--EAEKLRKQvAEETQ 1559
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEED-----KKKADELKKAAAAKKKADEAKKKAEEkkkADEAKKKAEEakKADEAKKK-AEEAK 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1560 K----KRKAEE-----ELKRKSEAEKDAAKEKKKAledlEKFKLQAEEAERhlKQAELEKQRQIQVVEEVAKKTAATQLE 1630
Cdd:PTZ00121 1458 KaeeaKKKAEEakkadEAKKKAEEAKKADEAKKKA----EEAKKKADEAKK--AAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1631 SKQVAltarlEESLKNEQVMVIQLQEEAEHLKKqqAEADKAREQAEKELE---TWRQKANEALRLRLQAEEEANKKTAAQ 1707
Cdd:PTZ00121 1532 EAKKA-----DEAKKAEEKKKADELKKAEELKK--AEEKKKAEEAKKAEEdknMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1708 EEAEKQKEEAKREAKKRA----KAEE-----AALKQKEAAEMELGNQRKMAEETAKQKlaAEQELIRLRADFEHAEQQRT 1778
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAeelkKAEEekkkvEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKK 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1779 VLDDELQRLKNDVNSAVKQKKelEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVA 1858
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKK--AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141751 1859 EEAKKQRQIAEEeaarQRAEAEKILKEKLTAINEATRLKTEAEI 1902
Cdd:PTZ00121 1761 HLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
833-899 |
6.23e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 97.72 E-value: 6.23e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 833 QLKPRNpaQPIKGKLPVQAVCDFKQMEITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSICFIVP 899
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
187-293 |
6.48e-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: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 187 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY--RQTNLENLEQAFSIAERDLGVTR 263
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1207141751 264 -LLDPEDVDvpHPDEKSIITYVSSMYDVMPR 293
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
188-292 |
1.52e-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: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 267
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1207141751 268 EDVDVPHPDEKSIITYVSSMYDVMP 292
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
54-176 |
2.15e-23 |
|
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: 98.56 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 54 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDvvrnsrlPREKgrMRFHKLQNVQ 133
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 134 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 176
Cdd:cd21310 81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1838-2722 |
5.46e-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: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1838 ESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRK 1917
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1918 AEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 1997
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1998 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2077
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2078 KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQE-AEKAKDNAEKEAALLHKKAEEAERQ 2156
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2157 kkaaeaeaakqakaqedaEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDE 2236
Cdd:pfam02463 471 ------------------EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2237 tDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLA 2316
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2317 E-EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQR 2395
Cdd:pfam02463 612 TlEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2396 LDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEV 2475
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE---EEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2476 QRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQE--KTILQQSFFAEKETLLKKEKAIEEEKK 2553
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEeqLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2554 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQsamdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNL 2633
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQK-------LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2634 REKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGvKKDVPLAFDGIREKVPASRLHEIGVLS 2713
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERL 1000
|
....*....
gi 1207141751 2714 KKEYDKLKK 2722
Cdd:pfam02463 1001 EEEKKKLIR 1009
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
191-291 |
6.71e-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: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 191 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPEDV 270
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1207141751 271 DVPHPDEKSIITYVSSMYDVM 291
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 ... |
1669-2528 |
1.10e-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: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1669 DKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1748
Cdd:pfam02463 168 KRKKKEALKKL---IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1749 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNdvnsavKQKKELEEELIKVRKEMEILLQQKSKAEKETmS 1828
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE------EELKLLAKEEEELKSELLKLERRKVDDEEKL-K 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1829 NTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 1908
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1909 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSG 1988
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1989 KQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGrlmKLAEE 2068
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV---IVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2069 AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAlLHK 2148
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK-DTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2149 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2228
Cdd:pfam02463 634 LTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2229 KVKVQLDETDKQKsvLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE 2308
Cdd:pfam02463 714 KLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2309 A-ENMKKLAEEAARLNIEAQEAA---RLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQK 2384
Cdd:pfam02463 792 KeEKLKAQEEELRALEEELKEEAellEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2385 LLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE-TEKHT 2463
Cdd:pfam02463 872 LLLKEEELEE-QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEaDEKEK 950
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2464 SEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2528
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 ... |
1773-2636 |
1.32e-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: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1773 AEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS-----KAEKETMSNTEKSKQL--LESEAAKMR 1845
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkEQAKKALEYYQLKEKLelEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1846 ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI-LKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 1924
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1925 RKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIAD 2004
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2005 ETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQV 2084
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2085 ILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEfEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEA 2164
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS-GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2165 AKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKL-------AEKTLKQKSSVEEELVKVKVQLDET 2237
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpilnLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2238 DKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEkenQELMKKDKDNTKKLLEEEAENMKKLAE 2317
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ---ELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2318 EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ-KLLEAKKEMQQRL 2396
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKeKELAEEREKTEKL 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2397 DQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2476
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2477 RLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLE 2556
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI------EERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2557 KQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDA-AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2635
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLmAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
.
gi 1207141751 2636 K 2636
Cdd:pfam02463 1021 E 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1365-2155 |
2.81e-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: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1365 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEkqkqlaeTHAKAIAKAEQEANE 1443
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1444 LKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1523
Cdd:TIGR02168 286 LQKELYALANEISRL----EQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1524 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledlekfklqaeeAERHL 1603
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------------------------LEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1604 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1683
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1684 QKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKAEEAALKQK 1735
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKKAIAFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1736 EA-----AEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLK--NDVNSAVKQKKELEEELIKV 1808
Cdd:TIGR02168 569 ELgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1809 RKEMEILLQQKS---KAEKETMSNTEKSKQLLESEaAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 1885
Cdd:TIGR02168 649 TLDGDLVRPGGVitgGSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1886 KLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEdQAAQHKQAIEEKIGQLKKssdtELDRQKKIVEETL 1965
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEA----QIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1966 KQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAAE 2045
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA--------------EIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2046 EEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEF-EK 2124
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEE 948
|
810 820 830
....*....|....*....|....*....|.
gi 1207141751 2125 AKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2155
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2111-2689 |
2.98e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.76 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2111 DSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAallhKKAEEAERQKKAAEAEAAKQAkaqedAEKLRK-E----AEKEA 2185
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEA----RKAEEAKKKAEDARKAEEARK-----AEDARKaEearkAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2186 SRRAEAEAAALKLKQEA-DSEMAKYKKLAEKTLKQKSSVE----EELVKVKV--------QLDETDKQKSVLDVELKRLK 2252
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEArKAEDAKKAEAARKAEEVRKAEElrkaEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2253 QEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKEN----QELMKKDK----DNTKKLLEEEAENMKKLAEEAARLNI 2324
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADElkkaEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2325 EAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQrLDQETEGFQ 2404
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2405 KSLEAERKRQlEITAEAEKLKVKvtqlSDAQSKAEEEAKKF--KKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2482
Cdd:PTZ00121 1392 KADEAKKKAE-EDKKKADELKKA----AAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2483 EadglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE--QLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFE 2560
Cdd:PTZ00121 1467 E----EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2561 DEVKKAEALKAEQERQRKlmeEERKKLQSAmdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLReklqql 2640
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKA---EEKKKAEEA-----KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK------ 1608
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1207141751 2641 qsSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGVKKD 2689
Cdd:PTZ00121 1609 --AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
58-172 |
5.45e-22 |
|
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: 93.53 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 58 KTFTKWVNKHLVKhwkaEAQRHITDLYEDLRDGHNLISLLEVLSgetlPRERDVVRNSRlprekGRMRFHKLQNVQIALD 137
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLS----PGLVDKKKVAA-----SLSRFKKIENINLALS 67
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141751 138 FLKHRQVKLVNIRNDDIADGnPKLTLGLIWTIILH 172
Cdd:smart00033 68 FAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
55-175 |
5.60e-22 |
|
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: 93.89 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 55 VQKKTFTKWVNKHLVKhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdvvrnsrlPREKGRMRFHKLQNVQI 134
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141751 135 ALDFLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:pfam00307 68 ALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
188-286 |
7.49e-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: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY-RQTNLENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1207141751 267 PEDVDVPHPDEKSIITYVSS 286
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1591-2481 |
8.92e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.14 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1591 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKktaatQLES--KQVALTARLEEslkneqvmviqLQEEAEHLKKQQAEA 1668
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELER-----QLKSleRQAEKAERYKE-----------LKAELRELELALLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1669 DKarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELgnqrkm 1748
Cdd:TIGR02168 233 RL--EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1749 aEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtms 1828
Cdd:TIGR02168 305 -QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ--- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1829 ntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIALKEK 1907
Cdd:TIGR02168 381 --------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1908 EAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLkkssdteldrqkkiveETLKQRKVVEEEihiLKLNFEKASS 1987
Cdd:TIGR02168 453 QEELERLEEALEE-------LREELEEAEQALDAAEREL----------------AQLQARLDSLER---LQENLEGFSE 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1988 GKQELELELKKLKGIADETQKSKAKAEEEaekfrKLALEEEKKRKEAEAKVKQIQAAEEEAARQhkaAQEEVGRLMKLAE 2067
Cdd:TIGR02168 507 GVKALLKNQSGLSGILGVLSELISVDEGY-----EAAIEAALGGRLQAVVVENLNAAKKAIAFL---KQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2068 EAKKQKEIAEKEAE--KQVILVQEAAQKCSAAEQKAQ--------NVLVQQNKDSmAQDKLKEEFEKAKKLAQEAEK--- 2134
Cdd:TIGR02168 579 DSIKGTEIQGNDREilKNIEGFLGVAKDLVKFDPKLRkalsyllgGVLVVDDLDN-ALELAKKLRPGYRIVTLDGDLvrp 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2135 ----AKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedaeklRKEAEKeasrraeaeaaalKLKQEADSEMAKYK 2210
Cdd:TIGR02168 658 ggviTGGSAKTNSSILERRRE--------------------------IEELEE-------------KIEELEEKIAELEK 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2211 KLAEkTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQME------DLLKLKL 2284
Cdd:TIGR02168 699 ALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEeleerlEEAEEEL 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2285 KIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKL 2364
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2365 KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ---ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2441
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1207141751 2442 AKKFKKQ-ADEIKIRLQETEKHTSEKHTVVEKLE--VQRLQSK 2481
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 ... |
1432-2310 |
1.61e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 104.28 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1432 KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrtRIEEEIHIIRLQ 1511
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK-----EEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1512 LETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEK 1591
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE-KEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1592 FKLQAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKqqaEADKA 1671
Cdd:pfam02463 354 EEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK---EEKKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1672 REQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEE 1751
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1752 TAKQKLAAEQELIRLRADFEHAEQQR---TVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL-QQKSKAEKETM 1827
Cdd:pfam02463 508 GLKVLLALIKDGVGGRIISAHGRLGDlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgARKLRLLIPKL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1828 SNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALKEK 1907
Cdd:pfam02463 588 KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES-GLRKGVSLEEGLAEKSEVKA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1908 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIgqlKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKass 1987
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIK---KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL--- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1988 gkqelelelkKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEvgrlmKLAE 2067
Cdd:pfam02463 741 ----------LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE-----ELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2068 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA-KDNAEKEAALL 2146
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2147 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKssVEEE 2226
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE--ERNK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2227 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE 2306
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELG 1043
|
....
gi 1207141751 2307 EEAE 2310
Cdd:pfam02463 1044 GSAE 1047
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1365-2202 |
3.98e-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: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1365 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1444
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1445 KTKMKDEVSK---RQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNT 1521
Cdd:pfam02463 246 LRDEQEEIESskqEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1522 AETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1601
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1602 HlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ------LQEEAEHLKKQQAEADKAREQA 1675
Cdd:pfam02463 406 E-AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelkllkDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1676 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR-AKAEEAALKQKEAAEMELGNQRKMAEETAK 1754
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1755 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND--VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEK 1832
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1833 SKQLLESEAAkMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEK-EAE 1910
Cdd:pfam02463 645 ESGLRKGVSL-EEGLAEKSEVKASLSELTKELLEIQELqEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1911 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ---LKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 1987
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKkeeKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1988 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2067
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2068 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKaqNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2147
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKE--NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2148 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEA 2202
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
192-290 |
4.15e-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: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 192 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 270
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141751 271 DVPHPDEKSIITYVSSMYDV 290
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1390-2472 |
7.10e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.21 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1390 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLA-ETHAKAIAKAEQeANELKTKMKdevskrqdvavdsekqKHN 1468
Cdd:NF041483 251 QARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAES-ANEQRTRTA----------------KEE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1469 IQRELQELKTLSEQeIKAKSQQVeealLSRTRIEEEihiiRLQLETTMKQKN-TAETELLQLRAKAVDADKLRNAAQEEA 1547
Cdd:NF041483 314 IARLVGEATKEAEA-LKAEAEQA----LADARAEAE----KLVAEAAEKARTvAAEDTAAQLAKAARTAEEVLTKASEDA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1548 EKLRKQVAEETQK-KRKAEEELKRKSEAEKDAAKEKKKALEDLEKfklqaeeaERHLKQAEL-EKQRQIqvveevakKTA 1625
Cdd:NF041483 385 KATTRAAAEEAERiRREAEAEADRLRGEAADQAEQLKGAAKDDTK--------EYRAKTVELqEEARRL--------RGE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1626 ATQLESKQVALTARLEESLKNEQVMviQLQEEA----EHLKKQQAEADKAREQAEKELETWRQKANE-ALRLRLQAEEEA 1700
Cdd:NF041483 449 AEQLRAEAVAEGERIRGEARREAVQ--QIEEAArtaeELLTKAKADADELRSTATAESERVRTEAIErATTLRRQAEETL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1701 NkktaaqeeaekqkeeakreaKKRAKAEEaalkqkeaaemelgnQRKMAEETA-KQKLAAEQELIRLRADFEHA-EQQRT 1778
Cdd:NF041483 527 E--------------------RTRAEAER---------------LRAEAEEQAeEVRAAAERAARELREETERAiAARQA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1779 VLDDELQRLKNDVNSAVKQKkelEEELIKVRKEMEILlqqkskaEKETMSNTEKskqlLESEAA-KMRELAEEATklrsv 1857
Cdd:NF041483 572 EAAEELTRLHTEAEERLTAA---EEALADARAEAERI-------RREAAEETER----LRTEAAeRIRTLQAQAE----- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1858 aEEAKKQRQIAEEEAARQRAEAEkilkekltaiNEATRLKTEAeialkekEAENDRLKRKAEEEGyQRKVLEDQAAQHKQ 1937
Cdd:NF041483 633 -QEAERLRTEAAADASAARAEGE----------NVAVRLRSEA-------AAEAERLKSEAQESA-DRVRAEAAAAAERV 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1938 AIEEkiGQLKKSSDTELDRQKKIVEETLkqrkvveeeihilklnfekassgkqelelelkklkgiadetqkskakaeeea 2017
Cdd:NF041483 694 GTEA--AEALAAAQEEAARRRREAEETL---------------------------------------------------- 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2018 ekfrklaleeekkrkeaeakvkqiQAAEEEAARQHKAAQEEVGRLMklaeeAKKQKEIAEKEAEKQViLVQEAAQKC--- 2094
Cdd:NF041483 720 ------------------------GSARAEADQERERAREQSEELL-----ASARKRVEEAQAEAQR-LVEEADRRAtel 769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2095 -SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAallhkkAEEAERqkkaaeaeaakqakAQ 2171
Cdd:NF041483 770 vSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEA------QEEADR--------------VR 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2172 EDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELvkvkvQLDETDKQKSVLDVELKRL 2251
Cdd:NF041483 822 SDAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL-----RSDASEYAQRVRTEASDTL 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2252 KQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMK-KLAEEAARLNIEA 2326
Cdd:NF041483 887 ASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEA 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2327 Q-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEAQKLL-EAKKEMQQRLDQETEGFQ 2404
Cdd:NF041483 967 TgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEADRTLdEARKDANKRRSEAAEQAD 1040
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2405 KSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEKHTSEKHTVVEK 2472
Cdd:NF041483 1041 TLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAEATVEGNSLVEK 1100
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1589-2522 |
7.22e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.21 E-value: 7.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1589 LEKFKLQAEE----AERHLKQAELEKQRQIQvveEVAKKTAATQLESKQVALTARLE------------ESLKNEQVM-V 1651
Cdd:NF041483 78 LRNAQIQADQlradAERELRDARAQTQRILQ---EHAEHQARLQAELHTEAVQRRQQldqelaerrqtvESHVNENVAwA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1652 IQLQEEAEH-----LKKQQAEADK----AREQAEKELETWRQK-ANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1721
Cdd:NF041483 155 EQLRARTESqarrlLDESRAEAEQalaaARAEAERLAEEARQRlGSEAESARAEAEAILRRARKDAERLLNAASTQAQEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1722 KKRAK------AEEAALKQKEAAEMELGNQRKMAE-ETAKQKLAAEQELIRLRAD---------FEHAEQQRT-VLDDEL 1784
Cdd:NF041483 235 TDHAEqlrsstAAESDQARRQAAELSRAAEQRMQEaEEALREARAEAEKVVAEAKeaaakqlasAESANEQRTrTAKEEI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1785 QRLkndVNSAVKQ----KKELEEELIKVRKEMEILLQQ-----KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATklR 1855
Cdd:NF041483 315 ARL---VGEATKEaealKAEAEQALADARAEAEKLVAEaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKATT--R 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1856 SVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAI---------------NEATRLKTEAEIALKEKEAENDRLKRKAEE 1920
Cdd:NF041483 390 AAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAEAVAEGERIRGEARR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1921 EGYQR---------------KVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQkkiVEETLkQRKVVEEEihilKLNFEKA 1985
Cdd:NF041483 470 EAVQQieeaartaeelltkaKADADELRSTATAESERVRTEAIERATTLRRQ---AEETL-ERTRAEAE----RLRAEAE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1986 SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRL-MK 2064
Cdd:NF041483 542 EQAEEVRAAAERAARELREETERAIAARQAEAA--EELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrTE 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2065 LAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEF-EKAKKLAQEAEKAKDNAEKE 2142
Cdd:NF041483 620 AAERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAVRLRSEAAAEaERLKSEAqESADRVRAEAAAAAERVGTE 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2143 AA-LLHKKAEEAERQkkaaeaeaakqakaqedaeklRKEAEKEASRRaeaeaaalklKQEADSEMAKYKKLAEKTLKQ-K 2220
Cdd:NF041483 697 AAeALAAAQEEAARR---------------------RREAEETLGSA----------RAEADQERERAREQSEELLASaR 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2221 SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQ-KAQVEDELS-----------KVKIQMEDLLKLKLKIEK 2288
Cdd:NF041483 746 KRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGlQEQAEEEIAglrsaaehaaeRTRTEAQEEADRVRSDAY 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2289 ENQELMKKDKDNTKKLLEEEAENMKKLAE--------EAARLNIEAQE-AARLRQIAESDLAKQRELAEKMLEEkkqAIQ 2359
Cdd:NF041483 826 AERERASEDANRLRREAQEETEAAKALAErtvseaiaEAERLRSDASEyAQRVRTEASDTLASAEQDAARTRAD---ARE 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2360 EAAKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLE-----ITAEAEKLKVKVTQ-LS 2432
Cdd:NF041483 903 DANRIRSDaAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEqliaeATGEAERLRAEAAEtVG 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2433 DAQSKAE---EEAKKFKKQADEikirlqETEKHTSEKHTVVEKL--EVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2507
Cdd:NF041483 983 SAQQHAErirTEAERVKAEAAA------EAERLRTEAREEADRTldEARKDANKRRSEAAEQADTLITEAAAEADQLTAK 1056
|
1050
....*....|....*
gi 1207141751 2508 LQKQSKEMANVQQEQ 2522
Cdd:NF041483 1057 AQEEALRTTTEAEAQ 1071
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1187-1900 |
1.70e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1187 RSEAEGK-QATFDRLEEELQRATEVNKRMSQLHSERDVeLEHYRQLVGNLRERwqavfaQIELRQRELDLLNRQMQAyre 1265
Cdd:COG1196 174 KEEAERKlEATEENLERLEDILGELERQLEPLERQAEK-AERYRELKEELKEL------EAELLLLKLRELEAELEE--- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1266 sydwlirwiadakqrqdklhavpiggskgLQEQLTQEKKLLEEIEKNKDKVEDcqkfakgyidaikdyelqlvtykalve 1345
Cdd:COG1196 244 -----------------------------LEAELEELEAELEELEAELAELEA--------------------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1346 piasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEErkkmAEMQAELEKQKQ 1425
Cdd:COG1196 268 ------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1426 LAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEI 1505
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1506 HIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKA 1585
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1586 LEDLEKFKLQAEEA-ERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKneqvmviQLQEEAEHLKKQ 1664
Cdd:COG1196 497 LEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE-------VAAAAIEYLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1665 QA--------EADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1736
Cdd:COG1196 570 KAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1737 AAEMELGNQRKMAEETAKQKLAAEQELIRLRAdfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1816
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL--EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1817 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI-------AEEEAARQRAEAEKILKEK--- 1886
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQRedl 807
|
730 740
....*....|....*....|.
gi 1207141751 1887 -------LTAINEATRLKTEA 1900
Cdd:COG1196 808 eearetlEEAIEEIDRETRER 828
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
188-285 |
6.05e-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: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 267
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90
....*....|....*....
gi 1207141751 268 ED-VDVPHPDEKSIITYVS 285
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLC 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2116-2664 |
1.05e-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: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2116 DKLKEEFEKAKK---LAQEAEKAK--------DNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKE 2184
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2185 ASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ 2264
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2265 VEDELSKVKIQMEDLLKLKLKIEKENQELMkKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQR 2344
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEAL-RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2345 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDqetegfqksLEAERKRQLEITAEAEKL 2424
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---------LLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2425 KVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEAdglhKAIADLEKEKEKLKKE 2504
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG----RATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2505 AADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEER 2584
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2585 KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEEL 2664
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 ... |
1172-1986 |
1.27e-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: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1172 NEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQavfAQIELRQR 1251
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ---ELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1252 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1331
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1332 dyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDE-----------EK 1400
Cdd:pfam02463 332 --KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElelkseeekeaQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1401 AAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvavdSEKQKHNIQRELQELKTLS 1480
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-----ELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1481 EQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR-KQVAEETQ 1559
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAtADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1560 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTAR 1639
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1640 LEESLKNEQVMV---------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKktaaqEEA 1710
Cdd:pfam02463 645 ESGLRKGVSLEEglaeksevkASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLK-----LEA 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1711 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1790
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1791 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN-------------TEKSKQLLESEAAKMRELAEEATKLRSV 1857
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELalelkeeqkleklAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1858 AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaEEEGYQRKVLEDQAAQHKQ 1937
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE--ELLLEEADEKEKEENNKEE 957
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1207141751 1938 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 1986
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1390-2277 |
2.47e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.20 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1390 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK---------QKQLAETHAKAIAKAEQEANELKTKMKDEVSK------ 1454
Cdd:NF041483 313 EIARLVGEATKEAEALKAEAEQALADARAEAEKlvaeaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKAttraaa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1455 ------RQDVAVDSEK---QKHNIQRELQELKTLSEQEIKAKSQQV-EEALLSRTRIEE-------EIHIIRLQLETTMK 1517
Cdd:NF041483 393 eeaeriRREAEAEADRlrgEAADQAEQLKGAAKDDTKEYRAKTVELqEEARRLRGEAEQlraeavaEGERIRGEARREAV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1518 QK-----NTAEtELLQlRAKAvDADKLRNAAQEEAEKLRKQVAEE-TQKKRKAEEELKRKSEAEKDAAKEKKKALedlEK 1591
Cdd:NF041483 473 QQieeaaRTAE-ELLT-KAKA-DADELRSTATAESERVRTEAIERaTTLRRQAEETLERTRAEAERLRAEAEEQA---EE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1592 FKLQAEEAERHLKQaELEK---QRQIQVVEEVAKK--TAATQLESKQVALT-ARLE-ESLKNEQVmviqlqEEAEHLKKQ 1664
Cdd:NF041483 547 VRAAAERAARELRE-ETERaiaARQAEAAEELTRLhtEAEERLTAAEEALAdARAEaERIRREAA------EETERLRTE 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1665 QAEADKA-REQAEKELETWRQKA------------NEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR------- 1724
Cdd:NF041483 620 AAERIRTlQAQAEQEAERLRTEAaadasaaraegeNVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvgteaae 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1725 --AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELI---RLRADFEHAEQQRTVldDELQRLKNDVNSAVKQ-- 1797
Cdd:NF041483 700 alAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQRLV--EEADRRATELVSAAEQta 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1798 ----------KKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLESEAAKMRELA-EEATKLRSVA-EEAKKQR 1865
Cdd:NF041483 778 qqvrdsvaglQEQAEEEIAGLRSAAE-------HAAERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAK 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1866 QIAEEEAARQRAEAEKILKEkltAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGyqRKVLEDQAAQHKQAIEEKIGQ 1945
Cdd:NF041483 851 ALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDA--NRIRSDAAAQADRLIGEATSE 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1946 LKKSSDTELDRQKKIVEETLKQRKvveeeihilKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLAl 2025
Cdd:NF041483 926 AERLTAEARAEAERLRDEARAEAE---------RVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEA- 995
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2026 eeekkrkeaeakvKQIQA-AEEEAARQHKAAQEEVGRLMKLAEE--AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQ 2102
Cdd:NF041483 996 -------------ERVKAeAAAEAERLRTEAREEADRTLDEARKdaNKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2103 NVLV--QQNKDSMAQDKLKEefekAKKLAQEA--------EKAKDNAE-------KEAALLHKKAEEAeRQKKAAEAEAA 2165
Cdd:NF041483 1063 RTTTeaEAQADTMVGAARKE----AERIVAEAtvegnslvEKARTDADellvgarRDATAIRERAEEL-RDRITGEIEEL 1137
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2166 KQAKAQEDAEKLRKEAEK-------EASRRAEAEAAALKLKQEADSEMAKYK----KLAEKTLKQKSSVEEELVKvkvql 2234
Cdd:NF041483 1138 HERARRESAEQMKSAGERcdalvkaAEEQLAEAEAKAKELVSDANSEASKVRiaavKKAEGLLKEAEQKKAELVR----- 1212
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*..
gi 1207141751 2235 dETDKQKSVLDVELKRL----KQEVSDAIKQKAQVEDELSKVKIQME 2277
Cdd:NF041483 1213 -EAEKIKAEAEAEAKRTveegKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
188-288 |
2.60e-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: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 267
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1207141751 268 EDVDV--PHPDEKSIITYVSSMY 288
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
54-176 |
2.63e-19 |
|
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: 87.06 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 54 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlpREKGRMRFHKLQNVQ 133
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVS 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 134 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 176
Cdd:cd21309 82 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
54-176 |
3.07e-19 |
|
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: 86.68 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 54 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDvvrnsrlprEKGRMRFHKLQNVQ 133
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVS 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 134 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 176
Cdd:cd21308 85 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
188-284 |
4.00e-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: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 267
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90
....*....|....*...
gi 1207141751 268 ED-VDVPHPDEKSIITYV 284
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYL 97
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
184-291 |
4.74e-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: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 184 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 263
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1207141751 264 LLDPEDV-DVPHPDEKSIITYVSSMYDVM 291
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
191-287 |
5.26e-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: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 191 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN----LENLEQAFSIAERDLGVTRLLD 266
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1207141751 267 PEDVDVPHPDEKSIITYVSSM 287
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1173-1818 |
1.41e-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: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1173 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRE 1252
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1253 LDLLNRQMQAYRE----SYDWLIRWIADAKQRQDKLHAVPIggsKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYID 1328
Cdd:TIGR02168 395 IASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAEL---KELQAELEELEEELEELQEELERLEEALEELREELE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1329 ----AIKDYELQLVTYKALV--------------EPIASPLKKAKMESASDDIIQEYVTLRTRYS------------ELM 1378
Cdd:TIGR02168 472 eaeqALDAAERELAQLQARLdslerlqenlegfsEGVKALLKNQSGLSGILGVLSELISVDEGYEaaieaalggrlqAVV 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1379 TLSSQYIKFIIETQRRlQDEEKAA-----EKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAE--------------- 1438
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQ-NELGRVTflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdd 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1439 -QEANELKTKMK----------DEVSKRQDVAVDSEKQKHNIQ------RELQELKTLSEQEIKAKSQQVEEALLSRTRI 1501
Cdd:TIGR02168 631 lDNALELAKKLRpgyrivtldgDLVRPGGVITGGSAKTNSSILerrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1502 EEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE 1581
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1582 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT--------ARLEESLKNEQVMVIQ 1653
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelsediESLAAEIEELEELIEE 870
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1654 LQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTaaqeeaekQKEEAKREAKKRAKAEEAALK 1733
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR--------EKLAQLELRLEGLEVRIDNLQ 942
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1734 QK--EAAEMELGNQRKMAEETAKQKLAAEQELIRLR--------------ADFEHAEQQRtvldDELQRLKNDVNSAVKQ 1797
Cdd:TIGR02168 943 ERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEnkikelgpvnlaaiEEYEELKERY----DFLTAQKEDLTEAKET 1018
|
730 740
....*....|....*....|.
gi 1207141751 1798 kkeLEEELIKVRKEMEILLQQ 1818
Cdd:TIGR02168 1019 ---LEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1554-2428 |
1.75e-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: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1554 VAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-QAELEKQRQIQVVEEvaKKTAATQLESK 1632
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAlLKEKREYEGYELLKE--KEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1633 QVALtARLEESLKneqvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRLRLQAEEEANKKTAAQEEAEK 1712
Cdd:TIGR02169 243 ERQL-ASLEEELE-------KLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1713 QKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1792
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1793 SAVKQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATklrSVAEEAKKQRQIAEEEA 1872
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEEL----ADLNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1873 ArQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ--------------AAQHKQA 1938
Cdd:TIGR02169 462 A-DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtvaqlgsvGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1939 IEEKIGQLKKS--SDTELDRQKKIveETLKQRKVveEEIHILKLNfEKASSGKQELELELKKLKGIA-------DETQKS 2009
Cdd:TIGR02169 541 IEVAAGNRLNNvvVEDDAVAKEAI--ELLKRRKA--GRATFLPLN-KMRDERRDLSILSEDGVIGFAvdlvefdPKYEPA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2010 KAKAEEEAEKFRKLALEEEKKRK-----------EAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEK 2078
Cdd:TIGR02169 616 FKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2079 EAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkk 2158
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE--- 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2159 aaeaeaakqakaqeDAEKLRKEAEKEASRraeaeaaalklkqEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETD 2238
Cdd:TIGR02169 773 --------------DLHKLEEALNDLEAR-------------LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2239 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnMKKLAEE 2318
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ-LRELERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2319 AARLNIEAQEA-ARLRQIAESDLAKQRELAEkmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-------LEAKK 2390
Cdd:TIGR02169 905 IEELEAQIEKKrKRLSELKAKLEALEEELSE--IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALepvnmlaIQEYE 982
|
890 900 910
....*....|....*....|....*....|....*...
gi 1207141751 2391 EMQQRLDqETEGFQKSLEAERKRQLEITAEAEKLKVKV 2428
Cdd:TIGR02169 983 EVLKRLD-ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
56-173 |
3.71e-17 |
|
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: 79.93 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 56 QKKTFTKWVNKHLVKHwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerDVVRNsrlPRekgrMRFHKLQNVQIA 135
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP---GIHSR---PK----TRAQKLENIQAC 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141751 136 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 173
Cdd:cd21212 68 LQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
192-290 |
4.09e-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: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 192 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 270
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141751 271 DVPHPDEKSIITYVSSMYDV 290
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1830-2493 |
4.53e-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: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1830 TEKSKQL--LESEAAKmrelAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLtainEATRLKTEAEIALKEK 1907
Cdd:COG1196 196 GELERQLepLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1908 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKigqlkkssdtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 1987
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1988 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2067
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2068 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2147
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2148 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEEL 2227
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2228 vkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVkIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2307
Cdd:COG1196 578 -----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV-LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2308 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLE 2387
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2388 AKKEMQQRLDQETEGFqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSK-------AEEEAkkfkkqaDEIKIRLQEte 2460
Cdd:COG1196 732 AEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEY-------EELEERYDF-- 799
|
650 660 670
....*....|....*....|....*....|...
gi 1207141751 2461 khtsekhtvvekLEVQRLQSKQEADGLHKAIAD 2493
Cdd:COG1196 800 ------------LSEQREDLEEARETLEEAIEE 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1719-2639 |
5.04e-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: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1719 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFEHAE-----QQRTVLDDELQRLKNDVNS 1793
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELElallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1794 AVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1873
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1874 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEgyqrkvleDQAAQHKQAIEEKIGQLKKssdtE 1953
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRS----K 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1954 LDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELElelkklkgiadetqkskakaeeeaekfRKLALEEEKKRKE 2033
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---------------------------KKLEEAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2034 AEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSM 2113
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2114 AQDKLKEEFEKAKKLAQEAEKA-----------KDNAEKEAALLHKKAEE-----------AERQKKAAEAEAAKQAKAQ 2171
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNELgrvtflpldsiKGTEIQGNDREILKNIEGF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2172 EDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKqkSSVEEELVKVK-VQLDETDKQKSVL---DVE 2247
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRI--VTLDGDLVRPGgVITGGSAKTNSSIlerRRE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2248 LKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ 2327
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2328 EAARLRQIAESDLAKQRElaekmleEKKQAIQEAAKLKAEAEKLQKQKDQ---AQVEAQKLLEAKKEMQQRLDQETEGFQ 2404
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEE-------ELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2405 KSLEAERKRQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQR 2477
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2478 LQSKQEADGLHKAIADlekekeklkkeaadlqkqskemANVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklek 2557
Cdd:TIGR02168 911 SELRRELEELREKLAQ----------------------LELRLEGLEVRIDNLQERLSEEYSLTLEE------------- 955
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2558 qFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2637
Cdd:TIGR02168 956 -AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
..
gi 1207141751 2638 QQ 2639
Cdd:TIGR02168 1035 KD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1361-2141 |
5.49e-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: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1361 DDIIQEyvtLRTRYSELMTLSSQYIKFiietqRRLQDEEKAAE-----KLKEEERKKMAEMQAELEKQKQLAETHAKAIA 1435
Cdd:TIGR02168 192 EDILNE---LERQLKSLERQAEKAERY-----KELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1436 KAEQEANELKTKMKdEVSKRQDVavdsekqkhnIQRELQELKtlseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETT 1515
Cdd:TIGR02168 264 ELEEKLEELRLEVS-ELEEEIEE----------LQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1516 MKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKekkkaleDLEKFKLQ 1595
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL-------QIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1596 AEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1675
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1676 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKA 1727
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1728 EEAALKQKEA-----AEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLK--NDVNSAVKQKKE 1800
Cdd:TIGR02168 561 AIAFLKQNELgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1801 LEEE---------------------------LIKVRKEMEILLQQKSKAEketmSNTEKSKQLLESEAAKMRELAEEATK 1853
Cdd:TIGR02168 641 LRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELE----EKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1854 LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA 1933
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1934 QHKQAIEE----------------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 1997
Cdd:TIGR02168 797 ELKALREAldelraeltllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1998 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEA-ARQHKAAQEEVGRLMKLAEEAKKQKEIA 2076
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 2077 EKEAEKQVILVQEAAQKCSAAEQKAQNvLVQQNKDSMAQ-DKLKEEFEKAKKLAQEAEKAKDNAEK 2141
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKE-LGPVNLAAIEEyEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1158-1973 |
7.13e-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: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1158 KYENQLREVnKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRE 1237
Cdd:TIGR02168 217 ELKAELREL-ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1238 RWQAVFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLhavpiggskglQEQLTQEKKLLEEIEKNkdkVE 1317
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDEL-----------AEELAELEEKLEELKEE---LE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1318 DCQKFAKGYIDAIKDYELQLVTykalvepiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQyIKFIIETQRRLQD 1397
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEE------------LEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1398 EEKAAEKLKEEERkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQELK 1477
Cdd:TIGR02168 422 EIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1478 TLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETeLLQLRAKAV-----DADKLRNAAQEEAEKLRK 1552
Cdd:TIGR02168 496 RL-QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA-ALGGRLQAVvvenlNAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1553 QVAEETQKKrkaEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA--------------ERHLKQAELEKQRQIQVVE 1618
Cdd:TIGR02168 574 TFLPLDSIK---GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddlDNALELAKKLRPGYRIVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1619 E---VAKKTAATQLESKQVALT-------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1688
Cdd:TIGR02168 651 DgdlVRPGGVITGGSAKTNSSIlerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1689 A----LRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE---AALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1761
Cdd:TIGR02168 731 LrkdlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1762 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA 1841
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1842 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALkeKEAENDRLKRKAEEE 1921
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--EEAEALENKIEDDEE 968
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 1922 GYQRKVledqaAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 1973
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 ... |
1726-2663 |
1.63e-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: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1726 KAEEAALK-QKEAAEMELGNQRKMAEETAKQ-KLAAEQELirlradFEHAEQQRTVL---DDELQRLKNDVNSAVKQKKE 1800
Cdd:pfam01576 16 KVKERQQKaESELKELEKKHQQLCEEKNALQeQLQAETEL------CAEAEEMRARLaarKQELEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1801 LEEELIKVRKEMeillQQKSKAEKETMSNTEKSKQLLESEA----AKMRELAEEATKLRSVAEEAKKQRQIAEE---EAA 1873
Cdd:pfam01576 90 RSQQLQNEKKKM----QQHIQDLEEQLDEEEAARQKLQLEKvtteAKIKKLEEDILLLEDQNSKLSKERKLLEErisEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1874 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEA---ENDRLKRKAEEEGYQrkvLEDQAAQHKQAIEEKIGQLKKSS 1950
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTD---LQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1951 DTELDRQKKIVEETLK----QRKVVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQkskakaeeeaekfrklALE 2026
Cdd:pfam01576 243 EELQAALARLEEETAQknnaLKKIRELEAQISELQ-EDLESERAARNKAEKQRRDLGEELE----------------ALK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2027 eekkrkeaeakvkqiqaAEEEAARQHKAAQEEVgrlmklaeEAKKQKEIAEkeaekqvilvqeaAQKCSAAEQKAQNVLV 2106
Cdd:pfam01576 306 -----------------TELEDTLDTTAAQQEL--------RSKREQEVTE-------------LKKALEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2107 QQ--NKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK-------AEEAERQKKAAEAEAAKQAKAQEDAEKL 2177
Cdd:pfam01576 348 QEmrQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2178 RKEAEKEASRRAEAEAAALKLKQEADSEmakykklAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD 2257
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGK-------NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2258 AIKQ-------KAQVEDELSKVKIQMEDLLKLKLKIEKENQEL------MKKDKDNTKKLLEEEAENMKKLAEEAARLNI 2324
Cdd:pfam01576 501 LQEQleeeeeaKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkkrLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2325 EAQEAA----RLRQIAeSDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQV----EAQKLLEAKKEM---- 2392
Cdd:pfam01576 581 ELDDLLvdldHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALslarALEEALEAKEELertn 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2393 -QQRLD---------------QETEGFQKSLEA---ERKRQLE------ITAEAEKLKVKVT----------QLSDAQSK 2437
Cdd:pfam01576 660 kQLRAEmedlvsskddvgknvHELERSKRALEQqveEMKTQLEeledelQATEDAKLRLEVNmqalkaqferDLQARDEQ 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2438 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2517
Cdd:pfam01576 740 GEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2518 VQQEQLQQEKTILQQSFFAEKETL-----LKKEKAIEEEKKKLEKQFEDEVKKAEALK-AEQERQRKL------MEEERK 2585
Cdd:pfam01576 820 SRDEILAQSKESEKKLKNLEAELLqlqedLAASERARRQAQQERDELADEIASGASGKsALQDEKRRLeariaqLEEELE 899
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2586 KLQSAMDAAIKKQKEAEE-------EMNGKQKEMQDLEKKRIEQEKllaeENKNLREKLQQLQSSQKASYTKEIEIQTDK 2658
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLqveqlttELAAERSTSQKSESARQQLER----QNKELKAKLQEMEGTVKSKFKSSIAALEAK 975
|
....*
gi 1207141751 2659 VPEEE 2663
Cdd:pfam01576 976 IAQLE 980
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
190-288 |
3.72e-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: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 190 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 269
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1207141751 270 -VDVPHPDEKSIITYVSSMY 288
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
57-171 |
4.42e-16 |
|
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: 76.61 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 57 KKTFTKWVNKHLVKhwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlpREKGRMRFHKLQNVQIAL 136
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFL 66
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141751 137 DFLKHRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 171
Cdd:cd00014 67 NACKKLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
190-289 |
9.92e-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: 9.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 190 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 269
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1207141751 270 VDV--PHPDEKSIITYVSSMYD 289
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
657-847 |
1.44e-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: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 657 QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAF 736
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 737 TAALQTQWSWILQLCCCIETHLKENTAYFQFFSDVKEAEDRMKKMEDTMKKKYVCDrsiTVTRLEDLLQDAVEEKEQLNE 816
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1207141751 817 FKTHLEGLNRRAKTIIQLKPRNPAQPIKGKL 847
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
188-285 |
3.15e-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: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1207141751 267 PEDVDVPHPDEKSIITYVS 285
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1655-2628 |
3.78e-15 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 83.34 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1655 QEEAEHLKKQQAEADKAREQAEK----------ELETWRQKANEALR------------LRLQAEEEANKKTAAQEEAEK 1712
Cdd:NF041483 11 RADDDHLSRFEAEMDRLKTEREKavqhaedlgyQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1713 QKEEAKREAKKRAK------AEEAALKQKE----------AAEMELGNQRKMAEETAKQKLA--------AEQELIRL-- 1766
Cdd:NF041483 91 DAERELRDARAQTQrilqehAEHQARLQAElhteavqrrqQLDQELAERRQTVESHVNENVAwaeqlrarTESQARRLld 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1767 --RADFEH------AEQQRtVLDDELQRLKNDVNSAvkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTE--KSKQL 1836
Cdd:NF041483 171 esRAEAEQalaaarAEAER-LAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDHAEqlRSSTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1837 LESEAAKMR----------ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE-------KILKEKLT-----AINEAT 1894
Cdd:NF041483 247 AESDQARRQaaelsraaeqRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1895 RLKTEAEIALKEKEAENDRLKRKAEEEGyQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEE 1974
Cdd:NF041483 327 ALKAEAEQALADARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1975 IHilKLNFEKASSGKQelelelkkLKGIA-DETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQA-AEEEAARQ- 2051
Cdd:NF041483 406 AD--RLRGEAADQAEQ--------LKGAAkDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGeARREAVQQi 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2052 HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLvqqnkdsmaqDKLKEEFEKAKKLAQE 2131
Cdd:NF041483 476 EEAARTAEELLTKAKADADELRSTATAESER---VRTEAIERATTLRRQAEETL----------ERTRAEAERLRAEAEE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2132 -AEKAKDNAEKEAALLHkkaEEAERqkkaaeAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAaalklkqEADSEMAKYK 2210
Cdd:NF041483 543 qAEEVRAAAERAARELR---EETER------AIAARQAEAAEELTRLHTEAEERLTAAEEALA-------DARAEAERIR 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2211 K-LAEKTLKQKSSVEEELVKVKVQLDEtdkqksvldvELKRLKQEVSdAIKQKAQVEDELSKVKIQMEdllklklkIEKE 2289
Cdd:NF041483 607 ReAAEETERLRTEAAERIRTLQAQAEQ----------EAERLRTEAA-ADASAARAEGENVAVRLRSE--------AAAE 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2290 NQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEkmlEEKKQAIQEAAKLKAEA 2368
Cdd:NF041483 668 AERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2369 eklQKQKDQAQVEAQKLLE------------AKKEMQQRLD----------QETEGFQKSLE--AERKRQlEITAEAEKL 2424
Cdd:NF041483 745 ---RKRVEEAQAEAQRLVEeadrratelvsaAEQTAQQVRDsvaglqeqaeEEIAGLRSAAEhaAERTRT-EAQEEADRV 820
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2425 KvkvtqlSDAQS---KAEEEAKKFKKQADEikirlqETE--KHTSEKhTVVEKL-EVQRLQSkQEADGLHKAIADLEKEK 2498
Cdd:NF041483 821 R------SDAYAereRASEDANRLRREAQE------ETEaaKALAER-TVSEAIaEAERLRS-DASEYAQRVRTEASDTL 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2499 EKLKKEAADLQKQSKEMANvqqeqlqqektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2578
Cdd:NF041483 887 ASAEQDAARTRADAREDAN------------RIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRAD 954
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2579 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQkemQDLEKKRIEQEKLLAE 2628
Cdd:NF041483 955 AAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2032-2592 |
4.29e-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: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2032 KEAEAKVKQIQAAEEEAARQHKAAQEEVGRLmkLAEEAKKQKEIAEKEAEKQVilvqeaaqkcsaAEQKAQNVLVQQNKD 2111
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEA--QAEEYELLAELARLEQDIAR------------LEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2112 SMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEA 2191
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2192 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSK 2271
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2272 VKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKL------AEEAARLNIEAQEAARLRQIAESDLAKQRE 2345
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2346 LAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-----LEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAE 2420
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2421 AEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETekhtsekhtvvEKLEVQRLQSKQEADGLHKAIADLEKEKEK 2500
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE-----------LEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2501 LKKEAADLQKQSKEMANVQQEQLQQEKTILQQsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-------------- 2566
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELL----EEEELLEEEALEELPEPPDLEELERELERLereiealgpvnlla 786
|
570 580 590
....*....|....*....|....*....|...
gi 1207141751 2567 -EALKAEQER------QRKLMEEERKKLQSAMD 2592
Cdd:COG1196 787 iEEYEELEERydflseQREDLEEARETLEEAIE 819
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1152-1818 |
4.87e-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: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1152 AEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkrmsqlhserdvELEHYRQL 1231
Cdd:COG1196 251 LEAELEELEAELAEL------EAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1232 VGNLRERwqavfaQIELRQRELDLLNRQMQAYREsydwLIRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK 1311
Cdd:COG1196 311 RRELEER------LEELEEELAELEEELEELEEE----LEELEEELEEAEEELEE--------AEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1312 NKDKVEdcqkfakgyidaikdyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRyselmtlssqyikfIIET 1391
Cdd:COG1196 373 ELAEAE----------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--------------LEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1392 QRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDvavdsEKQKHNIQR 1471
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----AAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1472 ELQELKTLSEQEIKAKSQQVEEALLSRTrieeeihiIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1551
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA--------VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1552 KQVAEEtqkkRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1631
Cdd:COG1196 570 KAGRAT----FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1632 KQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1711
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1712 KQKEEAKREAKKRAKAEEAALKQKEAAEMELgnQRKMAEETAKQKLA-AEQELIRL-----RADFEHAEQQRTVldDELQ 1785
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEEL--PEPPDLEELERELErLEREIEALgpvnlLAIEEYEELEERY--DFLS 801
|
650 660 670
....*....|....*....|....*....|...
gi 1207141751 1786 RLKNDVNSAvkqKKELEEELIKVRKEMEILLQQ 1818
Cdd:COG1196 802 EQREDLEEA---RETLEEAIEEIDRETRERFLE 831
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
190-293 |
6.59e-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: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 190 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 269
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1207141751 270 VDV--PHPDEKSIITYVSSMYDVMPR 293
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4082-4120 |
7.80e-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: 7.80e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 4082 LLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEMNGIL 4120
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1420-2355 |
8.72e-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: 8.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1420 LEKQKQLAETHAKAIAKAEQEANELKT------KMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSE--QEIKAKSQQV 1491
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQykekacEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKeiEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1492 EEALLSRTRIEEEIHIIRLQLETTMKQ--KNTAE--TELLQLRAKAV-DADKLRNAAQEEAEKLRKQVAEETQKKRKAEE 1566
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKvfQGTDEqlNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1567 ELKRKSEAEKDAAKEKKKALEDLEKFKLQAE--------EAERHLKQA-ELEKQRQIQVVEEVAKKTA--ATQLESKQVA 1635
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFhTLVIERQEDEAKTAAQLCAdlQSKERLKQEQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1636 LT------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEAdkarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEE 1709
Cdd:TIGR00606 428 ADeirdekKGLGRTIELKKEILEKKQEELKFVIKELQQL----EGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1710 AEKQKEEAKREAKKRAKAEEAALKQKEA---AEMELGNQRKMA--EETAKQKLAAEQELIRLRADFEHAEQqrtvLDDEL 1784
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQLNHHTttrTQMEMLTKDKMDkdEQIRKIKSRHSDELTSLLGYFPNKKQ----LEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1785 QRLKNDvnsavkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLES--EAAKMRELAEEATKLRSVAEEAK 1862
Cdd:TIGR00606 580 HSKSKE-------INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1863 KQRQIAEEEAARQRAEAEKILKEKLTAINEATR-LKTEAEIALKEKEAENDRLKRKAEEEGyqrkvLEDQAAQHKQAIEE 1941
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDLQSKLRLAPDKLKS-----TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1942 KIGqLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2021
Cdd:TIGR00606 728 MLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVER 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2022 KLA-LEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQK 2100
Cdd:TIGR00606 807 KIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE---LKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2101 AQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEaerqkkaaeaeaakqakaqedaeklRKE 2180
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS-------------------------NKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2181 AEKEASRRAEaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2260
Cdd:TIGR00606 939 AQDKVNDIKE------KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2261 QKAQVEDELSKVKIQMEdllklklkIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAArlNIEAQEAARLRQIAESDl 2340
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENE--------LKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID--LIKRNHVLALGRQKGYE- 1081
|
970
....*....|....*
gi 1207141751 2341 aKQRELAEKMLEEKK 2355
Cdd:TIGR00606 1082 -KEIKHFKKELREPQ 1095
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
190-288 |
8.81e-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: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 190 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 269
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1207141751 270 -VDVPHPDEKSIITYVSSMY 288
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
193-288 |
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 1207141751 193 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDPED-VD 271
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1207141751 272 VPHPDEKSIITYVSSMY 288
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
56-173 |
1.37e-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: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 56 QKKTFTKWVNKHLVKHwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerDVVRNsrlPREKGRMRfhklQNVQIA 135
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKV 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141751 136 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 173
Cdd:cd21213 68 LQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2117-2652 |
1.84e-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: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2117 KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaal 2196
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK--------------DLTFLLEESRDKAN---------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2197 KLKQEADSEMAKYKKLAEKtlkqKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQM 2276
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEK----KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2277 EDLLKLKLKIEKENQELMKKDKDNtkklLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQREL---AEKMLEE 2353
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQR----LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIlaeDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2354 KKQAIQEAAKLKAEAEKL-----QKQKDQAQVEAQklLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKV 2428
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllqAREKEIHDLEIQ--LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2429 TQLSDAQS-------KAEEEAKKFKKQADEIKIR---LQETEKH-TSEKHTVVEKLEVQRLQ-------SKQEADGLHKA 2490
Cdd:pfam05483 502 KELTQEASdmtlelkKHQEDIINCKKQEERMLKQienLEEKEMNlRDELESVREEFIQKGDEvkckldkSEENARSIEYE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2491 IADLEKEKEKLKKEAADLQKQSkEMANVQQEQLQQEKTILQQSFFAEKETLLK---KEKAIEEEKKKLEKQFEDEVKKAE 2567
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQI-ENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQ 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2568 ALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKN---LREKLQQLQSSQ 2644
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSA 740
|
....*...
gi 1207141751 2645 KASYTKEI 2652
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 ... |
1390-2485 |
2.49e-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: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1390 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKaEQEANELKTKMKDEVSKRQDVAVDSEKQKHNI 1469
Cdd:pfam01576 23 KAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR-KQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1470 QRELQELKT-LSEQEIKAKSQQVEEALLSRT--RIEEEIHIIRLQLETTMKQKNTAE-------TELLQLRAKAVDADKL 1539
Cdd:pfam01576 102 QQHIQDLEEqLDEEEAARQKLQLEKVTTEAKikKLEEDILLLEDQNSKLSKERKLLEeriseftSNLAEEEEKAKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1540 RNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKkkaledLEKFKLQAEEAERHLKQAELEKQR-QIQVVE 1618
Cdd:pfam01576 182 KNKHEAMISDLEERLKKE-EKGRQELEKAKRKLEGESTDLQEQ------IAELQAQIAELRAQLAKKEEELQAaLARLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1619 EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-------LQEEAEHLKKQ----------QAEADKAREQAEKELEt 1681
Cdd:pfam01576 255 ETAQKNNALKKIRELEAQISELQEDLESERAARNKaekqrrdLGEELEALKTEledtldttaaQQELRSKREQEVTELK- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1682 wRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE--AAEMELGNQRKMAEETAKQKLaa 1759
Cdd:pfam01576 334 -KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAelQAELRTLQQAKQDSEHKRKKL-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1760 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLles 1839
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNL--- 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1840 eAAKMRELAEEATKLRSVAEEAKKQRQIAEEE---AARQRAEAEKILKEKLTAINEATRLKTEAEialKEKEAENDRLKR 1916
Cdd:pfam01576 488 -STRLRQLEDERNSLQEQLEEEEEAKRNVERQlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ---RELEALTQQLEE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1917 KAEEegYQRkvLEDQAAQHKQAIEEKIgqlkkssdTELDRQKKIVEETLKQRKVVEEeihilKLNFEKASSGKqelelel 1996
Cdd:pfam01576 564 KAAA--YDK--LEKTKNRLQQELDDLL--------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISAR------- 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1997 kklkgIADETQKSKAKAEEEAEKFRKLAleeekkrkeaeAKVKQIQAAEEEAARQHKAAQEEVGRLM-------KLAEEA 2069
Cdd:pfam01576 620 -----YAEERDRAEAEAREKETRALSLA-----------RALEEALEAKEELERTNKQLRAEMEDLVsskddvgKNVHEL 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2070 KKQKEIAEKEAEKQVILVQEAAQKCSAAEQ------------KAQNVLVQQNKDSMAQDKLKEEFEKAKKLaqEAEKAKD 2137
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATEDaklrlevnmqalKAQFERDLQARDEQGEEKRRQLVKQVREL--EAELEDE 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2138 NAEKEAALLHKKAEEAErqkkaaeaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTL 2217
Cdd:pfam01576 762 RKQRAQAVAAKKKLELD---------LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESE 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2218 KQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkd 2297
Cdd:pfam01576 833 KKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQL------------------ 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2298 kdntKKLLEEEAENMKKLAEEAARLNIEAqEAARLRQIAESDLAKQRELAEKMLEEKKQAIQeaAKLkAEAEKLQKQKDQ 2377
Cdd:pfam01576 895 ----EEELEEEQSNTELLNDRLRKSTLQV-EQLTTELAAERSTSQKSESARQQLERQNKELK--AKL-QEMEGTVKSKFK 966
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2378 AQVEAqklLEAK-KEMQQRLDQETEGFQKSLEAERKRQleitaeaEKLKVKVTQLSDAQSKAEEeakkFKKQADEIKIRL 2456
Cdd:pfam01576 967 SSIAA---LEAKiAQLEEQLEQESRERQAANKLVRRTE-------KKLKEVLLQVEDERRHADQ----YKDQAEKGNSRM 1032
|
1130 1140
....*....|....*....|....*....
gi 1207141751 2457 QETEKHTSEKHTVVEKLEVQRLQSKQEAD 2485
Cdd:pfam01576 1033 KQLKRQLEEAEEEASRANAARRKLQRELD 1061
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2307-2667 |
2.90e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2307 EEAEnmKKLaeEAARLNIEaqeaaRL--------RQIAEsdLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQK 2375
Cdd:COG1196 175 EEAE--RKL--EATEENLE-----RLedilgeleRQLEP--LERQAEKAERYRElkeELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2376 DQAQVEAQKLLEAKKEMQQRLDQETegfqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR 2455
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAE------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2456 LQETEKhtsekhtVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFF 2535
Cdd:COG1196 318 LEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2536 AEKETLlkkekaieeekkklekqfedevkKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDL 2615
Cdd:COG1196 391 ALRAAA-----------------------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2616 EKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQM 2667
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
49-172 |
3.39e-14 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 71.54 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 49 ADERDrvqKKTFTKWVNKHLVKHwkaeaqrHITDLYEDLRDGhnlISLLEVLsgETLprERDVVRNSRLPREKGRMRFHK 128
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKK 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 172
Cdd:cd21219 64 VENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
53-169 |
5.64e-14 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 71.02 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 53 DRVQKKTFTKWVNKHLVKhwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDVVRNSRLPRekgrmrfhkLQNV 132
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK----RGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNL 68
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141751 133 QIALDFL-KHRQVKLVNIRNDDIADGNPKLTLGLIWTI 169
Cdd:cd21225 69 HLAMLFIeEDLKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
190-285 |
6.72e-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: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 190 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 268
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1207141751 269 DVDVPHPDEKSIITYVS 285
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3103-3141 |
7.08e-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: 7.08e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 3103 LLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPELHEKL 3141
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 ... |
1173-1941 |
1.53e-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: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1173 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQR-ATEVNKRMSQLHSERDV--ELEHYRQLVGNLRERWQAVFAQIELR 1249
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQlCEEKNALQEQLQAETELcaEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1250 QRELDLLNRQMQAYRESydwLIRWIADAKQRQDKLHAvpigGSKGLQ-EQLTQE---KKLLEEIEKNKDKVEDCQKFAKG 1325
Cdd:pfam01576 84 LEEEEERSQQLQNEKKK---MQQHIQDLEEQLDEEEA----ARQKLQlEKVTTEakiKKLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1326 YIDAIKDYELQLvtykalvepiASPLKKAKMesasddiiqeyvtlrtryseLMTLSSQYIKFIIETQRRLQDEEK----- 1400
Cdd:pfam01576 157 LEERISEFTSNL----------AEEEEKAKS--------------------LSKLKNKHEAMISDLEERLKKEEKgrqel 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1401 -----AAEKLKEEERKKMAEMQAELEKQK-QLA---ETHAKAIAKAEQEAN-----------------ELKTKMKDEVSK 1454
Cdd:pfam01576 207 ekakrKLEGESTDLQEQIAELQAQIAELRaQLAkkeEELQAALARLEEETAqknnalkkireleaqisELQEDLESERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1455 RQdvavDSEKQKHNIQRELQELK---------TLSEQEIKAKSQQvEEALLSRTrIEEEIHIIRLQLEtTMKQKNTAETE 1525
Cdd:pfam01576 287 RN----KAEKQRRDLGEELEALKteledtldtTAAQQELRSKREQ-EVTELKKA-LEEETRSHEAQLQ-EMRQKHTQALE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1526 -----LLQLRAKAVDADKLRNAAQEEAEKLRKQV-------AEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1593
Cdd:pfam01576 360 elteqLEQAKRNKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1594 LQAEEAERHLKQAElekQRQIQVVEEVAkkTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKARE 1673
Cdd:pfam01576 440 SELESVSSLLNEAE---GKNIKLSKDVS--SLESQLQDTQELLQEETRQKLNLST-RLRQLEDERNSLQEQLEEEEEAKR 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1674 QAEKELETWRQ------KANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK-EAAEMELGNQR 1746
Cdd:pfam01576 514 NVERQLSTLQAqlsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElDDLLVDLDHQR 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1747 KMAEETAKQ-----KLAAEQELIRLRA--DFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1819
Cdd:pfam01576 594 QLVSNLEKKqkkfdQMLAEEKAISARYaeERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1820 SKAEKeTMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAK------------------KQRQIAEEEAARQRA---- 1877
Cdd:pfam01576 674 DDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqferdlQARDEQGEEKRRQLVkqvr 752
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 1878 EAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1941
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEE 816
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1131-1915 |
1.77e-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: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1131 LSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVP-VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE 1209
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1210 VNKRmsQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYREsydwlirwiadakQRQDKLHAVpi 1289
Cdd:pfam15921 199 ASGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKS-------------ESQNKIELL-- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1290 ggskglqeqltqekklleeIEKNKDKVEDCqkfakgyidaIKDYELQLVtykALVEPIASPLKKAKMESASDDIIQEYVT 1369
Cdd:pfam15921 262 -------------------LQQHQDRIEQL----------ISEHEVEIT---GLTEKASSARSQANSIQSQLEIIQEQAR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1370 LRT-----RYSELMTLSSQYIKFIIETQRRLQDEEKaaeklkeeerkkmaemqaELEKQKQLAETHakaIAKAEQEANEL 1444
Cdd:pfam15921 310 NQNsmymrQLSDLESTVSQLRSELREAKRMYEDKIE------------------ELEKQLVLANSE---LTEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1445 KTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIkAKSQQVEEalLSRTRIEEEIHIIRLQ-LETTMKQKNTAE 1523
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDT-GNSITIDH--LRRELDDRNMEVQRLEaLLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1524 TEllqlraKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlekfKLQAEEAER-- 1601
Cdd:pfam15921 446 ME------RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK---------------------KMTLESSERtv 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1602 -HLKQAELEKQRQIQvveevAKKTAATQLESKqVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELE 1680
Cdd:pfam15921 499 sDLTASLQEKERAIE-----ATNAEITKLRSR-VDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1681 TWRQKANEALRL-------RLQAEEEANKKtaAQEEAEKQKEEAKREAKKRA-KAEEAALKQKEAAEMELGNQRKMAEET 1752
Cdd:pfam15921 573 NMTQLVGQHGRTagamqveKAQLEKEINDR--RLELQEFKILKDKKDAKIRElEARVSDLELEKVKLVNAGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1753 AKQKL--------AAEQELIRLRADFE--------HAEQQRTVLD----------DELQRLKNDVNS-------AVKQKK 1799
Cdd:pfam15921 651 IKQERdqllnevkTSRNELNSLSEDYEvlkrnfrnKSEEMETTTNklkmqlksaqSELEQTRNTLKSmegsdghAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1800 ELEEELIKVRKEMEIlLQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatKLRSVAEEakKQRQIAEEEAARQRaea 1879
Cdd:pfam15921 731 GMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ------ELSTVATE--KNKMAGELEVLRSQ--- 798
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1207141751 1880 EKILKEKLT----AINEATRLKTEAEIALKEKEAENDRLK 1915
Cdd:pfam15921 799 ERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
188-288 |
2.45e-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: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 267
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1207141751 268 ED-VDVPHPDEKSIITYVSSMY 288
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3763-3801 |
3.75e-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: 3.75e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 3763 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEFHDKL 3801
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2776-2814 |
4.14e-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: 4.14e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 2776 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPELHTKL 2814
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1224-1922 |
4.25e-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: 76.55 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1224 ELEHYRQLVGNLRERWQAVFAQIELRQRELDLL----NRQMQAYRESYDWLIRWIADAKQRQDKLhavpiggsKGLQEQL 1299
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLtlctPCMPDTYHERKQVLEKELKHLREALQQT--------QQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1300 TQEKKLLEEIEKNkdkvedcQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDIIQ-------EYVTLRT 1372
Cdd:TIGR00618 246 TQKREAQEEQLKK-------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieqqaqrIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1373 RYSELMTLSSQYIKFI-----IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAEtHAKAIAKAEQEANELKTK 1447
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVkqqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1448 MKDEVSKRQDVAVDSEKQkHNIQRELQELKTLSEQEIKAksqQVEEALLSRTRIEEE--IHIIRLQLETTMKQKNTAETE 1525
Cdd:TIGR00618 398 LCKELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTaqCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1526 LLQlRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQ 1605
Cdd:TIGR00618 474 QLQ-TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1606 AELEkqrQIQVVEEvaKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEhlKKQQAEADKAREQAEKELETWRQK 1685
Cdd:TIGR00618 553 SERK---QRASLKE--QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1686 ANEALRLRLQ--AEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1763
Cdd:TIGR00618 626 DLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1764 IR-----LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLE 1838
Cdd:TIGR00618 706 LRelethIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1839 SEAAKMRELAEEATKLRSVAEEAKKQ-------RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEN 1911
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
730
....*....|.
gi 1207141751 1912 DRLKRKAEEEG 1922
Cdd:TIGR00618 866 QEQAKIIQLSD 876
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1884-2682 |
4.46e-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: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1884 KEKLTAINEA---TRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvLEDqaaqhkqAIEEKIGQLKKssdteLDRQKKI 1960
Cdd:TIGR02168 155 EERRAIFEEAagiSKYKERRKETERKLERTRENLDR-----------LED-------ILNELERQLKS-----LERQAEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1961 VEETLKQRKVVEE-EIHILKLNFEKASSGKQELELELKKLKGIADETQKskakaeeeaekfrklaleeekkrkeaeaKVK 2039
Cdd:TIGR02168 212 AERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTA----------------------------ELQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2040 QIQAAEEEAARQHKAAQEEVGRLMKLAEEAKkqKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmaqDKLK 2119
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALA--NEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-----DELA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2120 EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEK----LRKEAEKEASRRAEAEAAA 2195
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiasLNNEIERLEARLERLEDRR 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2196 LKLKQEADSEMAKYKKLAEKTLKQK-SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2274
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2275 QME--DLLKLKLKIEKENQELMKKDKDNTKKLLEEEA-----------ENMKKLA---EEAARLNIEAQEAARL--RQIA 2336
Cdd:TIGR02168 497 LQEnlEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaaieaalgGRLQAVVvenLNAAKKAIAFLKQNELgrVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2337 ESDLAKQRELAEKMLEEKK-------------------------------------QAIQEAAKL--------------- 2364
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggvlvvddldNALELAKKLrpgyrivtldgdlvr 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2365 -------------------KAEAEKLQKQKDQAQV---EAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAE 2422
Cdd:TIGR02168 657 pggvitggsaktnssilerRREIEELEEKIEELEEkiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2423 KLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEkekeklk 2502
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2503 keaADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEE 2582
Cdd:TIGR02168 810 ---AELTLLNEEAANLRERLESLERRI------AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2583 ERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEenknLREKLQQLQSsqkasytkEIEIQTDKVPEE 2662
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ----LELRLEGLEV--------RIDNLQERLSEE 948
|
890 900
....*....|....*....|
gi 1207141751 2663 ELVQMTMVETTKKVLNGSTE 2682
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEE 968
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
58-176 |
7.94e-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: 68.03 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 58 KTFTKWVNKHLVkhwkaeaQRHITDLYEDLRDGHNLISLLEVLSgetlPRERDVVRNSRLPREKGRMrFHKLQNVQIALD 137
Cdd:cd21298 9 KTYRNWMNSLGV-------NPFVNHLYSDLRDGLVLLQLYDKIK----PGVVDWSRVNKPFKKLGAN-MKKIENCNYAVE 76
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141751 138 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 176
Cdd:cd21298 77 LGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
188-288 |
1.37e-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: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 267
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1207141751 268 ED-VDVPHPDEKSIITYVSSMY 288
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1666-2453 |
1.63e-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: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1666 AEADKAREQAEKELETWRQKANealRLRLQAEEEANKktaaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQ 1745
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIE---RLDLIIDEKRQQ--------------LERLRREREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1746 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRKEMEILLQQKSKAEK 1824
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1825 ETMSNTEKSKQLLESEA---AKMRELAEEATKL-RSVAEEAKKQRQIAEEEAARQ------RAEAEKILKEKLTAINEAT 1894
Cdd:TIGR02169 309 SIAEKERELEDAEERLAkleAEIDKLLAEIEELeREIEEERKRRDKLTEEYAELKeeledlRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1895 RLKTEAEIALKEKEAENDRLKRKAEEegyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKI------VEETLKQR 1968
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqewkLEQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1969 KVVEEEIHILKLNF---EKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-----------------LALEEE 2028
Cdd:TIGR02169 465 SKYEQELYDLKEEYdrvEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryaTAIEVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2029 KKRKEAEAKVKQIQAAEE--EAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLV 2106
Cdd:TIGR02169 545 AGNRLNNVVVEDDAVAKEaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-------DPKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2107 QQNKDSMaqdkLKEEFEKAKKLAQEAEK---AKDNAEKEAALLhKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2183
Cdd:TIGR02169 618 YVFGDTL----VVEDIEAARRLMGKYRMvtlEGELFEKSGAMT-GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2184 EASRRAEAEaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA 2263
Cdd:TIGR02169 693 LQSELRRIE----NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2264 QVEDELSKVKIQMEDllklklKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQ 2343
Cdd:TIGR02169 769 ELEEDLHKLEEALND------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2344 RELAEKMLEEKkqaiQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEK 2423
Cdd:TIGR02169 843 IDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830
....*....|....*....|....*....|
gi 1207141751 2424 LKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2453
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3179-3217 |
2.05e-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: 2.05e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 3179 LLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEMNQNL 3217
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
562-751 |
2.52e-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: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 562 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 638
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIeegHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 639 LQYAKLLTSSKTRLRSLD---QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNV 715
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207141751 716 QMTGDKLLKDGHP-ARKTIEAFTAALQTQWSWILQLC 751
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1719-2371 |
5.83e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1719 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVNSAVKQK 1798
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1799 KELEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLEsEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 1878
Cdd:PRK03918 248 ESLEGSK----RKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1879 AEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegYQR-KVLEDQAAQHKqaieekigqlKKSSDTELDRQ 1957
Cdd:PRK03918 323 INGI-EERIKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEaKAKKEELERLK----------KRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1958 KKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-LALEEEKKRKEAEA 2036
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKIT---ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2037 KVKQIQAAEEEAarqhKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQD 2116
Cdd:PRK03918 467 ELKEIEEKERKL----RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2117 KLKEEFEKAKKLaqeaekakdnaEKEAALLHKKAEEAERQKkaaeaeaakqakaqedaEKLRKEAEKEASRRAEAEAAAL 2196
Cdd:PRK03918 543 SLKKELEKLEEL-----------KKKLAELEKKLDELEEEL-----------------AELLKELEELGFESVEELEERL 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2197 KLKQEADSEMAKYKKlAEKTLKQKssvEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVE-DELSKVKIQ 2275
Cdd:PRK03918 595 KELEPFYNEYLELKD-AEKELERE---EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLE 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2276 MEDLLKLKLKIEKENQELMKKDKDNTKKlLEEEAENMKKLAEEAARLNIEAQEAARLRQ--------IAESDLAKQRELA 2347
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEK-LKEELEEREKAKKELEKLEKALERVEELREkvkkykalLKERALSKVGEIA 749
|
650 660
....*....|....*....|....
gi 1207141751 2348 EKMLEEKKQAIQEAAKLKAEAEKL 2371
Cdd:PRK03918 750 SEIFEELTEGKYSGVRVKAEENKV 773
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2073-2653 |
6.68e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2073 KEIAEKEAEKQVILVQEA--AQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKD---NAEKEAALLH 2147
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2148 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAeaaaLKLKQEadseMAKYKKLAEKTLKQKSSVEEEL 2227
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY----IKLSEF----YEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2228 VKVKVQLDETDKQKSVLDvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2307
Cdd:PRK03918 324 NGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2308 EAENMKKLAEEAARLNIEAQEaaRLRQIAESDLAKQ------RELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQKDQ 2377
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKE--LKKAIEELKKAKGkcpvcgRELTEehrkELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2378 AQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITA-EAEKLKVKVTQLSDAQSKAEEEAKK---FKKQADE 2451
Cdd:PRK03918 481 ELRELEKVLKKESELikLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2452 IKIRLQETEKHTSEKHTvveKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlq 2531
Cdd:PRK03918 561 LEKKLDELEEELAELLK---ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL-- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2532 qsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME-EERKKLQSAMDAAIKKQKEAEEEMNGKQK 2610
Cdd:PRK03918 636 ----AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAElEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1207141751 2611 EMQDLEKKRieqekllaEENKNLREKLQQLQSSQKASYTKEIE 2653
Cdd:PRK03918 712 ELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVG 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1398-2155 |
6.99e-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: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1398 EEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQ--------DVAVDSEKQKHNI 1469
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1470 QRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvdaDKLRNAAQEEAEK 1549
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE--------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL---EDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1550 LRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEKFKLQAEEAERHLKQAELEKQrqIQVVEEvAKKTAATQL 1629
Cdd:TIGR02169 380 FAETR-DELKDYREKLEKLKREINELKR------------ELDRLQEELQRLSEELADLNAA--IAGIEA-KINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1630 ESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAA 1706
Cdd:TIGR02169 444 EDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1707 QEEAEKQKEEAKREakkRAKAEEAA----------------------LKQKEAAEMELGNQRKMAEETAKQKLAAEQELI 1764
Cdd:TIGR02169 523 VHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavakeaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1765 RLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE-----LEEELIK---------VRKEMEILLQQKSKAEKE 1825
Cdd:TIGR02169 600 GFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKyrmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1826 TMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE----EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlK 1897
Cdd:TIGR02169 678 RLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkigEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---I 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1898 TEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHI 1977
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1978 LKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEKFRKLALEEEkkrkeaeakVKQIQAAEEEAARQHKAAQE 2057
Cdd:TIGR02169 827 EKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLNGKKEELEEE---------LEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2058 EVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL------------------VQQNKDSMAQD--- 2116
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledVQAELQRVEEEira 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1207141751 2117 ------KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2155
Cdd:TIGR02169 970 lepvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3430-3468 |
7.31e-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: 7.31e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 3430 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPEVHEKL 3468
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4006-4044 |
7.52e-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: 7.52e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 4006 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEFKDKL 4044
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1414-1930 |
7.71e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1414 AEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQelktLSEQEIKAKSQQVEE 1493
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEAG----LDDADAEAVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1494 ALLSRTRIEEEIHIIRLQLETTmkqKNTAETellqLRAKAVDADKLRNAAQEEAEKLRKQV--AEETQKKRKAE-EELKR 1570
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAH---NEEAES----LREDADDLEERAEELREEAAELESELeeAREAVEDRREEiEELEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1571 KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEES-----LK 1645
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSphvetIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1646 NEQVMVIQLQEEAEHLKKQQAEADKAREQA------EKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakr 1719
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRETIE------------------ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1720 eakkrAKAEEAALKQKEAAEMELGNQRKmAEETAKQKLAAEQELIRLRAdfehAEQQRTVLDDELQRLkNDVNSAVKQKK 1799
Cdd:PRK02224 534 -----EKRERAEELRERAAELEAEAEEK-REAAAEAEEEAEEAREEVAE----LNSKLAELKERIESL-ERIRTLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1800 ELEEELIKVRKemeillQQKSKAEKEtmsntEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARqraea 1879
Cdd:PRK02224 603 DAEDEIERLRE------KREALAELN-----DERRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQ----- 664
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 1880 ekiLKEKLTAINEA-TRLKTE---AEIALKEKEAENDRLKRKAEEEGYQRKVLED 1930
Cdd:PRK02224 665 ---VEEKLDELREErDDLQAEigaVENELEELEELRERREALENRVEALEALYDE 716
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4352-4390 |
1.07e-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: 1.07e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 4352 LLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMVDRI 4390
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
75-170 |
1.11e-11 |
|
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: 64.54 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 75 EAQRHITDLYEDLRDGHNLISLLEVLSGEtlpreRDVVRNSRLPrEKGRMRfhKLQNVQIALDFLKHRQV----KLVNIR 150
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGD-----WSLLSKLRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGIT 92
|
90 100
....*....|....*....|
gi 1207141751 151 NDDIADGNPKLTLGLIWTII 170
Cdd:cd21223 93 AKDIVDGHREKTLALLWRII 112
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
51-167 |
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 1207141751 51 ERDRvQKKTFTKWVNKHLVkhwkaeaQRHITDLYEDLRDGhnLIsLLEVLSGeTLPRERDVVRNSRLPREKGRMRFHKLQ 130
Cdd:cd21300 4 EGER-EARVFTLWLNSLDV-------EPAVNDLFEDLRDG--LI-LLQAYDK-VIPGSVNWKKVNKAPASAEISRFKAVE 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141751 131 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIW 167
Cdd:cd21300 72 NTNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1729-2635 |
1.26e-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: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1729 EAALKQKEAAEMELGNQRKMAEETAKQklaaeqeLIRLRADFEHAEQQRTVLDD----ELQRLKNDVNSAVKQKKELEEE 1804
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1805 LIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEatklrsvaEEAKKQRQIAEEEAarQRAEAEKILK 1884
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1885 EKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQ---AIEEKIGQLKKSSDTELDRQKKIV 1961
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeleDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1962 EETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLaleeekkrkeaEAKVKQI 2041
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-----------EWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2042 QAAEEEAARQHKAAQEEVGRLMKlaEEAKKQKEIAEKEAEKQVIlvqEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKE 2120
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEK--ELSKLQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlGSVGE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2121 EFEKAKKLAQEAEKA----KDNAEKEAALLHKKAEEAERQKKAaeaeaakqakaqedaeKLRKEAEKEASRRAEAEAAAL 2196
Cdd:TIGR02169 536 RYATAIEVAAGNRLNnvvvEDDAVAKEAIELLKRRKAGRATFL----------------PLNKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2197 KLKQEADSEMAKYKKlAEKTLKQKSSVEEELVKVKVQLDETdkQKSVLDVEL-----------KRLKQEVSDAIKQKAQV 2265
Cdd:TIGR02169 600 GFAVDLVEFDPKYEP-AFKYVFGDTLVVEDIEAARRLMGKY--RMVTLEGELfeksgamtggsRAPRGGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2266 E---DELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnmkklaeeaarlnieaqeaarlRQIAESDLAK 2342
Cdd:TIGR02169 677 QrlrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE----------------------IEQLEQEEEK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2343 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLD----QETEGFQKSLEAERKRQLEIT 2418
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2419 AEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvqrlqskQEADGLHKAIADLEKEK 2498
Cdd:TIGR02169 815 REIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-------EELEELEAALRDLESRL 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2499 EKLKKEAADLQKQSKEMANVQQEQ-LQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERqr 2577
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELeAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR-- 962
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2578 klMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2635
Cdd:TIGR02169 963 --VEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
190-289 |
1.32e-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: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 190 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN---LENLEQAFSIAER-DLGVTRLL 265
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1207141751 266 DPEDVdVPHPDEKSIITYVSSMYD 289
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1952-2666 |
1.40e-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: 71.54 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1952 TELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS-GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLA--LEEE 2028
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTqkREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2029 KKRKEAEAKVKQIQAAEEEAARQ---HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL--VQEAAQKCSAAEQKAQN 2103
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQeavLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHteLQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2104 VLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA---KDNAEKEAALLHK-KAEEAERQKKAAEAEAAKQAKAQEDAEKLRK 2179
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2180 EAEKEASRRAEAEAAALKLKQEADSEMAKYKKLA-EKTLKQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLKQEV 2255
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREqqlQTKEQIHLQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2256 SDAIKQKAQVEDELSKVKIQMEdLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQi 2335
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2336 AESDLAKQRElaekmleekkqaiqeaaKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrldqetegfqKSLEAERKRQL 2415
Cdd:TIGR00618 571 SFSILTQCDN-----------------RSKEDIPNLQNITVRLQDLTEKLSEAED--------------MLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2416 EITAEAEKLKVKVTQlsdaQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLE 2495
Cdd:TIGR00618 620 KLQPEQDLQDVRLHL----QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2496 KEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLlkkekaieEEKKKLEKQFEDEVKKAEALKAEQER 2575
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL--------NQSLKELMHQARTVLKARTEAHFNNN 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2576 QRKLMEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2654
Cdd:TIGR00618 768 EEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
730
....*....|..
gi 1207141751 2655 QTDKVPEEELVQ 2666
Cdd:TIGR00618 848 THQLLKYEECSK 859
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2057-2671 |
1.47e-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: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2057 EEVGRLMKLAEEAKKQKEIAEKEAEKQV----ILVQEAAQKCSAAEQKAQnvlVQQNKDSMAQDKLKEEFEKAKKLAQEA 2132
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTlrsqLLTLCTPCMPDTYHERKQ---VLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2133 EKAKDNAEKEAALLHKKAEEAE-RQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkQEADSEMAKYKK 2211
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-QSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2212 LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQevsdaikqKAQVEDELSKVKIQMEDLLKLKLKIEKENQ 2291
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI--------SCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2292 ELMKKDKDNTKKLLEEEAENmkklAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQaIQEAAKLKAEAEKL 2371
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFR----DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2372 QKQKDQAQVEAQK--LLEAKKEMQQRLDQETEGFQKSLEAERKRQLEitaeAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2449
Cdd:TIGR00618 476 QTKEQIHLQETRKkaVVLARLLELQEEPCPLCGSCIHPNPARQDIDN----PGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2450 DEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTI 2529
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2530 LQQSFFAEKETLLKKEKAIEEEKKKLEKQFED--EVKKAEALKAEQeRQRKLMEEERKKLQSAMDAAIKKQK-----EAE 2602
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHalSIRVLPKELLAS-RQLALQKMQSEKEQLTYWKEMLAQCqtllrELE 710
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 2603 EEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVE 2671
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 ... |
1653-2637 |
1.78e-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: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1653 QLQEEAEHLKKQQAEADKArEQAEKELETWRQKANE---ALRLRLQAEEE----ANKKTAAQEEAEKQKEEAKREAKKRA 1725
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEeknALQEQLQAETElcaeAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1726 KAEE------AALKQKEAAEMELGNQRKMAEETAKQKL-----AAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1794
Cdd:pfam01576 85 EEEEersqqlQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1795 VKQKKELEEE---LIKVRKEMEIL---LQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatklrsvaEEAKKQRQIA 1868
Cdd:pfam01576 165 TSNLAEEEEKaksLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQE------------QIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1869 EEEAARQRAEAEkiLKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRkvleDQAAQHKQAIEEKIGQLKK 1948
Cdd:pfam01576 233 ELRAQLAKKEEE--LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1949 SSDTELDRQKkiVEETLKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIA-DETQKSKAKAEEEAEKFRKLALEE 2027
Cdd:pfam01576 307 ELEDTLDTTA--AQQELRSKR--EQEVTELKKALEEETRSHEAQLQEMRQKHTQAlEELTEQLEQAKRNKANLEKAKQAL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2028 EKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQK-EIAEK----------------EAEKQVILVQEA 2090
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRaELAEKlsklqselesvssllnEAEGKNIKLSKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2091 AQKCSAAEQKAQNVLVQQNKDSMAQD----KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEA----ERQKKAAEA 2162
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMkkklEEDAGTLEA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2163 EAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEAD-------------SEMAKYKKLAEKTLKQKSSVEEELVK 2229
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdllvdldhqrqlvSNLEKKQKKFDQMLAEEKAISARYAE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2230 VKVQLDETDKQKSVLDVELKRlkqEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKkdkdnTKKLLEEEA 2309
Cdd:pfam01576 623 ERDRAEAEAREKETRALSLAR---ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER-----SKRALEQQV 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2310 ENMKKLAEEA---------ARL----NIEAQEAARLRQIAESD---------LAKQ-RELAEKMLEEKKQAIQEAA---- 2362
Cdd:pfam01576 695 EEMKTQLEELedelqatedAKLrlevNMQALKAQFERDLQARDeqgeekrrqLVKQvRELEAELEDERKQRAQAVAakkk 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2363 ------KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-------------ETEGFQKSLEAERKRQLEITAEAEK 2423
Cdd:pfam01576 775 leldlkELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEarasrdeilaqskESEKKLKNLEAELLQLQEDLAASER 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2424 LKVKVTQLSDA-QSKAEEEAKKFKKQADE---IKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKE 2499
Cdd:pfam01576 855 ARRQAQQERDElADEIASGASGKSALQDEkrrLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQ 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2500 KLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSF------FAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQ 2573
Cdd:pfam01576 935 KSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIaaleakIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE 1014
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 2574 ERQRKLMEEERKKLQSAMDAAIKKQKEAEEE---MNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2637
Cdd:pfam01576 1015 RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEasrANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3506-3542 |
2.36e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.36e-11
10 20 30
....*....|....*....|....*....|....*..
gi 1207141751 3506 LLDAQVATGGIIDPVNSHRLPNDVAIERGYFSKQLAK 3542
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1473-1786 |
2.76e-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: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1473 LQELKTLSEQEIKAKSQQVEEallSRTRIEEEIHIIRLQLETTMKQKNTAETELLQlRAKAVDADKLRNAAQEEAEKLRK 1552
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ---ERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1553 QvaeetQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK-----LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1627
Cdd:pfam17380 354 R-----QEERKRELERIRQEEIAMEISRMRELERLQMERQQknervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1628 QLESKQVALTaRLEESLKNEQVMV----IQLQEEAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANK- 1702
Cdd:pfam17380 429 QEEARQREVR-RLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKILEKELEERKq 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1703 -------KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgnQRKMAEETAKqklaAEQELIRLRADFEHAEQ 1775
Cdd:pfam17380 507 amieeerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE-----RRRIQEQMRK----ATEERSRLEAMEREREM 577
|
330
....*....|.
gi 1207141751 1776 QRTVLDDELQR 1786
Cdd:pfam17380 578 MRQIVESEKAR 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1155-1946 |
3.08e-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: 70.48 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1155 ILNKYENQLREVNKVPVNEKEIEASQTQLQKLRSEAEgkqatfDRLEEELQRATEVNKRMSQLHSERDVElehyrqlvgn 1234
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE------KRLEEIEQLLEELNKKIKDLGEEEQLR---------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1235 LRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiADAKQRQDKLhavpiggskglqeqltQEKKLLEEIEKNKD 1314
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELED------------AEERLAKLEA----------------EIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1315 KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASddiiqeyvtLRTRYSELmtlsSQYIKFIIETQRR 1394
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------YREKLEKL----KREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1395 LQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEvskrqdvavdsEKQKHNIQRELQ 1474
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-----------EQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1475 ELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQ---LETTMKQKNTAETELLQLRAKAVDAdkLRNAAqeeAEKLR 1551
Cdd:TIGR02169 480 RV----EKELSKLQRELAEAEAQARASEERVRGGRAVeevLKASIQGVHGTVAQLGSVGERYATA--IEVAA---GNRLN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1552 KQVAEETQKKRKAEEELKRK-----------------SEAEKDAAKEKKKALEDLEKFKLQ-----------------AE 1597
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRkagratflplnkmrderRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvedIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1598 EAERHLKQAelekqRQIQVVEEVAKKT--------AATQLESKQVALTARLEESLKNEQVMVIQ---LQEEAEHLKKQQA 1666
Cdd:TIGR02169 631 AARRLMGKY-----RMVTLEGELFEKSgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1667 EADKAREQAEKELETWRQKANealrlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAE-EAALKQKEAAEMELgnq 1745
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIE-----QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKElEARIEELEEDLHKL--- 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1746 rKMAEETAKQKLaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSaVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1825
Cdd:TIGR02169 778 -EEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1826 TMSNTEKSKQLLESEAAK----MRELAEEATKLRSVAEEAKKQR---QIAEEEAARQRAEAEKILKEkltaineatrLKT 1898
Cdd:TIGR02169 855 EIENLNGKKEELEEELEEleaaLRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSE----------LKA 924
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1207141751 1899 EAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKIGQL 1946
Cdd:TIGR02169 925 KLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAE-LQRVEEEIRAL 970
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1414-1871 |
6.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1414 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAvDSEKQKHNIQRELQELKtlSEQEIKAKSQQVEE 1493
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELR--EELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1494 ALLSRTRIEEEIHIIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKse 1573
Cdd:COG4717 130 LYQELEALEAELAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1574 aEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQiQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVM--- 1650
Cdd:COG4717 201 -LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1651 ------VIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKkTAAQEEAEKQKEEAKREAKKR 1724
Cdd:COG4717 279 lflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-EELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1725 AKAEEAALKQKEAAEMELGNQRKMA-EETAKQKLAAEQELIRLRADFEHAEQQ----------------RTVLDDELQRL 1787
Cdd:COG4717 358 ELEEELQLEELEQEIAALLAEAGVEdEEELRAALEQAEEYQELKEELEELEEQleellgeleellealdEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1788 KNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI 1867
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1207141751 1868 AEEE 1871
Cdd:COG4717 509 YREE 512
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1440-1760 |
8.79e-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: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1440 EANELKTKMKDEV-----SKRQDVAVDSEKQKH----NIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRL 1510
Cdd:NF033838 51 SGNESQKEHAKEVeshleKILSEIQKSLDKRKHtqnvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1511 QLETTMKQKNTAET----ELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakeKKKAL 1586
Cdd:NF033838 131 KKDTLEPGKKVAEAtkkvEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE----------EAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1587 EDLEKFKlqAEEAERHLKQAELEKQRQIQV----VEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1662
Cdd:NF033838 201 RDEEKIK--QAKAKVESKKAEATRLEKIKTdrekAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1663 KQQ-------------------------AEADKAREQAEKELETWRQK------ANEALRLRLQ-AEEEAN-KKTAAQEE 1709
Cdd:NF033838 279 KENdakssdssvgeetlpspslkpekkvAEAEKKVEEAKKKAKDQKEEdrrnypTNTYKTLELEiAESDVKvKEAELELV 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 1710 AEKQKEEAKREAKKRAKAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAE 1760
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVES-KKAEATRLEkIKTDRKKAEEEAKRKAAEE 409
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
190-288 |
8.88e-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: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 190 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 269
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1207141751 270 VdVPHPDEKSIITYVSSMY 288
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1269-1942 |
1.17e-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: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1269 WLIRWIADAKQRQDKLH---AVPIGGSKGLQE-QLTQEK---KLLEEIEKNKDKV--------------EDCQKFAKGYI 1327
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIkennatrhlcnllkETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1328 DAIKDYELQLVTYKAL---VEPIASPLKKAKMEsASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRR-----LQDEE 1399
Cdd:pfam05483 173 KYEYEREETRQVYMDLnnnIEKMILAFEELRVQ-AENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQvslllIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1400 KAAEKLKEEERKKMAEMQA-ELEKQKQLAETHAKAIAKAE----QEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQ 1474
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKAnQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1475 ELKTLSEQEIKAKSQQ---VEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1551
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1552 KQVAE------ETQKKRKAEEELKRKSEAEKdaakekkkaledlekFKLQAEEAERHLKQAEL-----EKQRQIQVVEEV 1620
Cdd:pfam05483 412 KILAEdeklldEKKQFEKIAEELKGKEQELI---------------FLLQAREKEIHDLEIQLtaiktSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1621 akKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA 1700
Cdd:pfam05483 477 --KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1701 NKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVL 1780
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1781 DDELQRLKNDVNSAvkqKKELEEELIKVRKEMEIllqqKSKAEKETMSNTEKSKQlleseaakmreLAEEATKLRSVAEE 1860
Cdd:pfam05483 635 EIKVNKLELELASA---KQKFEEIIDNYQKEIED----KKISEEKLLEEVEKAKA-----------IADEAVKLQKEIDK 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1861 aKKQRQIAEEEA--ARQRAEAEKILKEKLTAI-------NEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ 1931
Cdd:pfam05483 697 -RCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
730
....*....|.
gi 1207141751 1932 AAQHKQAIEEK 1942
Cdd:pfam05483 776 AKENTAILKDK 786
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2044-2401 |
1.18e-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: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2044 AEEEAARQHKAAQEEVGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL----VQQNKDSMAQDKL 2118
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEArireLEEDIKTLTQRVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2119 KEEfekakklaQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKL 2198
Cdd:pfam07888 147 ERE--------TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2199 KQEADSEMAKYKKLaEKTLKQKSSVEEELvkvkvqldETDKQKSVLdvelkrLKQEVSDAIKQKAQVEDELSKVKI---Q 2275
Cdd:pfam07888 219 TQKLTTAHRKEAEN-EALLEELRSLQERL--------NASERKVEG------LGEELSSMAAQRDRTQAELHQARLqaaQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2276 MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKK 2355
Cdd:pfam07888 284 LTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESR 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1207141751 2356 QAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETE 2401
Cdd:pfam07888 364 RELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3839-3877 |
1.29e-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: 1.29e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 3839 LLEAQVATGGLMDPEYYFRLPIDIAMQRGYMNKETSERI 3877
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1013-1800 |
1.87e-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: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1013 EQEPALIQKDSTSGEQDESVCKSyitQIKDLRLRLEGCESRTVN----RLRQMVDKEPL-KACTQRATEQKKVQTELEGI 1087
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLER---SIAEKERELEDAEERLAKleaeIDKLLAEIEELeREIEEERKRRDKLTEEYAEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1088 KKDLDKVVEKSEAVLATSQQSSSAPV-LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ----GAEDILNKYENQ 1162
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1163 LREVN-KVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELqraTEVNKRMSQLHSERDV---ELEHYRQLVGNLRER 1238
Cdd:TIGR02169 443 KEDKAlEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL---SKLQRELAEAEAQARAseeRVRGGRAVEEVLKAS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1239 WQAVFAQIelrqreldllnRQMQAYRESYDWLIRWIADAKqrqdkLHAVPIGGSKGLQE--QLTQEKKL--LEEIEKNKD 1314
Cdd:TIGR02169 520 IQGVHGTV-----------AQLGSVGERYATAIEVAAGNR-----LNNVVVEDDAVAKEaiELLKRRKAgrATFLPLNKM 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1315 KVEDCQKfAKGYIDAIKDYELQLVTYKALVEPI-----ASPLKKAKMESASDDIIQ-EYVTLRTRYSE---LMTLSSQYI 1385
Cdd:TIGR02169 584 RDERRDL-SILSEDGVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAP 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1386 KFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQ 1465
Cdd:TIGR02169 663 RGGILFSRSEPAEL--------------QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1466 KHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdadklrnaaQE 1545
Cdd:TIGR02169 729 EQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---------QA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1546 EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhlKQAELEKQrqiqvveevaKKTA 1625
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK--EIENLNGK----------KEEL 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1626 ATQLESKQVALtARLEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANK--- 1702
Cdd:TIGR02169 867 EEELEELEAAL-RDLESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSE-LKAKLEALEEELSeie 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1703 KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMelgnqrkmaeetakqklAAEQELIRLRADFEHAEQQRTVLDD 1782
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM-----------------LAIQEYEEVLKRLDELKEKRAKLEE 1000
|
810
....*....|....*...
gi 1207141751 1783 ELQRLKNDVNSAVKQKKE 1800
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKRE 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2371-2639 |
2.27e-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: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2371 LQKQKDQAQVEAQKLLEakKEMQQRLDQETEgfQKSLEAERKRQLEitaEAEKLKvKVTQLSDAQSKAEEEAKKFKKQAD 2450
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE--KMEQERLRQEKE--EKAREVERRRKLE---EAEKAR-QAEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2451 EIKIRLQETEKHTS-----------EKHTVVEKLEVQRLQS----KQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEM 2515
Cdd:pfam17380 350 LERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKnervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2516 ANVQQEQLQQektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQ-------RKLMEEERKKLQ 2588
Cdd:pfam17380 430 EEARQREVRR----LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraeeqrRKILEKELEERK 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 2589 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2639
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1385-2099 |
2.95e-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: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1385 IKFIIETQRRLQDEE-------------------------KAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQ 1439
Cdd:TIGR02169 193 IDEKRQQLERLRRERekaeryqallkekreyegyellkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1440 EANELKTKMKDEVSKRQ--------DVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQ 1511
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAE--------IDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1512 LETTMKQKNTAETELLQLRAKavdADKLRNAAQEEAEKLRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEK 1591
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEE---LEDLRAELEEVDKEFAETR-DELKDYREKLEKLKREINELKR------------EL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1592 FKLQAEEAERHLKQAELEKqrQIQVVEEvAKKTAATQLESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1671
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNA--AIAGIEA-KINELEEEKEDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1672 REQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREakkRAKAEEAA----------------- 1731
Cdd:TIGR02169 485 LSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavak 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1732 -----LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE- 1800
Cdd:TIGR02169 562 eaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKy 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1801 ----LEEELIK---------VRKEMEILLQQKSKAEKETMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE---- 1859
Cdd:TIGR02169 640 rmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkig 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1860 EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAI 1939
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1940 EEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHILKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEK 2019
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTLEKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2020 FRKLALeeekkrkeaEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQ 2099
Cdd:TIGR02169 861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1526-1956 |
3.08e-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: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1526 LLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELK------RKSEAEKDAAKEKKKALEDLEKFKLQAEE- 1598
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlNLVQTALRQQEKIERYQEDLEELTERLEEq 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1599 ----AERHLKQAELEKQRQiQVVEEVakKTAATQLESKQVALTARLEESLKNEQVmvIQLQEEAEHLkkqQAEADKAREQ 1674
Cdd:COG3096 367 eevvEEAAEQLAEAEARLE-AAEEEV--DSLKSQLADYQQALDVQQTRAIQYQQA--VQALEKARAL---CGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1675 AEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEETAK 1754
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLS----------------VADAARRQFEKAYELVCKIAGEVE----RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1755 qklaaeqELIRLRADFEHAEQQRTVLDDELQRLkndvnsavkqkkeleEELIKVRKEMEILLQQKSKAEKETMSNTEKSK 1834
Cdd:COG3096 499 -------ELLRRYRSQQALAQRLQQLRAQLAEL---------------EQRLRQQQNAERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1835 QLLESEAAKMRELAEEAtklRSVAEEAKKQRQiAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 1914
Cdd:COG3096 557 ELLAELEAQLEELEEQA---AEAVEQRSELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAM 632
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1207141751 1915 KRKAEEEgYQRKVLEDQAAQHKQAIEEKIGQLKK---SSDTELDR 1956
Cdd:COG3096 633 QQLLERE-REATVERDELAARKQALESQIERLSQpggAEDPRLLA 676
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2099-2482 |
5.39e-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: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2099 QKAQNVLVQQNK-DSMAQDKLKEEFEKakkLAQEAEKAKDNAEKEAAllhkKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2177
Cdd:pfam17380 281 QKAVSERQQQEKfEKMEQERLRQEKEE---KAREVERRRKLEEAEKA----RQAEMDRQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2178 RKEAEKEASRRAEaeaaalklKQEADSEMAKYKKLAektlkqkssveeelvkvKVQLDETDKQKsvldvelkRLKQEVSD 2257
Cdd:pfam17380 354 RQEERKRELERIR--------QEEIAMEISRMRELE-----------------RLQMERQQKNE--------RVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2258 AIKQKAQVEDELSKVKIQMEDllklklkiekenQELMKKDKDNTKKlleeeaENMKKLAEEAARlnieaqEAARLRQiae 2337
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVE------------MEQIRAEQEEARQ------REVRRLEEERAR------EMERVRL--- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2338 SDLAKQRElaekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEakKEMQQRLdqetegfQKSLEAERKRQLeI 2417
Cdd:pfam17380 454 EEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE--KELEERK-------QAMIEEERKRKL-L 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2418 TAEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2482
Cdd:pfam17380 519 EKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1543-1762 |
6.12e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1543 AQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledLEKFKLQA-EEAERHLKQAELEKQRQIQVVEEVA 1621
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQ-----------------LEKERLAAqEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1622 KKTAATQLESKQVAltARLEESLKneqvmviqlQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRlRLQAEEEA 1700
Cdd:PRK09510 140 KAAAAAKAKAEAEA--KRAAAAAK---------KAAAEAKKKAEAEAAkKAAAEAKKKAEAEAAAKAAAEA-KKKAEAEA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 1701 NKKTaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1762
Cdd:PRK09510 208 KKKA-------------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1590-1938 |
7.00e-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: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1590 EKFKLQAEEAERHLK------QAELEKQRQIQVVE----------------EVAKKTAATQLESK-QVALTARLEESLKN 1646
Cdd:NF033838 54 ESQKEHAKEVESHLEkilseiQKSLDKRKHTQNVAlnkklsdikteylyelNVLKEKSEAELTSKtKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1647 eqvmVIQLQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRA 1725
Cdd:NF033838 134 ----TLEPGKKVAEATKKVEEAEkKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1726 KAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAEQE--LIRLRADFEHAEQQRTVLDDELQRL------KNDVNS--- 1793
Cdd:NF033838 210 KAKVES-KKAEATRLEkIKTDREKAEEEAKRRADAKLKeaVEKNVATSEQDKPKRRAKRGVLGEPatpdkkENDAKSsds 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1794 ----------AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSkqlLESEAAKMRELAEEAtKLRSVAEEAKK 1863
Cdd:NF033838 289 svgeetlpspSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKT---LELEIAESDVKVKEA-ELELVKEEAKE 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 1864 QRQIAEEEAARQRAEAEKIlkekltainEATRL-KTEAEIALKEKEAendrlKRKAEEEgyqRKVLEDQAAQHKQA 1938
Cdd:NF033838 365 PRNEEKIKQAKAKVESKKA---------EATRLeKIKTDRKKAEEEA-----KRKAAEE---DKVKEKPAEQPQPA 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2211-2642 |
7.73e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2211 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkieken 2290
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2291 qelmkkdkdntkklLEEEAENMKKL-AEEAARLNIEAQEAARLRQIAEsdlaKQRELAEKMLEEKKQAIQEAAKLKAEAE 2369
Cdd:COG4717 141 --------------LAELPERLEELeERLEELRELEEELEELEAELAE----LQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2370 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQ-SKAEEEAKKFKKQ 2448
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLlSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2449 ADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2528
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2529 ILQQSFFAEKETLLKKEKAIEEEK-KKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ-KEAEEEMN 2606
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELE 442
|
410 420 430
....*....|....*....|....*....|....*...
gi 1207141751 2607 GKQKEMQDL--EKKRIEQEKLLAEENKNLREKLQQLQS 2642
Cdd:COG4717 443 ELEEELEELreELAELEAELEQLEEDGELAELLQELEE 480
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1590-2364 |
7.89e-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: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1590 EKFKLQAEEAERHLKQAELekqrqIQVVEEVAKKTAATQLESKQVaLTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAD 1669
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQA-----IAGIMKIRPEFTKLQQEFNTL-ESAELRLSHLHFGYKSDETLIASRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1670 KAREQAEKELEtWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA---KKRAKAEEAALKQKEAAEME----- 1741
Cdd:pfam12128 288 LNQLLRTLDDQ-WKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLDAdieTAAADQEQLPSWQSELENLEerlka 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1742 -LGNQRKMAEETAKQKLAAEQELIR--------LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKK---ELEEELIKVR 1809
Cdd:pfam12128 366 lTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELREQLEAGKlefNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1810 KEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 1889
Cdd:pfam12128 446 LGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1890 INEATRLKTEAEIALKEkeaendrlkrkaeeegyqrkVLEDQAAQHKQAIEEKIgqlkkssDTELDRQKKIVEETLKQRK 1969
Cdd:pfam12128 522 LDELELQLFPQAGTLLH--------------------FLRKEAPDWEQSIGKVI-------SPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1970 VVEEEIHILKLNFEKAS-----SGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAA 2044
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG--------------ELEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2045 EEEAARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcSAAEQKAQNVLVQQNKD----SMAQDKL 2118
Cdd:pfam12128 641 ETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQL-KQLDKKHQAWLEEQKEQkreaRTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2119 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER------------QKKAAEAEAAKQAKAQEDAEKLRKEA-EKEA 2185
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYkrdlaslgvdpdVIAKLKREIRTLERKIERIAVRRQEVlRYFD 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2186 SRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQK--- 2262
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKeda 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2263 --AQVEDELSKVKIQMED-LLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNieaqeAARLRQIAESD 2339
Cdd:pfam12128 880 nsEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQN-----DKGIRLLDYRK 954
|
810 820
....*....|....*....|....*.
gi 1207141751 2340 LAKQRE-LAEKMLEEKKQAIQEAAKL 2364
Cdd:pfam12128 955 LVPYLEqWFDVRVPQSIMVLREQVSI 980
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1542-1975 |
8.72e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1542 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1621
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1622 KKTAATQLESKQVALTARLEESLKNEqvmviqlQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEAN 1701
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEK-------AEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-IEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1702 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK--------QKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHA 1773
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAkkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1774 EQQRTVLDDELQRLKNDVNSAVKQKKELEE------------ELIKVRKEMEILLQQKSKAEKEtMSNTEKsKQLLESEA 1841
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTEehrkelleeytaELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1842 AKMRELAEEATKLRSV--------AEEAKKQRQIAEEEAARQRAEAeKILKEKLTAINEATRLKTEAEIALKEKEAENDR 1913
Cdd:PRK03918 496 IKLKELAEQLKELEEKlkkynleeLEKKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 1914 LKRKAEEEGYqrKVLEDqaaqhkqaIEEKIGQLKKSSD--TELDRQKKIVEETLKQRKVVEEEI 1975
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 ... |
2294-2456 |
9.64e-10 |
|
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: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2294 MKKDKDNTKKLLEEEAENMKK--LAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKL 2371
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKqrAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2372 QKQKDQAQveAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT--AEAEKLKVKVTQlsdAQSKAEEEAKKFKKQA 2449
Cdd:TIGR02794 142 RKAKEEAA--KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEakAKAEEAKAKAEA---AKAKAAAEAAAKAEAE 216
|
....*..
gi 1207141751 2450 DEIKIRL 2456
Cdd:TIGR02794 217 AAAAAAA 223
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2852-2890 |
1.21e-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: 1.21e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 2852 LLDCQYATGGIIDPVNSHHVPVQLACTQGQLDEDLSKIL 2890
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1145-1870 |
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 1207141751 1145 VIRSTQGAEDILNKYENqLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQatfDRLEEELQRATEVNKRMSQLHSERDvE 1224
Cdd:PRK03918 150 VVRQILGLDDYENAYKN-LGEV------IKEIKRRIERLEKFIKRTENIE---ELIKEKEKELEEVLREINEISSELP-E 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1225 LEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYdwlirwiadakqrqdklhavpiggsKGLQEQLTQEKK 1304
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-------------------------RELEERIEELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1305 LLEEIEKNKDKVEDCQKFAKGYIDAIKDYElqlvtykalvepiasplkkaKMESASDDIIQEYVTLRTRYSELmtlssqy 1384
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYE--------------------EYLDELREIEKRLSRLEEEINGI------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1385 ikfiietQRRLQDEEKaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKdevskrqdvavdsek 1464
Cdd:PRK03918 327 -------EERIKELEE------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE--------------- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1465 qkhNIQRELQELKTLSEQEIKAKSQQVEEAllsRTRIEEEIHII---RLQLETTMKQKNTAETELLQLRAKAV------- 1534
Cdd:PRK03918 373 ---ELERLKKRLTGLTPEKLEKELEELEKA---KEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPvcgrelt 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1535 --DADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1612
Cdd:PRK03918 447 eeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-----LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1613 qiqvveevAKKTAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL 1692
Cdd:PRK03918 522 --------KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1693 RLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEH 1772
Cdd:PRK03918 593 RLKELEPFYNEYL--------------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1773 AEQQRtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlqqksKAEKETMSNTEKSKQLLESEAAKMRELAEEAT 1852
Cdd:PRK03918 659 EEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKELEKLEKALERVEELREKVK 731
|
730 740
....*....|....*....|
gi 1207141751 1853 KLRSVAEEA--KKQRQIAEE 1870
Cdd:PRK03918 732 KYKALLKERalSKVGEIASE 751
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1653-1980 |
1.43e-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: 64.37 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1653 QLQEEAEHLKKQ---QAEADKAREQAEK----ELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREaKKRA 1725
Cdd:pfam17380 288 QQQEKFEKMEQErlrQEKEEKAREVERRrkleEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQEERKRE-LERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1726 KAEEAALKQKEAAEME-LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK--KELE 1802
Cdd:pfam17380 366 RQEEIAMEISRMRELErLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRleEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1803 EELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEeaaRQRAEAEKI 1882
Cdd:pfam17380 446 REMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE---RKRKLLEKE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1883 LKEKLTAINEATRLKTEAEIALKEKEAENDR----LKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 1958
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEERRriqeQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
330 340
....*....|....*....|..
gi 1207141751 1959 KIVEETLKQRKVVEEEIHILKL 1980
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 ... |
955-1763 |
1.67e-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: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 955 KTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRSVEQEPALIQKDSTSGEQDESVCK 1034
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1035 SYITQIKDLRLRLEGCESRTVNRLRQMVDKEplkactqraTEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVL 1114
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKAE---------KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1115 RSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVpvNEKEIEASQTQLQKLRSEAEGKQ 1194
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK--EEKKEELEILEEEEESIELKQGK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1195 ATFDRLEEELQRATEVNKRMS------QLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAY----- 1263
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELElkksedLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggrii 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1264 RESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEE----------IEKNKDKVEDCQKFAKGYIDAIKDY 1333
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALtelplgarklRLLIPKLKLPLKSIAVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1334 EL---------QLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEK 1404
Cdd:pfam02463 606 AQldkatleadEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1405 LKEEERkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvAVDSEKQKHNIQRELQELKTLSEQEI 1484
Cdd:pfam02463 686 ESELAK---EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI--NEELKLLKQKIDEEEEEEEKSRLKKE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1485 KAKSQQVEEALLSRTRIEEEIHIIRLQLEttmKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKA 1564
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVE---EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1565 EEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESL 1644
Cdd:pfam02463 838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1645 KNEQVMV------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL------RLQAEEEANKKTAAQEEAEK 1712
Cdd:pfam02463 918 EIEERIKeeaeilLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEElgkvnlMAIEEFEEKEERYNKDELEK 997
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 1713 QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1763
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2200-2421 |
1.72e-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: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2200 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2279
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2280 LKLKLKIEKENQElmkkDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2359
Cdd:COG4942 117 GRQPPLALLLSPE----DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2360 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegfqksLEAERKRQLEITAEA 2421
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR--------LEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1500-1855 |
1.80e-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: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1500 RIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKL-------RNAAQEEAEKLRKQVAEETQKKRKAEEELKRKS 1572
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1573 EAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL-EKQRQIQVVEEVAkktaatqleSKQVALTARLEESLKNEQVMV 1651
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEV---------SRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1652 IQLQEEAEHLKKQQAEADKAREQAEKELetwrqkanEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAA 1731
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEI--------ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1732 LKQKEaaemelgNQRKMAEETAKQKLAaeqeliRLRADFEHAEQQRTVLDDELQRLKNDVNSA------VKQKKELEEEL 1805
Cdd:TIGR02169 901 LERKI-------EELEAQIEKKRKRLS------ELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvQAELQRVEEEI 967
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1806 IKVrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 1855
Cdd:TIGR02169 968 RAL-EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
188-285 |
2.23e-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: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90
....*....|....*....
gi 1207141751 267 PEDVDVPHPDEKSIITYVS 285
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLS 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4428-4466 |
2.27e-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: 2.27e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 4428 FLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTAQKL 4466
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
57-170 |
2.47e-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: 57.97 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 57 KKTFTKWVNKHL-----VKHWKAEAQRHItDLYEDLRDGHNLISLLEVLSGETLPrERdvvrnsRLPREKGRMRFHKLQN 131
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDGD-DLFEALRDGVLLCKLINKIVPGTID-ER------KLNKKKPKNIFEATEN 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141751 132 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 170
Cdd:cd21217 75 LNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2116-2635 |
2.82e-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: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2116 DKLKEEFEKAKKLAQEAEKAKD-------NAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRR 2188
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDkflteikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2189 AEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEE---ELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ- 2264
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQn 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2265 ------VEDELSKVKIQMEDLLKLKlkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQI--- 2335
Cdd:TIGR04523 280 nkkikeLEKQLNQLKSEISDLNNQK------EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltn 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2336 AESD-LAKQRELAEKmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQ 2414
Cdd:TIGR04523 354 SESEnSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQINDLE---SKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2415 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADL 2494
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2495 EKEKEklkkeaaDLQKQSKEMaNVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklekqfeDEVKKAEALKAE-Q 2573
Cdd:TIGR04523 509 EEKVK-------DLTKKISSL-KEKIEKLESEKKEKESKISDLEDELNKD----------------DFELKKENLEKEiD 564
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2574 ERQRKLmeeerKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2635
Cdd:TIGR04523 565 EKNKEI-----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1332-1979 |
3.22e-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: 63.59 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1332 DYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKE---E 1408
Cdd:pfam05483 38 DPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1409 ERKKMAEMQAELEKqkqlaethakaiakaeqeaneLKTKMKDEVSKRQDVAVDSEKQKHnIQRELQELKTLSEQEIKAKS 1488
Cdd:pfam05483 118 QRKAIQELQFENEK---------------------VSLKLEEEIQENKDLIKENNATRH-LCNLLKETCARSAEKTKKYE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1489 QQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETEL-LQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE 1567
Cdd:pfam05483 176 YEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1568 LKRKSEAEKDAAKEKKKALedlEKFKLQAEeaerHLKQAELEKQRQIQVVEEVAKKTaatqleSKQVALTARLEESLKNE 1647
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLE---EKTKLQDE----NLKELIEKKDHLTKELEDIKMSL------QRSMSTQKALEEDLQIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1648 QVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL---RLQAEEEANKKTAAQEEAEKQKEEAKREAKKR 1724
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1725 AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRL----RADFEHAEQQRTVLD-------DELQRLKNDVNS 1793
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKtseehylKEVEDLKTELEK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1794 AVKQKKELEEELIKVRKEMEILLQQKS------KAEKETMSNTEKSKQ--------LLESEAAKMRELAEEATKLRSVAE 1859
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASdmtlelKKHQEDIINCKKQEErmlkqienLEEKEMNLRDELESVREEFIQKGD 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1860 EAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKV-------LE 1929
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGSAENKQLNAyeikvnkLE 642
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1930 DQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 1979
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
51-175 |
4.85e-09 |
|
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: 57.70 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 51 ERDRVQKKTFTKWVNKHLVkhwkaeaQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDVVRNSRLPREKGRMRfhKLQ 130
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207141751 131 NVQIALDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 175
Cdd:cd21331 86 NCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1590-2257 |
6.35e-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: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1590 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtaRLEESLKNEQVMVIQ----------LQE--- 1656
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSL--KLEEEIQENKDLIKEnnatrhlcnlLKEtca 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1657 -EAEHLKKQQAEADKARE-------------QAEKELETWRQKANEALRLRLQA--------EEEANKKTAAQEEAEKQK 1714
Cdd:pfam05483 166 rSAEKTKKYEYEREETRQvymdlnnniekmiLAFEELRVQAENARLEMHFKLKEdhekiqhlEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1715 EEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ----RTVLDDELQRLKND 1790
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1791 VNSAVKQKKELEEELIKVRKEMEIL----------LQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLrsvaee 1860
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAHSFVvtefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKF------ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1861 aKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIAL----KEKEAENDRLK---RKAEEEGYQRKVLEDQA 1932
Cdd:pfam05483 400 -KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFllqaREKEIHDLEIQltaIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1933 AQHKQAIE---------------EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELK 1997
Cdd:pfam05483 479 ELEKEKLKnieltahcdklllenKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1998 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2077
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2078 KEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAllHKKAEEAERQk 2157
Cdd:pfam05483 636 IKVNKLELELASAKQK---FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ--HKIAEMVALM- 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2158 kaaeaeaakqakaqedaEKLRKEAEkeasrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDET 2237
Cdd:pfam05483 710 -----------------EKHKHQYD--------------KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSL 758
|
730 740
....*....|....*....|
gi 1207141751 2238 DKQKSVLDVELKRLKQEVSD 2257
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKE 778
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1512-1756 |
6.37e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.40 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1512 LETTMKQKNTAETELLQLRAKAVDADKlrnaAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlEK 1591
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAK----KEQERQKKLEQQAEEAEKQRAAEQARQKE------------------LE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1592 FKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNeqvmviqlQEEAEHLKKQQAEADKA 1671
Cdd:TIGR02794 96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--------QAEEEAKAKAAAEAKKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1672 REQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAalkQKEAAEMELGNQRKMAEE 1751
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA---ERKADEAELGDIFGLASG 243
|
....*
gi 1207141751 1752 TAKQK 1756
Cdd:TIGR02794 244 SNAEK 248
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4350-4387 |
7.32e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 7.32e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1207141751 4350 QRLLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMV 4387
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1417-1958 |
7.73e-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: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1417 QAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAL 1495
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1496 LsRTRIEEEIHIIRL-QLETTMKQKNTAETELLQLRAKavdaDKLRNAAQEEAEKLRKQVaeetqkkrkaeEELKRksea 1574
Cdd:pfam12128 433 L-EFNEEEYRLKSRLgELKLRLNQATATPELLLQLENF----DERIERAREEQEAANAEV-----------ERLQS---- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1575 ekdaakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQiqvveevakKTAATQLESKQVALTARLEESLKNEqvmviqL 1654
Cdd:pfam12128 493 -------------ELRQARKRRDQASEALRQASRRLEER---------QSALDELELQLFPQAGTLLHFLRKE------A 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1655 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEAL---RLRLQAEEeankktaaQEEAEKQKEEAKREAKKRAKAEEAA 1731
Cdd:pfam12128 545 PDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvKLDLKRID--------VPEWAASEEELRERLDKAEEALQSA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1732 LKQKEAAEMELGNQRKMAEEtakqklaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRK 1810
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEK-------ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1811 EMEIL---LQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklRSVAEEAKKQRQIAEEEAARQRAEA-EKILKEK 1886
Cdd:pfam12128 690 QLKQLdkkHQAWLEEQKEQKREARTEKQ------AYWQVVEGA----LDAQLALLKAAIAARRSGAKAELKAlETWYKRD 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1887 LTA--INEATRLKTEAEIALKEKEAENDRLKRKA---------EEEGYQRKVLEDQAAQHKQAIEEKIGQL-KKSSDTEL 1954
Cdd:pfam12128 760 LASlgVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKL 839
|
....
gi 1207141751 1955 DRQK 1958
Cdd:pfam12128 840 RRAK 843
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2224-2451 |
8.45e-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: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2224 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekeNQELmkkdkdntKK 2303
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----------QAEI--------AE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2304 LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES----DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQ 2379
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2380 VEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2451
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1039-1769 |
1.07e-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: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1039 QIKDLRLRLEGCESR------TVNRLRQMVDKEPLKACTQRATEQKKVQTELEGIKKDLDKVvEKSEAVLATSQQSSSAP 1112
Cdd:TIGR02169 245 QLASLEEELEKLTEEiselekRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL-ERSIAEKERELEDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1113 V--LRSEIDITQKKMEhvyGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNK-VPVNEKEIEASQTQLQKLRSE 1189
Cdd:TIGR02169 324 LakLEAEIDKLLAEIE---ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKeFAETRDELKDYREKLEKLKRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1190 AEGKQATFDRLEEELQRATE-----------VNKRMSQLHSERDV-----------------ELEHYRQLVGNLRERWQA 1241
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEeladlnaaiagIEAKINELEEEKEDkaleikkqewkleqlaaDLSKYEQELYDLKEEYDR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1242 VFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLHAvPIGGSKGLQEQLTQ-EKKLLEEIE---------- 1310
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEER-------VRGGRAVEEVLKA-SIQGVHGTVAQLGSvGERYATAIEvaagnrlnnv 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1311 --KNKDKVEDCQKFAK------------------------GYIDAIKDYELQLVTYKALVEPI-----ASPLKKAKMESA 1359
Cdd:TIGR02169 553 vvEDDAVAKEAIELLKrrkagratflplnkmrderrdlsiLSEDGVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAA 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1360 SDDIIQ-EYVTLRTRYSE---LMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIA 1435
Cdd:TIGR02169 633 RRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRSEPAEL--------------QRLRERLEGLKRELSSLQSELR 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1436 KAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETT 1515
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1516 MKQKNTAETELLQLRAKAVdadklrnaaQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQ 1595
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEI---------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1596 AEEAERhlKQAELEKQrqiqvveevaKKTAATQLESKQVALtARLEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQA 1675
Cdd:TIGR02169 849 IKSIEK--EIENLNGK----------KEELEEELEELEAAL-RDLESRLGD-------LKKERDELEAQLRELERKIEEL 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1676 EKELETWRQKANEaLRLRLQAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1752
Cdd:TIGR02169 909 EAQIEKKRKRLSE-LKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKR 987
|
810 820
....*....|....*....|...
gi 1207141751 1753 ------AKQKLAAEQELIRLRAD 1769
Cdd:TIGR02169 988 ldelkeKRAKLEEERKAILERIE 1010
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1711-1920 |
1.34e-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: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1711 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKmaeetakqklAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1790
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----------ALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1791 VNSAVKQKKELEEELIKV---------RKEMEILLQQKSKAEKETMSNTEKS-KQLLESEAAKMRELAEEATKLRSVAEE 1860
Cdd:COG4942 92 IAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1861 AKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE 1920
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1064-1918 |
1.42e-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: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1064 KEPLKACTQRATEQKKVQT---ELEGIKKDLDKVVEKSEAVLATSQQSSS--APVLRSEIDITQKKMEHVYGlssvyldk 1138
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASleeELEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKEKIGELEA-------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1139 lkTIDLVIRSTQGAEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ-RATEVNKRMSQL 1217
Cdd:TIGR02169 302 --EIASLERSIAEKERELEDAEERLAKL------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAeLKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1218 HSErDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQE 1297
Cdd:TIGR02169 374 EEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1298 QLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPI--ASPLKKAKMESASDDIIQEYVTLRtrys 1375
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeeRVRGGRAVEEVLKASIQGVHGTVA---- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1376 ELMTLSSQYIKFI-IETQRRLQ-----DEEKAAEKLkeeerkkmaemqaELEKQKQLAETHAKAIAKAEQEANELKTKMK 1449
Cdd:TIGR02169 529 QLGSVGERYATAIeVAAGNRLNnvvveDDAVAKEAI-------------ELLKRRKAGRATFLPLNKMRDERRDLSILSE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1450 DEVSKRQDVAVDSEKQKHNIQRE-------LQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKnta 1522
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFKYvfgdtlvVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSE--- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1523 ETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaaKEKKKALEDLEKFKLQAEEAERH 1602
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEED 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1603 LKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMviQLQEEAEHLKKQQAEADKAREQAEKELet 1681
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKL-- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1682 wrqkaNEALRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALkqkEAAEMELGNQRKMAEETAKQKLAAEQ 1761
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQEL-----------QEQRIDLKEQIKSIEKEI---ENLNGKKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1762 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELikvrkemEILLQQKSKAEKETMSNTEKSKQLLESE- 1840
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEEELSLEd 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 1841 -AAKMRELAEEATKLRSVAEEAKKQrqiAEEEAARQraeaeKILKEKLtaineaTRLKTEAEiALKEKEAENDRLKRKA 1918
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 ... |
188-285 |
1.79e-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: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 188 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 266
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1207141751 267 PEDVDVPHPDEKSIITYVS 285
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2200-2478 |
1.98e-08 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 60.50 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2200 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQldetdkqksvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2279
Cdd:pfam03528 14 EKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE-------------DLKRQNAVLQEAQVELDALQNQLALARAEMENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2280 LKLKLKIEKENQELMkkdkDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQ 2359
Cdd:pfam03528 81 KAVATVSENTKQEAI----DEVKSQWQEEVASLQAIMKETVR-EYEVQFHRRLEQ-ERAQWNQYRESAEREIADLRRRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2360 EAAklkaEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ------ETEGFQKSLEAERKRQLEITAEAEK-----LKVKV 2428
Cdd:pfam03528 155 EGQ----EEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAEKscrtdLEMYV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2429 TQLSDAQSKAEEEAKKFKKQADEIKIRL-QETEKHTSEKHTVVEK----LEVQRL 2478
Cdd:pfam03528 231 AVLNTQKSVLQEDAEKLRKELHEVCHLLeQERQQHNQLKHTWQKAndqfLESQRL 285
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1739-2482 |
2.10e-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: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1739 EMELGNQRKMAEETAKQKLAaeqeliRLRADFEHAEQqrtvlddELQRLKNDVNSA-VKQKKELEEELIKVRKEMeillq 1817
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEHIE------RVLEEYSHQVK-------DLQRRLNESNELhEKQKFYLRQSVIDLQTKL----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1818 QKSKAEKETMSNTEKSkqllesEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK 1897
Cdd:pfam15921 120 QEMQMERDAMADIRRR------ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1898 TEAEIALKEKEAENDRL-----KRKAEEEGYQRKVLEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRk 1969
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISYLKGRIfpvEDQLEALKSESQNKIELLLQQHQDRIEQL- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1970 VVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQKskakaeEEAEKFRKLAleeekkrkEAEAKVKQIQAAEEEAA 2049
Cdd:pfam15921 273 ISEHEVEITGLT-EKASSARSQANSIQSQLEIIQEQARN------QNSMYMRQLS--------DLESTVSQLRSELREAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2050 RQHKAAQEEVGRLMKLAE----EAKKQKEIAEKEA-------EKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2118
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANseltEARTERDQFSQESgnlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2119 KEEFEKAKKLAQEAE--------KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKL--RKEAEKEASRR 2188
Cdd:pfam15921 418 RRELDDRNMEVQRLEallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtaKKMTLESSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2189 AEAEAAALKLKQEA----DSEMAKYK-----KLAE-KTLKQKS----SVEEELVKVKVQLDETDKQKSVLDVELKRLKQE 2254
Cdd:pfam15921 498 VSDLTASLQEKERAieatNAEITKLRsrvdlKLQElQHLKNEGdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2255 V------SDAIK-QKAQVEDELSKVKIQMEDLlklklkiekenqELMKKDKDNTKKLLEEEAENMkklaeEAARLNIEAQ 2327
Cdd:pfam15921 578 VgqhgrtAGAMQvEKAQLEKEINDRRLELQEF------------KILKDKKDAKIRELEARVSDL-----ELEKVKLVNA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2328 EAARLRqiAESDLAKQRElaeKMLEEKKQAIQEAAKLKAEAEKLQK----QKDQAQVEAQKLLEAKKEMQQRLDQeTEGF 2403
Cdd:pfam15921 641 GSERLR--AVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQ-TRNT 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2404 QKSLEAERKR--------QLEITA---EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEK 2472
Cdd:pfam15921 715 LKSMEGSDGHamkvamgmQKQITAkrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS---QELSTVATEKNKMAGE 791
|
810
....*....|
gi 1207141751 2473 LEVQRLQSKQ 2482
Cdd:pfam15921 792 LEVLRSQERR 801
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1780-2533 |
3.20e-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: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1780 LDDELQRLKNDVNSAVKQKKELEEELIKV--RKEMEILLQQKSKAEKETMSNT--------EKSKQLLESEAAK-MRELA 1848
Cdd:TIGR00618 83 LGTKIYRVHRTLRCTRSHRKTEQPEQLYLeqKKGRGRILAAKKSETEEVIHDLlkldyktfTRVVLLPQGEFAQfLKAKS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1849 EEATKLRSVAEEAKKQRQIAeeeaarqrAEAEKILKEkltaineatrLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVL 1928
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLA--------LMEFAKKKS----------LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1929 EDQAAQhkqaIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL-NFEKASSGKQELELELKKLKGIADETQ 2007
Cdd:TIGR00618 225 EKELKH----LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELrAQEAVLEETQERINRARKAAPLAAHIK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2008 ----------------KSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAA---QEEVGRLMKLAEE 2068
Cdd:TIGR00618 301 avtqieqqaqrihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQH 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2069 AKKQKEIAEKEAEKQVILVQE-----AAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEA 2143
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKEldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2144 ALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSV 2223
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2224 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK---------IQMEDLLKLKLKIEKENQELM 2294
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrlqdlTEKLSEAEDMLACEQHALLRK 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2295 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEA--------QEAARLRQIAESDLAKQRELAEKMLEEKKQAI-------- 2358
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQltltqervREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemla 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2359 QEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgFQKSLEAERKRQLEITAEAEKLK----VKVTQLSDA 2434
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFNNneevTAALQTGAE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2435 QSKAEEEAKKFKKQADEIKIRLQETE-KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKeaadLQKQSK 2513
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEaEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH----QLLKYE 855
|
810 820
....*....|....*....|
gi 1207141751 2514 EMANVQQEQLQQEKTILQQS 2533
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLS 875
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2560-2744 |
3.34e-08 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 60.23 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2560 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ--------KEAEEEMNGKQKEMQDLEKKRIEQ--EKLLAEE 2629
Cdd:PRK00409 533 EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAHELIEA 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2630 NKNLREKLQQLQSSQKASYTKEIEIQT-DKVPEEELVQMTMVETTKKvlngstevdgvKKDVPLAFDGIREKVPASRLHE 2708
Cdd:PRK00409 613 RKRLNKANEKKEKKKKKQKEKQEELKVgDEVKYLSLGQKGEVLSIPD-----------DKEAIVQAGIMKMKVPLSDLEK 681
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207141751 2709 IGVLSKKEydklKKGKTTVQELSKNDKVKMCLKGKD 2744
Cdd:PRK00409 682 IQKPKKKK----KKKPKTVKPKPRTVSLELDLRGMR 713
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2139-2642 |
3.50e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2139 AEKEAALLHKKAEEAErqkkaaeaeaakQAKAQEDAEKLRKEAEKEASRRAeaeaaalklKQEADSEMAKYkklaEKTLK 2218
Cdd:PRK02224 197 EEKEEKDLHERLNGLE------------SELAELDEEIERYEEQREQARET---------RDEADEVLEEH----EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2219 QKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD-----------------AIKQKAQVEDELSKVKIQMEDLLK 2281
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaeaglddaDAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2282 LKLKIEKENQELMKKDKDNTKKlLEEEAenmKKLAEEAARLNIEAQEAARLRQIAESDLAK-----------------QR 2344
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADD-LEERA---EELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdapvDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2345 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2424
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2425 KVKVTQLSDAQSKAeEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvQRLQSKQEADGLHKAIADLEKEKEKLKKE 2504
Cdd:PRK02224 488 EEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKR-ERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2505 AADLQKQSKEMANVQQEQLQQEKTILqqsffAEKETLLKKEKAIEEEKKKLEKQFED----EVKKAEALKAEQERQRKL- 2579
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelNDERRERLAEKRERKRELe 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2580 --MEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKK------RIEQEKLLAEENKNLREKLQQLQS 2642
Cdd:PRK02224 641 aeFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavenELEELEELRERREALENRVEALEA 712
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
183-285 |
3.60e-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: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 183 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGV 261
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....
gi 1207141751 262 TRLLDPEDVDVPHPDEKSIITYVS 285
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLS 103
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1729-2416 |
3.93e-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: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1729 EAALKQKEAAEMELGNQRKmaEETAKQKLAAEQELIRLRADFEHAEQQRTvLDDELQRLKNDVNSavkQKKELEEELIKV 1808
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHF--GYKSDETLIASRQEERQETSAELNQLLRT-LDDQWKEKRDELNG---ELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1809 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEE----ATKLRSVAEEAKKQRQIAEEEAARQRAEaekiLK 1884
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERlkalTGKHQDVTAKYNRRRSKIKEQNNRDIAG----IK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1885 EKLTAINEA-TRLKTEAEIALKEKEA----ENDRLKRKAEEEGYQrkvledqaaqhkqaIEEKIGQLKKSSDteldrQKK 1959
Cdd:pfam12128 397 DKLAKIREArDRQLAVAEDDLQALESelreQLEAGKLEFNEEEYR--------------LKSRLGELKLRLN-----QAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1960 IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQkskakaeeeaekfRKLALeeekkrkeAEAKVK 2039
Cdd:pfam12128 458 ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS-------------EALRQ--------ASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2040 QIQAAEEEAARQHKAAQeevGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL---------VQQN 2109
Cdd:pfam12128 517 ERQSALDELELQLFPQA---GTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvkldlkrIDVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2110 KDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEkeasrra 2189
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR--------------EETFARTALKNAR------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2190 eaeaaaLKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDEL 2269
Cdd:pfam12128 653 ------LDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2270 SKVKI-QMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES---------- 2338
Cdd:pfam12128 727 LDAQLaLLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwl 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2339 ----DLAKQRELAEKMLEEKKQ---AIQEAAKLK-AEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL-----DQETEGFQK 2405
Cdd:pfam12128 807 qrrpRLATQLSNIERAISELQQqlaRLIADTKLRrAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkeDANSEQAQG 886
|
730
....*....|.
gi 1207141751 2406 SLeAERKRQLE 2416
Cdd:pfam12128 887 SI-GERLAQLE 896
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2039-2183 |
4.11e-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: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2039 KQIQAAEEE---AARQHKAAQEEvgrlMKLAEEAKKQKEIAEKEAEKQviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ 2115
Cdd:TIGR02794 81 EKQRAAEQArqkELEQRAAAEKA----AKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEE 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2116 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2183
Cdd:TIGR02794 155 EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAA 222
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2303-2653 |
4.87e-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: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2303 KLLEEEAENMKKLAEEAARLnieaqeaarlrqiaeSDLAKQRELAEKMLEEKKQAIQE----AAKLKAEAEKLQKQKDQA 2378
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGI---------------SKYKERRKETERKLERTRENLDRlediLNELERQLKSLERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2379 QvEAQKLLEAKKEMQ--------QRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2450
Cdd:TIGR02168 213 E-RYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2451 EIKIRLQETEKhtsekhtvveklEVQRLQSKQEADglhkaiadlekekeklkkeaadlqKQSKEMANVQQEQLQQEKTIL 2530
Cdd:TIGR02168 292 ALANEISRLEQ------------QKQILRERLANL------------------------ERQLEELEAQLEELESKLDEL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2531 QQSFfAEKETLLKKEKAIEEekkklekQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQK 2610
Cdd:TIGR02168 336 AEEL-AELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1207141751 2611 EMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIE 2653
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1722-2458 |
5.94e-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: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1722 KKRAKAEEAALKQKEAaemELGNQRKM--AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR-----LKNDVNSA 1794
Cdd:pfam05483 91 KKWKVSIEAELKQKEN---KLQENRKIieAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1795 VKQKKELEEELIKVRkemEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 1874
Cdd:pfam05483 168 AEKTKKYEYEREETR---QVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1875 ---QRAEAEKILKEkLTAINEATRLKTEAeiaLKEK-EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIeekigqlkkSS 1950
Cdd:pfam05483 245 lliQITEKENKMKD-LTFLLEESRDKANQ---LEEKtKLQDENLKELIEKKDHLTKELEDIKMSLQRSM---------ST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1951 DTELDRQKKIVEETLKQRkVVEEEIHILKLNfeKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKK 2030
Cdd:pfam05483 312 QKALEEDLQIATKTICQL-TEEKEAQMEELN--KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2031 RKEAEAKVKQIQAAEEEAARQHKAAqeeVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQNK 2110
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKI---LAEDEKLLDEKKQFEKIAEELKGKE----QELIFLLQAREKEIHDLEIQLTA 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2111 DSMAQDKLKEEFEKAKKlaqEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAE 2190
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKT---ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2191 AEAAALKLKQEADSemakykklAEKTLKQKSSveeelvKVKVQLDETDKQKsvldvelKRLKQEVSDAIKQKAQVEDELS 2270
Cdd:pfam05483 539 LEEKEMNLRDELES--------VREEFIQKGD------EVKCKLDKSEENA-------RSIEYEVLKKEKQMKILENKCN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2271 KVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAE-NMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEk 2349
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE- 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2350 mLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLDQETE---GFQKSLEAERKR-QLEITAEAEKLK 2425
Cdd:pfam05483 677 -VEKAKAIADEAVKLQKEIDKRCQHK---IAEMVALMEKHKHQYDKIIEERDselGLYKNKEQEQSSaKAALEIELSNIK 752
|
730 740 750
....*....|....*....|....*....|...
gi 1207141751 2426 VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE 2458
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1468-1989 |
6.12e-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: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1468 NIQRELQELKTLSEQEIKAKSQQVEEaLLSRTRIEEEIhiiRLQLETTMKQKNTA--ETELLQLRAKAVD---ADKLRNA 1542
Cdd:pfam05701 46 KVQEEIPEYKKQSEAAEAAKAQVLEE-LESTKRLIEEL---KLNLERAQTEEAQAkqDSELAKLRVEEMEqgiADEASVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1543 AQE--EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKAledlekfklQAEEAERHLKQAElekqrqiQVVEEV 1620
Cdd:pfam05701 122 AKAqlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIK---------RAEEAVSASKEIE-------KTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1621 AKKTAATQlESKQVALTARLEeslKNEQVMVIQLQEEAEHLKKQqaeadKAREQAEKELETWRQK------------ANE 1688
Cdd:pfam05701 186 TIELIATK-ESLESAHAAHLE---AEEHRIGAALAREQDKLNWE-----KELKQAEEELQRLNQQllsakdlkskleTAS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1689 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKaeeAALKQKEAAEMElGNQRKMAEETAKQKLAAEQelirLRA 1768
Cdd:pfam05701 257 ALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAA---LASAKKELEEVK-ANIEKAKDEVNCLRVAAAS----LRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1769 DFehaEQQRTVLdDELQRLKNDVNSAVKQkkeLEEELIKVRKEMEiLLQQKSKAEKETMSNTEKskqlleseaaKMRELA 1848
Cdd:pfam05701 329 EL---EKEKAEL-ASLRQREGMASIAVSS---LEAELNRTKSEIA-LVQAKEKEAREKMVELPK----------QLQQAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1849 EEATKLRSVAEEAKKQRQIAEEEAARQRAEA-------EKILKEKLtAINEATRLKTEAEIALKEKEAEndrlKRKAEEE 1921
Cdd:pfam05701 391 QEAEEAKSLAQAAREELRKAKEEAEQAKAAAstvesrlEAVLKEIE-AAKASEKLALAAIKALQESESS----AESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1922 GYQRKV---LEDQAAQHKQA----------IEEKIGQLKKSSDTELDRQKKI--VEETLKQRKvveEEIHILKLNFEKAS 1986
Cdd:pfam05701 466 DSPRGVtlsLEEYYELSKRAheaeelankrVAEAVSQIEEAKESELRSLEKLeeVNREMEERK---EALKIALEKAEKAK 542
|
...
gi 1207141751 1987 SGK 1989
Cdd:pfam05701 543 EGK 545
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
58-169 |
6.21e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 53.50 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 58 KTFTKWVNKHLVKhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLpreRDVvrnSRLPREKGRMrfhkLQNVQIALD 137
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEKV---EDI---NGCPRSQSQM----IENVDVCLS 69
|
90 100 110
....*....|....*....|....*....|..
gi 1207141751 138 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 169
Cdd:cd21286 70 FLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1365-1967 |
7.87e-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: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1365 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1444
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-------------LEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1445 KTKMKDevskrqdvavdsekqkhNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTmkqkntaET 1524
Cdd:COG4913 329 EAQIRG-----------------NGGDRLEQL----EREIERLERELEERERRRARLEALLAALGLPLPAS-------AE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1525 ELLQLRAKAVDadkLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA----- 1599
Cdd:COG4913 381 EFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1600 -------------------------------------ERHLKQA-------ELEKQRQIQVVEEVAKKTAATQLESKQVA 1635
Cdd:COG4913 458 aelpfvgelievrpeeerwrgaiervlggfaltllvpPEHYAAAlrwvnrlHLRGRLVYERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1636 ---------LTARLEESLkNEQVMVIQLqEEAEHLKKqqaeADKA----------REQAEKELETWRQKA------NEAL 1690
Cdd:COG4913 538 gkldfkphpFRAWLEAEL-GRRFDYVCV-DSPEELRR----HPRAitragqvkgnGTRHEKDDRRRIRSRyvlgfdNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1691 RLRLQAEEEAnkktaaqeeaEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR---KMAEETAKQKLAAEQELIRLR 1767
Cdd:COG4913 612 LAALEAELAE----------LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1768 ADFEHAEQqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMREL 1847
Cdd:COG4913 682 ASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1848 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE-KLTAINEATRLKTEAEiALKEKEAENDRLkrkaEEEGyqrk 1926
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRL----EEDG---- 828
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1207141751 1927 vLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 1967
Cdd:COG4913 829 -LPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1117-1973 |
8.86e-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: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1117 EIDITQKKMEHVYGLSSVYLDKLKTIDLVIRST--------QGAEDILNKYENQLREVNKvpvNEKEIEASQTQLQKLRS 1188
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYENELDPLKN---RLKEIEHNLSKIMKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1189 EAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFaqielrQRELDLLNRQMQAYRESYD 1268
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDC------QRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1269 WLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKklLEEIEKNKDKVEDCQKFAKGYIDAIKDyelqlvtykalvepia 1348
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIKNFHTLVIERQED---------------- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1349 splkKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQR-RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLA 1427
Cdd:TIGR00606 406 ----EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKeILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1428 ETHAKaIAKAEQEANeLKTKMKDEVSkRQDVAVDSEKQKHNIQRELQELKTLSEQEikaksQQVEEALLSRTRIEEEIHI 1507
Cdd:TIGR00606 482 KAERE-LSKAEKNSL-TETLKKEVKS-LQNEKADLDRKLRKLDQEMEQLNHHTTTR-----TQMEMLTKDKMDKDEQIRK 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1508 IRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE------ 1581
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcg 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1582 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMVIQLQEEAEH 1660
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTeAELQEFISDLQSKLRLAPDKLKS 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1661 LKKQQAEADKAREQAEKELETwrqKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1740
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPG---RQSI-IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1741 ELGNQRKMAEETAK-----QKLAAEQELIRLRADFEHAEQQRTVLDDELQRlkndvnsaVKQKKELEEELIKVRKEMEIL 1815
Cdd:TIGR00606 790 DVTIMERFQMELKDverkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDT--------VVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1816 LQQKS---KAEKETMS-NTEKSKQLLESEAAKMRELAEEATKLRSVAEE------AKKQRQIAEEEAARQRAEAEKILKE 1885
Cdd:TIGR00606 862 LKSKTnelKSEKLQIGtNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLEKDQQEKEELISSKETSNKKAQD 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1886 KLTAINEATRLKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTElDRQKKIVEET 1964
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ-KIQERWLQDN 1020
|
....*....
gi 1207141751 1965 LKQRKVVEE 1973
Cdd:TIGR00606 1021 LTLRKRENE 1029
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2038-2242 |
9.79e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.55 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2038 VKQIQAAEEEAArqhKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDsmAQDK 2117
Cdd:TIGR02794 52 ANRIQQQKKPAA---KKEQERQKKLEQQAEEAEKQRA-AEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA--EEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2118 LKEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAL 2196
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAErKAKEEAAKQAEEEAKAKAAAEAKKKAEE--AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141751 2197 KLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKS 2242
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1597-2155 |
1.20e-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: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1597 EEAERHLKQAElEKQRQIQVVEEVAKK-TAATQLESKQVALTARLEesLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1675
Cdd:COG4913 238 ERAHEALEDAR-EQIELLEPIRELAERyAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1676 EKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKq 1755
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDR-----------------LEQLEREIERLERELEERERRRARLEALLAALGLPLP- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1756 klAAEQELIRLRADfehAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSkaeketmsntekskq 1835
Cdd:COG4913 377 --ASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS--------------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1836 LLESEAAKMRELAEEATK-----LRSVAEEAkkqrQIAEEEAARQRAeAEKIL--------------KEKLTAINE---A 1893
Cdd:COG4913 437 NIPARLLALRDALAEALGldeaeLPFVGELI----EVRPEEERWRGA-IERVLggfaltllvppehyAAALRWVNRlhlR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1894 TRLKTEaeialKEKEAENDRLKRKAEEEGYQRKVL-------------------------EDQAAQHKQAIEEKiGQLKK 1948
Cdd:COG4913 512 GRLVYE-----RVRTGLPDPERPRLDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdsPEELRRHPRAITRA-GQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1949 SSDT-ELDRQKKIVEE------TLKQRKVVEEEIHILKLNFEKASSgkqelelELKKLKGIADETQKskakaeeeaekfR 2021
Cdd:COG4913 586 NGTRhEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEE-------RLEALEAELDALQE------------R 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2022 KLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKA 2101
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQA 725
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2102 QNVL--VQQNKDSMAQDKLKEEFEKAKKLAQEA------EKAKDNAEKEAALLHKKAEEAER 2155
Cdd:COG4913 726 EEELdeLQDRLEAAEDLARLELRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEE 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2038-2619 |
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 1207141751 2038 VKQIQAAEEEAARQHKAAQEEVGRLMKLAE---EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQnVLVQQNKDSMA 2114
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2115 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAA 2194
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK--------------ELEEKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2195 ALKLKQEADS-EMAKYKKLAEKTLKQKSSvEEELVKVKVQLDETDKQKSVLDVELKRLKQEvsdaikqKAQVEDELSKVK 2273
Cdd:PRK03918 354 LEELEERHELyEEAKAKKEELERLKKRLT-GLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2274 IQMEDLLKLKLKIEKENQELmkkDKDNTKKLLEEEAENMKKLAEEAARL-NIEAQEAARLRQI-----AESDLAKQRELA 2347
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGREL---TEEHRKELLEEYTAELKRIEKELKEIeEKERKLRKELRELekvlkKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2348 EKMLE-EKKQAIQEAAKLKAEAEKLQKQKdqaqveaQKLLEAKKEmqqrldqetegfQKSLEAERKRQLEITAEAEKLKV 2426
Cdd:PRK03918 503 EQLKElEEKLKKYNLEELEKKAEEYEKLK-------EKLIKLKGE------------IKSLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2427 KVTQLSDAQSKAEEEAKKFK-KQADEIKIRLQETEKHTSEKHTVVE-KLEVQRLQSKQE--ADGLHKAIADLEKEKEKLK 2502
Cdd:PRK03918 564 KLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDaEKELEREEKELKklEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2503 KEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKkklekqfedevKKAEALKAEQERqrklMEE 2582
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK-----------KTLEKLKEELEE----REK 708
|
570 580 590
....*....|....*....|....*....|....*..
gi 1207141751 2583 ERKKLQSamdaaIKKQKEAEEEMNGKQKEMQDLEKKR 2619
Cdd:PRK03918 709 AKKELEK-----LEKALERVEELREKVKKYKALLKER 740
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2302-2625 |
1.27e-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: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2302 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQrELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2381
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ-ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2382 AQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA--DEIKIRLQET 2459
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNE-EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEekEREIARLRAQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2460 EKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffAEKE 2539
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREE--------EEFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2540 TLLkkekaieeekkklekqfEDEVKKAEALKAEQERQRKLMEEERKKLQSAMD---AAIKKQKEAEEEMNGKQKEMQDLE 2616
Cdd:pfam13868 265 RML-----------------RKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEereEQRAAEREEELEEGERLREEEAER 327
|
....*....
gi 1207141751 2617 KKRIEQEKL 2625
Cdd:pfam13868 328 RERIEEERQ 336
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2202-2443 |
1.33e-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: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2202 ADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlk 2281
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2282 lklkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLN-IEAQEAARLRQIAEsdlakQRELAEKMLEEKKQAIQE 2360
Cdd:COG3883 92 --------ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkIADADADLLEELKA-----DKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2361 AAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEE 2440
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
...
gi 1207141751 2441 EAK 2443
Cdd:COG3883 239 AAA 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1469-1976 |
1.41e-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: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1469 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE-----TELLQLRAKAVDADKLRNAA 1543
Cdd:COG4913 244 LEDAREQIELL--EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEleelrAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1544 QEEAEKLRKQVAE-ETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK 1622
Cdd:COG4913 322 REELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1623 K--TAATQLESKQVALTARLEEslkneqvmviqLQEEAEHLKKQQ----AEADKAREQAEKEL----------------- 1679
Cdd:COG4913 402 AleEALAEAEAALRDLRRELRE-----------LEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgelievr 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1680 ---ETWRQKANEAL---RLRL----QAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK---------EA 1737
Cdd:COG4913 471 peeERWRGAIERVLggfALTLlvppEHYAAALRwvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrAW 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1738 AEMELGNQRKMAeetakqKLAAEQELIRL-RA----------------DFEHAEQQRTVLddelqrlkndVNSAVKQKKE 1800
Cdd:COG4913 551 LEAELGRRFDYV------CVDSPEELRRHpRAitragqvkgngtrhekDDRRRIRSRYVL----------GFDNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1801 LEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEE-AKKQRQIAE--------EE 1871
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAE-LDALQERREALQ----RLAEYSWDEIDVASAEREiAELEAELERldassddlAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1872 AARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkVLEDQAAQHKQAIEEKIGQLKKSsd 1951
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA------AEDLARLELRALLEERFAAALGD-- 761
|
570 580
....*....|....*....|....*
gi 1207141751 1952 telDRQKKIVEETLKQRKVVEEEIH 1976
Cdd:COG4913 762 ---AVERELRENLEERIDALRARLN 783
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2326-2461 |
1.50e-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: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2326 AQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQK 2405
Cdd:TIGR02794 49 AQQANRIQQ-QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 2406 SlEAERKRQLEitAEAEKlkvkvTQLSDAQSKAEEEAKKfkKQADEIKIRLQETEK 2461
Cdd:TIGR02794 128 Q-AAEAKAKAE--AEAER-----KAKEEAAKQAEEEAKA--KAAAEAKKKAEEAKK 173
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4080-4116 |
1.65e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.17 E-value: 1.65e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1207141751 4080 IRLLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEM 4116
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1486-2086 |
1.67e-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: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1486 AKSQQVEeaLLSRT-----RIEEEIHIIRlqlETTMKQKNTAETELLQLRAKAVdADKlrnAAQEEAEKLRKQVAEETQK 1560
Cdd:pfam07111 60 ALSQQAE--LISRQlqelrRLEEEVRLLR---ETSLQQKMRLEAQAMELDALAV-AEK---AGQAEAEGLRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1561 KRKAEEELKR-----KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAA--TQLESKQ 1633
Cdd:pfam07111 131 RKNLEEGSQReleeiQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELlrKQLSKTQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1634 VALTAR--LEESLKN---EQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETWR-QKANEALRLRlqaEEEAN 1701
Cdd:pfam07111 211 EELEAQvtLVESLRKyvgEQVPPEVHSQTWELERQelldtmQHLQEDRADLQATVELLQVRvQSLTHMLALQ---EEELT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1702 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK-QKEAAEMELGNQRKmaeeTAKQKLAAEQELIRLRAdfehaeQQRTVL 1780
Cdd:pfam07111 288 RKIQPSDSLEPEFPKKCRSLLNRWREKVFALMvQLKAQDLEHRDSVK----QLRGQVAELQEQVTSQS------QEQAIL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1781 DDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE---TMSNTEKSKQLLESEAAKMRELAEEATKLRSV 1857
Cdd:pfam07111 358 QRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQlkfVVNAMSSTQIWLETTMTRVEQAVARIPSLSNR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1858 AEEAKKQRQIAEEEAARQRAEAEkILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvlEDQAAQHkq 1937
Cdd:pfam07111 438 LSYAVRKVHTIKGLMARKVALAQ-LRQESCPPPPPAPPVDADLSLELEQLREERNRLDA------------ELQLSAH-- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1938 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEea 2017
Cdd:pfam07111 503 LIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQ-- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2018 ekfRKLALEEEKKRKEAEAKVKQIQAAEEEAAR--------QHKAAQEE--VGRLMKLAEEAKKQ------KEIAEKEAE 2081
Cdd:pfam07111 581 ---EKVAEVETRLREQLSDTKRRLNEARREQAKavvslrqiQHRATQEKerNQELRRLQDEARKEegqrlaRRVQELERD 657
|
....*
gi 1207141751 2082 KQVIL 2086
Cdd:pfam07111 658 KNLML 662
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1774-1970 |
1.80e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 57.91 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1774 EQQRTVLDDELQRLKNDVNSAVKQKKELEEElikvRKEMEILLQQkskAEKETMSNTEKSKQLLESEAAKMRELAEEATK 1853
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQK----AEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1854 LRSVAEEAKKQ--RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE---NDRLK-RKAEEEGYQRKV 1927
Cdd:PRK00409 578 AIKEAKKEADEiiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkvGDEVKyLSLGQKGEVLSI 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141751 1928 LEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRKV 1970
Cdd:PRK00409 658 PDDKEAIVQAGImkmKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTV 703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1642-1881 |
2.04e-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: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1642 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakREA 1721
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-----------AEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1722 KKRAKAEEAALKQKEA--AEMELGNQRKMAEETAKQKLAAE--QELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQ 1797
Cdd:COG4942 89 EKEIAELRAELEAQKEelAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1798 KKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRA 1877
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1207141751 1878 EAEK 1881
Cdd:COG4942 249 AALK 252
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
192-285 |
2.13e-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: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 192 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-------------------------- 244
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141751 245 -----LENLEQAFSIAE---RDLG-VTRLLDPEDVDVPHPDEKSIITYVS 285
Cdd:cd21224 82 lsselLANEKRNFKLVQqavAELGgVPALLRASDMSNTIPDEKVVILFLS 131
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1078-1612 |
2.40e-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: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1078 KKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVyLDKLKTIDLVIRSTQGAEDILn 1157
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQSQLEII- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1158 kyENQLREVNKVPVNE-KEIEASQTQLqklRSE-AEGKQATFDRLEEELQRATEVNKRMSQLHSERDveleHYRQLVGNL 1235
Cdd:pfam15921 305 --QEQARNQNSMYMRQlSDLESTVSQL---RSElREAKRMYEDKIEELEKQLVLANSELTEARTERD----QFSQESGNL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1236 RERWQAVFAQIELRQRELDLLNRQMQAYRE-------SYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQE------ 1302
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqg 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1303 -KKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAkmESASDDIIQEYVTLRTRYsELMTLS 1381
Cdd:pfam15921 456 kNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNAEITKLRSRV-DLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1382 SQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVD 1461
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1462 SEKQKHNIQR--------ELQELKTLSE--------QEIKA-KSQQVEEALLSRTRIE---EEIHIIRL-------QLET 1514
Cdd:pfam15921 613 KDKKDAKIRElearvsdlELEKVKLVNAgserlravKDIKQeRDQLLNEVKTSRNELNslsEDYEVLKRnfrnkseEMET 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1515 TMK----QKNTAETELLQLR-------------------------AKAVDADKLRNAAQ-----------------EEAE 1548
Cdd:pfam15921 693 TTNklkmQLKSAQSELEQTRntlksmegsdghamkvamgmqkqitAKRGQIDALQSKIQfleeamtnankekhflkEEKN 772
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 1549 KLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1612
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1653-1909 |
3.11e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.99 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1653 QLQEEAEHLkkqQAEADKAREQAEkELETWRQKANEALRL------RLQAEEEANKKTaaqeeaekqkeeakreakkrAK 1726
Cdd:PRK10929 117 QLLEKSRQA---QQEQDRAREISD-SLSQLPQQQTEARRQlneierRLQTLGTPNTPL--------------------AQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1727 AEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFehAEQQRTVLDDELQRLKNDVNSAVKQK-------- 1798
Cdd:PRK10929 173 AQLTALQAESAALKALVDELELAQLSANNR----QELARLRSEL--AKKRSQQLDAYLQALRNQLNSQRQREaeralest 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1799 ---------------------KELEEELIKVRKEMEILLQQKSKAEKETM------------------SNT--------- 1830
Cdd:PRK10929 247 ellaeqsgdlpksivaqfkinRELSQALNQQAQRMDLIASQQRQAASQTLqvrqalntlreqsqwlgvSNAlgealraqv 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1831 ----EKSK-QLLESEAAKMR-------ELAEEATKLRSVAEE-----AKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 1893
Cdd:PRK10929 327 arlpEMPKpQQLDTEMAQLRvqrlryeDLLNKQPQLRQIRQAdgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILEL 406
|
330 340
....*....|....*....|
gi 1207141751 1894 TRLK---TEAEIALKE-KEA 1909
Cdd:PRK10929 407 TKLKvanSQLEDALKEvNEA 426
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1722-1922 |
3.24e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.71 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1722 KKRAKAEEAALKQKEAAEMElgnqrkmAEETAKQK-LAAEQELIRLRADFEhaeqqrtvlddelqrlkndvnsavKQKKE 1800
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-------AEAIKKEAlLEAKEEIHKLRNEFE------------------------KELRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1801 LEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA-KKQRQIAEEEAARQRAEA 1879
Cdd:PRK12704 80 RRNEL----QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207141751 1880 EKILKEKLTAineatrlKTEAEIALKEKEAENdrlkrKAEEEG 1922
Cdd:PRK12704 156 KEILLEKVEE-------EARHEAAVLIKEIEE-----EAKEEA 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1738-1942 |
3.44e-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: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1738 AEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM----- 1812
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1813 ------------EILLQQKSKAEkeTMSNTEKSKQLLESEAAKMRELAEEATKLrsvaEEAKKQRQIAEEEAARQRAEAE 1880
Cdd:COG3883 94 alyrsggsvsylDVLLGSESFSD--FLDRLSALSKIADADADLLEELKADKAEL----EAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 1881 KILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEK 1942
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2291-2453 |
3.64e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 56.76 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2291 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAE 2369
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAiKEAKKEAD 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2370 KLQK------QKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS------------------------LEAERKRQLEITA 2419
Cdd:PRK00409 588 EIIKelrqlqKGGYASVKAHELIEARKRLNKANEKKEKKKKKQkekqeelkvgdevkylslgqkgevLSIPDDKEAIVQA 667
|
170 180 190
....*....|....*....|....*....|....
gi 1207141751 2420 EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2453
Cdd:PRK00409 668 GIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2295-2508 |
3.79e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2295 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAE--SDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2372
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2373 KQKDQAQVEAqkllEAKKemqqrldQETEGFQKSLEAERKRQleitAEAEklkvkvtqlsdAQSKAEEEAKKFKKQADEI 2452
Cdd:PRK09510 156 AAAAAKKAAA----EAKK-------KAEAEAAKKAAAEAKKK----AEAE-----------AAAKAAAEAKKKAEAEAKK 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 2453 KIRLQETEKHTSEKHTVVEKLEVqrlQSKQEADGLHKAIADLEKEKEKLKKEAADL 2508
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2083-2658 |
4.04e-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: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2083 QVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEkAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEA 2162
Cdd:pfam15921 239 RIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE-ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2163 EAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkqeADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKS 2242
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2243 VLDVELKRL--------------KQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLlEEE 2308
Cdd:pfam15921 395 LEKEQNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL-EST 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2309 AENMKKLAEE--AARLNIEAQEaarlRQIaeSDLAKQRELAEKMLEEKKQAI-----------QEAAKLKAEAEKLQKQk 2375
Cdd:pfam15921 474 KEMLRKVVEEltAKKMTLESSE----RTV--SDLTASLQEKERAIEATNAEItklrsrvdlklQELQHLKNEGDHLRNV- 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2376 dQAQVEAQKLLEAKKemqqrlDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR 2455
Cdd:pfam15921 547 -QTECEALKLQMAEK------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2456 LQETEKHTSEKHtvVEKLEV-----QRLQS----KQEADGLHKAI----ADLEKEKEKLKKEAADLQKQSKEM---ANVQ 2519
Cdd:pfam15921 620 IRELEARVSDLE--LEKVKLvnagsERLRAvkdiKQERDQLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMettTNKL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2520 QEQLQQEKTILQQSffaeKETLLKKekaieeekkklekqfedEVKKAEALKAEQERQRKLMEEerkklQSAMDAAIKKQK 2599
Cdd:pfam15921 698 KMQLKSAQSELEQT----RNTLKSM-----------------EGSDGHAMKVAMGMQKQITAK-----RGQIDALQSKIQ 751
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2600 EAEEEMNGKQKEMQDL--EKKRIEQE-KLLAEENKNLREKLQQLQSSQKASYTK--EIEIQTDK 2658
Cdd:pfam15921 752 FLEEAMTNANKEKHFLkeEKNKLSQElSTVATEKNKMAGELEVLRSQERRLKEKvaNMEVALDK 815
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1183-1912 |
4.08e-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: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1183 LQKLRSEAEGKQATFDRLEEELQRATEVNK-------RMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELR------ 1249
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFgyksdetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaada 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1250 -----QRELDLLNRQMQAYR----ESY----DWLIRWIADAKQRQDKLHAVPigGSKGLQEQLTQEKKLLEEiEKNKDKV 1316
Cdd:pfam12128 316 avakdRSELEALEDQHGAFLdadiETAaadqEQLPSWQSELENLEERLKALT--GKHQDVTAKYNRRRSKIK-EQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1317 EDCQKfakgYIDAIKD-YELQLVTYKALVEPIASPLKKaKMESASDDIIQEYVTLRTRYSELMTL--SSQYIKFIIETQR 1393
Cdd:pfam12128 393 AGIKD----KLAKIREaRDRQLAVAEDDLQALESELRE-QLEAGKLEFNEEEYRLKSRLGELKLRlnQATATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1394 RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMkDEVSKRQDvavdseKQKHNIQREL 1473
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAL-DELELQLF------PQAGTLLHFL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1474 QELKTLSEQEIkakSQQVEEALLSRTRIEEEIhiirlqLETTMKQKNTAETelLQLRAKAVDADK---LRNAAQEEAEKL 1550
Cdd:pfam12128 541 RKEAPDWEQSI---GKVISPELLHRTDLDPEV------WDGSVGGELNLYG--VKLDLKRIDVPEwaaSEEELRERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1551 RKQVAEETQKKRKAEEELKRKSEAekdaakekkkaledLEKFKLQAEEAERHLKQAElEKQRQIQVVEEVAKKTAATQLE 1630
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGE--------------LEKASREETFARTALKNAR-LDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1631 SKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeea 1710
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG---------- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1711 ekqkeeakreakkrAKAEEAALKQKEAAEMElgnqRKMAEETAKQKLAAE-QELIRLRADFEHAEQQRTVLDDELQrlkn 1789
Cdd:pfam12128 745 --------------AKAELKALETWYKRDLA----SLGVDPDVIAKLKREiRTLERKIERIAVRRQEVLRYFDWYQ---- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1790 dvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET-MSNTEKSKQLLESEAAKMReLAEEATKLRSVaeeakkQRQIA 1868
Cdd:pfam12128 803 --ETWLQRRPRLATQLSNIERAISELQQQLARLIADTkLRRAKLEMERKASEKQQVR-LSENLRGLRCE------MSKLA 873
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141751 1869 EEEAARQRAEAEKILKEKLTAINEaTRLKTEAEIALKEKEAEND 1912
Cdd:pfam12128 874 TLKEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHF 916
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
48-173 |
4.18e-07 |
|
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: 51.82 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 48 CADERDRVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDVVRNSRLPrekgrmrfH 127
Cdd:cd21222 9 EAPEKLAEVKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDD--------E 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207141751 128 KLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 173
Cdd:cd21222 76 KLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1590-1910 |
4.41e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1590 EKFKLQAEEAERhlKQAELEKQRqiqvveevakktaatqLESKQvaltARLEEslkneqvmviqlqEEAEHLKKQQAEAD 1669
Cdd:PRK05035 434 AKAEIRAIEQEK--KKAEEAKAR----------------FEARQ----ARLER-------------EKAAREARHKKAAE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1670 KAREQAEKELetwrQKANEALRLRlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRK-- 1747
Cdd:PRK05035 479 ARAAKDKDAV----AAALARVKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA----DPKKaa 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1748 --MAEETAKQKLAAEQElirlradfEHAEQQRTVlDDELQRLKNDVNSAVKQKKELEEElikvrkemeillqQKSKAEKE 1825
Cdd:PRK05035 550 vaAAIARAKAKKAAQQA--------ANAEAEEEV-DPKKAAVAAAIARAKAKKAAQQAA-------------SAEPEEQV 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1826 TMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKqrqiAEEEAARQRAEAEKILKEKLTAINEAT----RLKTEAE 1901
Cdd:PRK05035 608 AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRK----AAVAAAIARAKARKAAQQQANAEPEEAedpkKAAVAAA 683
|
330
....*....|
gi 1207141751 1902 IA-LKEKEAE 1910
Cdd:PRK05035 684 IArAKAKKAA 693
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1595-1804 |
4.80e-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: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1595 QAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLEskqvalTARLEESLKneqvmviqlQEEAEHLKKQQAEADKAREQ 1674
Cdd:TIGR02794 76 QAEEAE---KQRAAEQARQKELEQRAAAEKAAKQAE------QAAKQAEEK---------QKQAEEAKAKQAAEAKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1675 AEKEletwRQKANEALRlrlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAK 1754
Cdd:TIGR02794 138 AEAE----RKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1755 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1804
Cdd:TIGR02794 211 AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1175-1703 |
4.89e-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: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1175 EIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELE-HYRQLVGNLRERWQAVFAQIELRQREL 1253
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1254 DLLNRQMQAYRESYDWL-------------IRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQ 1320
Cdd:pfam05557 83 KYLEALNKKLNEKESQLadarevisclkneLSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1321 KFAKGYIDAIKD--YELQLVTYKALVepiaspLKKAKMESAS-DDIIQEYVTLRTRYSELMTLSSQyiKFIIETQ----- 1392
Cdd:pfam05557 163 SSLAEAEQRIKEleFEIQSQEQDSEI------VKNSKSELARiPELEKELERLREHNKHLNENIEN--KLLLKEEvedlk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1393 RRLQDEEKaAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSE-KQKHNIQ 1470
Cdd:pfam05557 235 RKLEREEK-YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1471 RELQE-----LKTLSEQEIKAKSQQVEEALLSRTRI--EEEIHIIRLQL-----ETTMKQKNTAETELLQLRAKAVDADK 1538
Cdd:pfam05557 314 RELEQelaqyLKKIEDLNKKLKRHKALVRRLQRRVLllTKERDGYRAILesydkELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1539 LRNA--------AQEEAE--KLRKQVAEETQKKRKAEEELKRKSeaekDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL 1608
Cdd:pfam05557 394 AHNEemeaqlsvAEEELGgyKQQAQTLERELQALRQQESLADPS----YSKEEVDSLRRKLETLELERQRLREQKNELEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1609 EKQRQIQVVEEVAKKTAATQLESKQvalTARLEESLKNeqvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN- 1687
Cdd:pfam05557 470 ELERRCLQGDYDPKKTKVLHLSMNP---AAEAYQQRKN---QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFk 543
|
570
....*....|....*.
gi 1207141751 1688 EALRLRLQAeEEANKK 1703
Cdd:pfam05557 544 EVLDLRKEL-ESAELK 558
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
56-172 |
5.23e-07 |
|
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: 51.35 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 56 QKKTFTKWVNKhlvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSgetlPRERDVVRNSRLPRekgRMRFHKLQNVQIA 135
Cdd:cd21299 5 EERCFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVS----PGSVNWKHANKPPI---KMPFKKVENCNQV 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141751 136 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 172
Cdd:cd21299 71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1456-1678 |
5.28e-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: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1456 QDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvd 1535
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1536 aDKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-----QAELEK 1610
Cdd:COG4942 93 -AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAelaalRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 1611 QRQIQVV---EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKE 1678
Cdd:COG4942 172 ERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1746-1885 |
6.13e-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: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1746 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR---------KEMEILL 1816
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 1817 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 1885
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2039-2181 |
6.34e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2039 KQIQAAEEEAARQHKAAQEEVgrlmklAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKL 2118
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQA------EEAAAKAAAAAKAKAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKK 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2119 KEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEA 2181
Cdd:PRK09510 186 KAEAEAAAKAAAEAKkKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1278-1613 |
6.75e-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: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1278 KQRQDKLHavpiggsKGLQEQLTQEKK-LLEEIEKNKdKVEDCQKFAKGYID---AI-KDYELQLVTYKALVEPIASPLK 1352
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDrqaAIyAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1353 KAKMESASDDIIQEYVTlRTRYSELMTLSSQyikfiiETQRRLQDEEKAAEKLKEEERkkmaEMQAELEKQKQLAEThak 1432
Cdd:pfam17380 359 KRELERIRQEEIAMEIS-RMRELERLQMERQ------QKNERVRQELEAARKVKILEE----ERQRKIQQQKVEMEQ--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1433 aIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHniQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEihiirlql 1512
Cdd:pfam17380 425 -IRAEQEEARQREVRRLEEERAREMERVRLEEQER--QQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQ-------- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1513 ettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF 1592
Cdd:pfam17380 493 -----RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340
....*....|....*....|...
gi 1207141751 1593 KLQAEEAERHLKQ--AELEKQRQ 1613
Cdd:pfam17380 567 RLEAMEREREMMRqiVESEKARA 589
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4183-4211 |
6.96e-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: 6.96e-07
10 20
....*....|....*....|....*....
gi 1207141751 4183 IVDPETGKEMSVYEAYRKGLIDHQTYIEL 4211
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1419-1901 |
7.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1419 ELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIqRELQELKTLSEQ---------EIKAKSQ 1489
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEyiklsefyeEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1490 QVEEALlsrTRIEEEIHIIRLQL----------ETTMKQKNTAETELLQLRAKAVDADKLRnAAQEEAEKLRKQVAEETQ 1559
Cdd:PRK03918 311 EIEKRL---SRLEEEINGIEERIkeleekeerlEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1560 KKRKAE-EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQA---------ELEKQRQIQVVEEVAKKTAATql 1629
Cdd:PRK03918 387 EKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEYTAELKRI-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1630 eSKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANK-KTAAQE 1708
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1709 EAEKQKEEAKREAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR 1786
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELlkELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1787 LKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQ 1866
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
490 500 510
....*....|....*....|....*....|....*...
gi 1207141751 1867 IAEEEAARQRAEAEKILK--EKLTAINEATR-LKTEAE 1901
Cdd:PRK03918 701 EELEEREKAKKELEKLEKalERVEELREKVKkYKALLK 738
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1539-1980 |
9.25e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1539 LRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVE 1618
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1619 EVAKKTAATQLESKQVALTARLEEsLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA--------EKELETWRQKANEAL 1690
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1691 RLRLQAEEEANKKTAAQEEAEKQKEEAkrEAKKRAKAEEAALKQKE------AAEMELGNQRKMAEETAKQKLAAEQELI 1764
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1765 RLRAD-FEHAEQQRTVLDDELQRLkndvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAK 1843
Cdd:COG4717 284 GLLALlFLLLAREKASLGKEAEEL----QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1844 MRELAEEAtkLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEND--RLKRKAEEE 1921
Cdd:COG4717 360 EEELQLEE--LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1922 GYQRKVLEDQAAQHKQAIEEKIGQLKK-SSDTELDRQKKIVEETLKQRKVVEEEIHILKL 1980
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1754-2461 |
9.37e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1754 KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKeTMSNTEKS 1833
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK-NIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1834 KQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE---EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1910
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKdniEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1911 NDRLKRKAEEegyqrkvLEDQAAQHKQAIE----EKIGQLKKSSDTELDRQKKIVEETlkQRKVVEEEIHILKLNfekas 1986
Cdd:TIGR04523 276 LEQNNKKIKE-------LEKQLNQLKSEISdlnnQKEQDWNKELKSELKNQEKKLEEI--QNQISQNNKIISQLN----- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1987 sgkqelelelkklkgiadetqkskakaeeeaekfrklaleeekkrkeaeakvKQIQAAEEEaarqhkaaqeevgRLMKLA 2066
Cdd:TIGR04523 342 ----------------------------------------------------EQISQLKKE-------------LTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2067 EEAKKQKEIAEKEAEKQVILVQEAAQKcsaaeQKAQNVLVQQNkdsmaqdKLKEEFEKAKKLAQEAEKAKDNAEKEAALL 2146
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYK-----QEIKNLESQIN-------DLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2147 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLaEKTLKQKssvEEE 2226
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE----------SLETQLKVLSRSINKI-KQNLEQK---QKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2227 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDllklklkiekENQELMKKDKDNTKKLLE 2306
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD----------LEDELNKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2307 EEAENMKKLAEEaarlnieaqeaarLRQIAESDLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2383
Cdd:TIGR04523 561 KEIDEKNKEIEE-------------LKQTQKSLKKKQEEKQELIDQkekEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2384 KLLEAKK---EMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2460
Cdd:TIGR04523 628 KLSSIIKnikSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLP 707
|
.
gi 1207141751 2461 K 2461
Cdd:TIGR04523 708 K 708
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2039-2224 |
1.15e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2039 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmAQDKL 2118
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---AEAKK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2119 KEEFEKAKKLAQEA-EKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALK 2197
Cdd:PRK09510 170 KAEAEAAKKAAAEAkKKAEAEAAAKAAAEAKKKAEAEA------------------KKKAAAEAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*..
gi 1207141751 2198 LKQEADSEMAKYKKLAEKTLKQKSSVE 2224
Cdd:PRK09510 232 AEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1768-2507 |
1.35e-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: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1768 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKsKAEKETMSNTEKSKQLLESEAAKMREL 1847
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQR-KAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1848 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIAlkEKEAENDRLKrkaeeegYQRKV 1927
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAENARLE-------MHFKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1928 LEDQaaqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAssgkQELELELKKLKGIADETQ 2007
Cdd:pfam05483 218 KEDH---------EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES----RDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2008 KskakaeeeaekfrklalEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEV----GRLMKLAEEAKKQKEIAEKEAEKQ 2083
Cdd:pfam05483 285 K-----------------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiatKTICQLTEEKEAQMEELNKAKAAH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2084 VILVQE-AAQKCSAAEQ-KAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAE 2161
Cdd:pfam05483 348 SFVVTEfEATTCSLEELlRTEQQRLEKNEDQLKI--ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2162 AeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQK 2241
Cdd:pfam05483 426 Q-----------FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2242 SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ----------MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEN 2311
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQeermlkqienLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2312 MKKLAEEAarlnIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKE 2391
Cdd:pfam05483 575 ARSIEYEV----LKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKALKKKGSAE--NKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2392 MQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK-----------KFKKQADEIkIRLQETE 2460
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmeKHKHQYDKI-IEERDSE 726
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2461 -----KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2507
Cdd:pfam05483 727 lglykNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2409-2631 |
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 1207141751 2409 AERKRQLEitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLH 2488
Cdd:COG4942 19 ADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2489 KAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQ--QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2566
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2567 EALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENK 2631
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1438-1782 |
1.52e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1438 EQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSeqeikAKSQQVEEALLSRTRIEEEIHIIRLQlETTMK 1517
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERRQKRLQ-EALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1518 QKNTAETellQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE--LKRKSEAEKDAAKEKKKALEDLEKFKLQ 1595
Cdd:pfam02029 86 QKEFDPT---IADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1596 AEEAERHLKQAEL-EKQRQIQVVEEVAKKTAATQLESKQVALTarlEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQ 1674
Cdd:pfam02029 163 SEEAEEVPTENFAkEEVKDEKIKKEKKVKYESKVFLDQKRGHP---EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1675 AEKELETwrQKANEALRLRLQA--EEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEET 1752
Cdd:pfam02029 240 AEVFLEA--EQKLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE----RKLREEE 313
|
330 340 350
....*....|....*....|....*....|
gi 1207141751 1753 AKQKLaaEQELIRLRAdfEHAEQQRTVLDD 1782
Cdd:pfam02029 314 EKRRM--KEEIERRRA--EAAEKRQKLPED 339
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1773-1943 |
1.54e-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: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1773 AEQQRTVLDdeLQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLESEAAKMRELAEEAT 1852
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1853 KLrsvAEEAKKQRQIA-----EEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKV 1927
Cdd:COG1579 80 EQ---LGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1207141751 1928 LEDQAAQHKQAIEEKI 1943
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2432-2647 |
1.63e-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: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2432 SDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQ 2511
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2512 SKEmanvQQEQLQQEKTILQQSFFAEKETLL------KKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERK 2585
Cdd:COG4942 99 LEA----QKEELAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2586 KLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKAS 2647
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1755-1950 |
1.66e-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: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1755 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSK 1834
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1835 Q-----------LLESEAAKmrELAEEATKLRSVAEEAKK---QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 1900
Cdd:COG3883 96 YrsggsvsyldvLLGSESFS--DFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1901 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSS 1950
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1796-1943 |
1.76e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.11 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1796 KQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSV---------AEEAKKQRQ 1866
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEAnaerevqrqLEIAERERE 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 1867 IAEEEAARQRAEAEKILKEKLTAinEATRLKTEAEialKEKEAENDRLKRKAEEEGYQRKVlEDQAAQHKQAIEEKI 1943
Cdd:COG2268 292 IELQEKEAEREEAELEADVRKPA--EAEKQAAEAE---AEAEAEAIRAKGLAEAEGKRALA-EAWNKLGDAAILLML 362
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1779-1979 |
1.97e-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: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1779 VLDDelQRLKNDVNSAVKQKKEL---EEELIKVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAA--KMRELA 1848
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDLeraHEALEDAREQIELLepireLAERYAAARERLAELEYLRAALRLWFAqrRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1849 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA----INEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 1924
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 1925 ----RKVLEDQAAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 1979
Cdd:COG4913 375 lpasAEEFAALRAEAAALLEA-LEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
659-751 |
2.00e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 659 HAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTA 738
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1207141751 739 ALQTQWSWILQLC 751
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2308-2450 |
2.31e-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: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2308 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQkDQAQVEA- 2382
Cdd:COG2268 187 DALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAEleqeREIETARIAEAEAELAKKKAEERREA-ETARAEAe 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2383 QKLLEAKKEMQQRLDQETEgfqkslEAERKRQLEItAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2450
Cdd:COG2268 266 AAYEIAEANAEREVQRQLE------IAEREREIEL-QEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2327-2604 |
3.68e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.41 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2327 QEAARLRQIAE----SDLAKQR-ELAEKMLEEKKQAiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrlDQETE 2401
Cdd:PRK05035 433 QAKAEIRAIEQekkkAEEAKARfEARQARLEREKAA--REARHKKAAEARAAKDKDAVAAALARVKAKK------AAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2402 GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA----DEIKIRLQETEKHTSEKHTVVEKLEVQR 2477
Cdd:PRK05035 505 PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiarAKAKKAAQQAANAEAEEEVDPKKAAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2478 LQSKQEAdglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQ---QEQLQQEKTILQQSFFAEKETLlkkekaieeekkk 2554
Cdd:PRK05035 585 AIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARakaKKAEQQANAEPEEPVDPRKAAV------------- 648
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2555 lekqfEDEVKKAEALKAEQER--QRKLMEEERKKLQSAMDAAIKKQKEAEEE 2604
Cdd:PRK05035 649 -----AAAIARAKARKAAQQQanAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1431-1671 |
4.03e-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: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1431 AKAIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEallsrtrIEEEIHIIRL 1510
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1511 QLETTMKQKNTAETELLQLR---AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALE 1587
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1588 DLEKfKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQEEAEHLKKQQAE 1667
Cdd:COG4942 164 ALRA-ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAA 238
|
....
gi 1207141751 1668 ADKA 1671
Cdd:COG4942 239 AAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2297-2493 |
4.09e-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: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2297 DKDNTKKLLEEEAENMKKL--AEEAARlnIEAQEAARLRQI---------AESDLAKQREL--------AEKMLEEKKQA 2357
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLerAHEALE--DAREQIELLEPIrelaeryaaARERLAELEYLraalrlwfAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2358 I----QEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKvkvTQLSD 2433
Cdd:COG4913 297 LeelrAELARLEAELERLEARLDALR---EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2434 AQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAD 2493
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1794-2663 |
4.17e-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: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1794 AVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlRSVAEEAKKQRQIAEEEAA 1873
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITS-KEAQLESSREIVKSYENEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1874 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE-------------EGYQRKVLEDQaaQHKQAIE 1940
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyHNHQRTVREKE--RELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1941 EKIGQLKKSSdTELDRQKK--IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKA-KAEEEA 2017
Cdd:TIGR00606 326 RELEKLNKER-RLLNQEKTelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTlVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2018 EKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAK-KQKEIAEKEAEKQVILVQEAAQKCSA 2096
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKfVIKELQQLEGSSDRILELDQELRKAE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2097 AEqkaqnvLVQQNKDSMAQDKLKEEF----EKA---KKLAQEAEK-AKDNAEKEA-----ALLHKKAEEAERQKKAAEAE 2163
Cdd:TIGR00606 485 RE------LSKAEKNSLTETLKKEVKslqnEKAdldRKLRKLDQEmEQLNHHTTTrtqmeMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2164 AAKQAKAQEDAEKlRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSv 2243
Cdd:TIGR00606 559 SDELTSLLGYFPN-KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD- 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2244 LDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD------NTKKLLEEEAENMKKLAE 2317
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAElqefisDLQSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2318 EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKD--QAQVEAQKLLEAKKEMQQR 2395
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtiMPEEESAKVCLTDVTIMER 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2396 LDQETEGFQKSLEAERKR------QLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTV 2469
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKlqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2470 VE------KLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN-------VQQEQLQQEKTILQQSFFA 2536
Cdd:TIGR00606 877 GTnlqrrqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISsketsnkKAQDKVNDIKEKVKNIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2537 EKETllkkEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ----------------KE 2600
Cdd:TIGR00606 957 MKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqdnltlrkrenelKE 1032
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141751 2601 AEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEE 2663
Cdd:TIGR00606 1033 VEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1486-1735 |
4.89e-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: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1486 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1565
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1566 EELK-RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE----LEKQRQIQVVEEVAKKTAATQLESKQVALTARL 1640
Cdd:COG4942 97 AELEaQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkyLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1641 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKRE 1720
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA-----------------AAA 239
|
250
....*....|....*
gi 1207141751 1721 AKKRAKAEEAALKQK 1735
Cdd:COG4942 240 AERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1690-2108 |
4.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1690 LRLRLQAE-EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE------ETAKQKLAAEQE 1762
Cdd:COG4717 47 LLERLEKEaDELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEaeleelREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1763 LIRLRADFEHAEQQRTVLDDELQRLKN---DVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT--------- 1830
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaeeleelqq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1831 --EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAArQRAEAEKILKEKLTAINEATRLKTEAEIAL---- 1904
Cdd:COG4717 207 rlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1905 ------------KEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDT-----ELDRQKKIVEETLkQ 1967
Cdd:COG4717 286 lallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELEEEL-Q 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1968 RKVVEEEIHILkLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEE 2047
Cdd:COG4717 365 LEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 2048 AARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQ 2108
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELE----ELKAELRELAEEWAALKLALE 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2044-2588 |
5.09e-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: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2044 AEEEAARQHKAAQEEVGRLMKLAEEAkkQKEIAEKEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQ-------- 2115
Cdd:pfam05483 206 AENARLEMHFKLKEDHEKIQHLEEEY--KKEINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQleektklq 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2116 -DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE---KEASRRAEA 2191
Cdd:pfam05483 281 dENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2192 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVK----VQLDE-------------TDKQKSVLDVELKRLKQE 2254
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkeVELEElkkilaedeklldEKKQFEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2255 VSDAIKQKaqvEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQ 2334
Cdd:pfam05483 441 LIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVED-LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2335 IAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2414
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2415 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQ--ADEIKIRLQETEKHTSEK------HTVVEKLEVQRLQSKQEADG 2486
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQlnAYEIKVNKLELELASAKQkfeeiiDNYQKEIEDKKISEEKLLEE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2487 LHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2566
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
570 580
....*....|....*....|..
gi 1207141751 2567 EALKAEQERQRKLMEEERKKLQ 2588
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEKLK 773
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2238-2453 |
5.21e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2238 DKQKSVLDVELKRLKQEvsdaikqkAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE--AENMKKL 2315
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE--------QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2316 AEEAARLNIEAQeaarlrQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQr 2395
Cdd:PRK09510 141 AAAAAKAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA- 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2396 ldqetegfqkslEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2453
Cdd:PRK09510 214 ------------EAKKK------AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2173-2646 |
5.41e-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: 52.92 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2173 DAEKLRKEAEKEASRRAEAEAAALKLK---------QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqlDETDKQKSV 2243
Cdd:pfam12128 235 GIMKIRPEFTKLQQEFNTLESAELRLShlhfgyksdETLIASRQEERQETSAELNQLLRTLDDQWKEKR--DELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2244 LDVELKRLKQEVSDAIKQKAQVEDE-LSKVKIQMEDLLKLKLKIEKENQELmkkdkdntkKLLEEEAENMKKlAEEAARL 2322
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---------KALTGKHQDVTA-KYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2323 NIEAQEAARLRQIaESDLAKQRELAEKMLEEKKQAIQeaaKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET- 2400
Cdd:pfam12128 383 KIKEQNNRDIAGI-KDKLAKIREARDRQLAVAEDDLQ---ALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2401 --------EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEK-HTVVE 2471
Cdd:pfam12128 459 tpelllqlENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQaGTLLH 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2472 KLevqRLQSKQEADGLHKAIADLEKEKeklkkeaADLQKQSKEMANVQQEQLQQEKTILQQ----SFFAEKETLlkkeka 2547
Cdd:pfam12128 539 FL---RKEAPDWEQSIGKVISPELLHR-------TDLDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEEL------ 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2548 ieeekKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLA 2627
Cdd:pfam12128 603 -----RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK---NKALA 674
|
490
....*....|....*....
gi 1207141751 2628 EENKNLREKLQQLQSSQKA 2646
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQ 693
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2306-2442 |
5.53e-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: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2306 EEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA------------KLKAEAEKLQK 2373
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtsspkedkqvaeNQKREIEKAQI 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 2374 QKDQAQVEAQKLLEAKKE--MQQRLDQETEGFQKSLEAERKRqLEITAEAEKLKVKVtqlsDAQSKAEEEA 2442
Cdd:pfam05262 289 EIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQV----EAQPTSLNED 354
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1540-1755 |
5.60e-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: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1540 RNAAQEEAEKLRKQVAE----ETQKKRKAEEELKRkseAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQaELEKQRQIQ 1615
Cdd:pfam15709 328 REQEKASRDRLRAERAEmrrlEVERKRREQEEQRR---LQQEQLERAEKMREELELEQQRRFEEIRLRKQ-RLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1616 VVEEvakKTAATQLESKQVALTARLEESLKNEQvmviQLQEeaehlKKQQAEADKAREQAEKELETWRQKANEALRLRLQ 1695
Cdd:pfam15709 404 EEEE---RKQRLQLQAAQERARQQQEEFRRKLQ----ELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1696 AEEEankktaaqeEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQ 1755
Cdd:pfam15709 472 AEEE---------RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
177-285 |
5.90e-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: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 177 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIA 255
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|
gi 1207141751 256 ERDLGVTRLLDPEDVDVPHPDEKSIITYVS 285
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLS 107
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1719-2154 |
5.97e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1719 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1798
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1799 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 1878
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1879 AEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 1958
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1959 KIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKV 2038
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2039 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2118
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1207141751 2119 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAE 2154
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAAL 517
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1605-1825 |
6.36e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1605 QAELEKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvmviQLQEEaehlKKQQAEADKAREQAEKELETWRQ 1684
Cdd:PRK09510 74 AKRAEEQRKKKE------QQQAEELQQKQAAEQERLKQLEKERL----AAQEQ----KKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1685 KANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEli 1764
Cdd:PRK09510 140 KAAAAAKAKAEAEAKR-----------------AAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK-- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 1765 rlradfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1825
Cdd:PRK09510 201 ------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1653-1942 |
6.43e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1653 QLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLR-----LQ---AEEEANKKTAAQEEAEKQKEEAKREAKKR 1724
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREELAEEVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1725 AKAEEAAL----------------KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLK 1788
Cdd:PRK02224 297 DLLAEAGLddadaeavearreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1789 NDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnteksKQLLESEAAKMRE-LAEEATKLRSVAEEAKKQRQI 1867
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF--------LEELREERDELRErEAELEATLRTARERVEEAEAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1868 AEE-----------------EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEnDRLKRKAEeegyQRKVLED 1930
Cdd:PRK02224 449 LEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE----RREDLEE 523
|
330
....*....|..
gi 1207141751 1931 QAAQHKQAIEEK 1942
Cdd:PRK02224 524 LIAERRETIEEK 535
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
51-176 |
6.72e-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: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 51 ERDRVQKKTFTKWVNKHLVKHWkaeaqrhITDLYEDLRDGHNLISLLEVLSgetLPRERDVVRNSRLPREKGRMRfhKLQ 130
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141751 131 NVQIALDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 176
Cdd:cd21329 70 NCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1152-1812 |
7.27e-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: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1152 AEDILNKYENQLREVNKVPVNEKEI-EASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQ 1230
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1231 L------------VGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYD----------WLIRWIADAKQRQDKLHAVP 1288
Cdd:TIGR00606 504 KslqnekadldrkLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiksrhsdeltSLLGYFPNKKQLEDWLHSKS 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1289 iGGSKGLQEQLTQEKKLLEEIEKNKD--------KVEDCQKFAKGYIDAIKDYELQlVTYKALVEPIASPLKKAKMESAS 1360
Cdd:TIGR00606 584 -KEINQTRDRLAKLNKELASLEQNKNhinnelesKEEQLSSYEDKLFDVCGSQDEE-SDLERLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1361 DDIIQEYVTLRTRYSE----LMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAK 1436
Cdd:TIGR00606 662 TAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1437 AEQEANELKTKMkdevskrQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTM 1516
Cdd:TIGR00606 742 KEKEIPELRNKL-------QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1517 KQKNTAETELLQLRAKAVDAD-KLRNAAQ--EEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1593
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQhELDTVVSkiELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1594 LQAEEAERHLKQAElekqrqiqvVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHL--------KKQQ 1665
Cdd:TIGR00606 895 TEVQSLIREIKDAK---------EQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdieNKIQ 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1666 AEADKAREQAEKELETWRQKANEALRLRLQAEEEankktaaqeeaekqkEEAKREAKKRAKAEEAALkQKEAAEMELGNQ 1745
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLEECEKHQEKINED---------------MRLMRQDIDTQKIQERWL-QDNLTLRKRENE 1029
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 1746 RKMAEETAKQKLAAEQELIRLRADFEHAEqqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1812
Cdd:TIGR00606 1030 LKEVEEELKQHLKEMGQMQVLQMKQEHQK-----LEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1442-1989 |
7.27e-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: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1442 NELKTKmKDEVSKRQDVAVDSEKQKHNIQRELQELKTlSEQEIKAKSQQVEEALlsrTRIEEEIHIIRLQLETTMKQKNT 1521
Cdd:TIGR04523 47 NELKNK-EKELKNLDKNLNKDEEKINNSNNKIKILEQ-QIKDLNDKLKKNKDKI---NKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1522 AETELLQLRAKAvdadklrnaaqEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1601
Cdd:TIGR04523 122 LEVELNKLEKQK-----------KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1602 HLKQAELEKQRQIQVVEEvakktaatqLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAeKELET 1681
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKK---------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL-NQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1682 WRQKANEALRLRLQAEEEANKKTAAQEEAEkqkeeakreakKRAKAEEAALKQKEAAEMelgnQRKMAEETAKQklaaEQ 1761
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQL-----------NQLKSEISDLNNQKEQDW----NKELKSELKNQ----EK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1762 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKaEKETMSNTEKSKQLLESea 1841
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-YKQEIKNLESQINDLES-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1842 aKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEkltaINEATRLKTEAEIALKEKEAENDRLKRKAEEE 1921
Cdd:TIGR04523 399 -KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 1922 GYQRKVLEDQAAQHKQAIEEKIGQLKKssdteLDRQKKIVEETLkqrKVVEEEIHILKLNFEKASSGK 1989
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKK-----LNEEKKELEEKV---KDLTKKISSLKEKIEKLESEK 533
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2224-2653 |
7.42e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2224 EEELVKVKVQLDETDKQKSvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKK 2303
Cdd:PRK02224 212 ESELAELDEEIERYEEQRE----QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2304 LLEEEAENMKKLAE-EAARLNIEAQEAARlrqiaeSDLAKQRELAEKMLEEKKQAIQEAAKlkaEAEKLQKQKDQAQVEA 2382
Cdd:PRK02224 288 LEELEEERDDLLAEaGLDDADAEAVEARR------EELEDRDEELRDRLEECRVAAQAHNE---EAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2383 QKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKH 2462
Cdd:PRK02224 359 EELREEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2463 TSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLqkqSKEMANVQQEQLQQEKTILQQSFFAEketll 2542
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEEL---EAELEDLEEEVEEVEERLERAEDLVE----- 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2543 kkekaieeekkkLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQ 2622
Cdd:PRK02224 507 ------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
410 420 430
....*....|....*....|....*....|....*
gi 1207141751 2623 EKLLAE--ENKNLREKLQQLQSSQK--ASYTKEIE 2653
Cdd:PRK02224 575 AELNSKlaELKERIESLERIRTLLAaiADAEDEIE 609
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2206-2414 |
7.99e-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: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2206 MAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAikQKAQVEDELSKVKIQMEdllklklk 2285
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE--KAAKQAEQAAKQAEEKQ-------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2286 iekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARL-----NIEAQEAARLRQ-----IAESDLAKQRELAEKMLEEKK 2355
Cdd:TIGR02794 119 ----KQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQaeeeaKAKAAAEAKKKAeeakkKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 2356 QAIQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2414
Cdd:TIGR02794 195 KAKAEAAKAKAAAE--AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1353-1929 |
8.00e-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: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1353 KAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELE----KQKQLAE 1428
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1429 THAKAIAK--AEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEqEIKAKSQQVEEALLS-----RTRI 1501
Cdd:pfam05557 88 LNKKLNEKesQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNlekqqSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1502 EEEIHIIRLQLETTMKQKNTAETELLQLR-AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAeEELKRKSEAEKDAAK 1580
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIENKLLLKEEV-EDLKRKLEREEKYRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1581 EKKKALEDLEKFKLQAEEAERhlkqaeLEKQRQIQVVEEVAKKTAATQLESKQVALTAR---LEESLKNEQVMVIQLQEE 1657
Cdd:pfam05557 246 EAATLELEKEKLEQELQSWVK------LAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEnssLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1658 AEHLKKQQAEADKAREQAEKELETWRQKANEALRLR--LQAEEEANKKTAAQEEAEKQKEEAKREAKK---RAKAEEAAL 1732
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgYRAILESYDKELTMSNYSPQLLERIEEAEDmtqKMQAHNEEM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1733 K-QKEAAEMELGNQRKMAEetakqklAAEQELIRLRADFEHAEQQRTvlddelqrlKNDVNSAVKQKKELEEELIKVRKE 1811
Cdd:pfam05557 400 EaQLSVAEEELGGYKQQAQ-------TLERELQALRQQESLADPSYS---------KEEVDSLRRKLETLELERQRLREQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1812 MEILLQQKSKAEKETMSNTEKSK--QLLESEAAKMRE-LAEEATKLRsvaeeakkqrqiAEEEAARQRAEAEKILKEKLT 1888
Cdd:pfam05557 464 KNELEMELERRCLQGDYDPKKTKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVL 531
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1207141751 1889 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLE 1929
Cdd:pfam05557 532 RLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1636-1974 |
8.97e-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: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1636 LTARLEESLkneqvmviqlQEEAEHLKKQQAeadkAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqke 1715
Cdd:pfam07888 32 LQNRLEECL----------QERAELLQAQEA----ANRQREKEKERYKRDREQWERQRRELESRVAELKEEL-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1716 eakreAKKRAKAEEAALKQKEAAEMelgnQRKMAEETA---KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1792
Cdd:pfam07888 90 -----RQSREKHEELEEKYKELSAS----SEELSEEKDallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1793 SAVKQKKELEEElikvRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAkkQRQIAEEEA 1872
Cdd:pfam07888 161 KAGAQRKEEEAE----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA--HRKEAENEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1873 ARQRAEAekiLKEKLTAINEATR-LKTEaeiaLKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ------ 1945
Cdd:pfam07888 235 LLEELRS---LQERLNASERKVEgLGEE----LSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARwaqere 307
|
330 340 350
....*....|....*....|....*....|
gi 1207141751 1946 -LKKSSDTELDRQKKIVEETLKQRKVVEEE 1974
Cdd:pfam07888 308 tLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2291-2658 |
9.17e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2291 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES--DLAKQRELAEKMLEEKKQAIQ------EAA 2362
Cdd:COG4717 56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQllplyqELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2363 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2442
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2443 KKFKKQADEIKIRLQETEKhTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA--------------DL 2508
Cdd:COG4717 216 EEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallfllLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2509 QKQSKEMANVQQEQLQQEKTILQQsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-----EALKAEQERQRKLMEEE 2583
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEE---EELEELLAALGLPPDLSPEELLELLDRIEELqellrEAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2584 RKKLQSAMDA-----------AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENknLREKLQQLQSSQKASYTKEI 2652
Cdd:COG4717 372 IAALLAEAGVedeeelraaleQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELE 449
|
....*.
gi 1207141751 2653 EIQTDK 2658
Cdd:COG4717 450 ELREEL 455
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2509-2675 |
9.44e-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: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2509 QKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2588
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2589 SAMDaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKnlREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT 2668
Cdd:pfam15709 434 ELQR---KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE--EERLEYQRQKQEAEEKARLEAEERRQKEEEAARLA 508
|
....*..
gi 1207141751 2669 MVETTKK 2675
Cdd:pfam15709 509 LEEAMKQ 515
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1441-1901 |
9.50e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1441 ANELKTKMKDEVSKRQDVA-----VDSEKQKHN-IQRELQELK---TLSEQEIKAKS---QQVEEALLSRTRIE---EEI 1505
Cdd:PRK04863 278 ANERRVHLEEALELRRELYtsrrqLAAEQYRLVeMARELAELNeaeSDLEQDYQAASdhlNLVQTALRQQEKIEryqADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1506 HIIRLQLETTMKQKNTAETELLQLRAKAvdadklrNAAQEEAEKLRKQVAEETQkkrkAEEELKRKSeaekdaakekkka 1585
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARA-------EAAEEEVDELKSQLADYQQ----ALDVQQTRA------------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1586 ledlekfkLQAEEAerhlKQAeLEKQRQIQVVEEVAKKTAATQLEskqvALTARLEEslkneqvmviqLQEEAEHLKKQQ 1665
Cdd:PRK04863 414 --------IQYQQA----VQA-LERAKQLCGLPDLTADNAEDWLE----EFQAKEQE-----------ATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1666 AEADKAREQAEKELETWRQKANEALRLrlQAEEEAnkktaaqeeaekqkeeakREAKKRAKAEEAALKQKEAAEMELGnq 1745
Cdd:PRK04863 466 SVAQAAHSQFEQAYQLVRKIAGEVSRS--EAWDVA------------------RELLRRLREQRHLAEQLQQLRMRLS-- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1746 rkmaeeTAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEillQQKSKAEKE 1825
Cdd:PRK04863 524 ------ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALR---QQLEQLQAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1826 TMSNTEKSKQLLESEAA--KMRELAEEATK--------LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR 1895
Cdd:PRK04863 595 IQRLAARAPAWLAAQDAlaRLREQSGEEFEdsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPR 674
|
....*.
gi 1207141751 1896 LKTEAE 1901
Cdd:PRK04863 675 LNALAE 680
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2292-2466 |
9.69e-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: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2292 ELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEA--E 2369
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2370 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQEtegfqksLEAERKRQLEItAEAEKLKVKvTQLSDAQSKAEEEAKKFKKQA 2449
Cdd:pfam15709 431 KLQELQRKKQQEEAERAEAEKQRQKELEMQ-------LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEERRQKE 501
|
170
....*....|....*...
gi 1207141751 2450 DE-IKIRLQETEKHTSEK 2466
Cdd:pfam15709 502 EEaARLALEEAMKQAQEQ 519
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1812-2144 |
1.02e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1812 MEILLQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklrsVAEEAKKQRQIAEEEAARQRAeaekiLKEKLTAIN 1891
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQ------ERLRQEKEE------KAREVERRRKLEEAEKARQAE-----MDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1892 EATRLKTEAE-----IALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQlkkssDTELDRQKKIVEETlK 1966
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ-----ELEAARKVKILEEE-R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1967 QRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLalEEEKKRKEAEAKVKQIQAAEE 2046
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ--EEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2047 EAARQHKAAQEEVGRLMKLAEEAKKQKeIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEFEKA 2125
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRK-LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQmRKATEERSRL 568
|
330
....*....|....*....
gi 1207141751 2126 KKLAQEAEKAKDNAEKEAA 2144
Cdd:pfam17380 569 EAMEREREMMRQIVESEKA 587
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1618-1840 |
1.07e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1618 EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQA- 1696
Cdd:pfam15709 317 EEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRl 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1697 ------EEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEEtaKQKLAAEQELIRLRADF 1770
Cdd:pfam15709 397 eeerqrQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKEL--EMQLAEEQKRLMEMAEE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1771 EHAEQQRtvlddelqrlkndvnsavkQKKELEEeliKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESE 1840
Cdd:pfam15709 475 ERLEYQR-------------------QKQEAEE---KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1422-1813 |
1.15e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1422 KQKQLAEThAKAIAKAEQEANELKTKMKDevsKRQDVavdSEKQKHniqreLQELKTLSEQEIKAKSQQVEEALL----- 1496
Cdd:PRK10246 438 QQKRLAQL-QVAIQNVTQEQTQRNAALNE---MRQRY---KEKTQQ-----LADVKTICEQEARIKDLEAQRAQLqagqp 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1497 -------SRTRIEE----EIHIIRLQLETTMKQKNTAETELLQLRAKaVDAdklrnaaqeeaekLRKQV---AEETQKKR 1562
Cdd:PRK10246 506 cplcgstSHPAVEAyqalEPGVNQSRLDALEKEVKKLGEEGAALRGQ-LDA-------------LTKQLqrdESEAQSLR 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1563 KAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT-QLESKQVALTARLE 1641
Cdd:PRK10246 572 QEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1642 E-SLK-----NEQVMVIQLQEEAEHLKKQQAEADKAREQ---------------------AEKELETWRQKANEALRLR- 1693
Cdd:PRK10246 652 GyALTlpqedEEASWLATRQQEAQSWQQRQNELTALQNRiqqltplletlpqsddlphseETVALDNWRQVHEQCLSLHs 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1694 ---------LQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE---ETAKQKLAAEQ 1761
Cdd:PRK10246 732 qlqtlqqqdVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQtlvTQTAQALAQHQ 811
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 1762 ----ELIRLRADFEHAEQQRTVLDDEL-----------QRLKNDVNSAvKQKKELEEELIKVRKEME 1813
Cdd:PRK10246 812 qhrpDGLDLTVTVEQIQQELAQLAQQLrenttrqgeirQQLKQDADNR-QQQQALMQQIAQATQQVE 877
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2175-2447 |
1.15e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2175 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKV---KVQLDETDKQKSVLDVELKRL 2251
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2252 KQEVSDAIKQKAQVeDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAAR 2331
Cdd:COG1340 98 RKELAELNKAGGSI-DKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2332 LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAER 2411
Cdd:COG1340 175 EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELKKLR 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207141751 2412 KRQLEITAEAEKlkvkvtqlSDAQSKAEEEAKKFKK 2447
Cdd:COG1340 251 KKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1758-1957 |
1.20e-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: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1758 AAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLL 1837
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQA----EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1838 ESEA--AKMRELAEEATKLRSVAEEAKKQRQI-----AEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAE 1910
Cdd:TIGR02794 123 EAKAkqAAEAKAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141751 1911 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQ 1957
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2214-2618 |
1.20e-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: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2214 EKTLKQKSSVEEELVKVKVQLDETDKQK-----SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEK 2288
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2289 ENQELMKKDKDNTKKLLEEEAEN------MKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA 2362
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2363 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2442
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV----LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2443 KKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQE--ADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQ 2520
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2521 EQLQQEKTILQQsfFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKE 2600
Cdd:TIGR04523 593 QKEKEKKDLIKE--IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
410
....*....|....*...
gi 1207141751 2601 AEEEMNGKQKEMQDLEKK 2618
Cdd:TIGR04523 671 SKTKIDDIIELMKDWLKE 688
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2199-2394 |
1.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2199 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMED 2278
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2279 LLKLKLKIEK-----------ENQELMKKDKDNTKKLLEE------EAENMK-KLAEEAARLNIEAQEAARLRQIAESDL 2340
Cdd:COG3883 98 SGGSVSYLDVllgsesfsdflDRLSALSKIADADADLLEElkadkaELEAKKaELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2341 AKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQ 2394
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1659-1945 |
1.52e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 51.13 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1659 EHLKKQQAEadKAREQAEKELetwrqKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAAL-KQKEA 1737
Cdd:PRK07735 8 EDLKKEAAR--RAKEEARKRL-----VAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALaKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1738 A-----EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1812
Cdd:PRK07735 81 GteevtEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1813 EILLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKKqrqiaeeeAARQRAEAEKILKEKLTAIN- 1891
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQ----KAAEAGEGTEEVTEEEKAKAKAKA--------AAAAKAKAAALAKQKASQGNg 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141751 1892 --EATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA-------QHKQAIEEKIGQ 1945
Cdd:PRK07735 229 dsGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEEPSvnqpylnKYVEVIKEKLGE 291
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1153-1959 |
1.57e-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: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1153 EDILNKYENQLREVNKVPVN-EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkRMSQLHSERDVELEHYRQL 1231
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKlEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLEEETAQKNNALKKIREL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1232 VGNLRE------RWQAVFAQIELRQREldlLNRQMQAYR-ESYDWLirwiaDAKQRQDKLHavpiggSKGLQEqLTQEKK 1304
Cdd:pfam01576 270 EAQISElqedleSERAARNKAEKQRRD---LGEELEALKtELEDTL-----DTTAAQQELR------SKREQE-VTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1305 LLEEIEKNKD-KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQ 1383
Cdd:pfam01576 335 ALEEETRSHEaQLQEMRQKHTQALEELTEQLEQAKRNKANLEK-----AKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1384 YIKFIIETQRRLQDEEKAaeklKEEERKKMAEMQAELEK---------------QKQLA---------------ETHAK- 1432
Cdd:pfam01576 410 LEGQLQELQARLSESERQ----RAELAEKLSKLQSELESvssllneaegkniklSKDVSslesqlqdtqellqeETRQKl 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1433 ----AIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELKTLSEQEikakSQQVEEALLSRTRIEEEIHII 1508
Cdd:pfam01576 486 nlstRLRQLEDERNSLQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEED----AGTLEALEEGKKRLQRELEAL 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1509 RLQLETTM-------KQKNTAETELLQLrakAVDADKLR---NAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDA 1578
Cdd:pfam01576 558 TQQLEEKAaaydkleKTKNRLQQELDDL---LVDLDHQRqlvSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1579 AKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKtaATQLESKQVALTARLEEslkneqvMVIQLQEEA 1658
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKN--VHELERSKRALEQQVEE-------MKTQLEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1659 EHLkkqqaeadKAREQAEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakrEAKKRakaeeAALKQKEAA 1738
Cdd:pfam01576 706 DEL--------QATEDAKLRLEVNMQALKAQFERDLQARDEQG------------------EEKRR-----QLVKQVREL 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1739 EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlDDELQRLKNdvnsAVKQKKELEEELIKVRKEM-EILLQ 1817
Cdd:pfam01576 755 EAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGR---EEAVKQLKK----LQAQMKDLQRELEEARASRdEILAQ 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1818 QKskaeketmsNTEKSKQLLESEAAKMRELAeeatklrSVAEEAKKQRQIAEEEAARQRAEAekiLKEKLTAINEATRLk 1897
Cdd:pfam01576 828 SK---------ESEKKLKNLEAELLQLQEDL-------AASERARRQAQQERDELADEIASG---ASGKSALQDEKRRL- 887
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 1898 tEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKK 1959
Cdd:pfam01576 888 -EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNK 948
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1434-1700 |
1.58e-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: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1434 IAKAEQEaNELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQElktlsEQEIKAKsQQVEEALLSRTRIEEEIhiirlqle 1513
Cdd:pfam15709 325 LEKREQE-KASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ-----EQLERAE-KMREELELEQQRRFEEI-------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1514 ttmkqkntaetellQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtqKKRKAEEELKRKSEAEKDaakekkkaledlekfK 1593
Cdd:pfam15709 390 --------------RLRKQRLEEERQRQEEEERKQRLQLQAAQE--RARQQQEEFRRKLQELQR---------------K 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1594 LQAEEAERhlkqAELEKQRQIQvveevakktaatqleskqvaltarLEESLKNEQVMVIQLQEEA--EHLKKQQAEADKA 1671
Cdd:pfam15709 439 KQQEEAER----AEAEKQRQKE------------------------LEMQLAEEQKRLMEMAEEErlEYQRQKQEAEEKA 490
|
250 260 270
....*....|....*....|....*....|....
gi 1207141751 1672 REQAEKEletwRQKANEALRLRL-----QAEEEA 1700
Cdd:pfam15709 491 RLEAEER----RQKEEEAARLALeeamkQAQEQA 520
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1604-1760 |
1.60e-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: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1604 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1683
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1684 QKANEALRLRLQAE------EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKL 1757
Cdd:TIGR02794 126 AKQAAEAKAKAEAEaerkakEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
...
gi 1207141751 1758 AAE 1760
Cdd:TIGR02794 206 AAE 208
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1590-1892 |
1.70e-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: 50.30 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1590 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLK-NEQVMVIQLQEEAEHLKKQQAEA 1668
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1669 DKaREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1748
Cdd:pfam13868 123 EK-QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1749 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMS 1828
Cdd:pfam13868 202 ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 1829 NTEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINE 1892
Cdd:pfam13868 280 EAEKRRMKRLEHRRELEKQIEEREEQR--AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
210-286 |
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 1207141751 210 DNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSiAERDLGVTRLLDPEDVDVPHPDEKSIITYVSS 286
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQ 95
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1594-2461 |
1.74e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1594 LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvALTARlEESLKNEQVMVIQLQEEAEHLKKQQAEADKARE 1673
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRD-QITSK-EAQLESSREIVKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1674 ---QAEKELETWRQKANEALRLRLQAEEEAnKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEaaeMELGNQRKMAE 1750
Cdd:TIGR00606 263 kimKLDNEIKALKSRKKQMEKDNSELELKM-EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1751 ETAKQKLAAEQELIRLRADFEH-------AEQQRTVLDDELQRLKND------VNSAVKQKKELEEELIKVRKEMEILLQ 1817
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQehirardSLIQSLATRLELDGFERGpfserqIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1818 QKSKAEKETMSNTE-KSKQLLESEAAKMRELAEEATKLRSVAEEAKK----QRQIAEEEAARQRAEAEKILKEKltaiNE 1892
Cdd:TIGR00606 419 SKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQELRKAERELSKAEK----NS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1893 ATRLKTEAEIALKEKEAENDRLKRKAEEEGYQR------KVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQ------KKI 1960
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnKKQ 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1961 VEETL----KQRKVVEEEIHILKLNFEKASSGKQELELelkklkgiaDETQKSKAKAEEEAEKFRklaleeekkrkeaea 2036
Cdd:TIGR00606 575 LEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINN---------ELESKEEQLSSYEDKLFD--------------- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2037 kvkqiqaaeeeaARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSA----------AEQKAQNVLV 2106
Cdd:TIGR00606 631 ------------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAELQEFIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2107 Q-QNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEkea 2185
Cdd:TIGR00606 699 DlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG--- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2186 srraeAEAAALKLKQEADSEMAKYKKLAEKTlkqkSSVEEELVKVKVQLDETDKQKSVLDV-ELKRLKQEVSDAIKQKAQ 2264
Cdd:TIGR00606 776 -----TIMPEEESAKVCLTDVTIMERFQMEL----KDVERKIAQQAAKLQGSDLDRTVQQVnQEKQEKQHELDTVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2265 VEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQR 2344
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2345 ELAEKMLEEKKQAIQEAAKLKAEAE--------------------KLQKQKDQAQVEAQklLEAKKEMQQRLDQETEGFQ 2404
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVKnihgymkdienkiqdgkddyLKQKETELNTVNAQ--LEECEKHQEKINEDMRLMR 1004
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2405 KSLEAERKR------QLEITAEAEKLK---------------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEK 2461
Cdd:TIGR00606 1005 QDIDTQKIQerwlqdNLTLRKRENELKeveeelkqhlkemgqMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4176-4204 |
1.78e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.78e-05
10 20
....*....|....*....|....*....
gi 1207141751 4176 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4204
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1463-1942 |
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 1207141751 1463 EKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNA 1542
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1543 AQ--EEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfklQAEEAERHLKQAELEKQRQIqvveev 1620
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEELEERLEELR----------------------ELEEELEELEAELAELQEEL------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1621 akktaATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEK-ELETWRQKANEALR-------- 1691
Cdd:COG4717 180 -----EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKearlllli 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1692 ----------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1761
Cdd:COG4717 255 aaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1762 ELIRLRADFEHAEQQRTvLDDELQRLKNDVNSAVkQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQL---LE 1838
Cdd:COG4717 335 SPEELLELLDRIEELQE-LLREAEELEEELQLEE-LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELeeqLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1839 SEAAKMRELAEEATKlrsvaEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKA 1918
Cdd:COG4717 413 ELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
490 500
....*....|....*....|....*
gi 1207141751 1919 EEEGYQRKVLEDQA-AQHKQAIEEK 1942
Cdd:COG4717 488 LAEEWAALKLALELlEEAREEYREE 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1174-1863 |
1.85e-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: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1174 KEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE-VNKRMSQL-HSERdveLEHYRQLVGNLRERWQAVFAQIELRQR 1251
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhLNLVQTALrQQEK---IERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1252 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQeQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1331
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1332 DYELQLVTY------------KA--LVEPIASPLKKAKMESASDDIIQEY----------VTLRTRYSELMTLSSQYikf 1387
Cdd:COG3096 455 EEVLELEQKlsvadaarrqfeKAyeLVCKIAGEVERSQAWQTARELLRRYrsqqalaqrlQQLRAQLAELEQRLRQQ--- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1388 iiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQK-QLAETHAKAIAKA---EQEANELKTKMKdEVSKRQDVAVDSE 1463
Cdd:COG3096 532 --QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLeELEEQAAEAVEQRselRQQLEQLRARIK-ELAARAPAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1464 KQKHNIQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTA----ETELLQLR--------A 1531
Cdd:COG3096 609 DALERLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPggaeDPRLLALAerlggvllS 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1532 KAVDADKLRNAAQEEA--------------EKLRKQVAE-------------------------ETQKKR---KAEEELK 1569
Cdd:COG3096 688 EIYDDVTLEDAPYFSAlygparhaivvpdlSAVKEQLAGledcpedlyliegdpdsfddsvfdaEELEDAvvvKLSDRQW 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1570 RKSEAEKDAAKEKKKALEDLEKFKLQAEE-AERHLKQA-ELEK-QR-----------QIQVVEEVAKKTAATQLESKQVA 1635
Cdd:COG3096 768 RYSRFPEVPLFGRAAREKRLEELRAERDElAEQYAKASfDVQKlQRlhqafsqfvggHLAVAFAPDPEAELAALRQRRSE 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1636 LTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA------NKKTAAQEE 1709
Cdd:COG3096 848 LERELAQHRAQEQ----QLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLE 923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1710 AEK-------QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRK-MAEETAKQKLAAEQELI-RLRADFEHAEQQRTVL 1780
Cdd:COG3096 924 PLVavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAEEARREA 1003
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1781 DDELQRLKNDVNSA------------VKQK--KELEEEL----IKVRKEMEIL-------LQQKSKAEKETMSNTEKSKQ 1835
Cdd:COG3096 1004 REQLRQAQAQYSQYnqvlaslkssrdAKQQtlQELEQELeelgVQADAEAEERarirrdeLHEELSQNRSRRSQLEKQLT 1083
|
810 820 830
....*....|....*....|....*....|..
gi 1207141751 1836 LLESEAA----KMRELAEEATKLRSVAEEAKK 1863
Cdd:COG3096 1084 RCEAEMDslqkRLRKAERDYKQEREQVVQAKA 1115
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1171-1341 |
1.95e-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: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1171 VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ----RATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQI 1246
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAaheeRVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1247 ELRQRELDLLNRQMQAYRESYDwLIRWIADAKQRQDKLhaVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGY 1326
Cdd:cd00176 96 EERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEEL 172
|
170
....*....|....*
gi 1207141751 1327 IDAIKDYELQLVTYK 1341
Cdd:cd00176 173 LEEGHPDADEEIEEK 187
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1635-1941 |
1.99e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1635 ALTARLE-----ESLKNEQVMVIQLQEEAEhlkkQQAEADKAREQAEKELETWRQKANEALRLRLQ---AEEEANKKTaa 1706
Cdd:PRK04863 288 ALELRRElytsrRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAASDHLNLVQTALRQQEKierYQADLEELE-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1707 qeeaekqkeeakreakkrAKAEEAALKQKEAAEmelgnQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD 1781
Cdd:PRK04863 362 ------------------ERLEEQNEVVEEADE-----QQEENEA---RAEAAEEEVDELKsqlADYQQAldVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1782 --------DELQRLKNDVNSAVKQKKELEEELikVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAAKM---- 1844
Cdd:PRK04863 416 yqqavqalERAKQLCGLPDLTADNAEDWLEEF--QAKEQEATeellsLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrse 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1845 -----RELAEEATKLRSVAEEAK---------KQRQIAEEEAARQRAEAEKILKEKLTAINEATRLkteaeiaLKEKEAE 1910
Cdd:PRK04863 494 awdvaRELLRRLREQRHLAEQLQqlrmrlselEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-------QEELEAR 566
|
330 340 350
....*....|....*....|....*....|.
gi 1207141751 1911 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1941
Cdd:PRK04863 567 LESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1687-1919 |
2.05e-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: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1687 NEALRLRLQAEEEANKKTAaqeeaEKQKEEAKREAKKRAKAEEAALKQkeaaEMELGNQRKMAEETAKQKLAAEQeliRL 1766
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ----EREIETARIAEAEAELAKKKAEE---RR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1767 RADFEHAEQQRTVlddELQRlkndvnsaVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqllESEAAKMRE 1846
Cdd:COG2268 256 EAETARAEAEAAY---EIAE--------ANAEREVQRQLEIAEREREIELQEKEAEREE------------AELEADVRK 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141751 1847 LAeeatklrsvaeEAKKQRQIAEEEaarqrAEAEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 1919
Cdd:COG2268 313 PA-----------EAEKQAAEAEAE-----AEAEAI-RAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE 368
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1413-1568 |
2.10e-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: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1413 MAEMQAELEKQKQLAETHA-KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKAKSQQV 1491
Cdd:COG2268 194 IAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAK---KKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1492 EEALLSRTrIEEEIHIIRLQLETTMKQKNtAETELLQLRA---KAVDADKLRNAAQEEAE------KLRKQvAEETQKKR 1562
Cdd:COG2268 271 AEANAERE-VQRQLEIAEREREIELQEKE-AEREEAELEAdvrKPAEAEKQAAEAEAEAEaeairaKGLAE-AEGKRALA 347
|
....*.
gi 1207141751 1563 KAEEEL 1568
Cdd:COG2268 348 EAWNKL 353
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2039-2445 |
2.12e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.21 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2039 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEK--QVI-----LVQEAAQKCSAAEQKAQNVLVQQNKD 2111
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqQVIdnfpkLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2112 SMAQDKLK---EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedAEKLRKEAEKEasrr 2188
Cdd:PRK10929 106 ALEQEILQvssQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE----------------------ARRQLNEIERR---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2189 aeaeaaaLKLKQEADS--EMAKYKKLAEKTLKQKSSVEE-ELVkvkvQLDETDKQksvldvELKRLKQEVsdAIKQKAQV 2265
Cdd:PRK10929 160 -------LQTLGTPNTplAQAQLTALQAESAALKALVDElELA----QLSANNRQ------ELARLRSEL--AKKRSQQL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2266 EDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLeeeAENMKKLAEEAARLNIEAQE----AARLRQIAESDLa 2341
Cdd:PRK10929 221 DAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSI---VAQFKINRELSQALNQQAQRmdliASQQRQAASQTL- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2342 kQRELAEKMLEEKKQ------AIQEAakLKAEAEKL-------QKQKDQAQVEAQKL-LEAKKEMQQRLDQE-------- 2399
Cdd:PRK10929 297 -QVRQALNTLREQSQwlgvsnALGEA--LRAQVARLpempkpqQLDTEMAQLRVQRLrYEDLLNKQPQLRQIrqadgqpl 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 2400 TEGFQKSLEAERKRQ---------------LEITaeaeKLKVKVTQLSDAQSKAEEEAKKF 2445
Cdd:PRK10929 374 TAEQNRILDAQLRTQrellnsllsggdtliLELT----KLKVANSQLEDALKEVNEATHRY 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2313-2464 |
2.32e-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: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2313 KKLAEEAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-----AKLKAEAEKLQKQKDQAQVEAQKLLE 2387
Cdd:COG4913 288 RRLELLEAELEELRAELARLEA-ELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 2388 AKKEMQQRLDQETEGFQksleaerKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTS 2464
Cdd:COG4913 367 LLAALGLPLPASAEEFA-------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1414-1640 |
2.46e-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: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1414 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEE 1493
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1494 AllsRTRIEEEIHIIRLQLETTMKQKNTAETELL------------------QLRAKAVDADKLRnAAQEEAEKLRKQVA 1555
Cdd:COG4942 95 L---RAELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqylkyLAPARREQAEELR-ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1556 EETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVA 1635
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1207141751 1636 LTARL 1640
Cdd:COG4942 251 LKGKL 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2298-2532 |
2.52e-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: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2298 KDNTKKLLEEEAENMKKLAEEAARLNIEAQEAAR----LRQ-IAESDLAKQR-----ELAEKMLEE--KKQAIQEAAKLK 2365
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEevleLEQkLSVADAARRQfekayELVCKIAGEveRSQAWQTARELL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2366 AEAEKLQKQKDQAQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2443
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2444 KFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQeadglhkAIADLEKEKEKLKKEAADL--QKQSKEMANVQQE 2521
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGE-------ALADSQEVTAAMQQLLEREreATVERDELAARKQ 654
|
250
....*....|.
gi 1207141751 2522 QLQQEKTILQQ 2532
Cdd:COG3096 655 ALESQIERLSQ 665
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1775-2431 |
2.73e-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: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1775 QQRTVLDDELQRLKndvnsavkqkkELEEElikVRKEMEILLQQKSKAEKETMSntekskqlLESEAAKMRELAEEATKL 1854
Cdd:pfam07111 63 QQAELISRQLQELR-----------RLEEE---VRLLRETSLQQKMRLEAQAME--------LDALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1855 RSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEAtrlkteAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQ 1934
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQA------HEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1935 HKQAIEEKIGQLKKSSDtELDRQKKIVEETlkqRKVVEE----EIHILKLNFEKassgKQELELELKKLKGIADETQKSK 2010
Cdd:pfam07111 195 AQKEAELLRKQLSKTQE-ELEAQVTLVESL---RKYVGEqvppEVHSQTWELER----QELLDTMQHLQEDRADLQATVE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2011 AKAEEEAEKFRKLALEEEKKRKEaeakVKQIQAAEEEAARQHKAA----QEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL 2086
Cdd:pfam07111 267 LLQVRVQSLTHMLALQEEELTRK----IQPSDSLEPEFPKKCRSLlnrwREKVFALMVQLKAQDLEHRDSVKQLRGQVAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2087 VQEAAqkcsAAEQKAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEaallHKKAEEAERQKKAAEAEAAK 2166
Cdd:pfam07111 343 LQEQV----TSQSQEQAILQRALQDKAAE--VEVERMSAKGLQMELSRAQEARRRQ----QQQTASAEEQLKFVVNAMSS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2167 QAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKykKLAEKTLKQKSSVEEELV-----KVKVQLDETDKQK 2241
Cdd:pfam07111 413 TQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMAR--KVALAQLRQESCPPPPPAppvdaDLSLELEQLREER 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2242 SVLDVELKR----LKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkiekenQELMKKdkdntkkllEEEAENMKKLAE 2317
Cdd:pfam07111 491 NRLDAELQLsahlIQQEVGRAREQGEAERQQLSEVAQQLE-------------QELQRA---------QESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2318 EAARLNIEA-QEAARLRQiaesDLAKQRELAEKMLEEKKQAIQeaAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2396
Cdd:pfam07111 549 VARQGQQEStEEAASLRQ----ELTQQQEIYGQALQEKVAEVE--TRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRA 622
|
650 660 670
....*....|....*....|....*....|....*
gi 1207141751 2397 DQETEgfqKSLEAERKRQLEITAEAEKLKVKVTQL 2431
Cdd:pfam07111 623 TQEKE---RNQELRRLQDEARKEEGQRLARRVQEL 654
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3101-3136 |
2.75e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.75e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1207141751 3101 LNLLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPE 3136
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2065-2483 |
2.77e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2065 LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNA---EK 2141
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddlEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2142 EAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYK-KLAEKTLKQK 2220
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELReREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2221 SsVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLklklkiekenqelmkkdkdn 2300
Cdd:PRK02224 437 T-ARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVE-------------------- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2301 tKKLleEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEekkqaiqEAAKLKAEAEKLQKQKDQAQV 2380
Cdd:PRK02224 496 -ERL--ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE-------RAAELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2381 EAQKLLEAKKEMQQRLdqetegfqksleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2460
Cdd:PRK02224 566 EAEEAREEVAELNSKL------------AELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
410 420
....*....|....*....|...
gi 1207141751 2461 KHTSEKHTVVEKLEVQRLQSKQE 2483
Cdd:PRK02224 634 ERKRELEAEFDEARIEEAREDKE 656
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2232-2399 |
2.77e-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: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2232 VQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE----E 2307
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2308 EAENMKKlAEEAARLNIEAQEAARLrqiaesDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQAQVEAQKLL 2386
Cdd:COG1579 90 EYEALQK-EIESLKRRISDLEDEIL------ELMERIEELEEELAELEAELAELeAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|...
gi 1207141751 2387 EAKKEMQQRLDQE 2399
Cdd:COG1579 163 AEREELAAKIPPE 175
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1551-1759 |
2.89e-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: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1551 RKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQVVEeVAKKTAATQLE 1630
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERET--------------------EIAIAQANREAEEAELEQEREIETAR-IAEAEAELAKK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1631 skqvaltarleeslkneqvmviqlQEEAEhlkkqqAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEA 1710
Cdd:COG2268 250 ------------------------KAEER------REAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEA 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207141751 1711 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1759
Cdd:COG2268 300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2042-2220 |
2.90e-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: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2042 QAAEEEAARQHK--AAQEEVGRLMKLAEEAKKQkeiAEKEAEKQvilVQEAAQKcSAAEQKAQnvlvqqnkdSMAQDKLK 2119
Cdd:TIGR02794 119 KQAEEAKAKQAAeaKAKAEAEAERKAKEEAAKQ---AEEEAKAK---AAAEAKK-KAEEAKKK---------AEAEAKAK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2120 EEFE---KAKKLAQEAEKAKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEaeaaal 2196
Cdd:TIGR02794 183 AEAEakaKAEEAKAKAEAAKAKAAAEAA---AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR------ 253
|
170 180
....*....|....*....|....
gi 1207141751 2197 klKQEADSEMAKYKKLAEKTLKQK 2220
Cdd:TIGR02794 254 --GAAAGSEVDKYAAIIQQAIQQN 275
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1051-1633 |
2.94e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1051 ESRTVNRLRQMVDKEPLKACTQRATEQKKVqtelEGIKKDLDKVVEKSEAVLATSQQSS-SAPVLRSEIDITQKKMEHVY 1129
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKKADAAKKKAEEAKkAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1130 GLSSVylDKLKTIDlvirSTQGAEDILNKYEnqlrEVNKVPVNEKEIEASQTQLQKLRSEAEGKQATfdrleEELQRATE 1209
Cdd:PTZ00121 1364 EKAEA--AEKKKEE----AKKKADAAKKKAE----EKKKADEAKKKAEEDKKKADELKKAAAAKKKA-----DEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1210 VNKRMSQLHSERDvELEHYRQLVGNLRERWQAVFAQIELRQ-RELDLLNRQMQAYRESyDWLIRWIADAKQRQDKLHAVP 1288
Cdd:PTZ00121 1429 EKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1289 IGGSKGLQEQLTQEKKLLEEIEK--NKDKVEDCQKF--AKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDII 1364
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1365 QEyvTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEerkkmaemqaelEKQKQLAETHAKAIAKAEQEANEL 1444
Cdd:PTZ00121 1587 KK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA------------EEEKKKVEQLKKKEAEEKKKAEEL 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1445 KTKMKDEVSKRQDVAVDSEKQKhniqRELQELKTLSEQEIKAKSQQVEEALLSRtRIEEeihiirlqlettMKQKNTAET 1524
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDK----KKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEE------------LKKKEAEEK 1715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1525 EllqlrakavDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlEKFKLQAEEAERHLK 1604
Cdd:PTZ00121 1716 K---------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE-----------------EKKKIAHLKKEEEKK 1769
|
570 580
....*....|....*....|....*....
gi 1207141751 1605 QAELEKQRQIQVVEEVAKKTAATQLESKQ 1633
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2316-2521 |
2.98e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2316 AEEAARLNIEAQEAARLRQIAESDLAKQ-RELAEKMLEEKkQAIQEAAKLKAEAEKLQKQKDQAqveAQKLLEAKKEMQQ 2394
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQaEELQQKQAAEQ-ERLKQLEKERLAAQEQKKQAEEA---AKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2395 RLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQlSDAQSKAEEEAKkfKKQADEIKIRLQETEKHTSEKhtvvEKLE 2474
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAE-AEAAKKAAAEAK--KKAEAEAAAKAAAEAKKKAEA----EAKK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141751 2475 VQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE 2521
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
849-894 |
2.98e-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: 2.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1207141751 849 VQAVCDFKQME---ITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSI 894
Cdd:cd11768 2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPSN 50
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1641-1806 |
3.23e-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: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1641 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAE-EEANKKTAAQEEAEKQKEEAKR 1719
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1720 EAKKRAkaeEAALKQKEAAEMELGNQRKMAEETAKQKLaaeqelirlradfEHAEQQRTVLDDELQRLKNDVNSavkQKK 1799
Cdd:pfam05262 289 EIKKND---EEALKAKDHKAFDLKQESKASEKEAEDKE-------------LEAQKKREPVAEDLQKTKPQVEA---QPT 349
|
....*..
gi 1207141751 1800 ELEEELI 1806
Cdd:pfam05262 350 SLNEDAI 356
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2438-2654 |
3.30e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2438 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2517
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2518 VQQEQLQQEKTIlqqsffaekETLLKKEkaieeekkklekQFEDEVKKAEALKAEQERQRKLMEE---ERKKLQSAMDAA 2594
Cdd:COG3883 94 ALYRSGGSVSYL---------DVLLGSE------------SFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2595 IKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2654
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1168-1642 |
3.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1168 KVPVNEKEIEASQTQLQklrsEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGN--LRERWQAVFAQ 1245
Cdd:COG4717 65 KPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1246 IELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKG 1325
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1326 YIDAIKDyELQLVTYKALVEPIASPLKKAKMESASDDIIqeyVTLRTRYSELMTLSSQYIKFIIetqrrlqdeekAAEKL 1405
Cdd:COG4717 221 ELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLF-----------LVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1406 KEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIK 1485
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1486 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1565
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 1566 EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQ-IQVVEEVAKKTAATQLESKQVALTARLEE 1642
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAaLKLALELLEEAREEYREERLPPVLERASE 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1393-1601 |
3.67e-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: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1393 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRE 1472
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1473 LQELKTLSEQ---EIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNtaetELLQLRAKAVDADKLRNAAQEEAEK 1549
Cdd:COG4942 110 LRALYRLGRQpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 1550 LRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF--KLQAEEAER 1601
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAA 239
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2332-2778 |
3.91e-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: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2332 LRQIAES-DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQK----------QKDQAQVEAQKLLEAKKEMQQRLDQET 2400
Cdd:pfam05483 50 LEQVANSgDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkQKENKLQENRKIIEAQRKAIQELQFEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2401 EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQS 2480
Cdd:pfam05483 130 EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2481 KQEadgLHKAIADLEKEKEKlkkeaadLQKQSKEMANVQQEQLQqekTILQQSffAEKETLLKKEKAIEEEKKKLEKQFE 2560
Cdd:pfam05483 210 RLE---MHFKLKEDHEKIQH-------LEEEYKKEINDKEKQVS---LLLIQI--TEKENKMKDLTFLLEESRDKANQLE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2561 DEVK-KAEALKAEQERQRKLMEEeRKKLQSAMDAAIKKQKEAEEEMN-----------GKQKEMQDLEKKRIEQEKLLAE 2628
Cdd:pfam05483 275 EKTKlQDENLKELIEKKDHLTKE-LEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNKAKAAHSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2629 ENKN-------LREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT-----MVETTKKVLNGSTEVDGVKKDvplaFDG 2696
Cdd:pfam05483 354 FEATtcsleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkevELEELKKILAEDEKLLDEKKQ----FEK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2697 IREKVPASRLHEIGVLSKKEYD------KLKKGKTTVQELSKNDKVKMCLKGKDCIGGVIVEPNQKMsiyQALKDKMITQ 2770
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREKEihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK---LLLENKELTQ 506
|
....*...
gi 1207141751 2771 STAIMLLE 2778
Cdd:pfam05483 507 EASDMTLE 514
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2039-2447 |
4.23e-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: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2039 KQIQAAEEEAARQHKAAQEEVgrlmKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAaeqKAQNVLVQQNKDSMAQDKl 2118
Cdd:pfam09731 89 VKIPRQSGVSSEVAEEEKEAT----KDAAEAKAQLPKSEQEKEKALEEVLKEAISKAE---SATAVAKEAKDDAIQAVK- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2119 keefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAerqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKL 2198
Cdd:pfam09731 161 ----AHTDSLKEASDTAEISREKATDSALQKAEAL--------------------AEKLKEVINLAKQSEEEAAPPLLDA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2199 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqLDETDKQksVLDVELKRLKQEVSDAIKQK-AQVEDELSKVkiqME 2277
Cdd:pfam09731 217 APETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKE-LVASERI--VFQQELVSIFPDIIPVLKEDnLLSNDDLNSL---IA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2278 DLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQIAESdlakqrelaekmLEEKKQA 2357
Cdd:pfam09731 291 HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSA-RLEEVRAADEAQLRLE------------FEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2358 IQEAAKLKAEAEklqkQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS-LEAERKRQLEITAEAeKLKVK-VTQLSDAQ 2435
Cdd:pfam09731 358 IRESYEEKLRTE----LERQAEAHEEHLKDVLVEQEIELQREFLQDIKEkVEEERAGRLLKLNEL-LANLKgLEKATSSH 432
|
410
....*....|..
gi 1207141751 2436 SKAEEEAKKFKK 2447
Cdd:pfam09731 433 SEVEDENRKAQQ 444
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1293-1951 |
4.73e-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: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1293 KGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKAlvepiasplKKAKMESASDDIIQEYVTLRT 1372
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK---------EKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1373 RYSELMTLssqyikfiIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQlaethakAIAKAEQEANELK---TKMK 1449
Cdd:TIGR04523 202 LLSNLKKK--------IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT-------EISNTQTQLNQLKdeqNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1450 DEVSKRQDVAVDSEKQKHNIQRELQELKTlseqEIKAKSQQVEEALLSRtrieeeihiIRLQLETTMKQKNTAETELLQl 1529
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKS----EISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQISQ- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1530 rakavdADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHL-KQAEL 1608
Cdd:TIGR04523 333 ------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1609 EKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1688
Cdd:TIGR04523 407 NQQKDEQI------KKLQQEKELLEKEIERLKETIIKNNS-EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1689 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKrAKAEEAALKQKEaaemelgnqrkmaEETAKQKLAAEQELIRLRA 1768
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD-LTKKISSLKEKI-------------EKLESEKKEKESKISDLED 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1769 DFEHAEQQRTvlDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELA 1848
Cdd:TIGR04523 546 ELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1849 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAE--IALKEKEAENDRLKRKAEEEGYQRK 1926
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiIELMKDWLKELSLHYKKYITRMIRI 703
|
650 660
....*....|....*....|....*
gi 1207141751 1927 VLEDQAAQHKQAIEEKIGQLKKSSD 1951
Cdd:TIGR04523 704 KDLPKLEEKYKEIEKELKKLDEFSK 728
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1483-1761 |
4.96e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1483 EIKAKSQQVEEALLSRTRIEEEIhiIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKR 1562
Cdd:PRK05035 437 EIRAIEQEKKKAEEAKARFEARQ--ARLEREK-------AAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1563 KAEEELKRKSEAEKDAakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvalTARLEE 1642
Cdd:PRK05035 508 IKAGARPDNSAVIAAR---------EARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANA---EAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1643 SLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAK 1722
Cdd:PRK05035 576 DPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP---KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141751 1723 KRAKAEEAALKQKEAAEMELGNQRKMAEETA----KQKLAAEQ 1761
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1416-1571 |
5.16e-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: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1416 MQAELEKQKQLAETHAKaIAKAEQEANELK---TKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVE 1492
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKELPaelAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1493 --EALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKR 1570
Cdd:COG1579 77 kyEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
.
gi 1207141751 1571 K 1571
Cdd:COG1579 157 E 157
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
2245-2479 |
5.58e-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: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2245 DVELKRLK------QEVSDAIKQKAQVEDELSKVKIQMEDLLKLklkiekenqelmkKDKDNTkklLEEEAENMKKLAEE 2318
Cdd:cd07647 8 DTLLQRLKegkkmcKELEDFLKQRAKAEEDYGKALLKLSKSAGP-------------GDEIGT---LKSSWDSLRKETEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2319 AARLNIEaqeaarlrqiaesdLAKQ-RELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLd 2397
Cdd:cd07647 72 VANAHIQ--------------LAQSlREEAEKLEEFREKQKEERKKTEDIMKRSQKNK---KELYKKTMKAKKSYEQKC- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2398 QETEGFQKSleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEVQR 2477
Cdd:cd07647 134 REKDKAEQA--YEKSSSGAQPKEAEKLKKKAAQCKTSAEEADSAYKSSIGCLEDAR---VEWESEHATACQVFQNMEEER 208
|
..
gi 1207141751 2478 LQ 2479
Cdd:cd07647 209 IK 210
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
83-170 |
5.80e-05 |
|
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: 45.52 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 83 LYEDLRDGHNLISLLEVLSGETLPrerDVVRNSRLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLT 162
Cdd:cd21294 38 LFDECKDGLVLSKLINDSVPDTID---ERVLNKPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLI 114
|
....*...
gi 1207141751 163 LGLIWTII 170
Cdd:cd21294 115 LGLIWQII 122
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2297-2458 |
6.03e-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: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2297 DKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmleekkqAIQEAAKLKAEAEKLQKQKD 2376
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2377 QAQVEAQKLLEAKKEMQQRLDQETEGFQKSlEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRL 2456
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKR-EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
..
gi 1207141751 2457 QE 2458
Cdd:pfam05262 331 EP 332
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1421-1855 |
6.03e-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: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1421 EKQKQLaethakaiakaeQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQelkTLSEQeIKAKSQQVEEAllsRTR 1500
Cdd:pfam10174 363 KKTKQL------------QDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE---NLQEQ-LRDKDKQLAGL---KER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1501 IEEeihiirLQLETTmkqknTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAK 1580
Cdd:pfam10174 424 VKS------LQTDSS-----NTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1581 EKKKALEDL-EKFKLQAEEA---ERHLKQAELEkqrqIQVVEEVAKKTAATQLESKQVALTARLEESLKNE-QVMVIQLQ 1655
Cdd:pfam10174 493 EKESSLIDLkEHASSLASSGlkkDSKLKSLEIA----VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQEVA 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1656 EEAEHLKKQQAEADK---AREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakreakkraKAEEAAL 1732
Cdd:pfam10174 569 RYKEESGKAQAEVERllgILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI------------------KHGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1733 KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLradfehaEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1812
Cdd:pfam10174 631 KKKGAQLLEEARRREDNLADNSQQLQLEELMGAL-------EKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL 703
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1207141751 1813 EILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 1855
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1655-1883 |
6.12e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1655 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEalRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAK-AEEAALK 1733
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLE--KERLAAQEQKKQA-----------EEAAKQAALKQKqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1734 QKEAAemelgnqrkmaeetakqKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEElikVRKEME 1813
Cdd:PRK09510 141 AAAAA-----------------KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKK----AAAEAKKKAEAE---AAAKAA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1814 ILLQQKSKAEKETMSNTEkSKQLLESEAAKMRELAEEATKlrSVAEEAKKQRQIAEEEAARQRAEAEKIL 1883
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAE-AKKKAAAEAKAAAAKAAAEAK--AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1720-1968 |
6.48e-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: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1720 EAKKRAKAEEAALKQKEAAEMELGNQrkmAEETAKQKLAAEQELIRLRADFEHAEQQRTVlddELQRLKndvnsAVKQKK 1799
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQ---AEEAEKQRAAEQARQKELEQRAAAEKAAKQA---EQAAKQ-----AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1800 ELEEELIKVRKEmeillqQKSKAEKEtmsntekSKQLLESEAAKMRElaEEATKlrSVAEEAKKQRQIAE---EEAARQR 1876
Cdd:TIGR02794 120 QAEEAKAKQAAE------AKAKAEAE-------AERKAKEEAAKQAE--EEAKA--KAAAEAKKKAEEAKkkaEAEAKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1877 AEAE-KILKEKLTAINEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ-LKKSSDTEL 1954
Cdd:TIGR02794 183 AEAEaKAKAEEAKAKAEAAKAKAAAE-AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGaRGAAAGSEV 261
|
250
....*....|....
gi 1207141751 1955 DRQKKIVEETLKQR 1968
Cdd:TIGR02794 262 DKYAAIIQQAIQQN 275
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1635-2067 |
6.86e-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: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1635 ALTARLE-----ESLKNEQVMVIQLQEEAEHLkkqqaeadkarEQAEKELETWRQKANEALRLRLQAEEEANKKtaaqee 1709
Cdd:COG3096 287 ALELRRElfgarRQLAEEQYRLVEMARELEEL-----------SARESDLEQDYQAASDHLNLVQTALRQQEKI------ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1710 aekqkeeakreAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD- 1781
Cdd:COG3096 350 -----------ERYQEDLEELTERLEEQEEVveEAAEQLAEAEA---RLEAAEEEVDSLKsqlADYQQAldVQQTRAIQy 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1782 -DELQRLKN----------DVNSAVKQKKELEEELIKVRKEMeILLQQKSKAEKETMSNTEKSKQLLESEAA-------- 1842
Cdd:COG3096 416 qQAVQALEKaralcglpdlTPENAEDYLAAFRAKEQQATEEV-LELEQKLSVADAARRQFEKAYELVCKIAGeversqaw 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1843 -KMRELAEEATKLRSVAEEAKK-QRQIAE-EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 1919
Cdd:COG3096 495 qTARELLRRYRSQQALAQRLQQlRAQLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1920 EEGYQRKVLEdqaaQHKQAIEEKIGQLKKS------SDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKqele 1993
Cdd:COG3096 575 EAVEQRSELR----QQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVER---- 646
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 1994 lelkklkgiaDETQkskakaeeeaekFRKLALeeekkrkeaeakvkqiqaaEEEAARQHKAAQEEVGRLMKLAE 2067
Cdd:COG3096 647 ----------DELA------------ARKQAL-------------------ESQIERLSQPGGAEDPRLLALAE 679
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1760-1920 |
7.17e-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: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1760 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLles 1839
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEY--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1840 eAAKMRELaEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEatrLKTEAEIALKEKEAENDRLKRKAE 1919
Cdd:COG1579 92 -EALQKEI-ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
.
gi 1207141751 1920 E 1920
Cdd:COG1579 167 E 167
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2039-2177 |
7.47e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2039 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQkeiAEKEAEKQVilvQEAAQKCSAAEQKAQNVLVQQNKdSMAQDKL 2118
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKKA---EAEAAKKAAAEAKKKAEAEAAAK-AAAEAKK 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2119 KEEFEKAKKLAQEAEK-----AKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2177
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKkaaaeAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1468-1807 |
8.60e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1468 NIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEA 1547
Cdd:COG4372 32 QLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1548 EKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1627
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1628 QLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQ 1707
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1708 EEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRL 1787
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1207141751 1788 KNDVNSAVKQKKELEEELIK 1807
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2341-2608 |
8.91e-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: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2341 AKQRELAEKMLEEKKQAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLdQETEGFQKSLEAErkrqleitae 2420
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAE---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2421 aeklkvkvtqLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVeklevqrLQSKQEADGLHKAIADLEKEKEK 2500
Cdd:COG4942 85 ----------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL-------LLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2501 LKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLM 2580
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|....*...
gi 1207141751 2581 EEERKKLQSAMDAAIKKQKEAEEEMNGK 2608
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
53-169 |
9.12e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 44.95 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 53 DRVQKKTFTKWVNKHLVKhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLpreRDVvrnSRLPREKGRMrfhkLQNV 132
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDI---NGCPKNRSQM----IENI 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141751 133 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 169
Cdd:cd21285 75 DACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1371-1787 |
9.40e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.75 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1371 RTRYSELMTLSSQYIKF---IIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTK 1447
Cdd:COG5278 106 QARLDELEALIDQWLAEleqVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1448 MKDEVSKRQDVAVDSEKQKHNIQRELQELkTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELL 1527
Cdd:COG5278 186 LALAELLLLALARALAALLLLLLLEAELA-AAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1528 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1607
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1608 LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN 1687
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1688 EALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLR 1767
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410 420
....*....|....*....|
gi 1207141751 1768 ADFEHAEQQRTVLDDELQRL 1787
Cdd:COG5278 505 LAALLLAAAEAALAAALAAA 524
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2532-2654 |
1.02e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 47.67 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2532 QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRklmeEERKKLQSAMDAAIKKQKEAEEEMngKQKE 2611
Cdd:pfam02841 179 QEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLR----EKQKEEEQMMEAQERSYQEHVKQL--IEKM 252
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141751 2612 MQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2654
Cdd:pfam02841 253 EAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQD 295
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3761-3797 |
1.12e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1207141751 3761 IDLLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEF 3797
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2305-2516 |
1.14e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2305 LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdlAKQRELAekmLEEKKQAIQEAAKLKAEA-EKLQKQKDQAQVEAQ 2383
Cdd:pfam15709 309 MESEEERSEEDPSKALLEKREQEKASRDRLRAER--AEMRRLE---VERKRREQEEQRRLQQEQlERAEKMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2384 KLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAEAEK-------LKVKVTQLS-DAQSKAEEEAKKFKKQADEIKIR 2455
Cdd:pfam15709 384 RRFEEIRLRKQRLEEER---QRQEEEERKQRLQLQAAQERarqqqeeFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQ 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 2456 LQETEKHTSEKhTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMA 2516
Cdd:pfam15709 461 LAEEQKRLMEM-AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2310-2531 |
1.15e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2310 ENMKKLAEE-AARLNIEAQEAARLRQIAESDLAKQREL--AEKMLEEKKQAIQEAAKLKAEAEKLQkQKDQAQVEAQKLL 2386
Cdd:PRK10929 75 DNFPKLSAElRQQLNNERDEPRSVPPNMSTDALEQEILqvSSQLLEKSRQAQQEQDRAREISDSLS-QLPQQQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2387 eakKEMQQRLdqETEGFQKSLEAERKRQLeITAEAEKLKVKVTQLSDAQSKAEE-------EAKKFKKQADEIKIRLQET 2459
Cdd:PRK10929 154 ---NEIERRL--QTLGTPNTPLAQAQLTA-LQAESAALKALVDELELAQLSANNrqelarlRSELAKKRSQQLDAYLQAL 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2460 EKH-TSEKHTVVEK-LEVQRLQSKQEADgLHKAIADLEKEKEKLkkeAADLQKQSKEMANVQQEQLQQEKTILQ 2531
Cdd:PRK10929 228 RNQlNSQRQREAERaLESTELLAEQSGD-LPKSIVAQFKINREL---SQALNQQAQRMDLIASQQRQAASQTLQ 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2560-2652 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2560 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2639
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90
....*....|...
gi 1207141751 2640 LQSSQKASYTKEI 2652
Cdd:COG4942 113 LYRLGRQPPLALL 125
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2054-2267 |
1.19e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2054 AAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVilvQEAAQKCSAAEQKAQnvlvQQNKDSMAQDKLKEEFEKAKKLAQEAE 2133
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQA---EELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2134 KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAlKLKQEADSEM-AKYKKL 2212
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAeAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2213 AEKTLKQKSSVEEELVKVKvqldETDKQKSVLDVELKRLKQEVSDAIKQKAQVED 2267
Cdd:PRK09510 211 AAAEAKKKAAAEAKAAAAK----AAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1511-1934 |
1.21e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1511 QLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLE 1590
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1591 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADK 1670
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1671 AREQAEKELETWRQKANEALRLRLQAEEEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE 1750
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALA-----ELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1751 ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT 1830
Cdd:COG5278 346 LLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1831 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1910
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1207141751 1911 NDRLKRKAEEEGYQRKVLEDQAAQ 1934
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1768-2141 |
1.23e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1768 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKetmsntekskqllESEAAKMR-E 1846
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ-------------DYQAASDHlN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1847 LAEEAtklrsVAEEAKKQRQIAEEEAARQRAEAEKILKEkltainEATRLKTEAEIALKEKEAENDRLkrKAEEEGYQRK 1926
Cdd:PRK04863 339 LVQTA-----LRQQEKIERYQADLEELEERLEEQNEVVE------EADEQQEENEARAEAAEEEVDEL--KSQLADYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1927 --VLEDQAAQHKQAIE--EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGI 2002
Cdd:PRK04863 406 ldVQQTRAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2003 ADETQKSkakaeEEAEKFRKLaLEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQeevgRLMKLAEEAKKQKEIAEKEAEK 2082
Cdd:PRK04863 486 AGEVSRS-----EAWDVAREL-LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 2083 QVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEK 2141
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1642-1926 |
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 1207141751 1642 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1721
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE-LNAQVKELREEAQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1722 KKRAKAEEAALKQKEAaemELGNQRKMAEETAKQKLAAEQELIRLRAdfehaEQQRTVLD--------DELQRLKNDVNs 1793
Cdd:COG1340 80 RDELNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEW-----RQQTEVLSpeeekelvEKIKELEKELE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1794 AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1873
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHE----EMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1207141751 1874 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRK 1926
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKG 279
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
56-180 |
1.28e-04 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 45.03 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 56 QKKTFTKWVNKHLVKHWKAeaqRHIT-------DLYEDLRDGHNLISLLEVLSGETLPrERDVVRNSRLPrekgrmrFHK 128
Cdd:cd21323 25 EKVAFVNWINKALEGDPDC---KHVVpmnptdeSLFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTI 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 180
Cdd:cd21323 94 SENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1588-1888 |
1.35e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1588 DLEKFKLQAEEAERHLKQAELEKQRQIQvveevakktAATQLEsKQVALTARLEEslkneQVMVIQ---LQEEAEHLKKQ 1664
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRS---------QLEQAK-EGLSALNRLLP-----RLNLLAdetLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1665 QAEADKAR----------EQAEKELETWRQKANEALRLRLQAEEeankktaaqeeaekqkeeakreakkrAKAEEAALKQ 1734
Cdd:PRK04863 903 LDEAEEAKrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDYQQ--------------------------AQQTQRDAKQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1735 KEAAEMELgNQRK--MAEETAKQKLAAEQEL-IRLRADFEHAEQQRTVLDDEL--------------QRLKNDVNSAVKQ 1797
Cdd:PRK04863 957 QAFALTEV-VQRRahFSYEDAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQM 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1798 KKELEEEL--IKVR--KEMEILLQQKSKAEKETMSNT-------EKSKQLLESE----AAKMRELAEEATKLRSVAEEAK 1862
Cdd:PRK04863 1036 LQELKQELqdLGVPadSGAEERARARRDELHARLSANrsrrnqlEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAK 1115
|
330 340
....*....|....*....|....*.
gi 1207141751 1863 KqRQIAEEEAARQRAEAEKILKEKLT 1888
Cdd:PRK04863 1116 A-GWCAVLRLVKDNGVERRLHRRELA 1140
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
51-176 |
1.38e-04 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 44.60 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 51 ERDRVQKKTFTKWVNKHLVkhwkaeaQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDVVRNSRLPREKGRMRfhKLQ 130
Cdd:cd21330 9 EGETREERTFRNWMNSLGV-------NPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141751 131 NVQIALDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 176
Cdd:cd21330 77 NCNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4426-4463 |
1.49e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.49e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141751 4426 QRFLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTA 4463
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1609-1926 |
1.59e-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: 47.34 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1609 EKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETW 1682
Cdd:pfam15558 4 ERDRKIAALMLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQsqeqwqAEKEQRKARLGREERRRAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1683 RQKANEAL---RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALkQKEAAEMELGNQRKMAE--------- 1750
Cdd:pfam15558 84 RREKQVIEkesRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL-QALREQNSLQLQERLEEachkrqlke 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1751 --------ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKA 1822
Cdd:pfam15558 163 reeqkkvqENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1823 EKETMSNTEKSKQLLESEAAKMRelaeeatKLRSVAEEAKKQR--QIAEEEAARQRaeAEKILKEKLTAINEATRLKTEA 1900
Cdd:pfam15558 243 EEKEEERQEHKEALAELADRKIQ-------QARQVAHKTVQDKaqRARELNLEREK--NHHILKLKVEKEEKCHREGIKE 313
|
330 340
....*....|....*....|....*.
gi 1207141751 1901 EIALKEKEAENDRLKRKAEEEGYQRK 1926
Cdd:pfam15558 314 AIKKKEQRSEQISREKEATLEEARKT 339
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1812-2269 |
1.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1812 MEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEE-AKKQRQIAEEEAARQRAEAEKILKEKLTAI 1890
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1891 NEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKV--LEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 1967
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1968 RKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAeee 2047
Cdd:COG4717 208 LAELEEELEEAQ---EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL--- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2048 aarqhkaaqeEVGRLMKLAEEAKKQKEIAEKEAEKqvilVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKK 2127
Cdd:COG4717 282 ----------VLGLLALLFLLLAREKASLGKEAEE----LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2128 LAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEaeaaalkLKQEADSEMA 2207
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ-------LEELLGELEE 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2208 KYKKLAEKTLKQK-SSVEEELVKVKVQLDETDKQKSVLDVELKRLK--QEVSDAIKQKAQVEDEL 2269
Cdd:COG4717 421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAEL 485
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2317-2610 |
1.65e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2317 EEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2396
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2397 DQETEGFQKSLEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEE-----AKKFKKQADEIKIRLQETEKHTSEKHTVVE 2471
Cdd:pfam02029 140 YQENKWSTEVRQAEEE------GEEEEDKSEEAEEVPTENFAKEEvkdekIKKEKKVKYESKVFLDQKRGHPEVKSQNGE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2472 KlEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA----DLQKQSKEMANVQQEQLQQEktilQQSFFAEKETLLKKEKA 2547
Cdd:pfam02029 214 E-EVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqkleELRRRRQEKESEEFEKLRQK----QQEAELELEELKKKREE 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2548 IEEEKKKLEKQFEDEvkKAEALKAEQERQRKLMEE-ERKKlqsaMDAAIKKQKEAEEEMNGKQK 2610
Cdd:pfam02029 289 RRKLLEEEEQRRKQE--EAERKLREEEEKRRMKEEiERRR----AEAAEKRQKLPEDSSSEGKK 346
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2050-2639 |
1.68e-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: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2050 RQHKAA-QEEVGRLMKLAEEAKkQKEIAE------KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ--DKLKE 2120
Cdd:pfam12128 230 IQAIAGiMKIRPEFTKLQQEFN-TLESAElrlshlHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEkrDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2121 EfekakKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAaalkLKQ 2200
Cdd:pfam12128 309 E-----LSAADAAVAKDRSELEALEDQHGAFLDA------------------DIETAAADQEQLPSWQSELEN----LEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2201 EADSEMAKYKKLAEKTLKQKSSVEEELV-KVKVQLDETDKQKSVLDvelkrlkqevsdaiKQKAQVEDELSKVKIQMEDL 2279
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGIKDKLAKIREARD--------------RQLAVAEDDLQALESELREQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2280 LklklkiekenqELMKKDKDNTKKLLEEEAENMKklaeeaARLNIEAQEAARLRQIAESDlakqrELAEKMLEEKKQAIQ 2359
Cdd:pfam12128 428 L-----------EAGKLEFNEEEYRLKSRLGELK------LRLNQATATPELLLQLENFD-----ERIERAREEQEAANA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2360 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-ETEGFQKS------LEAE----RKRQLEITAEAEKLKVKV 2428
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElELQLFPQAgtllhfLRKEapdwEQSIGKVISPELLHRTDL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2429 TQLSDAQSKAEE-------------EAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLE 2495
Cdd:pfam12128 566 DPEVWDGSVGGElnlygvkldlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2496 KEKEKLKKeaaDLQKQSKEManvQQEQLQQEKTILQQSFFAEKEtlLKKEKAIEEEKKKLEKQFEDEVKKaEALKAEQER 2575
Cdd:pfam12128 646 TALKNARL---DLRRLFDEK---QSEKDKKNKALAERKDSANER--LNSLEAQLKQLDKKHQAWLEEQKE-QKREARTEK 716
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2576 Q--RKLMEEERKKLQSAMDAAI-KKQKEAEEEMNGKQKEM-QDLEKKRIEQEKL--LAEENKNLREKLQQ 2639
Cdd:pfam12128 717 QayWQVVEGALDAQLALLKAAIaARRSGAKAELKALETWYkRDLASLGVDPDVIakLKREIRTLERKIER 786
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2243-2613 |
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 1207141751 2243 VLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARL 2322
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2323 NIEAQEAARLRQIAESDLAKQRELAE--KMLEEKKQAIQ-EAAKLKAEAEKLQKQKDQAQVEaQKLLEAKKEMQQrldQE 2399
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEdiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE-RKQLQAKLQQTE---EE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2400 TEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKA---EEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2476
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2477 RLQSKQEadgLHKAiadlekekeklKKEAADLQKQSKEMANVQQE---QLQQEKTILQQSFFAEKETLLKKEKAIEEEKK 2553
Cdd:pfam07888 267 RDRTQAE---LHQA-----------RLQAAQLTLQLADASLALREgraRWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2554 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQ 2613
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1733-1938 |
1.77e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1733 KQKEAAEMElgNQRKMAEETAKQKLAAEQElirlradfehAEQQRtVLDDELQRLKndvnsAVKQKKELEEElikvrkEM 1812
Cdd:PRK09510 70 QQKSAKRAE--EQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERLA-----AQEQKKQAEEA------AK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1813 EILLQQKsKAEKETMSNTEKSKqlLESEAAKMReLAEEATKlrsvAEEAKKQRQIAE-----EEAARQRAEAEKILKEKL 1887
Cdd:PRK09510 126 QAALKQK-QAEEAAAKAAAAAK--AKAEAEAKR-AAAAAKK----AAAEAKKKAEAEaakkaAAEAKKKAEAEAAAKAAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 1888 TAINEATRLKTEAEIALKEKEAENDRlKRKAEEEGYQRKVLEDQAAQHKQA 1938
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAEA-KAAAAKAAAEAKAAAEKAAAAKAA 247
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2318-2454 |
1.80e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2318 EAARLNIeAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQEAAKLKaeaEKLQKQKDQAQ-VEAQKLLEAKKEMQQRL 2396
Cdd:PRK00409 505 EEAKKLI-GEDKEKLNELIASLEELERELEQK-AEEAEALLKEAEKLK---EELEEKKEKLQeEEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 2397 DQETEgfqkslEAERK-RQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKI 2454
Cdd:PRK00409 580 KEAKK------EADEIiKELRQLQKGGYASVKAHELIEARKrlnkaneKKEKKKKKQKEKQEELKV 639
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2565-2666 |
1.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2565 KAEALKAEQERQRKLMEEER-------KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2637
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKeaeaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100
....*....|....*....|....*....
gi 1207141751 2638 QQLQSSQKASYTKEIEIQTDKVPEEELVQ 2666
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1784-1953 |
2.00e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1784 LQRLKNDVNSAVKQKKELEEElikvrKEMEilLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKK 1863
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ-----QAEE--LQQKQAAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1864 QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENdrlKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 1943
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKKKAA 212
|
170
....*....|
gi 1207141751 1944 GQLKKSSDTE 1953
Cdd:PRK09510 213 AEAKKKAAAE 222
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1472-1805 |
2.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1472 ELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKavdadklRNAAQEEAEKLR 1551
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1552 KQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1631
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1632 KQVALTARLEESLKNEQVmVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1711
Cdd:COG4372 167 AALEQELQALSEAEAEQA-LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1712 KQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDV 1791
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 1207141751 1792 NSAVKQKKELEEEL 1805
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2342-2655 |
2.31e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2342 KQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL---LEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT 2418
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLeeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2419 AEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAdlEKEK 2498
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2499 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2578
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 2579 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQ 2655
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1017-1990 |
2.34e-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: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1017 ALIQKDSTSGEQDESVCKSYITQIKDLRLRLEGCESRTVNRLRQMVDKEPLKACTQRATEQKKVQTElegIKKDLDKVVE 1096
Cdd:TIGR01612 682 SIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGE---INKDLNKILE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1097 KSEAvlATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLkTIDlvirsTQGAEDILNKYENQLREVNKVPVNEKEI 1176
Cdd:TIGR01612 759 DFKN--KEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQI-NID-----NIKDEDAKQNYDKSKEYIKTISIKEDEI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1177 EASQTQLQKLRSEAEGKQATFDRLE---------EELQRATEVNKRMSQLHSERdveLEHYRQLVGNLRERWQAVFAQIE 1247
Cdd:TIGR01612 831 FKIINEMKFMKDDFLNKVDKFINFEnnckekidsEHEQFAELTNKIKAEISDDK---LNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1248 LRQRELDLLNRqmqayresYDWLIRWIADAKQRQDKLHavpiggskglqeqlTQEKKLLEEIEKNKDKVEDCQKFAKGYI 1327
Cdd:TIGR01612 908 EEYQNINTLKK--------VDEYIKICENTKESIEKFH--------------NKQNILKEILNKNIDTIKESNLIEKSYK 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1328 DaikDYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRY--SELMTLSSQYI---KFIIETQRRLQDEEKAA 1402
Cdd:TIGR01612 966 D---KFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLgkNKENMLYHQFDekeKATNDIEQKIEDANKNI 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1403 EKLKEEERKKMAEMQAELEKQ--KQLAETHAKAIAKAEQEA---NELKTKMK----------------DEVSK-RQDVAV 1460
Cdd:TIGR01612 1043 PNIEIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINItnfNEIKEKLKhynfddfgkeenikyaDEINKiKDDIKN 1122
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1461 DSEKQKHNIqRELQELKTLSEQ---EIKAKSQQVEEaLLSRTRIEEEIHIIRLQLETTM----KQKNTAE------TELL 1527
Cdd:TIGR01612 1123 LDQKIDHHI-KALEEIKKKSENyidEIKAQINDLED-VADKAISNDDPEEIEKKIENIVtkidKKKNIYDeikkllNEIA 1200
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1528 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEE--------------ELKRKSEAEKDAAKEKKKALEDLEKFK 1593
Cdd:TIGR01612 1201 EIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmikameayiedldEIKEKSPEIENEMGIEMDIKAEMETFN 1280
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1594 LQAEE-------AERHLKQAELEKQRQIQVVEEVAKKTAATQLESKqvaLTARLEESLKNEQVMVIQLQEEAE-----HL 1661
Cdd:TIGR01612 1281 ISHDDdkdhhiiSKKHDENISDIREKSLKIIEDFSEESDINDIKKE---LQKNLLDAQKHNSDINLYLNEIANiynilKL 1357
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1662 KKQQAEADKAREQAeKELETWRQKANEAL----RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAK-------AEEA 1730
Cdd:TIGR01612 1358 NKIKKIIDEVKEYT-KEIEENNKNIKDELdkseKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKelknhilSEES 1436
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1731 ALKQ--KEAAEME-----LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEE 1803
Cdd:TIGR01612 1437 NIDTyfKNADENNenvllLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHI--DKSKGCKDEADKNAKAIEKNKE 1514
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1804 ELIKVRKEMEILLQQKSKAE-KETMSNTEK-SKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEK 1881
Cdd:TIGR01612 1515 LFEQYKKDVTELLNKYSALAiKNKFAKTKKdSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKA 1594
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1882 ILKEKLTAINEATRL------KTEAEIALKEKEA------------ENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKi 1943
Cdd:TIGR01612 1595 AIDIQLSLENFENKFlkisdiKKKINDCLKETESiekkissfsidsQDTELKENGDNLNSLQEFLESLKDQ-KKNIEDK- 1672
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 1207141751 1944 gqlKKSSDtELDRQKKIVEETLKQRK------VVEEEIHILKLNFEKASSGKQ 1990
Cdd:TIGR01612 1673 ---KKELD-ELDSEIEKIEIDVDQHKknyeigIIEKIKEIAIANKEEIESIKE 1721
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1597-1973 |
2.43e-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: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1597 EEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESlkneqvmviqlqeeaEHLKKQQAEADKAREQAE 1676
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVS---------------SEVAEEEKEATKDAAEAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1677 KELETWRQKANEALRLRLQ-AEEEANKKTAAQEEAekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMaEETAKQ 1755
Cdd:pfam09731 117 AQLPKSEQEKEKALEEVLKeAISKAESATAVAKEA---------KDDAIQAVKAHTDSLKEASDTAEISREKA-TDSALQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1756 KLAAEQELIRLRADFEHAEQQrTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ 1835
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1836 LLESEAAKMREL-AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 1914
Cdd:pfam09731 266 IFPDIIPVLKEDnLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEA 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 1915 KRKAEeegYQRKVLEDQaaqhkQAIEEKIgqlkkssDTELDRQKKIVEETLKQRKVVEE 1973
Cdd:pfam09731 346 QLRLE---FEREREEIR-----ESYEEKL-------RTELERQAEAHEEHLKDVLVEQE 389
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1006-1371 |
2.67e-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: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1006 DNLLRSVEQEPALIQKDSTSGEQDESVCKSYITQIKDLRLRLEGCESRTVNRLRQMVDKepLKACTQRATEQKKVQTELE 1085
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED--LSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1086 GIKKDLDKVVEKSEAVLATSQQSSSapvlRSEIDITQKKMEHVYglssvylDKLKTIDLVIRSTQG-----------AED 1154
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLS----HSRIPEIQAELSKLE-------EEVSRIEARLREIEQklnrltlekeyLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1155 ILNKYENQLREV-NKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELqratevnkrmSQLHSERDVELEHYRQlvg 1233
Cdd:TIGR02169 834 EIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----------GDLKKERDELEAQLRE--- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1234 nLRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiadAKQRQDKlhavpIGGSKGLQEQLTQEKKLLEEIEKNK 1313
Cdd:TIGR02169 901 -LERKIEELEAQIEKKRKRLSELKAKLEA--------------LEEELSE-----IEDPKGEDEEIPEEELSLEDVQAEL 960
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 1314 DKVE-DCQKFAKGYIDAIKDYELQLVTYKALVEpiasplKKAKMESASDDI---IQEYVTLR 1371
Cdd:TIGR02169 961 QRVEeEIRALEPVNMLAIQEYEEVLKRLDELKE------KRAKLEEERKAIlerIEEYEKKK 1016
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2812-2849 |
2.73e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.73e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141751 2812 TKLLSAERAVTGFKDPFTGDTISVFEAMKKGLITEDQA 2849
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2332-2491 |
2.80e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2332 LRQIAESDLAKQRELAEKMLEE--------KKQAIQEA----AKLKAEAEKLQKQKDQaqvEAQKLLEAKKEMQQRLDQE 2399
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEakkeaeaiKKEALLEAkeeiHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2400 TEGFQK---SLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFkkQADEIK-IRLQETEKHTSEK--HTVVEKL 2473
Cdd:PRK12704 102 LELLEKreeELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKeILLEKVEEEARHEaaVLIKEIE 179
|
170
....*....|....*...
gi 1207141751 2474 EvqrlQSKQEADGLHKAI 2491
Cdd:PRK12704 180 E----EAKEEADKKAKEI 193
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2200-2433 |
3.08e-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: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2200 QEADSEMAKYKKLAEKTLKQKSsvEEELVKVKVQLDETDKQKSVLDVELKRLKQEVsdaikqkAQVEDELSKVKIQMEdl 2279
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQR--EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2280 lklklkIEKENQELMKKdkdnTKKLLEEEAENMKKL----AEEAARL-NIEAQ-EAARlrqiaESDLAKQRELAEKMLEE 2353
Cdd:pfam05667 381 ------ELEKQYKVKKK----TLDLLPDAEENIAKLqalvDASAQRLvELAGQwEKHR-----VPLIEEYRALKEAKSNK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2354 KKqaiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSleAERKRQLEITAEAEKLKVKVTQ-LS 2432
Cdd:pfam05667 446 ED----ESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRS--AYTRRILEIVKNIKKQKEEITKiLS 519
|
.
gi 1207141751 2433 D 2433
Cdd:pfam05667 520 D 520
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2329-2533 |
3.20e-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: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2329 AARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLE 2408
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2409 AERKRQ-----LEITAEAEKLK------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKL--EV 2475
Cdd:COG3883 94 ALYRSGgsvsyLDVLLGSESFSdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2476 QRLQSKQEADgLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQS 2533
Cdd:COG3883 174 EAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3178-3213 |
3.20e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.20e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1207141751 3178 RLLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEM 3213
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4316-4349 |
3.53e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.53e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141751 4316 EETGPVAGILDTDTLEKVSVTEAMHRNLVDNITG 4349
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1528-1689 |
3.67e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1528 QLRAKAVDADKLRN--AAQEEAEKLRKQVAE-----ETQKKRKAEEELKRKSEAEKDAAKEKKKALED-----LEKFKLQ 1595
Cdd:PRK09510 69 QQQKSAKRAEEQRKkkEQQQAEELQQKQAAEqerlkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEaaakaAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1596 AEEAERHL----KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1671
Cdd:PRK09510 149 AEAEAKRAaaaaKKAAAEAKKKAE--AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170
....*....|....*...
gi 1207141751 1672 REQAEKELETWRQKANEA 1689
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAA 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1480-1731 |
3.70e-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: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1480 SEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELlqlrakavdadklrNAAQEEAEKLRKQVAEETQ 1559
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------------EALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1560 KKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQ---RQIQVVEEVakKTAATQLESKQval 1636
Cdd:COG3883 80 EIEERREELGE-----RARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKiadADADLLEEL--KADKAELEAKK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1637 tARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEE 1716
Cdd:COG3883 150 -AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*
gi 1207141751 1717 AKREAKKRAKAEEAA 1731
Cdd:COG3883 229 AAAAAAAAAAAAAAA 243
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1674-1986 |
4.00e-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: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1674 QAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQ--RKMAEE 1751
Cdd:pfam15964 321 SSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKemKKEREE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1752 TAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQrlkndvnSAVKQKKELEEELIKVRKEMEILLQQkSKAEKEtmsntE 1831
Cdd:pfam15964 401 LGATMLALSQNVAQLEAQVEKVTREKNSLVSQLE-------EAQKQLASQEMDVTKVCGEMRYQLNQ-TKMKKD-----E 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1832 KSKQLLESEAAKMRELA---EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKIlkekltaineaTRLKTEAEIALKEKE 1908
Cdd:pfam15964 468 AEKEHREYRTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQDAARAREECLKL-----------TELLGESEHQLHLTR 536
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 1909 AENDRLKRKAEEEGyqrKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 1986
Cdd:pfam15964 537 LEKESIQQSFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT 611
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2211-2488 |
4.06e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2211 KLAEKTLKQKSSVEEelvkVKVQLDETDKQKSVLDVELKRLKQEVSD-----------AIkQKAQVEDELSKVKIQMEDL 2279
Cdd:PRK04863 359 ELEERLEEQNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtrAI-QYQQAVQALERAKQLCGLP 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2280 LKLKLKIEKENQELMKKDKDNTKKLLEEE-----AENMKKLAEEAARL------NIEAQEAARLRQIAESDLAKQRELAE 2348
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAE 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2349 KM---------LEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITA 2419
Cdd:PRK04863 514 QLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141751 2420 EAEKLKVKVTQLSDAQSKAEE------EAKKFKKQADEIKIRLQETEKHTSEkhtVVEKLEVQRLQSKQEADGLH 2488
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALARlreqsgEEFEDSQDVTEYMQQLLERERELTV---ERDELAARKQALDEEIERLS 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2239-2490 |
4.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2239 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLkiekenqelmkkdkdntkklLEEEAENMKKLAEE 2318
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE--------------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2319 AARLNieaQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ 2398
Cdd:COG4913 670 IAELE---AELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2399 ETEgfqKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKL-EVQR 2477
Cdd:COG4913 746 ELR---ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN---REWPAETADLDADLESLpEYLA 819
|
250
....*....|...
gi 1207141751 2478 LQSKQEADGLHKA 2490
Cdd:COG4913 820 LLDRLEEDGLPEY 832
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1769-2653 |
4.26e-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: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1769 DFEHAEQQRTVLDDELQRLKNDVNSAVK-QKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ-LLESEAAKMRE 1846
Cdd:TIGR00606 55 DFPPGTKGNTFVHDPKVAQETDVRAQIRlQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHgEKVSLSSKCAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1847 LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR----LKTEAEIAL------KEKEAENDRLKR 1916
Cdd:TIGR00606 135 IDREMISHLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRyikaLETLRQVRQtqgqkvQEHQMELKYLKQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1917 KAEEEGYQRKVLEDQAAQhkQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekasSGKQELELEL 1996
Cdd:TIGR00606 215 YKEKACEIRDQITSKEAQ--LESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK-------SRKKQMEKDN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1997 KKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeakvKQIQAAEEEAARQHKaaqeEVGRLMKLAEEAKKQKeiA 2076
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQ----------------RTVREKERELVDCQR----ELEKLNKERRLLNQEK--T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2077 EKEAEKQVILVQEAAQKCsaaEQKAQNVLVQQNKDSMAQDKLKE------EFEKAKKLAQE--AEKAKDNAEKEAALLHK 2148
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQE---HIRARDSLIQSLATRLELDGFERgpfserQIKNFHTLVIErqEDEAKTAAQLCADLQSK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2149 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2228
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2229 KVKVQLDEtdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD--NTKKL-- 2304
Cdd:TIGR00606 501 KEVKSLQN---EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpNKKQLed 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2305 -LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLaKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2383
Cdd:TIGR00606 578 wLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-ESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2384 KLLEAKKEMQQRLDQETEGFQKSL---EAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEI----KIRL 2456
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglaPGRQ 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2457 QETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAiADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFA 2536
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2537 EKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALK---------------------------AEQERQRKLMEEERKKLQS 2589
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktnelkseklqiGTNLQRRQQFEEQLVELST 895
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 2590 AMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSS--QKASYTKEIE 2653
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkNIHGYMKDIE 961
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1114-1318 |
4.74e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1114 LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAediLNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGK 1193
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAAL------EAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1194 QATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRW 1273
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207141751 1274 IADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVED 1318
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1596-1921 |
5.02e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.01 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1596 AEEAERHLKQAELEKQRQIQVVEEVAK------KTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAd 1669
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGqvtesvEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1670 karEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKeeakreaKKRAKAEEAALKQKEAAEMELGNQRKMA 1749
Cdd:pfam02029 83 ---LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR-------LGRYKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1750 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN 1829
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1830 T----EKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQiaeEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALK 1905
Cdd:pfam02029 233 SqereEEAEVFLEAEQ-KLEELRRRRQEKESEEFEKLRQKQ---QEAELELEELKKKREER-RKLLEEEEQRRKQEEAER 307
|
330
....*....|....*.
gi 1207141751 1906 EKEAENDRLKRKAEEE 1921
Cdd:pfam02029 308 KLREEEEKRRMKEEIE 323
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2050-2374 |
5.10e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2050 RQHKAAQEEVGRLMKLAEEAK-----KQ----KEIAEKEAEKqvilvQEAAQKCSAAEQKAqnvlVQQNKDSMAQDKLKE 2120
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeaRQarleREKAAREARH-----KKAAEARAAKDKDA----VAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2121 EFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqaKAQEDAEKLRKEAekeasrraeaeaaalklkQ 2200
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAE--------------KQAAAAADPKKAA------------------V 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2201 EADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqldetdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLL 2280
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAV-------AAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIAR 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2281 KLKLKIEKENQElmkkdkdntkklLEEEAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRElaekmLEEKKQAIqE 2360
Cdd:PRK05035 624 AKAKKAEQQANA------------EPEEPVDPRKAAVAAAI----ARAKARKAAQQQANAEPEEA-----EDPKKAAV-A 681
|
330
....*....|....
gi 1207141751 2361 AAKLKAEAEKLQKQ 2374
Cdd:PRK05035 682 AAIARAKAKKAAQQ 695
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
56-181 |
5.25e-04 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 43.51 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 56 QKKTFTKWVNKHLVKHWKAeaqRHIT-------DLYEDLRDGHNLISLLEVLSGETLPrERDVVRNSRLPrekgrmrFHK 128
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVIpmnpntdDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FII 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 181
Cdd:cd21325 94 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2564-2653 |
5.97e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2564 KKAEALKAEQ-ERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMngKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQS 2642
Cdd:cd16269 200 IEAERAKAEAaEQERKLLEEQQRELEQKLEDQERSYEEHLRQL--KEKMEEERENLLKEQERALESKLKEQEALLEEGFK 277
|
90
....*....|.
gi 1207141751 2643 SQKASYTKEIE 2653
Cdd:cd16269 278 EQAELLQEEIR 288
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2312-2451 |
5.98e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2312 MKKLAEEAARLNIEAQEAARlRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL--LEAK 2389
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAE-EKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLdnLENQ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2390 KEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2451
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE 168
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2323-2602 |
6.65e-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: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2323 NIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiqEAAKLKAEAEKlQKQKDqAQVEAQKLLEAKKemQQRLDQETEG 2402
Cdd:NF012221 1533 NVVATSESSQQADAVSKHAKQDDAAQNALADKERA--EADRQRLEQEK-QQQLA-AISGSQSQLESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2403 FQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQ-ADEIKIRLQEteKHTSEKHTVVEKLEVQRLQSK 2481
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQE--QLDDAKKISGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2482 QEADGLHKAIADLEkekeklkkeaADLQKQSKEMANVQQEqLQQEKTilqQSFFAEKETLLKKEKAIEEEkkklekqfed 2561
Cdd:NF012221 1682 DNQQKVKDAVAKSE----------AGVAQGEQNQANAEQD-IDDAKA---DAEKRKDDALAKQNEAQQAE---------- 1737
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141751 2562 evKKAEAL--KAEQERQRKLMEEERKKLQSAMDAAIKKQKEAE 2602
Cdd:NF012221 1738 --SDANAAanDAQSRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2231-2473 |
6.71e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2231 KVQLDETDKQKSVLDVELKRLKQEVsdAIKQKAQVE-DELSKVKIQ----MEDLLKLKLKIEKENQELMKKDKDNTKKLL 2305
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQI--KTYNKNIEEqRKKNGENIArkqnKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2306 EEEAENMKKLAEEAARLNIEAQEAARLrqiaesdlakqrelaEKMLEEK------KQAIQEAAKLkaeAEKLQKQKDQAQ 2379
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKV---------------IKMYEKGgvcptcTQQISEGPDR---ITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2380 VEAQKLLEAKKEMQQRLDQETE------GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2453
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEqskkllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|
gi 1207141751 2454 IRLQETEKHTSEKHTVVEKL 2473
Cdd:PHA02562 393 KTKSELVKEKYHRGIVTDLL 412
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2107-2453 |
7.01e-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: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2107 QQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKA----EEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE 2182
Cdd:NF033838 112 EAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAkdqkEEDRRNYPTNTYKTLELEIAESDVEVKKAELE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2183 --KEASRRAEAEAAALKLKQEADSEMAKYKKLaEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2260
Cdd:NF033838 192 lvKEEAKEPRDEEKIKQAKAKVESKKAEATRL-EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2261 QKAQVEDElSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAARLR-QIAESD 2339
Cdd:NF033838 271 GEPATPDK-KENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKV--EEAKKKAKDQKEEDRRNYPTNTYKTLElEIAESD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2340 LAKQRELAEKMLEEKKQAIQEAAKLKAEAEklqkqkdqaqveaqklLEAKKEMQQRLDQ-ETEGFQKSLEAERKrqleiT 2418
Cdd:NF033838 348 VKVKEAELELVKEEAKEPRNEEKIKQAKAK----------------VESKKAEATRLEKiKTDRKKAEEEAKRK-----A 406
|
330 340 350
....*....|....*....|....*....|....*..
gi 1207141751 2419 AEAEKLKVKVTQLSDAQS--KAEEEAKKFKKQADEIK 2453
Cdd:NF033838 407 AEEDKVKEKPAEQPQPAPapQPEKPAPKPEKPAEQPK 443
|
|
| DUF2968 |
pfam11180 |
Protein of unknown function (DUF2968); This family of proteins has no known function. |
2309-2385 |
7.53e-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: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2309 AENMKKLAE-EAARLNIEAQEAARLRQIAES---------DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2378
Cdd:pfam11180 88 ARQTAQLADvEIRRAQLEAQKAQTERQIAASearaarlqaDLQVARQQEQQVASRQKQTRQEAAALEAQRQAAQAQLRAL 167
|
....*..
gi 1207141751 2379 QVEAQKL 2385
Cdd:pfam11180 168 QRQIRQL 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2200-2404 |
7.56e-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: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2200 QEADSEMAKYKK---------LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA--QVEDE 2268
Cdd:COG3206 192 EEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2269 LSKVKIQMedllklklkiekenQELMKKDKDNT---KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQre 2345
Cdd:COG3206 272 LAELEAEL--------------AELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ-- 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 2346 laekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQ 2404
Cdd:COG3206 336 -----LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1521-1753 |
7.79e-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: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1521 TAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaLEDLEKFKLQAEEAe 1600
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL--------------QAEIDKLQAEIAEA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1601 rhlkQAELEKQRqiqvvEEVAKKTAATQLESKQVALTARLEES----------------LKNEQVMVIQLQEEAEHLKKQ 1664
Cdd:COG3883 78 ----EAEIEERR-----EELGERARALYRSGGSVSYLDVLLGSesfsdfldrlsalskiADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1665 QAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGN 1744
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
....*....
gi 1207141751 1745 QRKMAEETA 1753
Cdd:COG3883 229 AAAAAAAAA 237
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
562-656 |
7.80e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 562 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 638
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIeegHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1207141751 639 LQYAKLLTSSKTRLRSLD 656
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3430-3463 |
7.83e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.83e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141751 3430 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPE 3463
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2776-2809 |
8.14e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 8.14e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141751 2776 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPE 2809
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1729-1972 |
8.78e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1729 EAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKV 1808
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1809 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLT 1888
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1889 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQR 1968
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
....
gi 1207141751 1969 KVVE 1972
Cdd:COG4372 288 LEEA 291
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1782-2455 |
1.02e-03 |
|
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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1782 DELQRLKNDVNSaVKQK-----KELEEELIKVRKEMEILLQQKSKAEK---ETMSN-----TEKSKQLLESEAAKMRELA 1848
Cdd:TIGR01612 1111 DEINKIKDDIKN-LDQKidhhiKALEEIKKKSENYIDEIKAQINDLEDvadKAISNddpeeIEKKIENIVTKIDKKKNIY 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1849 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKV 1927
Cdd:TIGR01612 1190 DEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKK-KSEHMIKAMEAYIEDlDEIKEKSPEIENEMGI 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1928 LEDQAAQ--------------------HKQAI----------------EEKIGQLKKSSDTELDRQKKIVEETLKQRKVV 1971
Cdd:TIGR01612 1269 EMDIKAEmetfnishdddkdhhiiskkHDENIsdirekslkiiedfseESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1972 EEEIHILKLNFEKA--SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfrKLALEEEKKRKEAEAKVKQIqaaeEEAA 2049
Cdd:TIGR01612 1349 ANIYNILKLNKIKKiiDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD---DINLEECKSKIESTLDDKDI----DECI 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2050 RQHKAAQEEVgrlmkLAEEAKKQKEIAE-KEAEKQVILVqeaAQKCSAAEQKAQNVLVQQnKDSMAQD------KLKEEF 2122
Cdd:TIGR01612 1422 KKIKELKNHI-----LSEESNIDTYFKNaDENNENVLLL---FKNIEMADNKSQHILKIK-KDNATNDhdfninELKEHI 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2123 EKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER--QKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQ 2200
Cdd:TIGR01612 1493 DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKTKKDSEIIIKEIKDAHK----------KFIL 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2201 EADSEMAKYKKLAektlKQKSSVEEELVKV-KVQLDETDKQKSVLDVELKRLK-----QEVSDAIKQKAQVEDELSKVKI 2274
Cdd:TIGR01612 1563 EAEKSEQKIKEIK----KEKFRIEDDAAKNdKSNKAAIDIQLSLENFENKFLKisdikKKINDCLKETESIEKKISSFSI 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2275 QMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEK-MLEE 2353
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKeEIES 1718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2354 KKQAIQEAAKLKAEA------------EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAEA 2421
Cdd:TIGR01612 1719 IKELIEPTIENLISSfntndlegidpnEKLEEYNTEIGDIYEEFIELYNIIAGCLETVS---KEPITYDEIKNTRINAQN 1795
|
730 740 750
....*....|....*....|....*....|....
gi 1207141751 2422 EKLKVKvtqlsdaqskaeEEAKKFKKQADEIKIR 2455
Cdd:TIGR01612 1796 EFLKII------------EIEKKSKSYLDDIEAK 1817
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1769-1938 |
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 1207141751 1769 DFEHAEQQRTVLDDELQRL---------KNDVNSAVKQKKELEEELIkvrkemeillqQKSKAEKetmsnTEKSKQLLES 1839
Cdd:pfam04147 126 DDDSEEEEDGQLDLKRVRRahfgggeddEEEEPERKKSKKEVMEEVI-----------AKSKLHK-----YERQKAKEED 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1840 EAakMRE-----LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE--KILKEkLTAINEAT---RLKTEAEIALKEKE- 1908
Cdd:pfam04147 190 EE--LREeldkeLKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLVRE-LAFDKRAKpsdRTKTEEELAEEEKEr 266
|
170 180 190
....*....|....*....|....*....|....
gi 1207141751 1909 ---AENDRLKR-KAEEEGYQRKvlEDQAAQHKQA 1938
Cdd:pfam04147 267 lekLEEERLRRmRGEEDEEEED--GKKKKKHKSA 298
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2209-2424 |
1.11e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2209 YKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiek 2288
Cdd:PRK09510 64 YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA--------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2289 enQELMKKDKDNTKKLLEEEAenmKKLAEEAARlnieAQEAARLRQIAESDlAKQRELAEKMLEEKKQAiQEAAKLKAEA 2368
Cdd:PRK09510 135 --EEAAAKAAAAAKAKAEAEA---KRAAAAAKK----AAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAA-KAAAEAKKKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 2369 EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2424
Cdd:PRK09510 204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2303-2533 |
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 1207141751 2303 KLLEEEAENMKKLAEEaarlniEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ-KQKDQAQVE 2381
Cdd:pfam17045 38 DIREEELLSARNTLER------KHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQrKQLKEAREE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2382 AQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITaeaeklkvKVTQLsDAQSKA-EEEAKKFKKQADEIKI--RLQE 2458
Cdd:pfam17045 112 AKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQ--------QVASL-EAQRKAlAEQSSLIQSAAYQVQLegRKQC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2459 TEKHTSEKHTVVEKLEVQR---LQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKeMANVQQEQLQQEKTILQQS 2533
Cdd:pfam17045 183 LEASQSEIQRLRSKLERAQdslCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELR-MSQRQLQVLQNELMELKAT 259
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
56-180 |
1.19e-03 |
|
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: 42.30 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 56 QKKTFTKWVNKHLVKHWKAeaqRHIT-------DLYEDLRDGHNLISLLEVLSGETLPrERDVVRNSRLPrekgrmrFHK 128
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVIpmnpntdDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTI 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 129 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 180
Cdd:cd21324 94 QENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2233-2466 |
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 1207141751 2233 QLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKL------LE 2306
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkeeRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2307 EEAENMKKLAEEAARLNIEAQEAARLR-----------------QIAESDLAKQRELAEKM------LEEKKQAIQEAAK 2363
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGgsidklrkeierlewrqQTEVLSPEEEKELVEKIkelekeLEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2364 LKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2443
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE-ADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|...
gi 1207141751 2444 KFKKQADEIKIRLQETEKHTSEK 2466
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKE 263
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3467-3503 |
1.24e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.24e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141751 3467 KLLSAEKAVTGYKDPYTGNKISLLQAMQKQLVLREHA 3503
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1647-1813 |
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 1207141751 1647 EQVMVIQLQE---EAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKtaaqeeAEKQKEEAKREAKK 1723
Cdd:COG1579 5 DLRALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1724 RAKAEEAA-LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELE 1802
Cdd:COG1579 79 EEQLGNVRnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|.
gi 1207141751 1803 EELIKVRKEME 1813
Cdd:COG1579 159 EELEAEREELA 169
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1544-1759 |
1.39e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1544 QEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhLKQAELEKQRQIQVVE----- 1618
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAK-AKAAALAKQKREGTEEvteee 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1619 -EVAKKTAATQLESKQVALTArleeslkneqvmviQLQEEAEHLKKQQAEADKAREQAEKeletwRQKANEALRLRLQAE 1697
Cdd:PRK07735 90 kAKAKAKAAAAAKAKAAALAK--------------QKREGTEEVTEEEKAAAKAKAAAAA-----KAKAAALAKQKREGT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 1698 EEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1759
Cdd:PRK07735 151 EEV-----TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKA 207
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1349-1699 |
1.48e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1349 SPLKKA--KMESASD------DIIQEYVTLRTRYSELMTLSSQYIK---FIIETQRRLQDEEK--------AAEKLKEEE 1409
Cdd:PRK04863 226 SGVRKAfqDMEAALRenrmtlEAIRVTQSDRDLFKHLITESTNYVAadyMRHANERRVHLEEAlelrrelyTSRRQLAAE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1410 RKKMAEMQAELEKQK--------------------QLAETHAKAIAKAEQEANELKTKMKD--EVSKRQDVAVD-SEKQK 1466
Cdd:PRK04863 306 QYRLVEMARELAELNeaesdleqdyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEqnEVVEEADEQQEeNEARA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1467 HNIQRELQELKT--------LSEQEIKA-KSQQVEEAL-----------LSRTRIEEEIHIIRLQLEttmkqknTAETEL 1526
Cdd:PRK04863 386 EAAEEEVDELKSqladyqqaLDVQQTRAiQYQQAVQALerakqlcglpdLTADNAEDWLEEFQAKEQ-------EATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1527 LQLRAKAVDADKLRNAAQEEAEKLRKQVAE--ETQKKRKAEEELK--RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERH 1602
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVRKIAGEvsRSEAWDVARELLRrlREQRHLAEQLQQLRMRLSELEQRLRQQQRAERL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1603 LKQAElekQRQIQVVEevakktAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHlkkQQAEADKAREQAEKELETW 1682
Cdd:PRK04863 539 LAEFC---KRLGKNLD------DEDELEQLQEELEARL-ESLSESVSEARERRMALRQ---QLEQLQARIQRLAARAPAW 605
|
410
....*....|....*...
gi 1207141751 1683 RQkANEAL-RLRLQAEEE 1699
Cdd:PRK04863 606 LA-AQDALaRLREQSGEE 622
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1542-1871 |
1.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1542 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1621
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1622 KktAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAN 1701
Cdd:COG4372 122 K--ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1702 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLD 1781
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1782 DELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA 1861
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
330
....*....|
gi 1207141751 1862 KKQRQIAEEE 1871
Cdd:COG4372 360 SKGAEAGVAD 369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1661-1980 |
1.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1661 LKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1740
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1741 ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS 1820
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1821 KAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 1900
Cdd:COG4372 168 ALEQE---LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1901 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL 1980
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
1719-1929 |
1.70e-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: 44.70 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1719 REAKKRAKAEEAALkQKEAAemelgNQRKMAEETAKQKLAAEQE---------LIRLRADFEHAEQQRTVLD-------- 1781
Cdd:NF033875 66 SETPKTAVSEEATV-QKDTT-----SQPTKVEEVASEKNGAEQSsatpndttnAQQPTVGAEKSAQEQPVVSpettnepl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1782 ---DELQRLKNDVNSAVKQKKELE-----EELIKVRKEMEILLQQKSKaekETMSNTEkSKQLleseAAKMRElaeeatk 1853
Cdd:NF033875 140 gqpTEVAPAENEANKSTSIPKEFEtpdvdKAVDEAKKDPNITVVEKPA---EDLGNVS-SKDL----AAKEKE------- 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 1854 lrsVAEEAKKQRQIAEEEAARQRAEAEKILKEKltaineatrlkteAEIALKEkeaendrlkrKAEEEGYQRKVLE 1929
Cdd:NF033875 205 ---VDQLQKEQAKKIAQQAAELKAKNEKIAKEN-------------AEIAAKN----------KAEKERYEKEVAE 254
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1719-1975 |
1.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1719 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1798
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1799 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA---AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQ 1875
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdleQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1876 RAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELD 1955
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260
....*....|....*....|
gi 1207141751 1956 RQKKIVEETLKQRKVVEEEI 1975
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEE 262
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1528-1819 |
1.83e-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: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1528 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1607
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1608 LEKQRQIQVVEEVAKKTAATQLESKQVALTAR----LEESLKNEQVMVIQLQ----EEAEHLKKQQAEADKAREQ----A 1675
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekEEEREEDERILEYLKEkaerEEEREAEREEIEEEKEREIarlrA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1676 EKELETWRQKANEALRLRLQAEE---EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1752
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEqerKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 1753 AKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1819
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1195-1790 |
2.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1195 ATFDRLEEELQRATE---VNKRMSQLHSERDVELEHYRQLVGnLRERWQAVFAQielrqRELDLLNRQMQAYRESYDWLI 1271
Cdd:COG4913 235 DDLERAHEALEDAREqieLLEPIRELAERYAAARERLAELEY-LRAALRLWFAQ-----RRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1272 RWIADAKQRQDKLHAVpiggSKGLQEQLTQ-----EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVT----YKA 1342
Cdd:COG4913 309 AELERLEARLDALREE----LDELEAQIRGnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1343 LVEPIASplKKAKMESASDDIIQEYVTLRTRYSELMtlssqyikfiiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK 1422
Cdd:COG4913 385 LRAEAAA--LLEALEEELEALEEALAEAEAALRDLR-----------RELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1423 QKQLAETHAKAIA-----KAEQEA---------NELKTKM------KDEVSKrqdvAVDSEKQKHNIQ-------RELQE 1475
Cdd:COG4913 452 ALGLDEAELPFVGelievRPEEERwrgaiervlGGFALTLlvppehYAAALR----WVNRLHLRGRLVyervrtgLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1476 LKTLSEQ----EIKAKSQQVEEALlsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAV-----DADKLR------ 1540
Cdd:COG4913 528 RPRLDPDslagKLDFKPHPFRAWL--EAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGNGTrhekdDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1541 --NAAQEEAekLRKQVAEETQKKRKAEEELKrkseaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQvVE 1618
Cdd:COG4913 606 fdNRAKLAA--LEAELAELEEELAEAEERLE-----------------------ALEAELDALQERREALQRLAEYS-WD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1619 EVAKKTAATQLESKQVALtarleESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEE 1698
Cdd:COG4913 660 EIDVASAEREIAELEAEL-----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1699 EANKKTAAQEEAEKQkeeakrEAKKRAKAEEAALKQKEAAEmELGNQRKMAEETAKQklaAEQELIRLRADF------EH 1772
Cdd:COG4913 735 RLEAAEDLARLELRA------LLEERFAAALGDAVERELRE-NLEERIDALRARLNR---AEEELERAMRAFnrewpaET 804
|
650 660
....*....|....*....|...
gi 1207141751 1773 AEQQRTVLD-----DELQRLKND 1790
Cdd:COG4913 805 ADLDADLESlpeylALLDRLEED 827
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1658-1882 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1658 AEHLKKQQAEADKAREQAEKELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEeAALKQKEA 1737
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR-AELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1738 AEMELGNQRKMAEETAKQkLAAEQELIRLRADFEHAEQQRTVL-------DDELQRLKNDVNSAVKQ-KKELEEELIKVR 1809
Cdd:COG3206 241 RLAALRAQLGSGPDALPE-LLQSPVIQQLRAQLAELEAELAELsarytpnHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141751 1810 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI 1882
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4043-4074 |
2.09e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.09e-03
10 20 30
....*....|....*....|....*....|..
gi 1207141751 4043 KLLSAERAVTGYKDPYSGKVISLFQAMKKGLI 4074
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1402-1638 |
2.22e-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: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1402 AEKLKEEERKKMAEMQAELEK-QKQLAETHAKaIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKT-L 1479
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAaQAELDALQAE-LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1480 SEQEIKAKSQQVEEALLSRTRIEEEIHiiRLQLETTMKQKNTAETELLQLRAKAVDADKlrNAAQEEAEKLRKQVAEETQ 1559
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLD--RLSALSKIADADADLLEELKADKAELEAKK--AELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 1560 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTA 1638
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1750-1880 |
2.26e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1750 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsN 1829
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE---R 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141751 1830 TEKSKQLLEsEAAKMRELAEEAT------KLRSVAEEAKKQR----QIAEEEAARQRAEAE 1880
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETrilidqQLRKAGWEADSKTlrfsKGARPEKGRNLAIAE 274
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3140-3176 |
2.45e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.45e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141751 3140 KLLSAERAVCGYKDPYTGKTVSLFEAMQKDLIKKEQG 3176
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1837-1967 |
2.57e-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: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1837 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAarqRAEAEKILKEkltAINEATRLKTEaeiALKEKEAENDRLKR 1916
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 1917 KAEEEGYQ-----RKVLEDQAAQHKQAIEEKIgqLKKSSDTelDRQKKIVEETLKQ 1967
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKI--LGKELDA--AAQAALVDRFIAE 151
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3968-4006 |
2.60e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.60e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 3968 YLEGISSIAGVFVEATKDRLSVYQAMKKTMIRPGTAFEL 4006
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2221-2461 |
2.64e-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: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2221 SSVEEELVKVKVQLDETDKQKSVLDVEL-KRLKQEVSDAIKQKAQVEDELSKVkiqMEDLLKLKLKIEKENQELMKKdkd 2299
Cdd:COG5185 206 SIKESETGNLGSESTLLEKAKEIINIEEaLKGFQDPESELEDLAQTSDKLEKL---VEQNTDLRLEKLGENAESSKR--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2300 ntkklLEEEAENMKKLAEEAARLNIEAQEAARLRQ-IAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2377
Cdd:COG5185 280 -----LNENANNLIKQFENTKEKIAEYTKSIDIKKaTESLEEQLAAAEAEQELEESKRETETGiQNLTAEIEQGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2378 AQVEAQKLLEAKKEMQQ--RLDQETEGFQKSLEAERKRQLEITAEAEK-LKVKVTQLSDAQSKAEEEAKKFKKQADEIKI 2454
Cdd:COG5185 355 NLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGyAQEILATLEDTLKAADRQIEELQRQIEQATS 434
|
....*..
gi 1207141751 2455 RLQETEK 2461
Cdd:COG5185 435 SNEEVSK 441
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1762-1910 |
2.71e-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: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1762 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAE----KETMSNTEKSKQLL 1837
Cdd:pfam05911 682 ENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAEtqlkCMAESYEDLETRLT 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1838 ESEaAKMRELAEEATKLRSVAEEakkQRQIAEEEAAR--------QRAEAEKILKEklTAINEATRLKTEAEI-ALKEKE 1908
Cdd:pfam05911 762 ELE-AELNELRQKFEALEVELEE---EKNCHEELEAKclelqeqlERNEKKESSNC--DADQEDKKLQQEKEItAASEKL 835
|
..
gi 1207141751 1909 AE 1910
Cdd:pfam05911 836 AE 837
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2302-2449 |
2.73e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2302 KKLLEEEAENMKKLAEEAARLNIEAQEAAR---LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2378
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2379 QVEAQKLLEAKKEMQQRLDQETEGFQK--SLEAERKRQ-----LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2449
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKlllklLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
2371-2453 |
2.91e-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: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2371 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgfQKSLEAERKRQLeiTAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2450
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDD--EKQELLAEYRAL--KAELESLEVYNRQLERLVASQEQEIASLERQIE 86
|
...
gi 1207141751 2451 EIK 2453
Cdd:pfam11932 87 EIE 89
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2222-2460 |
3.03e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2222 SVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklKIEKENQELMKKDKDnt 2301
Cdd:PRK01156 194 SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-------MKNRYESEIKTAESD-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2302 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2381
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141751 2382 AQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2460
Cdd:PRK01156 345 KSRYDDLNNQILE-LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2213-2530 |
3.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2213 AEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenQE 2292
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA-----------QE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2293 LMKKDKDNTKKLLEEeaenMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2372
Cdd:COG4372 102 ELESLQEEAEELQEE----LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2373 KQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEI 2452
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2453 KIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2530
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
56-170 |
3.35e-03 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 41.11 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 56 QKKTFTKWVNKHLVKhwKAEAQRHI------TDLYEDLRDGHNLISLLEVLSGETLPrERDVVRNSRLPrekgrmrFHKL 129
Cdd:cd21292 25 EKVAFVNWINKNLGD--DPDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTID-ERAINKKKLTV-------FTIH 94
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141751 130 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 170
Cdd:cd21292 95 ENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1791-2328 |
3.50e-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: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1791 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA---KKQRQI 1867
Cdd:COG5185 3 QRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQndvKKSESS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1868 AEEEAARQRA-EAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 1943
Cdd:COG5185 83 VKARKFLKEKkLDTKILQEYVNSLIKLPNYEWSADILislLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1944 GQLKKSSDTELDRQKK--IVEETLKQRKVVEEEihiLKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2021
Cdd:COG5185 163 DIFGKLTQELNQNLKKleIFGLTLGLLKGISEL---KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2022 KLALEEEKKRKEA---EAKVKQIQAAEEEAARQH----KAAQEEVGRLMKLAEEAKKQkeIAEKEAEKQVILVQEAAQKC 2094
Cdd:COG5185 240 DPESELEDLAQTSdklEKLVEQNTDLRLEKLGENaessKRLNENANNLIKQFENTKEK--IAEYTKSIDIKKATESLEEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2095 SAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedA 2174
Cdd:COG5185 318 LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEE------------------L 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2175 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEK-------TLKQKSSVEEELVKVKVQLDE--TDKQKSVLD 2245
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRqieelqrQIEQATSSNEEVSKLLNELISelNKVMREADE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2246 VELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIE 2325
Cdd:COG5185 460 ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
...
gi 1207141751 2326 AQE 2328
Cdd:COG5185 540 ALE 542
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1719-2155 |
3.50e-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: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1719 REAKKRAKAEEAALKQKEAAEMElgnQRKMAEETAKQKLAAEQELIRLRADFEHAEQQrtvlddelqrlkndvnsAVKQK 1798
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEE-----------------AREAK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1799 KELEEELIKVRKEMEillQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE----EEAAR 1874
Cdd:COG3064 62 AEAEQRAAELAAEAA---KKLAEAEKAA----AEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAkrkaEEEAK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1875 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTEL 1954
Cdd:COG3064 135 RKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1955 DRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEA 2034
Cdd:COG3064 215 ALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2035 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMA 2114
Cdd:COG3064 295 LVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGA 374
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1207141751 2115 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2155
Cdd:COG3064 375 LLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAA 415
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4322-4352 |
3.50e-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: 3.50e-03
10 20 30
....*....|....*....|....*....|.
gi 1207141751 4322 AGILDTDTLEKVSVTEAMHRNLVDNITGQRL 4352
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1176-1702 |
3.56e-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: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1176 IEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLrERWQAVFAQIELRQRELDL 1255
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNL-EKKQKKFDQMLAEEKAISA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1256 lnrqmqAYRESYDwliRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK-NKDKVEDCQKFAKGYIDAIKDYE 1334
Cdd:pfam01576 619 ------RYAEERD---RAEAEAREKETRALS--------LARALEEALEAKEELERtNKQLRAEMEDLVSSKDDVGKNVH 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1335 lQLVTYKALVEPIASPLkKAKMESASDDI-IQEYVTLRTRYSeLMTLSSQYikfiietQRRLQDEEKAAEKLKEEERKKM 1413
Cdd:pfam01576 682 -ELERSKRALEQQVEEM-KTQLEELEDELqATEDAKLRLEVN-MQALKAQF-------ERDLQARDEQGEEKRRQLVKQV 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1414 AEMQAELE---KQKQLAETHAKaiaKAEQEANELKTKMkDEVSKRQDVAVDSEK----QKHNIQRELQELKtLSEQEIKA 1486
Cdd:pfam01576 752 RELEAELEderKQRAQAVAAKK---KLELDLKELEAQI-DAANKGREEAVKQLKklqaQMKDLQRELEEAR-ASRDEILA 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1487 KSQQVEEALLSrtrIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVA---EETQKKRK 1563
Cdd:pfam01576 827 QSKESEKKLKN---LEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAqleEELEEEQS 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1564 AEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK---KTAATQLESKQVALTARL 1640
Cdd:pfam01576 904 NTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKskfKSSIAALEAKIAQLEEQL 983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1641 EESLKNEQVMVIQLQEEAEHLKK-------QQAEADKAREQAEKELETWRQkaneaLRLRL-QAEEEANK 1702
Cdd:pfam01576 984 EQESRERQAANKLVRRTEKKLKEvllqvedERRHADQYKDQAEKGNSRMKQ-----LKRQLeEAEEEASR 1048
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2305-2451 |
3.85e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2305 LEEEAENMKKLAEEAARLNIEAQE--AARLRQIAESDLAKQ-RELAEKMLEEKKQAIQ----EAAKLKAEAEKLQKQKDQ 2377
Cdd:PRK07735 37 LEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAALAKQkREGTEEVTEEEKAKAKakaaAAAKAKAAALAKQKREGT 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2378 AQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2451
Cdd:PRK07735 117 EEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGE 190
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2302-2451 |
3.91e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2302 KKLLEEEAENMKKLAE---EAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2377
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLE-AKEEIHKLRNEFEKELRERRNELQKLeKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141751 2378 AQVEAQKLLEAKKEMQQRLDQ--ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2451
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQEleKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
58-167 |
4.13e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.39 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 58 KTFTKWVNKHLVKHwkaeaqrHITDLYEDLRDGhnlISLLEVLSGETLPRERDVVRNSRLPREKGRM-RFHKLQNVQIAL 136
Cdd:COG5069 382 RVFTFWLNSLDVSP-------EITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRFKAFENENYAV 451
|
90 100 110
....*....|....*....|....*....|.
gi 1207141751 137 DFLKHRQVKLVNIRNDDIADGNpKLTLGLIW 167
Cdd:COG5069 452 DLGITEGFSLVGIKGLEILDGI-RLKLTLVW 481
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1842-1985 |
4.17e-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: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1842 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEE 1921
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1922 GYQRKVLEDQAAQHKQAIEE------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKA 1985
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2116-2424 |
4.32e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2116 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAA 2195
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2196 LKLKQEADSEMAKYKKLAEKTLKQKSSVEEelvkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ 2275
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDE-------FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2276 MEDLLKLKLKIEKENQELMKKDKDN-----TKKLLEEEAENMKKLAEEAARLNIEAQEA---ARLRQIAESDLAKQRElA 2347
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAErdelrAKLYQEEQERKERQKEREEAEKKARQRQElqqAREEQIELKERRLAEE-A 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2348 EKMLEEKKQAIQEAAKL----KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET-EGFQKSLEAERKRQLEITAEAE 2422
Cdd:pfam13868 257 EREEEEFERMLRKQAEDeeieQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEElEEGERLREEEAERRERIEEERQ 336
|
..
gi 1207141751 2423 KL 2424
Cdd:pfam13868 337 KK 338
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2419-2628 |
4.37e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2419 AEAEKLKVKVtqlsdAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEK 2498
Cdd:PRK09510 75 KRAEEQRKKK-----EQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2499 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKEtllkkekaieeekkkLEKQFEDEVKKaealKAEQERQRK 2578
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAE---------------AAAKAAAEAKK----KAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2579 LMEEERKKlqSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE 2628
Cdd:PRK09510 211 AAAEAKKK--AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
2303-2425 |
4.49e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.17 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2303 KLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdLAKQrelAEKMLEEKKQAIQEAAKLKAEA-----EKLQKQKDQ 2377
Cdd:PRK00290 499 GLSDEEIERMVKDAEANAEEDKKRKELVEARNQADS-LIYQ---TEKTLKELGDKVPADEKEKIEAaikelKEALKGEDK 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2378 AQVEA--QKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLK 2425
Cdd:PRK00290 575 EAIKAktEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDDVVDAEFEEVK 624
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2211-2541 |
4.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2211 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkieken 2290
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2291 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEK 2370
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2371 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2450
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2451 EIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2530
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
330
....*....|.
gi 1207141751 2531 QQSFFAEKETL 2541
Cdd:COG4372 312 ALEDALLAALL 322
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1461-1672 |
4.95e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1461 DSEKQKHNIQRElqelktlSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdADKlr 1540
Cdd:COG2268 200 DARIAEAEAERE-------TEIAIAQANREAEEA---ELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEA-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1541 nAAQEEAEKLRKQVAEETQKKRKAEE-ELKRKseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQRQIQVVE- 1618
Cdd:COG2268 267 -AYEIAEANAEREVQRQLEIAEREREiELQEK------------------EAEREEAELEADVRKPAEAEKQAAEAEAEa 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141751 1619 --EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-LQEEAEHLKKQQAEADKAR 1672
Cdd:COG2268 328 eaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEkLPEIAEAAAKPLEKIDKIT 384
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2305-2640 |
4.97e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2305 LEEEAENMKKLAEE----AARLNIeAQEAARLR-QI--AESDLAkqrELAEKmLEEKKQAIQEAAKLKAEAEKlqkQKDQ 2377
Cdd:PRK04863 316 LAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER-LEEQNEVVEEADEQQEENEA---RAEA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2378 AQveaQKLLEAKKEM---QQRLD-QETEG--FQKSLEA-ERKRQL----------------EITAEAEKLKVKV----TQ 2430
Cdd:PRK04863 388 AE---EEVDELKSQLadyQQALDvQQTRAiqYQQAVQAlERAKQLcglpdltadnaedwleEFQAKEQEATEELlsleQK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2431 LSDAQSKAEEEAKKFK---KQADEI-KIRLQETEKHTSEKHTVvEKLEVQRLQSKQEAdglHKAIADLEKEKEKLKKEAA 2506
Cdd:PRK04863 465 LSVAQAAHSQFEQAYQlvrKIAGEVsRSEAWDVARELLRRLRE-QRHLAEQLQQLRMR---LSELEQRLRQQQRAERLLA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2507 DLQKQSKEMANVQQ--EQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME--- 2581
Cdd:PRK04863 541 EFCKRLGKNLDDEDelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsg 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 2582 ---EERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLAEENKNLrEKLQQL 2640
Cdd:PRK04863 621 eefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI---ERLSQPGGSED-PRLNAL 678
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1071-1494 |
5.05e-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: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1071 TQRATEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ 1150
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1151 GAE-DILNKYENQLREVNKVPVNEKEIEASQ----TQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVEL 1225
Cdd:pfam05483 436 GKEqELIFLLQAREKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1226 EHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESY----DWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQ 1301
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1302 EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMEsasddiIQEYVTLRTRYSELMTLS 1381
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK------FEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1382 SQYIKFIIETQRRLQDEE-KAAEKLKEEERKKMAEMQAELEKQKQlaeTHAKAIAKAEQEANELKTKMKDEVSKRqdvaV 1460
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAvKLQKEIDKRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAK----A 742
|
410 420 430
....*....|....*....|....*....|....
gi 1207141751 1461 DSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEA 1494
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1794-1920 |
5.25e-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: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1794 AVKQKKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1873
Cdd:pfam20492 4 AEREKQELEERLKQYEEETK-------KAQEELEESEETAEELEE----ERRQAEEEAERLEQKRQEAEEEKERLEESAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141751 1874 RQRAEAEKILKEKLTAINEATRLKTEAEialkEKEAENDRLKRKAEE 1920
Cdd:pfam20492 73 MEAEEKEQLEAELAEAQEEIARLEEEVE----RKEEEARRLQEELEE 115
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1538-1703 |
5.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1538 KLRNAAQEEAEKLRKQVAEETQK-----KRKAEEELKrkseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQR 1612
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKeaeaiKKEALLEAK--------------------EEIHKLRNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1613 Q----IQVVEEVAKKTAAtqLESKQVALTARlEESLKNEQVMVIQLQEEAEHLKKQQAE---------ADKAR----EQA 1675
Cdd:PRK12704 87 LekrlLQKEENLDRKLEL--LEKREEELEKK-EKELEQKQQELEKKEEELEELIEEQLQelerisgltAEEAKeillEKV 163
|
170 180
....*....|....*....|....*...
gi 1207141751 1676 EKELETwrQKANEALRLRLQAEEEANKK 1703
Cdd:PRK12704 164 EEEARH--EAAVLIKEIEEEAKEEADKK 189
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2050-2154 |
5.43e-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: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2050 RQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLA 2129
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREA-------QQNYERELVLHAEDIKALQALREELNELKAEI 73
|
90 100
....*....|....*....|....*
gi 1207141751 2130 QEAEKAKDNAEKEAALLHKKAEEAE 2154
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQK 98
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1605-1922 |
5.58e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1605 QAELEKQRQiQVVEevAKKTAATQLESKQVALTARLEESLKNE---QVMVIQLQEEAEHLKKQQAEADKAREQAEKELET 1681
Cdd:PLN03229 435 EGEVEKLKE-QILK--AKESSSKPSELALNEMIEKLKKEIDLEyteAVIAMGLQERLENLREEFSKANSQDQLMHPVLME 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1682 WRQKANEALRLRL-QAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR-KMA---EETAKQK 1756
Cdd:PLN03229 512 KIEKLKDEFNKRLsRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKeKMEalkAEVASSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1757 LAAEQELirlradfehaeqqrtvlDDELqrlkndVNSAVKQKKELEEELIKVRKEME---ILLQQKSKAEKETMSNTEKS 1833
Cdd:PLN03229 592 ASSGDEL-----------------DDDL------KEKVEKMKKEIELELAGVLKSMGlevIGVTKKNKDTAEQTPPPNLQ 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1834 KQL--LESEAAKMRELAEEATKLRSVAEEAKKqrQIAEEEAARQRAEAEKI------LKEKLTAINEATRLKT-----EA 1900
Cdd:PLN03229 649 EKIesLNEEINKKIERVIRSSDLKSKIELLKL--EVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSELKEkfeelEA 726
|
330 340
....*....|....*....|....
gi 1207141751 1901 EIALKEK--EAENDRLKRKAEEEG 1922
Cdd:PLN03229 727 ELAAAREtaAESNGSLKNDDDKEE 750
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1766-2153 |
5.77e-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: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1766 LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMR 1845
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1846 ELAEEATKLrSVAEEAKKQRqIAEEEAARQRAEAEKILKEkltaiNEATRLKTEAEIA---LKEKEAENDRLKRKAEEEG 1922
Cdd:pfam07888 112 ELSEEKDAL-LAQRAAHEAR-IRELEEDIKTLTQRVLERE-----TELERMKERAKKAgaqRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1923 YQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIveeTLKQRKVVEEEIHILKLNF--EKASSGKQELELELKKLK 2000
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL---TTAHRKEAENEALLEELRSlqERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2001 GIAdeTQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE---------EVGRLMKLAEEAKK 2071
Cdd:pfam07888 262 SMA--AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrieklsaELQRLEERLQEERM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2072 QKEIAEKE--AEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKlKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK 2149
Cdd:pfam07888 340 EREKLEVElgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK-QELLEYIRQLEQRLETVADAKWSEAALTSTE 418
|
....
gi 1207141751 2150 AEEA 2153
Cdd:pfam07888 419 RPDS 422
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1529-1687 |
5.80e-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: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1529 LRAKAVDADKLRNAAQEEAEK------LRKQVAEETQK---KRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA 1599
Cdd:pfam13904 61 LAAKQRQRQKELQAQKEEREKeeqeaeLRKRLAKEKYQewlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1600 ERHLKQAELEKQRQIQvveevAKKtaatqleskqvaltarleeslkneqvmviqlQEEAEHLKKQQAEADKAREQAEKEL 1679
Cdd:pfam13904 141 KEVLQEWERKKLEQQQ-----RKR-------------------------------EEEQREQLKKEEEEQERKQLAEKAW 184
|
....*...
gi 1207141751 1680 ETWRQKAN 1687
Cdd:pfam13904 185 QKWMKNVK 192
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2316-2460 |
6.52e-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: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2316 AEEAARLNIEAQEAARLRQIAESDLAKQRELAEKML--EEKKQAIQEAAKLKAEAEKL-QKQKDQAQVEAQKLLEAKKEM 2392
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLEKEEEERLRkeELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEER 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141751 2393 QQRLDQETEGFQKSLEAERKRQLEitaEAEKLKVKVTQLsdaQSKAEEEAKKFKKQADEIKIRLQETE 2460
Cdd:pfam05672 89 EQREQEEQERLQKQKEEAEAKARE---EAERQRQEREKI---MQQEEQERLERKKRIEEIMKRTRKSD 150
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1417-1677 |
6.53e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1417 QAELEKQKQlaethAKAiAKAEQEANELKTKMKDEVSKrqdvAVDSEKQKHNIQRELQELKTLSEQEIKA-KSQQVEEAL 1495
Cdd:PRK05035 459 QARLEREKA-----ARE-ARHKKAAEARAAKDKDAVAA----ALARVKAKKAAATQPIVIKAGARPDNSAvIAAREARKA 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1496 LSRTRIEEEihiirlqlettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKlrKQVAEETQKKRKAEEEL---KRKS 1572
Cdd:PRK05035 529 QARARQAEK-------------QAAAAADPKKAAVAAAIARAKAKKAAQQAANA--EAEEEVDPKKAAVAAAIaraKAKK 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1573 EAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAtqleskqVALTARLEESLKNEQVMVI 1652
Cdd:PRK05035 594 AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-------VAAAIARAKARKAAQQQAN 666
|
250 260
....*....|....*....|....*
gi 1207141751 1653 QLQEEAEHLKKQQAEADKAREQAEK 1677
Cdd:PRK05035 667 AEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1837-2079 |
6.61e-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: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1837 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTeAEIALKEKEAENDRLK 1915
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1916 RKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekassgkqelele 1995
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---------------- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1996 lkklkgiadetqkskakaeeeaEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEI 2075
Cdd:COG4913 366 ----------------------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
....
gi 1207141751 2076 AEKE 2079
Cdd:COG4913 424 LEAE 427
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1588-1804 |
6.62e-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: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1588 DLEKFKLQAEEAERHLKQAE-----LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1662
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKkeekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1663 KQQAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAkaeEAALKQKEAAEMEL 1742
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAEL---EAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141751 1743 GNQRKmaeETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1804
Cdd:COG4942 184 EEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1393-1703 |
6.67e-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: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1393 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEAN---ELKTKMKDEVSKRQDVAVDSEKQKHNI 1469
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrqELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1470 QRELQELKTLSEQEIKAKSQQVEEALlsrtriEEEIHIIRLQLEttMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEK 1549
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLR------EEIDEFNEEQAE--WKELEKEEEREEDERILEYLKEKAEREEEREAER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1550 LRKQVAEETQKKRKAEEELKRKseaekdaakeKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQL 1629
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQ----------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 1630 ESKQVALTARLEESlKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKK 1703
Cdd:pfam13868 246 ELKERRLAEEAERE-EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGE 318
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2295-2441 |
6.68e-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: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2295 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQ---EAAKLKAEAEKL 2371
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141751 2372 QKQKDQA---QVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2441
Cdd:COG1579 102 KRRISDLedeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4006-4040 |
7.09e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 7.09e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141751 4006 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEF 4040
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
2291-2398 |
7.14e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 40.06 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2291 QELMKKDKDNTKKLLEEEAEnmkkLAEEAARLNIEAQEAARlrQIAESDLAKQRELAEKMLEEKKQAIqeAAKLKAEAEK 2370
Cdd:PRK08476 40 NASIKNDLEKVKTNSSDVSE----IEHEIETILKNAREEAN--KIRQKAIAKAKEEAEKKIEAKKAEL--ESKYEAFAKQ 111
|
90 100
....*....|....*....|....*....
gi 1207141751 2371 LQKQKDQAQVEAQ-KLLEAKKEMQQRLDQ 2398
Cdd:PRK08476 112 LANQKQELKEQLLsQMPEFKEALNAKLSK 140
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2560-2642 |
7.15e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.67 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2560 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEE----MNGKQKEM--QDLEK--KRIEQeklLAEEN- 2630
Cdd:pfam13779 495 QERLSEALERGASDEEIAKLMQELREALDDYMQALAEQAQQNPQDlqqpDDPNAQEMtqQDLQRmlDRIEE---LARSGr 571
|
90
....*....|...
gi 1207141751 2631 -KNLREKLQQLQS 2642
Cdd:pfam13779 572 rAEAQQMLSQLQQ 584
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
671-751 |
7.39e-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: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 671 WLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTAALQTQWSWILQL 750
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 1207141751 751 C 751
Cdd:pfam00435 96 A 96
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1834-1948 |
7.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1834 KQLLESEAAKMRELA----EEATKlrsVAEEAKKQRQI-AEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 1908
Cdd:PRK12704 26 KKIAEAKIKEAEEEAkrilEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141751 1909 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKK 1948
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1786-1903 |
7.78e-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: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1786 RLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 1865
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141751 1866 qiaeEEAARQRAEAEKILKEKLTAINEATRLK----TEAEIA 1903
Cdd:COG0542 481 ----EQRYGKIPELEKELAELEEELAELAPLLreevTEEDIA 518
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
859-893 |
7.79e-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: 7.79e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141751 859 EITVHKGDECALVNNSQPYkWKVRDSSGNEAVVPS 893
Cdd:cd11764 15 ELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
2343-2459 |
7.91e-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: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 2343 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKR-QLEITAEA 2421
Cdd:pfam16535 37 QQQKGLELSDEFQTALSEAEEATDAYEKAINKLKNAKSKAKAAEKKIDQAQTRLQSLAPDSPGKAKLEAAEqQAGIKKDA 116
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141751 2422 EKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQET 2459
Cdd:pfam16535 117 LQADRTLDKALDAASKLTTKAMAKEKEADDFSAKFQGT 154
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1604-1943 |
7.94e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1604 KQAELEKQRQIQVVEEVAKKTAATQLESKQV-ALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETW 1682
Cdd:COG5022 822 LQKTIKREKKLRETEEVEFSLKAEVLIQKFGrSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVN 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1683 RQKANEALRLRLQAEEEANKKTAaqeeaekqkeeakreakkrakaeeaaLKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1762
Cdd:COG5022 902 LELESEIIELKKSLSSDLIENLE--------------------------FKTELIARLKKLLNNIDLEEGPSIEYVKLPE 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1763 LIRLRadfehaeQQRTVLDDELQRLKNdvnsAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESE-- 1840
Cdd:COG5022 956 LNKLH-------EVESKLKETSEEYED----LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPve 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1841 ----AAKMRELAEEATKLRSVAEEaKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKR 1916
Cdd:COG5022 1025 vaelQSASKIISSESTELSILKPL-QKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340
....*....|....*....|....*..
gi 1207141751 1917 KAEEEGYQRKVLEDQAAQHKQAIEEKI 1943
Cdd:COG5022 1104 TNRNLVKPANVLQFIVAQMIKLNLLQE 1130
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
62-169 |
8.03e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 39.20 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 62 KWVNKHLvkhWKAEAQR-HITDLYEDLRDGHNLISLLEVLSGETLPR--------ERDVVRNSRlprekgrmrfHKLQNV 132
Cdd:cd21218 17 RWVNYHL---KKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKelvlevlsEEDLEKRAE----------KVLQAA 83
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141751 133 QiALDFLKHrqvklvnIRNDDIADGNPKLTLGLIWTI 169
Cdd:cd21218 84 E-KLGCKYF-------LTPEDIVSGNPRLNLAFVATL 112
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1662-1815 |
8.70e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1662 KKQQAEADK---AREQAEK-ELEtwRQK-----ANEALR---LRLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEE 1729
Cdd:PTZ00491 662 KSQEAAARHqaeLLEQEARgRLE--RQKmhdkaKAEEQRtklLELQAESAAVESSG--------------QSRAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1730 AALKQKEAAEMELGNQRkmaeeTAKQKLAAEQELIRLRadfehaeqQRTVLDDELQRLKNDVnsAVKQKKELEE-ELIKV 1808
Cdd:PTZ00491 726 EARLIEAEAEVEQAELR-----AKALRIEAEAELEKLR--------KRQELELEYEQAQNEL--EIAKAKELADiEATKF 790
|
....*..
gi 1207141751 1809 RKEMEIL 1815
Cdd:PTZ00491 791 ERIVEAL 797
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2558-2629 |
8.75e-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: 8.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2558 QFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMN--GKQKEMQDLEKKRIEQEKLLAEE 2629
Cdd:pfam20492 17 QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKErlEESAEMEAEEKEQLEAELAEAQE 90
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1542-1777 |
9.11e-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: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1542 AAQEEAEKLRKQVaEETQKKRKAEEELKRKseaekdAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1621
Cdd:COG4942 17 AQADAAAEAEAEL-EQLQQEIAELEKELAA------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1622 KKTAA--TQLESKQVALTARLEESLKNEQ---VMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQA 1696
Cdd:COG4942 90 KEIAElrAELEAQKEELAELLRALYRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1697 EEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ 1776
Cdd:COG4942 170 EAERAEL-----------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 1207141751 1777 R 1777
Cdd:COG4942 239 A 239
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1662-1759 |
9.54e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 39.76 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141751 1662 KKQQAEADKAREQAEKELETWRQKANEalrLRLQAEEEANKKtaaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEME 1741
Cdd:PRK05759 48 ERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQI----------------IEEAKAEAEAEAARIKAQAQAE 108
|
90
....*....|....*...
gi 1207141751 1742 LGNQRKMAEETAKQKLAA 1759
Cdd:PRK05759 109 IEQERKRAREELRKQVAD 126
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3392-3430 |
9.55e-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: 9.55e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141751 3392 YLQGSDCIAGVFFQKTKEKLSIYQAMKQKLLTSDTGMSL 3430
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
2302-2373 |
9.72e-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: 9.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141751 2302 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESD--LAKQRELAEKMLEEKKQAiqeAAKLKAEAEKLQK 2373
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQdrRAEELEELKHLLEERKEA---LEKLRAEAREEAE 71
|
|
| |
