|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
183-304 |
1.07e-71 |
|
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: 235.76 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 183 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNV 262
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNV 63
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237940 263 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 304
Cdd:cd21188 64 QTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
317-422 |
1.21e-69 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 229.91 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 317 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 396
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1920237940 397 PEDVDVPQPDEKSIITYVSSLYDAMP 422
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
180-315 |
1.22e-68 |
|
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: 227.60 E-value: 1.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 180 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRFHKL 259
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 260 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 315
Cdd:cd21235 64 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
178-313 |
5.23e-67 |
|
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: 223.32 E-value: 5.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 178 AADERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRFH 257
Cdd:cd21236 10 YKDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRFH 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 258 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 313
Cdd:cd21236 73 RLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
318-422 |
4.25e-64 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 213.79 E-value: 4.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 397
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1920237940 398 EDVDVPQPDEKSIITYVSSLYDAMP 422
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
180-314 |
1.38e-58 |
|
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: 198.72 E-value: 1.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 180 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKL 259
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 260 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 314
Cdd:cd21237 64 QNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
318-422 |
1.48e-56 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 192.51 E-value: 1.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 397
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1920237940 398 EDVDVPQPDEKSIITYVSSLYDAMP 422
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
316-422 |
5.08e-50 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 173.69 E-value: 5.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 316 DMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 395
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1920237940 396 DPEDVDVPQPDEKSIITYVSSLYDAMP 422
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
185-305 |
9.24e-46 |
|
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: 9.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 185 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQI 264
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTG------------KKLKPEKGRMRVHHLNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237940 265 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21186 66 ALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
318-418 |
6.89e-45 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 159.11 E-value: 6.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 397
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1920237940 398 EDVDVPQPDEKSIITYVSSLY 418
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 ... |
179-301 |
1.01e-44 |
|
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: 159.07 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 179 ADERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHK 258
Cdd:cd21246 10 ADEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKMRIHC 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 301
Cdd:cd21246 74 LENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-99 |
1.05e-44 |
|
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the cytoskeletal muscle protein plectin as well as the ribosomal S10 protein. This domain may be involved in RNA binding.
Pssm-ID: 427337 Cd Length: 92 Bit Score: 158.07 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 7 MPLDQLRTIYEVLFREGVMVAKKDRRPrSLHPHVpGVTNLQVTRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKDFNL-PKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 1920237940 87 HLPPEIVPASLQR 99
Cdd:pfam03501 79 HLPAEIVPATLKR 91
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
179-529 |
2.52e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 170.51 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 179 ADERDRVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLprerdvIRSSRLPRekgrMRFHK 258
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGCQ-GL 337
Cdd:COG5069 69 MENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 338 RCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYV 414
Cdd:COG5069 146 DTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 415 S------SLYD----AMPRVPDVQDGVKANElQLRwQEYRELVLLLLQWIRAHTAGFEERRFPSSFEEIEILWCQFLKFK 484
Cdd:COG5069 226 SwyiirfGLLEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLN 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237940 485 ETE--LPAKEAD-KNRSKGIYQSLEgAVQAGQLKVPPGYHPLDVEKEW 529
Cdd:COG5069 304 ALCsrAPLETTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
318-418 |
4.79e-43 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 153.71 E-value: 4.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 397
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237940 398 EDVDVPQPDEKSIITYVSSLY 418
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
181-305 |
6.51e-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: 150.99 E-value: 6.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 181 ERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHK 258
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHF 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21241 66 LSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
181-305 |
2.56e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 149.26 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 181 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHK 258
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHK 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21190 66 LSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
317-422 |
5.54e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 147.85 E-value: 5.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 317 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 396
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1920237940 397 PEDVDVPQPDEKSIITYVSSLYDAMP 422
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
179-301 |
4.08e-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: 145.90 E-value: 4.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 179 ADERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHK 258
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRLRVQK 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 259 LQNVQIALDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 301
Cdd:cd21193 74 IENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
305-420 |
8.94e-40 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 144.81 E-value: 8.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 305 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 384
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 385 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 420
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1461-2036 |
3.73e-38 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 158.18 E-value: 3.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1461 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEErERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1540
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-AELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1541 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQA 1620
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1621 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1700
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1701 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaEAERARAEAERELERWQLK 1780
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--------AGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1781 ANEALRLRLQAeevAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1860
Cdd:COG1196 536 YEAALEAALAA---ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1861 LRAETEQGEqqrqLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1940
Cdd:COG1196 613 ARYYVLGDT----LLGRTLVAARLEAALRR--AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1941 ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 2020
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570
....*....|....*.
gi 1920237940 2021 RLLEEQAAQHKADIEA 2036
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
314-418 |
2.14e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 138.27 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 314 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 393
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1920237940 394 LLDPEDVDVPQPDEKSIITYVSSLY 418
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1489-2194 |
2.31e-37 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 156.84 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1489 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiqEELQHL 1568
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA--EDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1569 RQSSEAEIQAKARQVEAAERSRlRIEEEIRVVRLQlEATERQRGGAEGELQALRaRAEEAeaqkRQAQEEAERLRRQVQD 1648
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDAR-KAEAARKAEEER-KAEEARKAEDAKKAEAVK-KAEEA----KKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1649 ETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF 1728
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1729 AEKTAQ-LERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAlrlRLQAEEVAQQKSLTQaeaek 1807
Cdd:PTZ00121 1327 AKKKADaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA---KKKAEEKKKADEAKK----- 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1808 qkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQLLE-----EELAR 1881
Cdd:PTZ00121 1399 -------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEeakkaEEAKK 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1882 LQREAAAATQKRRELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARLRAlAEEAK 1957
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1958 RQRQLAEEDAVRQRAEAERvlAEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 2037
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2038 LAQLRKASESELERQKGLVEDTLRQRrqveEEILALKGSFEKAAAGKAELELELGRIRGT-----AEDTLRSKEQA--EQ 2110
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakkAEEDKKKAEEAkkAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2111 EAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQLQLAQEAA 2186
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
....*...
gi 1920237940 2187 QKRLQAEE 2194
Cdd:PTZ00121 1765 EEEKKAEE 1772
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
170-301 |
2.97e-37 |
|
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: 138.62 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 170 RPGPEPAPA------------ADERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR 237
Cdd:cd21318 11 RPWDEPAATaklfecsrikalADEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 238 ErdvirssrlprEKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 301
Cdd:cd21318 86 P-----------TRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
314-418 |
4.63e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 137.06 E-value: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 314 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 393
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1920237940 394 LLDPEDVDVPQPDEKSIITYVSSLY 418
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1494-2095 |
4.89e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 154.32 E-value: 4.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1494 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAQGLQrrmqeevarreevaveAQEQKRSIQEELQHLRQSs 1572
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELK----------------EELKELEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1573 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQR 1652
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1653 KRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEAELQSEHASFAEKT 1732
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1733 AQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEA 1812
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1813 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR------LRAETEQGEQQRQLLEEELARLQREA 1886
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavlIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1887 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1966
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1967 AVRQRAEAERVLAEKLAA--ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKA 2044
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2045 SESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 2095
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
181-305 |
7.76e-37 |
|
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: 136.11 E-value: 7.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 181 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRMRFHKLQ 260
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1920237940 261 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21242 66 NIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
179-301 |
4.15e-36 |
|
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: 135.18 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 179 ADERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHK 258
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMRIHC 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 301
Cdd:cd21317 89 LENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
317-418 |
1.17e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 132.68 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 317 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 396
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1920237940 397 PEDVDVPQPDEKSIITYVSSLY 418
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1621-2221 |
1.20e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 150.09 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1621 LRARAEEAEAQKRQAQEEAERL---RRQVqdETQR---KRQAE-AELALRVQAEAEAaREKQRALQALEELRLQAEEAER 1693
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLeplERQAEkAERYRELKEELKE-LEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1694 RLRQAEAERARqvqvaLETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERE 1773
Cdd:COG1196 247 ELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1774 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1853
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---------AELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1854 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1933
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1934 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA----AISEATRLKTEAEIALKEKEAENERL 2009
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2010 RRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELEL 2089
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2090 ELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2169
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2170 RAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLER 2221
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
183-301 |
1.53e-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: 132.13 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 183 DRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNV 262
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANV 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237940 263 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 301
Cdd:cd21214 67 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1824-2392 |
9.13e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.01 E-value: 9.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1903
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1904 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLA 1983
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1984 AISEATRLKTEAEIALKEKEAENERLRRlaedEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 2063
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2064 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEA 2143
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2144 ARQRKAALEEVERLKAKVEEAR---RLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2215
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAAlaaALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2216 QSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2295
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2296 EQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2375
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 1920237940 2376 LRVQMEELGKLKARIEA 2392
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
302-418 |
1.07e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 130.94 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 302 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQA 381
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 382 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 418
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
321-422 |
1.27e-34 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 129.47 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 321 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 399
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237940 400 VDVPQPDEKSIITYVSSLYDAMP 422
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
185-303 |
1.55e-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: 129.44 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 185 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprEKGRMRFHKLQNVQI 264
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNK 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237940 265 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 303
Cdd:cd21215 69 ALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
180-305 |
2.70e-33 |
|
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: 126.19 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 180 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKL 259
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTG------------QKLVKEKGSTRVHAL 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1920237940 260 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21231 65 NNVNKALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
318-418 |
5.85e-32 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 122.13 E-value: 5.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 397
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237940 398 EDVDVPQPDEKSIITYVSSLY 418
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-114 |
1.78e-31 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 121.28 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 5 MLMPLDQLRTIYEVLFREGVMVAKKDRrPRSLHPHVpGVTNLQVTRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQ 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKDP-KGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90 100 110
....*....|....*....|....*....|
gi 1920237940 85 YLHLPPEIVPASLQRVRRPVAMVMPARRTP 114
Cdd:PTZ00034 80 YLHLPPDVFPATHKKKSVNFERKTEEEGSR 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
317-415 |
3.89e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 119.84 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 317 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 396
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1920237940 397 PEDVDVPQPDEKSIITYVS 415
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1482-2086 |
4.01e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 136.04 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQRAE------------ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1549
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEavkkaeeakkdaEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1550 V--AVEAQ--EQKRSIQEELQHLRQSSEAEiQAKARQVEA---AERSRLRIEEEirvvRLQLEATERQRGGAEGELQALR 1622
Cdd:PTZ00121 1289 KkkADEAKkaEEKKKADEAKKKAEEAKKAD-EAKKKAEEAkkkADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAE 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1623 ARAEEAEAQKRQAQEEAERLRRQVQ-----DETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRlQAEEAERRLRQ 1697
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1698 A--------EAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLR--EEATRRAQQQAEAERAR 1767
Cdd:PTZ00121 1443 AkkadeakkKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1768 AEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKQKEEAEREARRRgKAEEqavrQRELAEQELEKQRQLAEGT 1847
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKK----AEEKKKADELKKAEELKKAEEKKKAEEAK-KAEE----DKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1848 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1927
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1928 SKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEedaVRQRAEAERVLAEKLAAISEATRLKteAEIALKEKEAENE 2007
Cdd:PTZ00121 1674 KKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEE---LKKKEAEEKKKAEELKKAEEENKIK--AEEAKKEAEEDKK 1744
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2008 RLRRLAEDEAFQRRLleeqaAQHKADIEARLAQLRKASESELErqKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAE 2086
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKI-----AHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1482-2114 |
5.70e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 135.65 E-value: 5.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQRAEERERLAEVEAALE--KQRQLAEAHAQAKAQAEREAQGLQR----------RMQEEVARREE 1549
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedakkaeavKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1550 VAVEAQEQKRSIQ-EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRAR-AEE 1627
Cdd:PTZ00121 1241 EAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKkADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1628 AEAQKRQAQEEAERLRRQVQdETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAERRlrqaeAERARQV 1706
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKK-----AEEKKKA 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1707 QVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARaeaerelerwqlKANEALR 1786
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------------EAKKAEE 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1787 LRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQElIRLRAETE 1866
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAK 1540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1867 QGEQQR---QLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaEAGRFRELA 1943
Cdd:PTZ00121 1541 KAEEKKkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAK 1619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1944 EEAARLRALAEEAKRQRQLAEEDA--------VRQRAEAERVLAEKLAAISEATrlKTEAEIALKEKEAENERLRRLAED 2015
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKE 1697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2016 EAFQRRLleEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVeEEILALKGSFEKAAAGKAELELELGRIR 2095
Cdd:PTZ00121 1698 AEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
650
....*....|....*....
gi 1920237940 2096 GTAEDTLRSKEQAEQEAAR 2114
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRR 1793
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
317-415 |
1.20e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.40 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 317 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 396
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1920237940 397 PEDVDVPQPDEKSIITYVS 415
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
305-420 |
1.65e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.40 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 305 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 384
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 385 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 420
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
185-305 |
1.69e-30 |
|
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: 118.16 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 185 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdVIRssrlpreKGRMRFHKLQNVQI 264
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIK-------KPLNQHQKLENVTL 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237940 265 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21227 69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
321-422 |
1.86e-30 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 117.75 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 321 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 399
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237940 400 VDVPQPDEKSIITYVSSLYDAMP 422
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1037-1114 |
2.66e-30 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 116.16 E-value: 2.66e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 1037 LAWQSLGRDMQLIRSWSLATFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 1114
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1891-2602 |
3.59e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 132.37 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1891 QKRRELEAELAKVRAEMEvllaskaRAEEEsrsTSEKSKQ--RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedav 1968
Cdd:COG1196 172 ERKEEAERKLEATEENLE-------RLEDI---LGELERQlePLERQA----EKAERYRELKEELKELEAELLLLK---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1969 RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadiEARLAQLRKASESE 2048
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL------LAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2049 LERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRRE 2128
Cdd:COG1196 308 EERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2129 AEERVQKSLAAEEEAARQRKAALEEVERLKAkvEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQEL 2208
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2209 QQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2288
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2289 AARRAQAEQAALRQKQAAdaemekhkqfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRgq 2368
Cdd:COG1196 542 AALAAALQNIVVEDDEVA----------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2369 vEEELFSLRVQMEELGklkarieaenRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2448
Cdd:COG1196 610 -EADARYYVLGDTLLG----------RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2449 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERL 2528
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2529 RLRVAEMSRAQARAEEDARRFRK-------QAEDIGERLyrTELATQekvmlVQTLETQRqqsdrdaERLREAIAELEHE 2601
Cdd:COG1196 759 PPDLEELERELERLEREIEALGPvnllaieEYEELEERY--DFLSEQ-----REDLEEAR-------ETLEEAIEEIDRE 824
|
.
gi 1920237940 2602 K 2602
Cdd:COG1196 825 T 825
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
184-306 |
7.11e-30 |
|
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: 116.78 E-value: 7.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 184 RVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprEKGRMRFHKLQNVQ 263
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFN----------KRPTFRSQKLENVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1920237940 264 IALDYLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 306
Cdd:cd21311 79 VALKFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
179-301 |
2.83e-29 |
|
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: 116.30 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 179 ADERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHK 258
Cdd:cd21316 47 ADEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMRIHC 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 301
Cdd:cd21316 111 LENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
321-423 |
3.03e-29 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 114.64 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 321 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 398
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1920237940 399 DVDVPQPDEKSIITYVSSLYDAMPR 423
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
185-305 |
3.45e-29 |
|
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: 114.34 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 185 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQI 264
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237940 265 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21232 66 VLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
323-418 |
3.56e-29 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 113.98 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 323 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 401
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1920237940 402 VPQPDEKSIITYVSSLY 418
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
181-307 |
5.05e-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: 5.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 181 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvIRSSRlprekgrMRFHKLQ 260
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQE---YKPSS-------HRIFRLN 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237940 261 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 307
Cdd:cd21191 68 NIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1651-2366 |
1.31e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.98 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1651 QRKRQAEAELAlrvQAEAEAAR--------EKQralqaLEELRLQAEEAERRLRQAEAERARQVQVALetaqrsaeAELQ 1722
Cdd:COG1196 172 ERKEEAERKLE---ATEENLERledilgelERQ-----LEPLERQAEKAERYRELKEELKELEAELLL--------LKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1723 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkanEALRLRLQAEEvaqqksltq 1802
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAEL--------------------------EELRLELEELE--------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1803 aeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1882
Cdd:COG1196 281 ------------------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1883 QREAAAATQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1962
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1963 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLR 2042
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2043 KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEE 2122
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2123 ERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2202
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2203 QKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLR 2282
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2283 KEAEQEAARRAQAEQAALRQKQAADAEMEKHKqfAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLK-- 2356
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELER--LEREIEALGPVnllaIEEYEELEERYDFLSEQREDLEEARETLEea 817
|
730
....*....|.
gi 1920237940 2357 -AEVTEAARQR 2366
Cdd:COG1196 818 iEEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1337-1955 |
1.36e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.98 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1337 QTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVpLANSQAVREQLRQEKALLED-IERHGEKveecqrfa 1415
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELeLEEAQAE-------- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1416 kqyinaikdyELQLVTYKAQLEPVASPAKkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAE 1495
Cdd:COG1196 290 ----------EYELLAELARLEQDIARLE--------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1496 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqglqrrmqeEVARREEVAVEAQEQKRSIQEELQHLRQSSEAE 1575
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL---------EALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1576 IQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRqvQDETQRKRQ 1655
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA--RLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1656 AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE----K 1731
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflplD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1732 TAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEE 1811
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1812 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1891
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 1892 KRRELEAELAKVRAEMEvllaskaraEEESRSTSEKSKQRLEAEAGRF--------RELAEEAARLRALAEE 1955
Cdd:COG1196 741 LLEEEELLEEEALEELP---------EPPDLEELERELERLEREIEALgpvnllaiEEYEELEERYDFLSEQ 803
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
303-420 |
3.12e-28 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 112.10 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 303 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAF 382
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237940 383 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 420
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
184-303 |
1.37e-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: 109.88 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQ 263
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1920237940 264 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 303
Cdd:cd21183 69 TALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1865-2755 |
1.93e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 124.10 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1865 TEQGEQQRQLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1942
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1943 AEEAARlralAEEAKRQrqlAEEdaVRQRAEAERvlAEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDeafQR 2020
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAED---AK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2021 RLLEEQAAqhkadIEARLA-QLRKASESELERQKGLVEDTlrqrRQVEEeilalkgsfekaaAGKAELELELGRIRGTAE 2099
Cdd:PTZ00121 1177 KAEAARKA-----EEVRKAeELRKAEDARKAEAARKAEEE----RKAEE-------------ARKAEDAKKAEAVKKAEE 1234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2100 DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEeaarQRKAalEEVErlkaKVEEARRLRERAEQESARQL 2179
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE----ARKA--DELK----KAEEKKKADEAKKAEEKKKA 1304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2180 QLAQEAAQKRLQAEE-KAHAFAVQQKEQELQQTLqqeqsvlerlrseaeaarraaeeaeaareraereaaQSRRQVEEAE 2258
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKA------------------------------------EEAKKAAEAA 1348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2259 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQaLRQKAQVEQELTALRLQL 2338
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKA 1427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2339 EETDHQksildEELQRLKAEVTEAARQRGQVEEelfslRVQMEELGKlkaRIEAENRALVLRDKDSAQRLLQE---EAEK 2415
Cdd:PTZ00121 1428 EEKKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEE 1494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2416 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQE 2491
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2492 DKeQMAQQLAQETQgfqktlETERQRQLEMSAEAERLRLRVAEmsraQARAEEDARrfrKQAEDIGErlyrtelaTQEKV 2571
Cdd:PTZ00121 1575 DK-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAK---IKAEELKK--------AEEEK 1632
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2572 MLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsflsekdslLQRErc 2651
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------------LKKE-- 1697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2652 iEQEKAKLEQL---FQDEVAKAQALREEQQRQQQqmqqekqqlaaSMEEARRRQHE----AEEgVRRQQEELQRLAQQQQ 2724
Cdd:PTZ00121 1698 -AEEAKKAEELkkkEAEEKKKAEELKKAEEENKI-----------KAEEAKKEAEEdkkkAEE-AKKDEEEKKKIAHLKK 1764
|
890 900 910
....*....|....*....|....*....|....*
gi 1920237940 2725 QQEKLLAEENQR----LRERLQHLEEERRAALARS 2755
Cdd:PTZ00121 1765 EEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDKK 1799
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
321-420 |
9.50e-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: 107.37 E-value: 9.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 321 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 399
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1920237940 400 VDVPQPDEKSIITYVSSLYDA 420
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
305-420 |
1.70e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 107.09 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 305 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 384
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 385 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 420
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2031-2757 |
3.33e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.86 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2031 KADIEARLAQLRKASESELERQKGLVEDTlRQRRQVEEEilalKGSFE---KAAAGKAELELELGRIRGTAEDTLRSKE- 2106
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDN-RADEATEEA----FGKAEeakKTETGKAEEARKAEEAKKKAEDARKAEEa 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2107 -QAE-----QEAARQRQLAAEEERRRREAEERVQKSLAAEE----EAARQ----RKAA----LEEVERLKA--KVEEARR 2166
Cdd:PTZ00121 1134 rKAEdarkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDakkaEAARKaeevRKAEelrkAEDARKAEAarKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2167 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAERE 2246
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2247 AAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA--EMEKHKQFAEQALRQK 2324
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2325 AQVEQELTALRLQLEETDHQksildEELQRLKAEVTEAARQRGQVEEElfslrvqmeelgKLKARiEAENRALVLRDKDS 2404
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAA------------KKKAD-EAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2405 AQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQlAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2482
Cdd:PTZ00121 1436 AKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKK-ADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2483 QEqARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQA--RAEEDARRFRKQAEDigerL 2560
Cdd:PTZ00121 1513 DE-AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKAEEakKAEEDKNMALRKAEE----A 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2561 YRTELATQEKVM-LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFL 2639
Cdd:PTZ00121 1587 KKAEEARIEEVMkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2640 SEKDsllqrerciEQEKAKLEQLFQDEVAKAQAlreeqqrqqqqmqqeKQQLAASMEEARRrqheAEEgVRRQQEELQRL 2719
Cdd:PTZ00121 1667 AKKA---------EEDKKKAEEAKKAEEDEKKA---------------AEALKKEAEEAKK----AEE-LKKKEAEEKKK 1717
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1920237940 2720 AQQQQQQEkllaEENQRLRERLQHLEEE--RRAALARSEE 2757
Cdd:PTZ00121 1718 AEELKKAE----EENKIKAEEAKKEAEEdkKKAEEAKKDE 1753
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1557-2359 |
5.42e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.09 E-value: 5.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1557 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEaEAQKRQAQ 1636
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE-ARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1637 EEAERLR-----RQVQD--ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE----AERARQ 1705
Cdd:PTZ00121 1122 KKAEDARkaeeaRKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEelrkAEDARK 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1706 VQVAletaqRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1785
Cdd:PTZ00121 1202 AEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1786 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLAEGTAQQrlaAEQEliRLRAET 1865
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKK---AEEA--KKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1866 EQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEmEVLLA--SKARAEEESRSTSEKSKQrlEAEAGRFRELA 1943
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKAdeAKKKAEEDKKKADELKKA--AAAKKKADEAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1944 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 2023
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2024 EEQAAQHKADiEARLAQLRKASEsELERQKglvedtlrQRRQVEEeilaLKGSFEKAAAGKAELELELGRirgtAEDTlR 2103
Cdd:PTZ00121 1504 KAAEAKKKAD-EAKKAEEAKKAD-EAKKAE--------EAKKADE----AKKAEEKKKADELKKAEELKK----AEEK-K 1564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2104 SKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRlrerAEQESARQLQLaq 2183
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK----AEEEKKKVEQL-- 1638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2184 eaaqKRLQAEEKAHAFAVQQKEQELQQTLqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQs 2263
Cdd:PTZ00121 1639 ----KKKEAEEKKKAEELKKAEEENKIKA-------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2264 aeeQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADaemEKHKQFAEQALRQKAQVEQELTALRLQLEETDH 2343
Cdd:PTZ00121 1707 ---LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
810
....*....|....*.
gi 1920237940 2344 QKSILDEELQRLKAEV 2359
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEV 1796
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
305-420 |
7.43e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 105.58 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 305 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 384
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 385 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 420
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1494-2705 |
2.70e-25 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 116.46 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1494 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAEREAQGLQRRMQ--EEVARREEvAVEAQEQKRSIQEELQHLRQ 1570
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAELHTEAVQRRQQldQELAERRQ-TVESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1571 SSEA-----EIQAKARQVEAAERSRlrieeeirVVRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERLRRQ 1645
Cdd:NF041483 162 ESQArrlldESRAEAEQALAAARAE--------AERLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1646 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQaeEAERRLRQAEAERARQVQVALETA-QRSAEAELQSE 1724
Cdd:NF041483 227 ASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAaKQLASAESANE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1725 hasfaektaQLERTLKEEhvaVVQLREEATRRAQQQAEAERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQA 1803
Cdd:NF041483 305 ---------QRTRTAKEE---IARLVGEATKEAEALKAEAEQALADARAEAEKLVaEAAEKARTVAAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1804 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEELARL 1882
Cdd:NF041483 373 AEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEARRL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1883 QREAAaatQKRRELEAELAKVRAEmevllaskARAEeesrstsekSKQRLEAEAGRFRELAEEAarlRALAEEAKRQrql 1962
Cdd:NF041483 446 RGEAE---QLRAEAVAEGERIRGE--------ARRE---------AVQQIEEAARTAEELLTKA---KADADELRST--- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1963 aeedavrQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA-QHKADIEARLAQL 2041
Cdd:NF041483 500 -------ATAESERVRTE---AIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAArELREETERAIAAR 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2042 RKASESELERQKGLVEdtlrQRRQVEEEilALKGSFEKAAAGKAELELELGRIRGTAEDTLRS-KEQAEQEAARQRqlaa 2120
Cdd:NF041483 570 QAEAAEELTRLHTEAE----ERLTAAEE--ALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLR---- 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2121 eeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLR-------ERAEQESARQLQLAQ-EAAQKRLQ 2191
Cdd:NF041483 640 -----TEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQEsADRVRaeaaaaaERVGTEAAEALAAAQeEAARRRRE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2192 AEE---KAHAFAVQQKEQELQQTLQQEQSVLERLrseaeaarraaeeaeaareraEREAAQSRRQVEEAERlkqsaeeqa 2268
Cdd:NF041483 715 AEEtlgSARAEADQERERAREQSEELLASARKRV---------------------EEAQAEAQRLVEEADR--------- 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2269 qaqaqaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-DHQKSI 2347
Cdd:NF041483 765 --------------------------------RATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAaERTRTE 812
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2348 LDEELQRLKAEvteAARQRGQVEEELFSLRVQ-MEELGKLKARIEAEnralVLRDKDSAQRLLQEEAEKMKQVAEEAA-R 2425
Cdd:NF041483 813 AQEEADRVRSD---AYAERERASEDANRLRREaQEETEAAKALAERT----VSEAIAEAERLRSDASEYAQRVRTEASdT 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2426 LSVAAQEAARLRQLAEEDLAQQRALA---EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAq 2502
Cdd:NF041483 886 LASAEQDAARTRADAREDANRIRSDAaaqADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIA- 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2503 etqgfqktleterqrqlEMSAEAERLRLRVAE-MSRAQARAE---EDARRFRKQAEDIGERLyRTELATQEKVMLVQTLE 2578
Cdd:NF041483 965 -----------------EATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEAERL-RTEAREEADRTLDEARK 1026
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2579 TQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLL----QETQALQQSFLSEKDSLLQRERcieq 2654
Cdd:NF041483 1027 DANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVgaarKEAERIVAEATVEGNSLVEKAR---- 1102
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2655 ekAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLaasMEEARRRQHEA 2705
Cdd:NF041483 1103 --TDADELLVGARRDATAIRERAEELRDRITGEIEEL---HERARRESAEQ 1148
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1837-2660 |
2.93e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 116.78 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1837 LEKQRQLAEGTAQQRLAAEQELIRLRAE-TEQGEQQRQLLEEELARLQREAA----AATQKRRELEA-ELAKVRAEmEVL 1910
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDgNHEGKAEAKAHVGQDEGLKPSYKdfdfDAKEDNRADEAtEEAFGKAE-EAK 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1911 LASKARAEEESRStsEKSKQRLEaEAGRFREL--AEEAARlralAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAIS-- 1986
Cdd:PTZ00121 1105 KTETGKAEEARKA--EEAKKKAE-DARKAEEArkAEDARK----AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAkk 1177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1987 -EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEA--RLAQLRKASESELERQKGLVEDTLRQR 2063
Cdd:PTZ00121 1178 aEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKDAEEAKKAEEERNNEEIRKF 1257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2064 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRqlaAEEERRRreaeervqkslaaeEEA 2143
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK---AEEAKKA--------------DEA 1320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2144 ARQRKAALEEVERLKAKVEEARRLRERAEQEsarqlqlAQEAAQKRLQAEEKAHAfavqqkeqelqqtlqqeqsvLERLR 2223
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-------AEAAADEAEAAEEKAEA--------------------AEKKK 1373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2224 SEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKlRKEAEQEAARRAQAEQAALRQK 2303
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKK 1452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2304 QAADAEMEKHKQFAEQA-----LRQKAQVEQELTALRLQLEETDHQKsildEELQRlKAEVTEAARQRGQVEEelfslRV 2378
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAkkadeAKKKAEEAKKADEAKKKAEEAKKKA----DEAKK-AAEAKKKADEAKKAEE-----AK 1522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2379 QMEELGKLKARIEAEnRALVLRDKDSAQRLlqEEAEKMKQvAEEAARLSVAAQEAARlRQLAEEDLAQQRALAEKMLKEK 2458
Cdd:PTZ00121 1523 KADEAKKAEEAKKAD-EAKKAEEKKKADEL--KKAEELKK-AEEKKKAEEAKKAEED-KNMALRKAEEAKKAEEARIEEV 1597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2459 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQqlaqetqgFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2538
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ--------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2539 QARAEEDARRFRKQAED---IGERLYRTElatqEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLK 2615
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDekkAAEALKKEA----EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2616 SEEMQTVRQE-----QLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLE 2660
Cdd:PTZ00121 1746 AEEAKKDEEEkkkiaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
305-420 |
2.07e-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: 101.30 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 305 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 384
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 385 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 420
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
184-303 |
2.34e-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: 100.64 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQ 263
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1920237940 264 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 303
Cdd:cd21228 69 VALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1531-2467 |
2.40e-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: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1531 REAQGLQRRMQEEVARREEVAVEAQEQKRSIQ------EELQHLR-QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1603
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKaELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1604 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1683
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1684 LRLQAEEAERRLrqaeaerarqvqvaletaqrsaeAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaea 1763
Cdd:TIGR02168 335 LAEELAELEEKL-----------------------EELKEELESLEAELEELEAELEELESRLEELEEQLE--------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1764 eraraeaerelerwQLKANEALRLRLQAEEVAQQKSLTQAEaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQl 1843
Cdd:TIGR02168 383 --------------TLRSKVAQLELQIASLNNEIERLEARL-------------------ERLEDRRERLQQEIEELLK- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1844 aEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS 1923
Cdd:TIGR02168 429 -KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1924 TSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaeEDAVRQRAEAERVLAEKLAAiSEATRLKTEAEIALKE 2001
Cdd:TIGR02168 508 VKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL---QAVVVENLNAAKKAIAFLKQ-NELGRVTFLPLDSIKG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2002 KEAENERLRRLAEDEAFQRRL--LEEQAAQHKADIEARLAQLRKASEselerqkglVEDTLRQRRQVEEEIL-------- 2071
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRivtldgdl 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2072 -----ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerRRREAEERVQKSLAAEEEAARQ 2146
Cdd:TIGR02168 655 vrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK-------ELEELEEELEQLRKELEELSRQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2147 RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLERLRSEA 2226
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2227 EAARRAAEEAEAARERAEREAAQSRRQVEEAERLkqsaeeqaqaqaqaqaaaekLRKEAEQEAARRAQAEQAALRQKQAA 2306
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERR--------------------LEDLEEQIEELSEDIESLAAEIEELE 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2307 DAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL-GK 2385
Cdd:TIGR02168 866 ELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqER 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2386 L--KARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAarLRQLAE--EDLAQQRALAEKMLKEKMQA 2461
Cdd:TIGR02168 945 LseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEE--YEELKEryDFLTAQKEDLTEAKETLEEA 1022
|
....*.
gi 1920237940 2462 VQEATR 2467
Cdd:TIGR02168 1023 IEEIDR 1028
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
317-423 |
6.40e-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: 6.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 317 MTAKEKLLLWSQRMVEGC-QGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 393
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1920237940 394 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 423
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
323-418 |
6.63e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 99.15 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 323 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 401
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1920237940 402 VPQPDEKSIITYVSSLY 418
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1457-2193 |
1.46e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 110.92 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1457 QEYVDLRTRYSELS-TLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAL--------EKQRQLAEA------ 1521
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrlevsELEEEIEELqkelya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1522 HAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE------ELQHLRQSSEAEIQAKARQVEAAERSRLRIEE 1595
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeelaELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1596 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQ 1675
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1676 RALQALEELRLQAEEAERRLRQAEAERarqvqvaletaqRSAEAELQsEHASFAEKTAQLERTLKEEHVAVVQLREEAtr 1755
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQAL------------DAAERELA-QLQARLDSLERLQENLEGFSEGVKALLKNQ-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1756 raQQQAEAERARAEAERELERWQLKANEALRLRLQA---EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1832
Cdd:TIGR02168 516 --SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1833 AEQELEKQRQLAE---GTAQQRLAAEQELIRLR-AETEQG--EQQRQLLEEELA------------RLQREAAAATQKRR 1894
Cdd:TIGR02168 594 LKNIEGFLGVAKDlvkFDPKLRKALSYLLGGVLvVDDLDNalELAKKLRPGYRIvtldgdlvrpggVITGGSAKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1895 ELEAELAKVRAEMEvLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA 1974
Cdd:TIGR02168 674 ERRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1975 ERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED-----EAFQRRLLEEQAAQHKADIEARLAQLRKAS-ESE 2048
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLLNEEAANLRERLESlERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2049 LERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRRE 2128
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 2129 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERA--EQESARQLQLAQEAAQKRLQAE 2193
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYslTLEEAEALENKIEDDEEEARRR 973
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
180-305 |
1.81e-23 |
|
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: 98.68 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 180 DERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKL 259
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRVHFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237940 260 QNVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21247 81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
184-306 |
1.85e-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: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlPREKgrMRFHKLQNVQ 263
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 264 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 306
Cdd:cd21310 81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1849-2641 |
1.97e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 110.53 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1849 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKS 1928
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKA-ERYKELKAELRELELA---LLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1929 KQRLEAEagrFRELAEEAARLRALAEEAKRQRQLAEEDAvrqrAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENER 2008
Cdd:TIGR02168 248 LKEAEEE---LEELTAELQELEEKLEELRLEVSELEEEI----EELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2009 LRRLAEDEAFQRRLLEEQAAQHKADIEaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFekaaagkAELE 2088
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-------AQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2089 LELGRIRGTAEDTLRSKEQAEQEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL 2167
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2168 RERAEQESARQLQLAQE--AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2245
Cdd:TIGR02168 473 AEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2246 EAAQSRRQVEEAerLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAaDAEMEKHKQFAeqaLRQKA 2325
Cdd:TIGR02168 553 ENLNAAKKAIAF--LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF-DPKLRKALSYL---LGGVL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2326 QVEQELTALRLQlEETDHQKSI--LDEELQRLKAEVTEAARQRGQVeeeLFSLRVQMEELGKLKARIEAENRAL--VLRD 2401
Cdd:TIGR02168 627 VVDDLDNALELA-KKLRPGYRIvtLDGDLVRPGGVITGGSAKTNSS---ILERRREIEELEEKIEELEEKIAELekALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2402 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM-----------QAVQEATRLKA 2470
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEaeieeleerleEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2471 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRAQARAEEDARRFR 2550
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2551 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTvRQEQLLQE 2630
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVR 937
|
810
....*....|.
gi 1920237940 2631 TQALQQSFLSE 2641
Cdd:TIGR02168 938 IDNLQERLSEE 948
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1485-2196 |
2.55e-23 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 110.30 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1485 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQE 1563
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIAR---LVGEATKEAEALKA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1564 ELQHLRQSSEAEiqAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLR 1643
Cdd:NF041483 331 EAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATTRAAAEEAERIR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1644 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRLQaEEAeRRLRqAEAERARqvqvaletaqrsaeaelqs 1723
Cdd:NF041483 400 REAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLR------------------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1724 ehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELErwqlkANEALRLRLQAEEVAqqKSLTQA 1803
Cdd:NF041483 454 -----AEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTA-----TAESERVRTEAIERA--TTLRRQ 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1804 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAETEQ----GEQQRQLLEEE 1878
Cdd:NF041483 522 AEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEErltaAEEALADARAE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1879 LARLQREAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALA 1953
Cdd:NF041483 602 AERIRREAAEETERLRTEAAErirtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEA------AAEAERLKSEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1954 EE-AKRQRQLAEEDAVRQRAEAERVLAeklAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrllEEQAAQHKA 2032
Cdd:NF041483 676 QEsADRVRAEAAAAAERVGTEAAEALA---AAQEEAARRRREAEETLGSARAEADQERERAREQS------EELLASARK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2033 DIEARLAQLRKASESELERQKGLV---EDTLRQRR--------QVEEEILALKGSFEKAAA-GKAELELELGRIRGtaeD 2100
Cdd:NF041483 747 RVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAGLRSAAEHAAErTRTEAQEEADRVRS---D 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2101 TLRSKEQAEQEAARQRQlaaeeerrrreaeERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERAeqeSARQL 2179
Cdd:NF041483 824 AYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEA---SDTLA 887
|
730
....*....|....*..
gi 1920237940 2180 QLAQEAAQKRLQAEEKA 2196
Cdd:NF041483 888 SAEQDAARTRADAREDA 904
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1828-2598 |
3.64e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.38 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1828 RQRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETeqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEM 1907
Cdd:TIGR02168 207 RQAEKAERYKELKAELRE--------LELALLVLRLEE---------LREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1908 EVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1987
Cdd:TIGR02168 270 EELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1988 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQH---KADIEARLAQLRKASeSELERQKGLVEDTLRQRR 2064
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIASLN-NEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2065 QVEEEILALKGSFEKAAagKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRrreaeervQKSLAAEEEAA 2144
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2145 RQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQK 2204
Cdd:TIGR02168 488 QARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2205 EQELQQTLQQEQSVLER-LRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE-------AERLKQSAEEQAQAQAQAQA 2276
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRI 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2277 AAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK 2356
Cdd:TIGR02168 648 VTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2357 AEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ----- 2431
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrea 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2432 ------------EAARLRQLAEEDLAQQRALAEKML----KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2495
Cdd:TIGR02168 805 ldelraeltllnEEAANLRERLESLERRIAATERRLedleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2496 MAQQLAQ---ETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDigerLYRTELATQEKvm 2572
Cdd:TIGR02168 885 LEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE----EYSLTLEEAEA-- 958
|
810 820
....*....|....*....|....*.
gi 1920237940 2573 LVQTLETQRQQSDRDAERLREAIAEL 2598
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1481-2197 |
4.12e-23 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 109.53 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1481 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAEREAQGLQRRMQEEVAR-REEV 1550
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1551 AVEAQEQKRSIQEELQHLRqsSEAEiQAKARQVEAAERSRLRIEEEIRVVRLQLE-ATERQRGGAEGELQALRARAEE-- 1627
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1628 --AEAQKRQAQEEAERLRRQVQDETQRKRQAEAE--LALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEAER 1702
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLRTEAAEriRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRsEAAAEA 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1703 ARQVQVALETAQRsaeaeLQSEHASFAEKTAQlertlkeehvavvqlreeatrraqqqaeaeraraeaerelerwqlKAN 1782
Cdd:NF041483 669 ERLKSEAQESADR-----VRAEAAAAAERVGT---------------------------------------------EAA 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1783 EALrlrlqaeevaqqksltqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI--- 1859
Cdd:NF041483 699 EAL----------------------------------AAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasa 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1860 RLRAETEQGEQQRqLLEEELARLQREAAAATQKRRELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAE 1935
Cdd:NF041483 745 RKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSD 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1936 AGRFRELA-EEAARLRALA-EEAKRQRQLAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLA 2013
Cdd:NF041483 824 AYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADA 900
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2014 EDEAFQRRllEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAElelelgR 2093
Cdd:NF041483 901 REDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------R 972
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2094 IRGTAEDTLRSkeqAEQEAARQRQLAAEEERRrreaeervqkslaAEEEAARQRKAALEEVERL--KAKVEEARRLRERA 2171
Cdd:NF041483 973 LRAEAAETVGS---AQQHAERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAA 1036
|
730 740
....*....|....*....|....*.
gi 1920237940 2172 EQESARQLQLAQEAAQKRLQAEEKAH 2197
Cdd:NF041483 1037 EQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2020-2661 |
6.09e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2020 RRLLEEQA--AQHKADIEARLAQLRKASE---------SELERQKglveDTLRQRRQVEEEILALKGSFEKAaagkaELE 2088
Cdd:COG1196 158 RAIIEEAAgiSKYKERKEEAERKLEATEEnlerledilGELERQL----EPLERQAEKAERYRELKEELKEL-----EAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2089 LELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2168
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2169 ERAEQESARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAA 2248
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELE-----------------------EELEELEEELEEAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2249 QSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKeaeqeaarraqAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2328
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAA-----------QLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2329 QELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRvqmEELGKLKARIEAENRALVLRDKDSAQRL 2408
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL---EELAEAAARLLLLLEAEADYEGFLEGVK 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2409 LQEEAEKMKQVA---------EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAV--QEATRLKAEAELLQQ 2477
Cdd:COG1196 512 AALLLAGLRGLAgavavligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtfLPLDKIRARAALAAA 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2478 QKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIG 2557
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2558 ERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQS 2637
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
650 660
....*....|....*....|....
gi 1920237940 2638 FLSEKDSLLQRERcIEQEKAKLEQ 2661
Cdd:COG1196 752 ALEELPEPPDLEE-LERELERLER 774
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
188-302 |
9.72e-23 |
|
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: 95.46 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 188 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVirssrlprEKGRMRFHKLQNVQIALD 267
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALS 67
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237940 268 YLRHRQVKLVNIRNDDIADGnPKLTLGLIWTIILH 302
Cdd:smart00033 68 FAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
319-418 |
1.09e-22 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 95.71 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 319 AKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 398
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1920237940 399 D-VDVPQPDEKSIITYVSSLY 418
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
321-421 |
1.35e-22 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 95.22 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 321 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 400
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1920237940 401 DVPQPDEKSIITYVSSLYDAM 421
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1932-2747 |
1.56e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.45 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1932 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAVR------------QRAEAERVLAEKLAAISEATRlKTEAE 1996
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1997 IALKEKEAENERLRRLAEDEAFQRRLLEEQAAQhKADIEARLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEILAL 2073
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2074 KGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2153
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2154 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ-QKEQELQQTLQQEQSVLERLRSEAEAAR 2230
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2231 RAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQaeqaaLRQKQAADAEM 2310
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-----LSELISVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2311 EKHKQFAEQALRQKAQVEQELTALRLQleetDHQKsilDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARI 2390
Cdd:TIGR02168 536 EAAIEAALGGRLQAVVVENLNAAKKAI----AFLK---QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2391 EAENRA-----------LVLRDKDSAQRLLQEEAEKMKQVAEEAARLS---VAAQEAARLRQLAeedLAQQRALAEkmLK 2456
Cdd:TIGR02168 609 KFDPKLrkalsyllggvLVVDDLDNALELAKKLRPGYRIVTLDGDLVRpggVITGGSAKTNSSI---LERRREIEE--LE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2457 EKMQAVQEAtrlkaEAELLQQQKELAQEQarrlqedkeqmaQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMS 2536
Cdd:TIGR02168 684 EKIEELEEK-----IAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2537 RAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS 2616
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2617 EEMQTvRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASME 2696
Cdd:TIGR02168 827 ESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELR 904
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2697 EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2747
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
185-305 |
1.71e-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: 95.05 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 185 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQI 264
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237940 265 ALDYLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:pfam00307 68 ALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
318-416 |
2.15e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 94.61 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 396
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1920237940 397 PEDVDVPQPDEKSIITYVSS 416
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1159-1723 |
2.71e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.56 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1159 ARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1238
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1239 RSTQEAEEVLRAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVE 1318
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1319 RWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL 1398
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1399 EDIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLtsqyir 1478
Cdd:COG1196 477 AALAE-----------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1479 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA----HAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1554
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1555 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1634
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1635 AQEEAERLRRQvqdETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVA-LETA 1713
Cdd:COG1196 692 ELELEEALLAE---EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEeLERE 768
|
570
....*....|
gi 1920237940 1714 QRSAEAELQS 1723
Cdd:COG1196 769 LERLEREIEA 778
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
318-418 |
3.08e-22 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 94.41 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 397
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1920237940 398 EDVDVPQ-PDEKSIITYVSSLY 418
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2135-2750 |
3.58e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2135 KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQ 2214
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2215 EQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQ 2294
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2295 AEQAALRQKQAADAEMEKHKQFAEQALRQkaqvEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2374
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2375 SLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2454
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2455 LKEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRV 2532
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2533 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2612
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2613 QLKSEEMQTVRQEQLLQETQALQQsflsekdsLLQRERCIEQEKAKLEQlfqdevakaqalreeqqrqqqqmqqekqqlA 2692
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAE--------EEEERELAEAEEERLEE------------------------------E 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 2693 ASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA 2750
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-112 |
3.82e-22 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 94.22 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 5 MLMPLDQLRTIYEVLFREGVMVAKKDRRpRSLHPHVpGVTNLQVTRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQ 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|....*...
gi 1920237940 85 YLHLPPEIVPASLQRVRRPVAmvMPARR 112
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQ--RPQRR 104
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
318-422 |
7.09e-22 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 93.32 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGcQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 397
Cdd:cd21245 3 KAIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1920237940 398 EDVDVPQPDEKSIITYVSSLYDAMP 422
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1240-2044 |
2.96e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 103.21 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1240 STQEAEEVLRAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1319
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1320 WRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLE 1399
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1400 DIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQyirf 1479
Cdd:TIGR02168 401 EIER-----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE---- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1480 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQE-EVARREEVAVEAQ--- 1555
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAAlgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1556 -------EQKRSIQEELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR 1622
Cdd:TIGR02168 546 rlqavvvENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1623 ARAEEAEAQKRQAQEEAERLR-------------------RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1683
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1684 LRLQAEEAERRLRQAEAERARQVqvaleTAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaea 1763
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE----- 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1764 eraraeaerelerwQLKANEALRLRLQAeEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELaEQELEKQRQL 1843
Cdd:TIGR02168 776 --------------ELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL-ERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1844 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLL--ASKARAE-EE 1920
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1921 SRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAVRQRAEAERvLAEKLAAISEATRLkteaeiAL 1999
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AI 992
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1920237940 2000 KEKEAENERLRRLaedeafqrrlleeqaAQHKADIEARLAQLRKA 2044
Cdd:TIGR02168 993 EEYEELKERYDFL---------------TAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2141-2760 |
1.43e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2141 EEAARQRKAALEEVERLKAKVEEARR----LRERAEQ-ESARQLQlaqeAAQKRLQAEEKAHAFAVQQKEqelqqtlqqe 2215
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERqlepLERQAEKaERYRELK----EELKELEAELLLLKLRELEAE---------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2216 qsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQsaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQA 2295
Cdd:COG1196 241 ---LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------------EAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2296 EQAALRQKQAADAEMEKHKQfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2375
Cdd:COG1196 305 ARLEERRRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2376 LRVQMEELgklkARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2455
Cdd:COG1196 384 LAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2456 KEKmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAER---LRLRV 2532
Cdd:COG1196 460 ALL-ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveAAYEA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2533 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2612
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2613 Q--LKSEEMQTVRQEQLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQlfqdEVAKAQALREEQQRQQQQMQQE 2687
Cdd:COG1196 619 GdtLLGRTLVAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLTGGSRRELLA----ALLEAEAELEELAERLAEEELE 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2688 KQQLAASMEEARRRQHEAEEGVRRQQEELQRLAqqqqqqEKLLAEENQRLRERLQHLEEERRAALARSEEIAP 2760
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALE------EQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1242-2042 |
1.88e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 100.52 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1242 QEAEEVLRAHEEQLKEAQAVpatlpeLEATKAALKKLRAQAEAQQPvFDALRDELRgaqevgerlqqrHGERDVEVERWR 1321
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI------LNELERQLKSLERQAEKAER-YKELKAELR------------ELELALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1322 ErvtlLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVRE---QLRQEKALL 1398
Cdd:TIGR02168 236 E----LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1399 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPV-----ASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLT 1473
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1474 SQYIRFISETLRRMEEE-ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAV 1552
Cdd:TIGR02168 392 ELQIASLNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1553 EAQEQKRSIQEELQHLR------QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALR 1622
Cdd:TIGR02168 472 EAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1623 ARAEEAEAQKRQAQEEAERLRR----------QVQDETQRKRQAEAELALRVQAEAEAAREK-QRALQALEELRLQAEEA 1691
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1692 ERRLRQAEAERARQVQVALE---------TAQRSAEAEL-----QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRA 1757
Cdd:TIGR02168 632 DNALELAKKLRPGYRIVTLDgdlvrpggvITGGSAKTNSsilerRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1758 QQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQkeeaerearrrgkaeeqavrqRELAEQEL 1837
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---------------------IEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1838 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARA 1917
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1918 EEEsRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEI 1997
Cdd:TIGR02168 851 SED-IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1920237940 1998 ALKEKEAENERLR-RLAEDEafqrRLLEEQAAQHKADIEARLAQLR 2042
Cdd:TIGR02168 930 RLEGLEVRIDNLQeRLSEEY----SLTLEEAEALENKIEDDEEEAR 971
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1488-2224 |
4.03e-20 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 99.52 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1488 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQh 1567
Cdd:NF041483 560 EETERAIAARQAEAAEELTRLHTEAEERLTAAE---EALADARAEAERIRREAAEETER---LRTEAAERIRTLQAQAE- 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1568 lrqsSEAEiqaKARQVEAAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1646
Cdd:NF041483 633 ----QEAE---RLRTEAAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1647 QDETQRKRQAEAELAlrvQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQVqvalETAQRSAeaelqSEHA 1726
Cdd:NF041483 706 EEAARRRREAEETLG---SARAEADQERERAREQSEEL---LASARKRVEEAQAEAQRLV----EEADRRA-----TELV 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1727 SFAEKTAQLERTlkeehvAVVQLREEATRraqqqaeaeraraeaerelerwqlkanEALRLRLQAEEVAQQksLTQAEAE 1806
Cdd:NF041483 771 SAAEQTAQQVRD------SVAGLQEQAEE---------------------------EIAGLRSAAEHAAER--TRTEAQE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1807 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ--------------- 1871
Cdd:NF041483 816 EADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqd 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1872 ----RQLLEEELARLQREAAA-----ATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrel 1942
Cdd:NF041483 893 aartRADAREDANRIRSDAAAqadrlIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA------ 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1943 AEEAARLRALAEEAKRQrqlAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEialkekeAENERLRRLAEDEAFQRR- 2021
Cdd:NF041483 967 TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE---AAAEAERLRTEAR-------EEADRTLDEARKDANKRRs 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2022 ---------LLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 2092
Cdd:NF041483 1034 eaaeqadtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDADELLVGAR 1113
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2093 R----IRGTAEDtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK--------AK 2160
Cdd:NF041483 1114 RdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANseaskvriAA 1192
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2161 VEEARRLRERAEQESARQLQLAQ------EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2224
Cdd:NF041483 1193 VKKAEGLLKEAEQKKAELVREAEkikaeaEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEALES 1262
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
322-419 |
1.54e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 87.02 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 322 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 400
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237940 401 DVPQPDEKSIITYVSSLYD 419
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2312-2759 |
2.72e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.54 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2312 KHKQFAEQALRQKAQVEQELTALRLQLEEtdhqksiLDEELQRLKAEVtEAARQRGQVEEELFSLRVQmeelgklkarie 2391
Cdd:COG1196 169 KYKERKEEAERKLEATEENLERLEDILGE-------LERQLEPLERQA-EKAERYRELKEELKELEAE------------ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2392 aenraLVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE 2471
Cdd:COG1196 229 -----LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2472 AELLQQQ-KELAQEQAR------RLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEE 2544
Cdd:COG1196 304 IARLEERrRELEERLEEleeelaELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2545 DARR-FRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVR 2623
Cdd:COG1196 384 LAEElLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2624 QEQLLQETQALQQSFLSEKDSLLQRERcieQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQH 2703
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAA---ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2704 EAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLrERLQHLEEERRAALARSEEIA 2759
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA-TFLPLDKIRARAALAAALARG 595
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
184-306 |
2.86e-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: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQ 263
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVS 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 264 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 306
Cdd:cd21308 85 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
184-306 |
4.48e-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: 86.29 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlpREKGRMRFHKLQNVQ 263
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVS 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 264 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 306
Cdd:cd21309 82 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
318-417 |
1.66e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 83.68 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 397
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237940 398 ED-VDVPQPDEKSIITYVSSL 417
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1482-2070 |
1.97e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 93.83 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AQGLQRRMQEEVARREEVAVEA 1554
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1555 QEQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1612
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1613 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELrLQAEEAE 1692
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1693 RRLRQAeAERarqvqvALETAQRSaeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAER 1772
Cdd:COG4913 474 ERWRGA-IER------VLGGFALT----LLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1773 ELERWQLKANEALRLR---LQAEEVAQ----QKSLTQAEAEKQKEEAEREARRRGKAEE-----QAVRQRELAEQELEK- 1839
Cdd:COG4913 543 KPHPFRAWLEAELGRRfdyVCVDSPEElrrhPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEl 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1840 QRQLAEGTAQ-QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLLASKA 1915
Cdd:COG4913 623 EEELAEAEERlEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1916 RAEEESRSTSEKsKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRlKTEA 1995
Cdd:COG4913 703 ELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID-ALRA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1996 EIALKEKEAENERLRRLAEDEAFQ-------------RRLLEEQAAQHKADIEARLAQLRKasESELERQKGLVEDTLRQ 2062
Cdd:COG4913 781 RLNRAEEELERAMRAFNREWPAETadldadleslpeyLALLDRLEEDGLPEYEERFKELLN--ENSIEFVADLLSKLRRA 858
|
....*...
gi 1920237940 2063 RRQVEEEI 2070
Cdd:COG4913 859 IREIKERI 866
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
936-1002 |
3.51e-18 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 81.15 E-value: 3.51e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 936 QLKPRSpaHPMRGRVPLLAVCDYKQVEVTVHKGDECQMVGPAQPFYWKVLGSSCSEAAMPSVCFLVP 1002
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
314-419 |
3.57e-18 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 83.07 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 314 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 393
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1920237940 394 LLDPEDV-DVPQPDEKSIITYVSSLYD 419
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
318-418 |
4.21e-18 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 82.78 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 397
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1920237940 398 EDVDV--PQPDEKSIITYVSSLY 418
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
321-417 |
4.77e-18 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 82.36 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 321 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 396
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1920237940 397 PEDVDVPQPDEKSIITYVSSL 417
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1480-2051 |
5.88e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.03 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1480 ISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAEREAQGLQRRMQEEVARREE 1549
Cdd:PRK02224 218 LDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1550 vaveaqeqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1626
Cdd:PRK02224 291 -----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1627 EAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQAEAErarqv 1706
Cdd:PRK02224 360 ELREEAAELESELEEAREAV--EDRREEIEELEEEIEELRERFGDAPVDL--GNAEDFLEELREERDELREREAE----- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1707 qvaLETAQRSAEAELQSEHASFAE-KTAQLERTLKE-EHVAVVQLREEatrraqqqaeaeraraeaerelerwQLKANEA 1784
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEAgKCPECGQPVEGsPHVETIEEDRE-------------------------RVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1785 LRLRLQAEEVAQQKSLTQAEAEKqkeeaerearrrgKAEEQAVR---QRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1861
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLV-------------EAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1862 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAeMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1941
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRER 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1942 LAEEAARLRALAEEAKRQRqLAEEDAVRQRAEA--ERVlAEKLAAISEAtRLKTEAEIALKEKEAEN-ERLR-RLAEDEA 2017
Cdd:PRK02224 629 LAEKRERKRELEAEFDEAR-IEEAREDKERAEEylEQV-EEKLDELREE-RDDLQAEIGAVENELEElEELReRREALEN 705
|
570 580 590
....*....|....*....|....*....|....*.
gi 1920237940 2018 FQRRL--LEEQAAQHKADIEARLAQLRKASESELER 2051
Cdd:PRK02224 706 RVEALeaLYDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1540-2445 |
6.58e-18 |
|
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: 92.34 E-value: 6.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1540 MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrlriEEEIRVVRLQLEATERQRGGAEGELQ 1619
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-----KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1620 ALRARAEEAEAQKRQAQEEAERLRRQVQDetqrKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE 1699
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1700 AERARQVQVALETAQRSAEAELQSEHASFAEKtaqleRTLKEEHVAVVQLREEatrraqqqaeaeraraeaerelerwql 1779
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEE--------------------------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1780 kANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1859
Cdd:pfam02463 357 -EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1860 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA----- 1934
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKvllal 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1935 -EAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 2013
Cdd:pfam02463 516 iKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2014 EDEAFQRRLLeeqAAQHKADIEARLAQ---------LRKASESELERQKGLVEDTLRQRRQVEEEILALKG---SFEKAA 2081
Cdd:pfam02463 596 VLEIDPILNL---AQLDKATLEADEDDkrakvvegiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEvkaSLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2082 AGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV 2161
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2162 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARE 2241
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK---VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2242 RAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaadAEMEKHKQFAEQAL 2321
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE---EKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2322 RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEvteaarQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRD 2401
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE------EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAI 980
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1920237940 2402 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLA 2445
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1487-2358 |
7.99e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 91.96 E-value: 7.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1487 MEEEERLAEQQRAEERERLAEVEaaLEKQRQLAEAHAQAKAQAEREAQGLqrRMQEEVARREEVAVEAQEQKRSIQEELQ 1566
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELEEEYL--LYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1567 HLRQSSEAEIQakarqvEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1644
Cdd:pfam02463 255 SSKQEIEKEEE------KLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1645 QVQDETQRKRQAEAELAL--RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEAE 1720
Cdd:pfam02463 329 ELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAakLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1721 LQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSL 1800
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1801 TQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEE 1877
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1878 ELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeagrfRELAEEAARLRALAEEAK 1957
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV------VEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1958 RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 2037
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2038 LAQLRKaseSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ 2117
Cdd:pfam02463 723 LADRVQ---EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2118 laaeeerrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2197
Cdd:pfam02463 800 ----------------EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2198 AFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAA 2277
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2278 AEKLRKEAEQEAARRAQAEQAALRQKQAadAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA 2357
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEE--LGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
.
gi 1920237940 2358 E 2358
Cdd:pfam02463 1022 F 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1109-2018 |
8.12e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.05 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1109 QQLLQSLEQGEQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSA 1188
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1189 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL---------KTISLVIRSTQEAEEVLRAHEEQLKEAQ 1259
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1260 AVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERvtlllerwqavlaqT 1338
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--------------L 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1339 DVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAvplansqavreqlrqekalleDIERHGEKVEECQRFAKQY 1418
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1419 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR 1498
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1499 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGlqrRMQEEVARREEVAVEAQEQKRS-------------IQEEL 1565
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1566 QHLRQSSEA--------------EIQAKARQV-------EAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1620
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1621 LRARAEEAEAQkrQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeAEAAREKQRALQALEELRLQAEEAERRlRQAEA 1700
Cdd:TIGR02169 667 LFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKLK 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1701 ERARQVQVALETAQRSAEAElQSEHASFAEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaeRELERWQLK 1780
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENV-KSELKELEARIEELEEDLHKLEEALNDLEAR-------------------LSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1781 ANEalrLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIR 1860
Cdd:TIGR02169 797 QAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEE 872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1861 LRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAEAGRFR 1940
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDPKGEDE 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1941 ELAEEAARLRALAEEAKR-QRQLAEEDAVRQRA--EAERVLAEKLAAISEATRLKTEAEiALKEKEAENERLRRLAEDEA 2017
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKREVFMEA 1023
|
.
gi 1920237940 2018 F 2018
Cdd:TIGR02169 1024 F 1024
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1477-2111 |
1.69e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 90.90 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1477 IRFISETLRRMEEE--------ERLAEQQRAEERERLAEVEAALEK----QRQLAEAHAQaKAQAEREAQGLQRRMQEEV 1544
Cdd:TIGR02169 193 IDEKRQQLERLRRErekaeryqALLKEKREYEGYELLKEKEALERQkeaiERQLASLEEE-LEKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1545 ARREEVAVE----AQEQKRSIQEELQHL---RQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRG----- 1612
Cdd:TIGR02169 272 QLLEELNKKikdlGEEEQLRVKEKIGELeaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerkr 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1613 ---------GAEGELQALRARAEEAEAQKR--------------QAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAE 1669
Cdd:TIGR02169 352 rdklteeyaELKEELEDLRAELEEVDKEFAetrdelkdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1670 AAREKQRALQA-LEELRLQAEEAERRLRQAEAER--ARQVQVALETAQRSAEAELQS--EHASFAEKTAQLERTLKEEHV 1744
Cdd:TIGR02169 431 GIEAKINELEEeKEDKALEIKKQEWKLEQLAADLskYEQELYDLKEEYDRVEKELSKlqRELAEAEAQARASEERVRGGR 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1745 AVVQLREEatrraqQQAEAERARAEAERELERWQLKANEALRLRLQA-----EEVAQQK---------------SLTQAE 1804
Cdd:TIGR02169 511 AVEEVLKA------SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1805 AEKQKEEAEREARRRGKA---------EEQAVR---QRELAEQELEKQRQL--------------------------AEG 1846
Cdd:TIGR02169 585 DERRDLSILSEDGVIGFAvdlvefdpkYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1847 TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLL----ASKARAEEESR 1922
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEE 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1923 STSEKSKQRLEAEAgrfrELAEEAARLRALaEEAKRQRQLAEED--------AVRQRAEAERVLAEKLAAISEATRlktE 1994
Cdd:TIGR02169 745 DLSSLEQEIENVKS----ELKELEARIEEL-EEDLHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLR---E 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1995 AEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALK 2074
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELE 895
|
730 740 750
....*....|....*....|....*....|....*..
gi 1920237940 2075 GSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 2111
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1267-2193 |
4.28e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 89.65 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1267 ELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerlqqrhgerdveverwrervtlllerwqavlaqtdvRQRELE 1346
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------------------------------------------ELKLKE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1347 QLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL-EDIERHGEKVEECQRFAKQYINAIKDY 1425
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1426 ELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRtryselstltsqyIRFISETLRRMEEEERLAEQQRAEERERL 1505
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE-------------KKKAEKELKKEKEEIEELEKELKELEIKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1506 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaeiQAKARQVEA 1585
Cdd:pfam02463 352 EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ------LEDLLKEEK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1586 AERSRLRIEEEIRVVRLQLEATERQrggaegelqaLRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1665
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEK----------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1666 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ-LERTLKEEHV 1744
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQkLVRALTELPL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1745 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGK--A 1822
Cdd:pfam02463 576 GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVslE 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1823 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK 1902
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1903 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKL 1982
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1983 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDT-LR 2061
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELeSK 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2062 QRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAArQRQLAAEEERRRREAEERVQKSLAAEE 2141
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE-EADEKEKEENNKEEEEERNKRLLLAKE 970
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2142 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAE 2193
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1285-2195 |
6.72e-17 |
|
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: 89.08 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1285 QQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1354
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1355 YRESADPLGAWLRDAKQR-QEQIQAVP--LANSQAVREQLRQEKALLE-DIERHGEKVEECQRFAKQYINAIKDYELQLV 1430
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKmQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1431 TYKAQLEPVASPAKK-PKVQSGSESIIQEyVDLRTRYSElstltsqyirfisETLRRMEEEERLAEQQRAEERERLAEVE 1509
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEE-------------KGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1510 AalekqrQLAEAHAQAkAQAEREAQGLQRRMQEEVARREevavEAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERS 1589
Cdd:pfam01576 229 A------QIAELRAQL-AKKEEELQAALARLEEETAQKN----NALKKIRELEAQISELQEDLESERAARNK----AEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1590 RLRIEEEIRVVRLQLEATErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeA 1668
Cdd:pfam01576 294 RRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1669 EAAREKQRALQALEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQ 1748
Cdd:pfam01576 363 EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1749 LREEATRRAQQQAEAERARAEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVR 1828
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL---------------EDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1829 QRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK------ 1902
Cdd:pfam01576 501 LQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektkn 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1903 -VRAEMEVLLAS-------------------KARAEEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQ 1961
Cdd:pfam01576 577 rLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLAEEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1962 LAEEDAVRQRAEAERVLAEKLAA---ISEATRLKTEAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADI 2034
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDL 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2035 EARlaqlrkaSESELERQKGLVedtlRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAAR 2114
Cdd:pfam01576 734 QAR-------DEQGEEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2115 QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAE 2193
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQD 882
|
..
gi 1920237940 2194 EK 2195
Cdd:pfam01576 883 EK 884
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1573-2499 |
1.02e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.20 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1573 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA-----QKRQAQEEAERLRRQVQ 1647
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1648 DETQRKRQAEAELALRVQAEAEAAR------EKQRALQALEELRLQAEEAE-----RRLRQAEAERARQVQVALETaqrs 1716
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSIAEKERELEDAEER---- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1717 aEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQaeaeraraeaerelerwqlkanEALRLRLQAEEVAQ 1796
Cdd:TIGR02169 324 -LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------------------EDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1797 QKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1875
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1876 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAGRFRELAEeaarlral 1952
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVAQLGS-------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1953 aeeAKRQRQLAEEDAVRQRAEAERVLAEKLAAiseatrlktEAEIALKEKEAENER---LRRLAEDEAFQRRLLEEQAAQ 2029
Cdd:TIGR02169 533 ---VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRDERRDLSILSEDGVIG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2030 HKADIEARLAQLRKASESELeRQKGLVEDTLRQRRQVEE-EILALKGS-FEKAAA--GKAElelelgRIRGTAEDTLRSK 2105
Cdd:TIGR02169 601 FAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKyRMVTLEGElFEKSGAmtGGSR------APRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2106 EQAEQEAARqrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ-----ESARQLQ 2180
Cdd:TIGR02169 674 AELQRLRER-------------------------LEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiEKEIEQL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2181 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraAEEAEAARERAEREAAQSRRQVEEAERL 2260
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2261 KQSAEeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEE 2340
Cdd:TIGR02169 800 LSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2341 tdhqksiLDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRlLQEEAEKMKQVA 2420
Cdd:TIGR02169 866 -------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIE 937
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2421 EEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2499
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
318-417 |
1.25e-16 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 78.36 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 397
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237940 398 ED-VDVPQPDEKSIITYVSSL 417
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
186-303 |
1.43e-16 |
|
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: 78.01 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 186 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdvirssrlPREKGRMRFHKLQNVQIA 265
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQAC 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237940 266 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 303
Cdd:cd21212 68 LQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
187-301 |
1.72e-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: 77.76 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 187 KKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpREKGRMRFHKLQNVQIAL 266
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFL 66
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 267 DYLRHRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 301
Cdd:cd00014 67 NACKKLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1064-1752 |
2.10e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.42 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1064 EQRQALRSLELHYQA----FLRDSQDAGgfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQE----ESRCQRCISELKDI 1135
Cdd:TIGR02168 217 ELKAELRELELALLVlrleELREELEEL---QEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1136 RLQLEACETRTVH---RLRlPLDKEPARECAQRITEQQK---AQAEVDGLGKGVARLSAEAEkvlALPEPSPAAPTLRSE 1209
Cdd:TIGR02168 294 ANEISRLEQQKQIlreRLA-NLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELE---SLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1210 LELTLGKL-EQVRSLSAIYLEKLKTISLvIRSTQEaeeVLRAHEEQLKEAQAVPATlpelEATKAALKKLRAQAEAQQPV 1288
Cdd:TIGR02168 370 LESRLEELeEQLETLRSKVAQLELQIAS-LNNEIE---RLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1289 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLL---LERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAW 1365
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1366 LRDAKQR---------------QEQIQAVPLANSQAVR---EQLRQEK----ALLEDIERHGEKVEECQRFAKQYINAIK 1423
Cdd:TIGR02168 522 LGVLSELisvdegyeaaieaalGGRLQAVVVENLNAAKkaiAFLKQNElgrvTFLPLDSIKGTEIQGNDREILKNIEGFL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1424 DYELQLVTYKAQLEPVASP---------------AKKPKVQSGSESIIQEYVDLRTRYS--------ELSTL-TSQYIRF 1479
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1480 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKR 1559
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1560 SIQEELQHLRQSSEAEIQAKARQVEAaersrlriEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1639
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEEL--------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1640 ERLRRQVQDETQRKRQAEAELAlrvqaeaeaarekqRALQALEELRLQAEEAERRLRQAEAERArQVQVALETAqRSAEA 1719
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIE--------------SLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELE 897
|
730 740 750
....*....|....*....|....*....|....*
gi 1920237940 1720 ELQSEHASFAEKTAQLERTLKE--EHVAVVQLREE 1752
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEElrEKLAQLELRLE 932
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1500-2062 |
5.09e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.12 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1500 EERERLAEVEAALEKQRQLAEAHAQAKaQAEReaqglQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRqsseaeIQAK 1579
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALE-DARE-----QIELLEPIRELAERYAAARERLAELEYLRAALR------LWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1580 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-AQKRQAQEEAERLRRQvQDETQRKRQAEA 1658
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERE-LEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1659 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS-EH------ASFAEK 1731
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlERrksnipARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1732 TAQLERTLKEEHVAV------VQLREEAtrraqqqaeaeraraeaerelERWQLKANEAL---RLRL--------QAEEV 1794
Cdd:COG4913 446 RDALAEALGLDEAELpfvgelIEVRPEE---------------------ERWRGAIERVLggfALTLlvppehyaAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1795 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG--- 1868
Cdd:COG4913 505 VNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAGqvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1869 ------------------------EQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRST 1924
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1925 S-EKSKQRLEAEagrFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 2003
Cdd:COG4913 665 SaEREIAELEAE---LERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2004 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRkaseSELERQKGLVEDTLRQ 2062
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALR----ARLNRAEEELERAMRA 795
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1457-2113 |
6.38e-16 |
|
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: 85.66 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1457 QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE-EERLAE--QQRAEERERLAEVEAALEKQRQLAEAhAQAKAQAEREA 1533
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFGYKSDETLIASRQEErQETSAElnQLLRTLDDQWKEKRDELNGELSAADA-AVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1534 QGLQRRMQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAeIQAKARQVEAA-ERSRLRIEEEIR--VVRL------QL 1604
Cdd:pfam12128 327 LEDQHGAFLDA--DIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKyNRRRSKIKEQNNrdIAGIkdklakIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1605 EATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEA-----EAAREKQ--- 1675
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENfderiERAREEQeaa 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1676 -----RALQALEELRLQAEEAERRLRQAEAeRARQVQVALETAQR-------------SAEAELQSEHASFAEKTAQLER 1737
Cdd:pfam12128 484 naeveRLQSELRQARKRRDQASEALRQASR-RLEERQSALDELELqlfpqagtllhflRKEAPDWEQSIGKVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1738 TLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkaneALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREAR 1817
Cdd:pfam12128 563 TDLDPEVWDGSVGGELNLY---------------------------GVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1818 RRGKAEEQAvRQRELAEQELEKQrQLAEGTAQQRLA-AEQELIRLraeTEQGEQQRQLLEEELARLQREaaaATQKRREL 1896
Cdd:pfam12128 616 AREKQAAAE-EQLVQANGELEKA-SREETFARTALKnARLDLRRL---FDEKQSEKDKKNKALAERKDS---ANERLNSL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1897 EAELAKVraEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQraeaer 1976
Cdd:pfam12128 688 EAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRD------ 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1977 vLAEKlaAISEATRLKTEAEIalKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKG-L 2055
Cdd:pfam12128 760 -LASL--GVDPDVIAKLKREI--RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI-SELQQQLArL 833
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 2056 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTlrSKEQAEQEAA 2113
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDA--NSEQAQGSIG 889
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
322-419 |
9.78e-16 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 76.07 E-value: 9.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 322 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 400
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237940 401 DVPQPDEKSIITYVSSLYD 419
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2136-2758 |
1.43e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2136 SLAAEEEAARQRKAALEEVERLKAKVEEARRlRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2215
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2216 QSVLERLrseaeaarraaeeaeaareraereaaQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2295
Cdd:PTZ00121 1154 VEIARKA--------------------------EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2296 EQAALRQKQAADAEMEKHKQFAEQA--LRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVE--E 2371
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2372 ElfslRVQMEELGKLKARIEAENRALVLRDKDSAQRLlQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALA 2451
Cdd:PTZ00121 1288 E----KKKADEAKKAEEKKKADEAKKKAEEAKKADEA-KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2452 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLaqetqgfqKTLETERQRQLEMSAEAERLRlr 2531
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADEL--------KKAAAAKKKADEAKKKAEEKK-- 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2532 VAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKvmlvqtletQRQQSDRDAERLREAiAELEHEKDKLKQEAQL 2611
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---------KADEAKKKAEEAKKA-DEAKKKAEEAKKKADE 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2612 LQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALReeqqrqqqqmqqekqql 2691
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK----------------- 1564
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2692 aaSMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA--LARSEEI 2758
Cdd:PTZ00121 1565 --KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeeLKKAEEE 1631
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1891-2758 |
1.92e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.35 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1891 QKRRELEAELAKVrAEMEVLLAsKARAEEEsrsTSEKSKQRLEAeagRFRELAEEAARLRALAEEAKRQRQLAEEdavRQ 1970
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFDRKKE-KALEELE---EVEENIERLDL---IIDEKRQQLERLRREREKAERYQALLKE---KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1971 RAEAERVLAEKLAAisEATRLKTEAEIAlkEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASESELE 2050
Cdd:TIGR02169 222 EYEGYELLKEKEAL--ERQKEAIERQLA--SLEEELEKLTEEISE-------LEKRLEEIEQLLEELNKKIKDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2051 RQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDtlrSKEQAEQEAARQRQLAAEEERRRREAE 2130
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2131 ERVQKSLAAEEEAARQR---KAALEEVERLKAKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHA 2198
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRdelKDYREKLEKLKREINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2199 FAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAA 2278
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELY----------------------DLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2279 EKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTAlrlqleetdhQKSIldEELQRLKA- 2357
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVA----------KEAI--ELLKRRKAg 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2358 EVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENR-----------ALVLRDKDSAQRLLQ---------EEAEKMK 2417
Cdd:TIGR02169 574 RATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARRLMGkyrmvtlegELFEKSG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2418 QVA----EEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2484
Cdd:TIGR02169 654 AMTggsrAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2485 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARaeEDARRFRKQAEDIGERLYRTE 2564
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2565 LATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsfLSEKDS 2644
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD------LESRLG 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2645 LLQRERC-IEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG---------VRRQQE 2714
Cdd:TIGR02169 886 DLKKERDeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvqaeLQRVEE 965
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1920237940 2715 ELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEEI 2758
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRldeLKEKRAKLEEERKAILERIEEY 1012
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2948-2986 |
2.28e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.36 E-value: 2.28e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 2948 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 2986
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1006-1736 |
2.46e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.95 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1006 QEAQEAIARLEAQHQALVALWHQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQD 1085
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1086 AggfgpEDRLQA-EREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQ 1164
Cdd:TIGR02168 370 L-----ESRLEElEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1165 RITEQQKAQAEVDGLGKGVARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLS---AIYLEKLKTISLVIRS 1240
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvKALLKNQSGLSGILGV 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1241 TQEAEEVlrahEEQLKeaQAVPATLPE---------LEATKAALKKLrAQAEAQQPVFDALrDELRGAQEVGERLQQRHG 1311
Cdd:TIGR02168 525 LSELISV----DEGYE--AAIEAALGGrlqavvvenLNAAKKAIAFL-KQNELGRVTFLPL-DSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1312 ERDV-----EVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYR------ESADPLGAWLRDAKQRqeqiQAVP 1380
Cdd:TIGR02168 597 IEGFlgvakDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgDLVRPGGVITGGSAKT----NSSI 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1381 LANSQAVREqLRQEKALLEDIERHGEKveecqrfakqyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYV 1460
Cdd:TIGR02168 673 LERRREIEE-LEEKIEELEEKIAELEK-------------ALAELRKELEELEEELE---------QLRKELEELSRQIS 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1461 DLRTRYSELST---LTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ 1537
Cdd:TIGR02168 730 ALRKDLARLEAeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1538 ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQR 1611
Cdd:TIGR02168 810 aelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1612 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA-LRVQAEAEAAREKQRALQALEELRLQAEE 1690
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237940 1691 AERRLRQAEAERARQVQVALEtaqrsAEAELQSEHASFAEKTAQLE 1736
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLA-----AIEEYEELKERYDFLTAQKE 1010
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1242-1742 |
3.54e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.17 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1242 QEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfDALRDELRGAQEVGERLQQRHGERDVEVERWR 1321
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1322 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ---AVPLANSQAVREQLRQEKALL 1398
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1399 EDIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESIIQEYVDLRTRYSELSTLtsqyir 1478
Cdd:PRK02224 387 EELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT------ 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1479 fISETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAK--AQAEREAQG 1535
Cdd:PRK02224 435 -LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEdlVEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1536 LQRR---MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvRLQLEATERQRG 1612
Cdd:PRK02224 514 LEERredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1613 GAEGELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDETQRKRQAEAELAlrvQAEAEAARE-KQRALQALeelrlq 1687
Cdd:PRK02224 592 ERIRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYL------ 662
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 1688 aEEAERRLRQAEAERARqVQVALETAQRSAE--AELQSEHASFAEKTAQLErTLKEE 1742
Cdd:PRK02224 663 -EQVEEKLDELREERDD-LQAEIGAVENELEelEELRERREALENRVEALE-ALYDE 716
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1202-1955 |
4.24e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 83.09 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1202 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLkeaqavPATLPELEATKAALKKLRAQ 1281
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCM------PDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1282 AEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEverwrervtllLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdp 1361
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPLAAHIK-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1362 lgAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAS 1441
Cdd:TIGR00618 301 --AVTQIEQQAQRIHTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1442 PAKKPKVQSGSESIIQEyvDLRTRYSELSTLTSQYIRFISETLRRMEEEERL--AEQQRAEERERLAEVEAALEKQRQ-- 1517
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQce 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1518 -LAEAHAQAKAQAERE-------AQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA--EIQAKARQVEAAE 1587
Cdd:TIGR00618 455 kLEKIHLQESAQSLKEreqqlqtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1588 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE 1667
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1668 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVV 1747
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1748 QLREEATRRAQQQAEAERARAEAERELERWQLkANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREArrrgkaEEQAV 1827
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE------AHFNN 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1828 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKRRELEAELAK 1902
Cdd:TIGR00618 767 NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 1903 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1955
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1482-1973 |
4.88e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.12 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA--QAKAQAEREAQGLQRRMQEEVARREEVAvEAQEQKR 1559
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR-ELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1560 SIQEELQHLRQSSEaeiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1639
Cdd:COG4717 167 ELEAELAELQEELE----------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1640 ER--LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSA 1717
Cdd:COG4717 237 EAaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1718 EAElqsehasfaektaQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAqq 1797
Cdd:COG4717 317 EEE-------------ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1798 ksltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQqrqlLEE 1877
Cdd:COG4717 382 -----------------------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1878 ELARLQREAAAATQKRRELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAK 1957
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
|
490
....*....|....*....
gi 1920237940 1958 RQRQLAEED---AVRQRAE 1973
Cdd:COG4717 504 EAREEYREErlpPVLERAS 522
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1387-2051 |
4.88e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.66 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1387 VREQLRQEKALLEDIERhgekveecqrfAKQYINAIKDYELQLVTYKAQ---LEPVaspakkpkvqsgsESIIQEYVDLR 1463
Cdd:COG4913 213 VREYMLEEPDTFEAADA-----------LVEHFDDLERAHEALEDAREQielLEPI-------------RELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1464 TRYSELSTLTSQY-IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEREAQGLQR 1538
Cdd:COG4913 269 ERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1539 RMQEEVARREEVAVEAQEQKRSI--------------QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1604
Cdd:COG4913 349 RLERELEERERRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1605 EATERQRGGAEGELQALRARAEEAeaqkrqAQEEAERLR-----RQVQDETQRKRQAeAELALRVQA-----EAEAAREK 1674
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEA------LGLDEAELPfvgelIEVRPEEERWRGA-IERVLGGFAltllvPPEHYAAA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1675 QRALQALE-ELRLQAEEAERRLRQAEAER------ARQVQVALETAQRSAEAELQSehaSFAEKTAQLERTLKEEHVAV- 1746
Cdd:COG4913 502 LRWVNRLHlRGRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELGR---RFDYVCVDSPEELRRHPRAIt 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1747 --VQLREEATrraqqqaeaERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAE 1823
Cdd:COG4913 579 raGQVKGNGT---------RHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL----------EAE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQREAAAATQKRRELEAEL 1900
Cdd:COG4913 640 LDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEI 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1901 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1980
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1981 -KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELER 2051
Cdd:COG4913 796 fNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4185-4223 |
5.21e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 5.21e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 4185 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 4223
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3607-3645 |
5.21e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 5.21e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 3607 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEMNRVL 3645
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1476-2195 |
7.04e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 82.32 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1476 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQ 1555
Cdd:TIGR00618 140 YKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1556 EQKRSIQEELQHLR--QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL---RARAEEAEA 1630
Cdd:TIGR00618 219 ERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1631 QKRQAQEEAERLRRQVQ-DETQRKRQAEAELALRVQAEAEAAREKQRALQAL--EELRLQAEEAERRLRQAEAERARQVQ 1707
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATSIREISCQQHTLT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1708 VALETAQRSAEAELQSEHASFAEKTaqlertlkeehvavvQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL 1787
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELD---------------ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1788 RLQAEEVAQQKSLTQAEAEKQKEEAerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQ 1867
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSL--------KEREQQLQTKEQIHLQETRKKAVVL----ARLLELQEEPCPLCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1868 GEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLAS----KARAEEESRSTSEKSKQR---------LEA 1934
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQraslKEQMQEIQQSFSILTQCDnrskedipnLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1935 EAGRFRELAEEAARLR-ALAEEAKRQ-RQLAEEDAVRQRAEAERVLAEKLAaiSEATRLKTEAEIALKEKEAENERLRRL 2012
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEdMLACEQHALlRKLQPEQDLQDVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALSIRV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2013 AEDEAFQRRLLEEQAAQHKADieaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 2092
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKE---QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2093 RIRGTAEDTLRSKEQAEQEAARQrqlaaeeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2172
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEE----------VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
|
730 740
....*....|....*....|....
gi 1920237940 2173 QE-SARQLQLAQEAAQKRLQAEEK 2195
Cdd:TIGR00618 817 DIlNLQCETLVQEEEQFLSRLEEK 840
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
320-431 |
9.06e-15 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 73.49 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 320 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 399
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1920237940 400 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 431
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1469-2380 |
1.03e-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: 81.76 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1469 LSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAkAQAEREAQGLQRRMQEEV 1544
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQAQIAELRAQL-AKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1545 ARREEvaveAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERSRLRIEEEIRVVRLQLEATErqrgGAEGELQALRAR 1624
Cdd:pfam01576 257 AQKNN----ALKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1625 AE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaeaEAAREKQRALQALEELRlQAEEAERRLRQAEAERA 1703
Cdd:pfam01576 325 REqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1704 RQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1783
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1784 ALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRA 1863
Cdd:pfam01576 475 ELL----QEETRQKLNLSTRLRQL---------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1864 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK-------VRAEMEVLLAS-------------------KARA 1917
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1918 EEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---ISEATRLKT 1993
Cdd:pfam01576 612 EEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVgknVHELERSKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1994 EAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADIEARlaqlrkaSESELERQKGLVedtlRQRRQVEEE 2069
Cdd:pfam01576 689 ALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDLQAR-------DEQGEEKRRQLV----KQVRELEAE 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2070 ILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2149
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKN 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2150 ALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSVLERLRSEAE 2227
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2228 AARR---AAEEAEAARERAEREAAQSRRQVEEAeRLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQ 2304
Cdd:pfam01576 918 QVEQlttELAAERSTSQKSESARQQLERQNKEL-KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2305 AADAE---------MEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2375
Cdd:pfam01576 997 VRRTEkklkevllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVST 1076
|
....*
gi 1920237940 2376 LRVQM 2380
Cdd:pfam01576 1077 LKSKL 1081
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1294-2073 |
1.05e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.65 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1294 DELRGAQEVGERLQQRHGERDvEVERWRERVTLLLERwqaVLAQTDVRQRELEQLGRqlryYREsadplgawLRDAKQRQ 1373
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDE---KRQQLERLRREREKAER----YQA--------LLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1374 EQiqAVPLANSQAVREQLRQEKALLEDIERHGEKVEEcqrfakqyinAIKDYELQLVTYKAQLEPVASPAKKpkvqSGSE 1453
Cdd:TIGR02169 224 EG--YELLKEKEALERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELNKKIKD----LGEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1454 SIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA 1533
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1534 QGLQRRMQEEVARREEVAVEAQEQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGG 1613
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1614 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEEL---RLQA-- 1688
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVlkaSIQGvh 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1689 ----------EEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFA-----EKTAQLERTLKEEHVA-------- 1745
Cdd:TIGR02169 525 gtvaqlgsvgERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplNKMRDERRDLSILSEDgvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1746 --------------------VVQLREEATRRAQQQAEAERA--------------RAEAERELERWQLKAnEALRLRLQA 1791
Cdd:TIGR02169 605 lvefdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEgelfeksgamtggsRAPRGGILFSRSEPA-ELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1792 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAV---RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1868
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeieKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1869 EQQRQLLEEELARLQreAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAAR 1948
Cdd:TIGR02169 764 EARIEELEEDLHKLE--EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1949 LRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA 2028
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2029 QHKADIEA---RLAQLRKASESELE-RQKGLVEDTLRQRRQ-VEEEILAL 2073
Cdd:TIGR02169 921 ELKAKLEAleeELSEIEDPKGEDEEiPEEELSLEDVQAELQrVEEEIRAL 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1092-1643 |
1.62e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1092 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLrlpldkeparecAQRITEQQK 1171
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL------------EELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1172 AQAEVDGLGKGVARLSAEAEKVLAlpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1251
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE---------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1252 EEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERw 1331
Cdd:COG1196 413 LERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1332 qavlaqtdvRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIERHGEKVEEC 1411
Cdd:COG1196 486 ---------LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1412 QRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEE 1490
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1491 ERLAEQQRAEERERLAEVEAALEKQRqLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQ 1570
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1571 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ-------AQEEAERLR 1643
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELE 794
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
320-419 |
2.01e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 72.31 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 320 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 399
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1920237940 400 VDV--PQPDEKSIITYVSSLYD 419
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1218-1721 |
4.85e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1218 EQVRSLSAI--YLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPatlpELEATKAALKKLRAQAEAQQPVFDALRDE 1295
Cdd:COG4913 249 EQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEA----ELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1296 LRGAQEV-----GERLQQRhgERDVE-VERWRERVTLLLERWQAVLAQTDVR---------------QRELEQLGRQLRY 1354
Cdd:COG4913 325 LDELEAQirgngGDRLEQL--EREIErLERELEERERRRARLEALLAALGLPlpasaeefaalraeaAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1355 YRESADPLGAWLRDAKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IE 1402
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1403 R--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAqlEPVASPAKKPKVQSGS--------ESIIQEYVD--LRT 1464
Cdd:COG4913 482 RvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERV--RTGLPDPERPRLDPDSlagkldfkPHPFRAWLEaeLGR 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1465 RYS--------ELST----LTSQYIRFISETLRRMEEEERL---------AEQQRAEERERLAEVEAALEKQRQLAEAHA 1523
Cdd:COG4913 558 RFDyvcvdspeELRRhpraITRAGQVKGNGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1524 QAKAQAEREAQGLQRRmqEEVARREEVAVEAQEQKRSIQEELQHLRQSSeAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1603
Cdd:COG4913 638 AELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1604 LEATERQRGGAEGELQALRARAEEAE------------------AQKRQAQEEAERLRRQVQDETQRKRQAEAEL----- 1660
Cdd:COG4913 715 IGRLEKELEQAEEELDELQDRLEAAEdlarlelralleerfaaaLGDAVERELRENLEERIDALRARLNRAEEELeramr 794
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 1661 ---------ALRVQAEAEAAREKQRALQALEELRL---QAEEAERRLRQAEAERArQVQVALETAQRSAEAEL 1721
Cdd:COG4913 795 afnrewpaeTADLDADLESLPEYLALLDRLEEDGLpeyEERFKELLNENSIEFVA-DLLSKLRRAIREIKERI 866
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
179-302 |
4.89e-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: 71.16 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 179 ADERDrvqKKTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLsgDSLprERDVIRSSRLPREKGRMRFHK 258
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKK 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 302
Cdd:cd21219 64 VENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1778-2638 |
5.10e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 79.34 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1778 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1853
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1854 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1931
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1932 LEAEAGRFRELAEEAARLRALAEEAKRQRQlaeedavrQRAEAERVLAEKLAAISEatrLKTEAEIALKEKEAENERLRR 2011
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSE--------ELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2012 LAED-EAFQRRLLEEQAAQhkADIEARLAQLRKaSESELERQKGLVEDTLRQRRQVEEeilalkgsfekaaagkaELELE 2090
Cdd:TIGR02169 460 LAADlSKYEQELYDLKEEY--DRVEKELSKLQR-ELAEAEAQARASEERVRGGRAVEE-----------------VLKAS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2091 LGRIRGTAEDTLRSKEQ---AEQEAARQRqlaaeeerrrrEAEERVQKSLAAEE--EAARQRK---AALEEVERLKAKVE 2162
Cdd:TIGR02169 520 IQGVHGTVAQLGSVGERyatAIEVAAGNR-----------LNNVVVEDDAVAKEaiELLKRRKagrATFLPLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2163 EARRLRERAEQESARQLqlaQEAAQKRlqaeEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2242
Cdd:TIGR02169 589 DLSILSEDGVIGFAVDL---VEFDPKY----EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2243 AEREAAQSRRQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2319
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2320 ALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQveEELFSLRVQMEELGKLKARIEAENRALvl 2399
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREI-- 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2400 rDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQK 2479
Cdd:TIGR02169 818 -EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKER 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2480 ELAQEQARRLQEDKEQMAQQlaqetqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfRKQAEDIGER 2559
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAE 959
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2560 LYRTELAtqekvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSF 2638
Cdd:TIGR02169 960 LQRVEEE-------IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENF 1031
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
318-415 |
5.28e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.87 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 393
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 1920237940 394 LLDPEDVDVPQPDEKSIITYVS 415
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
320-423 |
5.36e-14 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 71.23 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 320 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 399
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1920237940 400 VDV--PQPDEKSIITYVSSLYDAMPR 423
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
323-418 |
6.26e-14 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 70.85 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 323 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 401
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1920237940 402 VPQPDEKSIITYVSSLY 418
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1859-2672 |
8.14e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.86 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1859 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEAea 1936
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLMN-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1937 grfrelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAErvlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 2016
Cdd:TIGR00618 172 ------LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2017 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEeilalkgsfeKAAAGKAELELELGRIRG 2096
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2097 TAEdtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2176
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2177 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2256
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2257 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2336
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2337 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLkarIEAENRAlvlrdKDSAQRLLQEEAEKm 2416
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLSEA-----EDMLACEQHALLRK- 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2417 KQVAEEAARLSVAAQEAARLRQLAEEDLAQqraLAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQ--EDKE 2494
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQltYWKE 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2495 QMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEdigERLYRTELATQEKVMLV 2574
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK---ARTEAHFNNNEEVTAAL 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2575 QTLeTQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQ 2654
Cdd:TIGR00618 775 QTG-AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
810
....*....|....*...
gi 1920237940 2655 EKAKLEQlfQDEVAKAQA 2672
Cdd:TIGR00618 854 YEECSKQ--LAQLTQEQA 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1209-1731 |
8.82e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1209 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEvLRAHEEQLKEAQAvpaTLPELEATKAALKKLRAQAEAQQpv 1288
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE-LARLEAELERLEA---RLDALREELDELEAQIRGNGGDR-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1289 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLRD 1368
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1369 AKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IER--HGEK----VEE 1410
Cdd:COG4913 417 LRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIERvlGGFAltllVPP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1411 cQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsiiqeyvdlrtrysELSTLTSQYIRFISETLRRM- 1487
Cdd:COG4913 496 -EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRf 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1488 -----EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAKAQAEREAQGLQRRMQEEVARREEVAvE 1553
Cdd:COG4913 560 dyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-A 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1554 AQEQKRSIQEELQHLRQSSEAEIQakarqVEAAERSRLRIEEEIRvvrlQLEAterqrggAEGELQALRARAEEAEAQKR 1633
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1634 QAQEEAERLRRQVQDETQRKRQAEAEL-ALRVQAEAEAAREKQRALQALEELRlqAEEAERRLRQAEAERARQVQVALET 1712
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRA 780
|
570
....*....|....*....
gi 1920237940 1713 AQRSAEAELQSEHASFAEK 1731
Cdd:COG4913 781 RLNRAEEELERAMRAFNRE 799
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1499-2605 |
9.14e-14 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 78.85 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1499 AEERERLaeVEAALEKQRQLAEAHAQAKAQAEReaqglqrrmQEEVARREEvavEAQEQKRSIQEELQ----HLRQSSEA 1574
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAEQYR---------LVEMARELA---ELNEAESDLEQDYQaasdHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1575 EIQAKA--RQVEAAERSRLRIEEEIRVVRlqlEATERQrggaegelqalraraEEAEAQKRQAQEEAERLRRQVQDETQr 1652
Cdd:PRK04863 344 LRQQEKieRYQADLEELEERLEEQNEVVE---EADEQQ---------------EENEARAEAAEEEVDELKSQLADYQQ- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1653 krqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVALETAQRSAEAElqsEH 1725
Cdd:PRK04863 405 --------ALDVQQTR--AIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ---AA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1726 ASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALRlrlqaeevaqqksltqaea 1805
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVS-----RSEA-----------------------WD-VARELLR------------------- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1806 ekqkeeaerearrrgkaeeQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1885
Cdd:PRK04863 504 -------------------RLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1886 AAAAtqkRRELEAELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1965
Cdd:PRK04863 563 LEAR---LESLSESVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1966 dAVRQRAEAERVLAEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAEDeaFQRRLLEEQ----AAQHKADIEARLAQ 2040
Cdd:PRK04863 632 -YMQQLLERERELTVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER--FGGVLLSEIyddvSLEDAPYFSALYGP 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2041 LRKASeseLERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG--KAElELELGRIRGTAEDTLR-SKEQAEQ---EAAR 2114
Cdd:PRK04863 709 ARHAI---VVPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSvfSVE-ELEKAVVVKIADRQWRySRFPEVPlfgRAAR 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2115 QRQLaaeeerrrreaeervqkslaaeEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLA---------QEA 2185
Cdd:PRK04863 785 EKRI----------------------EQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeaelRQL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2186 AQKRLQAEEKahafavqqkeqelqqtlqqeqsvLERLRSeaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSae 2265
Cdd:PRK04863 843 NRRRVELERA-----------------------LADHES---------------------QEQQQRSQLEQAKEGLSA-- 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2266 eqaqaqaqaqaaaekLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRlqleeTDhqk 2345
Cdd:PRK04863 877 ---------------LNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ-----SD--- 933
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2346 silDEELQRLKAEVTEAARQRGQVEEELFSLrvqmEELGKLKARIEAENRALVLRDKDSAQRLLQ---EEAEKMKQVAEE 2422
Cdd:PRK04863 934 ---PEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEDAAEMLAKNSDLNEKLRqrlEQAEQERTRARE 1006
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2423 AARlsvaaQEAARLRQLAE--EDLAQQRALAEKMLKEKMQAVQEAT-RLKAEAE-LLQQQKELAQEQARRLQEDKEQMAQ 2498
Cdd:PRK04863 1007 QLR-----QAQAQLAQYNQvlASLKSSYDAKRQMLQELKQELQDLGvPADSGAEeRARARRDELHARLSANRSRRNQLEK 1081
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2499 QLaqetqgfqkTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEkvmlvqtLE 2578
Cdd:PRK04863 1082 QL---------TFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLS-------AD 1145
|
1130 1140
....*....|....*....|....*..
gi 1920237940 2579 TQRQQSDRDAERLREAIAELEHEKDKL 2605
Cdd:PRK04863 1146 ELRSMSDKALGALRLAVADNEHLRDVL 1172
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
186-303 |
9.80e-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: 70.02 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 186 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerDVIRSsrlPREKGRMRfhklQNVQIA 265
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKV 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237940 266 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 303
Cdd:cd21213 68 LQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3866-3904 |
1.06e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.74 E-value: 1.06e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 3866 LLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPELHDRL 3904
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2300-2759 |
1.29e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2379
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2380 MEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2459
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2460 QAVQEATRLKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2538
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2539 QARAEEDARRFRKQAEDIGERLYRTE-----------------------------LATQEKV------------------ 2571
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVdegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2572 MLVQTLETQRQ--QSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE-----------------------MQTVRQEQ 2626
Cdd:TIGR02168 550 VVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsylLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2627 LLQETQALQ------------------------QSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQ 2682
Cdd:TIGR02168 630 DLDNALELAkklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 2683 QMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2759
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1265-1724 |
1.54e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.50 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1265 LPELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTL--LLERWQAVLAQTDVRQ 1342
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1343 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQekaLLEDIERHGEKVEECQRFAKQYINAI 1422
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1423 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESII-------QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE--EE 1491
Cdd:COG4717 223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1492 RLAEQQRAEERERL--AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKrsIQEELQHLR 1569
Cdd:COG4717 303 EAEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1570 QSSEAEIQAKARQVEAAErsrlRIEEEIRVVRLQLEA--TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1647
Cdd:COG4717 381 VEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1648 DETQRKRQAEAElalrvqaeaeaarekqralQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQRSAEAELQSE 1724
Cdd:COG4717 457 ELEAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALklALELLEEAREEYREERLPP 516
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1486-2610 |
1.71e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 77.91 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1486 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHAQAKAQAEREAqglqrrmqEEVARREEVAVEAQEQKRSI 1561
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNALQEQLQAET--------ELCAEAEEMRARLAARKQEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1562 QEELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAER 1641
Cdd:pfam01576 74 EEILHEL----ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR-------QKLQLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1642 LRRQVQDETQRKRQAE---AELALRVQAEAEAA------REKQRALQALEELRLQAEEAERRlrqaEAERARQVQVALET 1712
Cdd:pfam01576 143 LEDQNSKLSKERKLLEeriSEFTSNLAEEEEKAkslsklKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1713 AQRSAEAELQsehASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKANEALRLRLQaE 1792
Cdd:pfam01576 219 DLQEQIAELQ---AQIAELRAQLAKKEEELQAALARLEEETAQKNNALK----------------KIRELEAQISELQ-E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1793 EVAQQKSltqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGT-----AQQRLAA--EQELIRLR--- 1862
Cdd:pfam01576 279 DLESERA----------------------ARNKAEKQRRDLGEELEALKTELEDTldttaAQQELRSkrEQEVTELKkal 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1863 -AETEQGEQQRQ-----------LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQ 1930
Cdd:pfam01576 337 eEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK-RKKLEGQLQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1931 RLEA---EAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERV---LAEKLAAISEATRLKTEAEIALKEKE 2003
Cdd:pfam01576 416 ELQArlsESERQRaELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqLQDTQELLQEETRQKLNLSTRLRQLE 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2004 AENERLRRLAEDEAFQRRLLEEQAAQHkadiEARLAQLRKASESELERQKGLVEDtlrqRRQVEEEILALKGSFEKAAAG 2083
Cdd:pfam01576 496 DERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2084 KAELELELGRIRGTAEDTLRSKEQaeqeaarQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEE 2163
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDH-------QRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDRAEAEAREKE 635
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2164 ARRLRERAEQESARQLQLAQEAAQKRLQAEekahafavqqkeqelqqtlqqeqsvLERLRSEAEAARRAAEEAEAARERA 2243
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELERSKRAL 690
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2244 EREAAQSRRQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKQfaeQALRQ 2323
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQ 750
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2324 KAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKD 2403
Cdd:pfam01576 751 VRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE 830
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2404 SAQRLLQEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2483
Cdd:pfam01576 831 SEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2484 EQARRLQEDKEQMAQQLAQETQGFQKtLETERQrqlEMSAEAERLRLRVAEMSRAQ---------------ARAEEDARR 2548
Cdd:pfam01576 910 DRLRKSTLQVEQLTTELAAERSTSQK-SESARQ---QLERQNKELKAKLQEMEGTVkskfkssiaaleakiAQLEEQLEQ 985
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2549 FRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQ 2610
Cdd:pfam01576 986 ESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
183-299 |
1.90e-13 |
|
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: 69.48 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 183 DRVQKKTFTKWVNKHLIKhwRAEAQrhISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPRekgrmrfhkLQNV 262
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNL 68
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237940 263 QIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTI 299
Cdd:cd21225 69 HLAMLFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2302-2832 |
5.54e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2302 QKQAADAEMEKHKQFAEQALRqkaqVEQELTAlrlqleETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV-QM 2380
Cdd:PTZ00121 1121 KKKAEDARKAEEARKAEDARK----AEEARKA------EDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrKA 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2381 EELGKLKA--RIEAENRALVLRDKDSAQRllQEEAEKMKQV--AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2456
Cdd:PTZ00121 1191 EELRKAEDarKAEAARKAEEERKAEEARK--AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2457 EKMQAVQEATrlKAEaELLQQQKELAQEQARRLQEDKEqmAQQLAQETQGFQKTLETERQRQlEMSAEAERLRLRVAEMS 2536
Cdd:PTZ00121 1269 QAAIKAEEAR--KAD-ELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAE-EAKKKADAAKKKAEEAK 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2537 RAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLEtQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlKS 2616
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-KA 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2617 EEMQTvRQEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQ--DEVAKAQALREEQQRqqqqmqqekqqlAAS 2694
Cdd:PTZ00121 1421 DEAKK-KAEEKKKADEAKKKAEEAKKADEAKKK---AEEAKKAEEAKKkaEEAKKADEAKKKAEE------------AKK 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2695 MEEARRRQHEAeegvRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR-SEEIAPSRA-AAARALPNG 2772
Cdd:PTZ00121 1485 ADEAKKKAEEA----KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkAEEKKKADElKKAEELKKA 1560
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2773 QDAADGPAAAAEPEHAFDGLRR-----KVPAQRLQEVGVL-------SAEELQQLAQGRTTVAELAQREDVR 2832
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLyeeekkmKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1243-1739 |
6.30e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1243 EAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELrgAQEVGERLQQRHGERDVEVERWRE 1322
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1323 RVTLLLERWQAVLAQ-TDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDI 1401
Cdd:COG4913 317 RLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1402 ERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFIS 1481
Cdd:COG4913 397 EEELEALEEALAEAEA---ALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAEREAQGLQRRM- 1540
Cdd:COG4913 465 ELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLd 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1541 ----------QEEVARREEVA-VEAQEQ----KRSIQEELQ--------------HLRQ------SSEAEIQAKARQVEA 1585
Cdd:COG4913 542 fkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1586 AERSRLRIEEEIRVVRLQLEATERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDETQRK 1653
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1654 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEAELQSEHASFAEK 1731
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRAR 781
|
....*...
gi 1920237940 1732 TAQLERTL 1739
Cdd:COG4913 782 LNRAEEEL 789
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1468-1685 |
6.69e-13 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 74.52 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1468 ELSTLTSQYIR-----FISETLRRMEEEERLAEQQRAEeRERLAEVEAAlEKQRQLAEAHAQAKAQAER----EAQGLQR 1538
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREIETariaEAEAELA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1539 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqLEATERQRGGAEGEL 1618
Cdd:COG2268 248 KKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE-------LEADVRKPAEAEKQA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 1619 QALRARAeEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR 1685
Cdd:COG2268 321 AEAEAEA-EAEAIRAKGLAEAEGKRALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
320-415 |
7.05e-13 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 67.80 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 320 KEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 398
Cdd:cd21229 5 KKLMLAWLQAVLPEL---KITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1920237940 399 DVDVPQPDEKSIITYVS 415
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3200-3238 |
7.49e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 7.49e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 3200 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPELHEKL 3238
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1616-2194 |
8.47e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 8.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1616 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaEAELALRVQAEAEAAREKQRALQALEELRLQAEEA--ER 1693
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1694 RLRQAEAERARQVQVALETA---QRSAEAELQSEHASFAEKTAQLERTLKEehvavvqLREEATRRAQQQAEAERARAEA 1770
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1771 ERELERWQlKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELA---EQELEKQRQLAEGT 1847
Cdd:PRK02224 313 EARREELE-DRDEELRDRLEECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAaelESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1848 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR---AEMEVLLA------------ 1912
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqpve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1913 --SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAVRQRAEAERVLAEKLAAISEA 1988
Cdd:PRK02224 463 gsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1989 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE---------ARLAQLRKASESELERQKGLVE-- 2057
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAEln 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2058 ----DTLRQRRqveEEILALKGSFEKAAAGKAELELElgrirgTAEDTLRSKEQAEQEAARQRQlaaeeerrrreaeeRV 2133
Cdd:PRK02224 623 derrERLAEKR---ERKRELEAEFDEARIEEAREDKE------RAEEYLEQVEEKLDELREERD--------------DL 679
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2134 QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2194
Cdd:PRK02224 680 QAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1485-1987 |
8.71e-13 |
|
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: 75.37 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1485 RRMEEEERLAEQQRAEERERLAE----VEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRS 1560
Cdd:COG3096 242 RMTLEAIRVTQSDRDLFKHLITEatnyVAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1561 iQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQE 1637
Cdd:COG3096 322 -ESDLEQDYQAASdhlNLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1638 EAERLRRQVQDETQrkrqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVAL 1710
Cdd:COG3096 390 EVDSLKSQLADYQQ---------ALDVQQTR--AIQYQQAVQALEKARalcglpdLTPENAEDYLAAFRAKEQQATEEVL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1711 ETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALR---- 1786
Cdd:COG3096 459 ELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQA-----------------------WQ-TARELLRryrs 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1787 LRLQAEEVAQQKSltqaeaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETE 1866
Cdd:COG3096 507 QQALAQRLQQLRA------------------QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1867 QGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEA 1936
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLERER 640
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 1937 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1987
Cdd:COG3096 641 EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLLSEIYD 691
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
320-421 |
9.57e-13 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 67.80 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 320 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 399
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1920237940 400 -VDVPQPDEKSIITYVSSLYDAM 421
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
318-418 |
1.14e-12 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 67.41 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 397
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1920237940 398 ED-VDVPQPDEKSIITYVSSLY 418
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1539-2637 |
1.38e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 74.83 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1539 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEA--AERSRLRIEEEIRvVRLQLEATErqrggAEG 1616
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqAETELCAEAEEMR-ARLAARKQE-----LEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1617 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDetqrkrqAEAELalrvqAEAEAAREKqralqaleeLRLQAEEAERRLR 1696
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQD-------LEEQL-----DEEEAARQK---------LQLEKVTTEAKIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1697 QAEAErarqvqVALETAQRSaeaELQSEHASFAEKTAQLERTLKEEHVAVVQL-----REEATRRAQQQAEAERARAEAE 1771
Cdd:pfam01576 135 KLEED------ILLLEDQNS---KLSKERKLLEERISEFTSNLAEEEEKAKSLsklknKHEAMISDLEERLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1772 RELERWQLKAnEALRLRlqaEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1851
Cdd:pfam01576 206 LEKAKRKLEG-ESTDLQ---EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE--LQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1852 LAAEqelirlRAETEQGEQQRQLLEEELARLQRE---AAAATQKRRELEAelakvRAEMEVLLASKArAEEESRSTSEKS 1928
Cdd:pfam01576 280 LESE------RAARNKAEKQRRDLGEELEALKTEledTLDTTAAQQELRS-----KREQEVTELKKA-LEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1929 KQRLEAEAGRFRELAEE---AARLRALAEEAK--------------RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1991
Cdd:pfam01576 348 QEMRQKHTQALEELTEQleqAKRNKANLEKAKqalesenaelqaelRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1992 KTEAEIALKEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASE--SELERQKGLVEDTLrqrRQVEEE 2069
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNE-------AEGKNIKLSKDVSSLESQLQDTQEllQEETRQKLNLSTRL---RQLEDE 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2070 ILALKGSFEKAAAGKAELELELGRIRGTAEDTlrsKEQAEQEAARQRQLaaeeerrrreaeERVQKSLAAEEEAARQRka 2149
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM---KKKLEEDAGTLEAL------------EEGKKRLQRELEALTQQ-- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2150 aLEEVERLKAKVEEAR-RLRERAE-----QESARQLQLAQEAAQKR---LQAEEKA-HAFAVQQKEQELQQTLQQEQSVL 2219
Cdd:pfam01576 561 -LEEKAAAYDKLEKTKnRLQQELDdllvdLDHQRQLVSNLEKKQKKfdqMLAEEKAiSARYAEERDRAEAEAREKETRAL 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2220 ERLRSeaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAA 2299
Cdd:pfam01576 640 SLARA----------------------LEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQaadaEMEKHKQFAEQA-LR-------QKAQVEQELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQvee 2371
Cdd:pfam01576 698 KTQLE----ELEDELQATEDAkLRlevnmqaLKAQFERDLQARDEQGEE---KRRQLVKQVRELEAELEDERKQRAQ--- 767
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2372 eLFSLRVQME-ELGKLKARIEAENRAlvlrdKDSAQRLLQEEAEKMKQVAeeaarlsvaaqeaarlRQLAEEDLAQQRAL 2450
Cdd:pfam01576 768 -AVAAKKKLElDLKELEAQIDAANKG-----REEAVKQLKKLQAQMKDLQ----------------RELEEARASRDEIL 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2451 AEKMLKEKmqavqeatRLKA-EAELLQQQKELA-QEQARR-LQEDKEQMAQQLAQETQGfqKTLETERQRQLEmsaeaER 2527
Cdd:pfam01576 826 AQSKESEK--------KLKNlEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE-----AR 890
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2528 LRLRVAEMSRAQARAEEDARRFRKQAEDIgERLyRTELATQEKvmLVQTLETQRQQSDRDAERLREAIAELEHE-KDKLK 2606
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQV-EQL-TTELAAERS--TSQKSESARQQLERQNKELKAKLQEMEGTvKSKFK 966
|
1130 1140 1150
....*....|....*....|....*....|.
gi 1920237940 2607 QEAQLLQLKSEEMqtvrQEQLLQETQALQQS 2637
Cdd:pfam01576 967 SSIAALEAKIAQL----EEQLEQESRERQAA 993
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3942-3980 |
2.91e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 2.91e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 3942 LLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDTHDQL 3980
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2019-2759 |
3.25e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.47 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2019 QRRLLEEQAA---QHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 2095
Cdd:pfam02463 153 ERRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2096 GTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQES 2175
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2176 ARQLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRR 2252
Cdd:pfam02463 313 EEKLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2253 QVEEAErlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELT 2332
Cdd:pfam02463 393 KEEELE--LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2333 ALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEE 2412
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2413 AEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqralaekmlkekmqavqeaTRLKAEAELLQQQKELAQEQARRLQED 2492
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARK------------------------LRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2493 KEQMAQQLAQETQGFQKTLETERQRQLEMSaeaERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVM 2572
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2573 LVQTLETQRQQSdrdaERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCI 2652
Cdd:pfam02463 684 KAESELAKEEIL----RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2653 EQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGvrrQQEELQRLAQQQQQQEKLLAE 2732
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELE 836
|
730 740
....*....|....*....|....*..
gi 1920237940 2733 ENQRLRERLQHLEEERRAALARSEEIA 2759
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEI 863
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1829-2751 |
3.47e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 73.29 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1829 QRELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAe 1906
Cdd:pfam01576 109 EEQLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1907 MEVLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAIS 1986
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1987 EATRLktEAEIALKEKEAENERLRRlAEDEAFQRRLLEE--------------QAAQH--KADIEARLAQLRKASESELE 2050
Cdd:pfam01576 265 KIREL--EAQISELQEDLESERAAR-NKAEKQRRDLGEElealkteledtldtTAAQQelRSKREQEVTELKKALEEETR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2051 RQKGLVEDTLRQRRQVEEEilaLKGSFEKAAAGKAELE-----LELGRIRGTAEdtLRSKEQAEQEAARQRQlaaeeerr 2125
Cdd:pfam01576 342 SHEAQLQEMRQKHTQALEE---LTEQLEQAKRNKANLEkakqaLESENAELQAE--LRTLQQAKQDSEHKRK-------- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2126 rrEAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARqlqLAQEAAQKRLQaeekahafaVQQKE 2205
Cdd:pfam01576 409 --KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKDVSSLESQ---------LQDTQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2206 QELQQTLQQEQSVLERLRSEAEAARRAaeeaeaareraereaaqsRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEA 2285
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSL------------------QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2286 EQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLeetDHQKSILDEELQRLKAEVTEAArq 2365
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVSNLEKKQKKFDQMLA-- 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2366 rgqvEEELFSLRVQMEelgklKARIEAENRalvlrDKDSAQRLLQEEAEKMKQVAEEAARlsvaaqeAARLRQLAEEDLA 2445
Cdd:pfam01576 612 ----EEKAISARYAEE-----RDRAEAEAR-----EKETRALSLARALEEALEAKEELER-------TNKQLRAEMEDLV 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2446 QQRALAEKMLKE----KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLEtERQRQL-- 2519
Cdd:pfam01576 671 SSKDDVGKNVHElersKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvk 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2520 ---EMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERlyRTELATQEKVMLVQTLETQRQQSDRDAERLREAIA 2596
Cdd:pfam01576 750 qvrELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQ 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2597 ELEHEKDKLKQEAQLLQLKSEEMQTVRQE-QLLQETQALQQ---SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQA 2672
Cdd:pfam01576 828 SKESEKKLKNLEAELLQLQEDLAASERARrQAQQERDELADeiaSGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL 907
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2673 LREEQQRQQQQMQQEKQQLAAS---------------------------MEEARRRQHEA-----EEGVRRQQEELQRLA 2720
Cdd:pfam01576 908 LNDRLRKSTLQVEQLTTELAAErstsqksesarqqlerqnkelkaklqeMEGTVKSKFKSsiaalEAKIAQLEEQLEQES 987
|
970 980 990
....*....|....*....|....*....|.
gi 1920237940 2721 QQQQQQEKLLAEENQRLRERLQHLEEERRAA 2751
Cdd:pfam01576 988 RERQAANKLVRRTEKKLKEVLLQVEDERRHA 1018
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1229-2114 |
3.66e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.47 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1229 EKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfdalrdelrgaqevgerlqq 1308
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----------------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1309 rhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplgawlrDAKQRQEQIQAVPLANSQAVR 1388
Cdd:pfam02463 231 ---YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE--------KEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1389 EQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsesiIQEYVDLRTRYSE 1468
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL-----EKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1469 LSTLTSQYIRFISETLRR--MEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL---QRRMQEE 1543
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLkeEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGkltEEKEELE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1544 VARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR-IEEEIRVVRLQLEATERQRGGAEGELQALR 1622
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESkARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1623 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ-AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1701
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVrALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1702 RARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERELERWQLKA 1781
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE----GLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1782 NEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1861
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1862 RAETEQGEQQRQLLEEELARLQREAAAATQKrrELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1941
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEE--ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1942 LAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 2021
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2022 LLEEQAAQHKADIEARLAQLRKASESELERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDT 2101
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEE---RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 1920237940 2102 LRSKEQAEQEAAR 2114
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1821-2042 |
3.73e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 71.72 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1900
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1901 AKVRAE----------------MEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1963
Cdd:COG4942 100 EAQKEElaellralyrlgrqppLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1964 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeafqrRLLEEQAAQHKADIEARLAQLR 2042
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA------RLEAEAAAAAERTPAAGFAALK 252
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3531-3569 |
4.43e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.43e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 3531 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3569
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4454-4492 |
4.56e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.56e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 4454 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4492
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1160-1745 |
4.76e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.06 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1160 RECAQRITEQQKAQAEVDGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEqvrslsaiylEKLKTISLVIR 1239
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------------ELEELLAELE----------AQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1240 STQEAEEVLRAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQqpvFDALRDELRGAQEVGERLQQRHGERDvEVE 1318
Cdd:COG3096 575 EAVEQRSELRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA---LADSQEVTAAMQQLLEREREATVERD-ELA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1319 RWRERVTLLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLGAWLRDAKQrqeqiqAVPLANSQAVREQL 1391
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPARH------AIVVPDLSAVKEQL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1392 RQEKALLED---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKVQSGSESIIQEYVDL 1462
Cdd:COG3096 725 AGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEELRAERDELAEQYAKA 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1463 RTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQE 1542
Cdd:COG3096 805 SFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLKEQLQLLNKLLP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1543 EV---------ARREEVAVE---AQEQKRSIQEELQHLRQSSE--AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE 1608
Cdd:COG3096 882 QAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1609 --RQR------GGAEGEL-------QALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE 1673
Cdd:COG3096 962 evVQRrphfsyEDAVGLLgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQE 1041
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1674 -KQRALQALEELRLQAEEaERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF--AEKTAQLERTLKEEHVA 1745
Cdd:COG3096 1042 lEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLrkAERDYKQEREQVVQAKA 1115
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2344-2751 |
5.18e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2344 QKSILDEELQRLKAEVTEAARQRG---QVEEELFSLRVQMEELGKLKARIEAENRAL--------VLRDKDSAQRLLQEE 2412
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLekllqllpLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2413 AEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2492
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2493 KEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEED---------------ARRFRKQAEDIG 2557
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2558 ERLYRTELATQEkvmlvQTLETQRQQSDRDAERLREAI--AELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL- 2634
Cdd:COG4717 302 KEAEELQALPAL-----EELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALl 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2635 QQSFLSEKDSLLQRERCIEQEKAKLEQLfqdEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2714
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237940 2715 ELQRLAQQQQQQEK-----LLAEENQRLRERLQHLEEERRAA 2751
Cdd:COG4717 454 ELAELEAELEQLEEdgelaELLQELEELKAELRELAEEWAAL 495
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
320-419 |
5.48e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.05 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 320 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 395
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1920237940 396 DPEDVdVPQPDEKSIITYVSSLYD 419
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2318-2642 |
7.26e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 72.08 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2318 EQALRQKAQVEQELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSL--RVQMEELGKLK-------A 2388
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2389 RIEAENRALVLRDKDSAQRLLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2468
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2469 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARR 2548
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2549 fRKQAEDIGERLYRTELATQEKVM--------LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2620
Cdd:pfam17380 486 -RKRAEEQRRKILEKELEERKQAMieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
330 340
....*....|....*....|..
gi 1920237940 2621 TVRQEQLLQETQALQQSFLSEK 2642
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEK 586
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
761-939 |
8.28e-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: 67.86 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 761 LHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQ 840
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 841 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTATRLEDLLQDAQDEKEQLSEY 920
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 1920237940 921 RGHLSGLAKRAKAIVQLKP 939
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
188-306 |
9.89e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 64.95 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 188 KTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLsgdslprERDVIRSSRLPREKGRMR--FHKLQNVQIA 265
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKI-------KPGVVDWSRVNKPFKKLGanMKKIENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237940 266 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 306
Cdd:cd21298 75 VELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1456-1954 |
1.01e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.91 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1456 IQEYVDLRTRYSELSTLTSQYirFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqg 1535
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARES-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1536 lqrrmqeevarreevAVEAQEQKRSiqeelQHLrqsseAEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAE 1615
Cdd:COG3096 324 ---------------DLEQDYQAAS-----DHL-----NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1616 GELqalraraEEAEAQKRQAQEEAERLRRQVQDETQrkrqaeaelALRVQaeAEAAREKQRALQALEELR-------LQA 1688
Cdd:COG3096 375 EQL-------AEAEARLEAAEEEVDSLKSQLADYQQ---------ALDVQ--QTRAIQYQQAVQALEKARalcglpdLTP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1689 EEAERRLRQAEAERARQVQVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEATRRAQQQAEAERARA 1768
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQAWQTARELLRRYRSQQ 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1769 EAERELERWQLKANEA-LRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGT 1847
Cdd:COG3096 509 ALAQRLQQLRAQLAELeQRLRQQQNAERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQLEEL 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1848 AQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRRELEAE----LAKVRAEMEVLLaSKARAEEESRS 1923
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKEL-AARAPAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREATVERD 647
|
490 500 510
....*....|....*....|....*....|....*
gi 1920237940 1924 TSEKSKQRLEAEAgrfRELA----EEAARLRALAE 1954
Cdd:COG3096 648 ELAARKQALESQI---ERLSqpggAEDPRLLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4109-4147 |
1.06e-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: 1.06e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 4109 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4147
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1550-1753 |
1.10e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.18 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1550 VAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE 1629
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1630 AQKRQAQEEAERLRRQVQDET----QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEA 1700
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 1701 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1753
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3276-3314 |
1.19e-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: 1.19e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 3276 LLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKETSAAL 3314
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1517-1887 |
1.23e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 71.31 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1517 QLAEAHAQAKAQAEREAQGLQRRMQEEVARREevaveaqeqKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1589
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQE---------KEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1590 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQ-AEA 1668
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1669 EAAREKQRALQALEELRLQAEEA-ERRLRQAEAERARQVQ-VALETAQRSAEAE-LQSEHASFAEKTAQLERTLKEEHVA 1745
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMErVRLEEQERQQQVErLRQQEEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1746 VVQLREeatrraqqqaeaeraraeaereLERWQLKANEalrlRLQAEEVAQQKSLTQAEAEKQKEEAEREARRrgKAEEQ 1825
Cdd:pfam17380 490 EEQRRK----------------------ILEKELEERK----QAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEE 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 1826 AVRQrelaeQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1887
Cdd:pfam17380 542 RRKQ-----QEMEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1488-2194 |
1.42e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.41 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1488 EEEERLAEQQRAEERERLAEVEAALEKQ-----RQLAEAHAQAKAQAEREAQGLQRRMQEEVARR-------------EE 1549
Cdd:pfam12128 104 RLDDFIKANNDFVKCETVAELGRFMKNAgiqrtNLLNTREYRSIIQNDRTLLGRERVELRSLARQfalcdsesplrhiDK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1550 VAVEAQEQK------RSIQEELQHLRQSSEAEIQAKARQVEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL 1621
Cdd:pfam12128 184 IAKAMHSKEgkfrdvKSMIVAILEDDGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1622 RARAEEAEAQKRQAQEEAE----RLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQ 1697
Cdd:pfam12128 264 HFGYKSDETLIASRQEERQetsaELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1698 AEAERARQVQVALETAQRSAEAeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAerelerw 1777
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED------- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1778 qlkANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRG-KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ 1856
Cdd:pfam12128 416 ---DLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQLENFDERIERAREEQEAANAEVERLQS 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1857 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ----KRRELEAELAKVRAEMEVLLASKARAEEESRS------TSE 1926
Cdd:pfam12128 493 ELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTdldpevWDG 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1927 KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQR---AEAERVLAEKLAAISEATRLKTEAEIALKEKE 2003
Cdd:pfam12128 573 SVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSARekqAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2004 aenERLRRLAEDEAFQRRLLEEQAAQHKA-------DIEARLAQLRKASESELERQKG---------------LVEDTLR 2061
Cdd:pfam12128 653 ---LDLRRLFDEKQSEKDKKNKALAERKDsanerlnSLEAQLKQLDKKHQAWLEEQKEqkreartekqaywqvVEGALDA 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2062 QRRQVEEEILALKGSFE-------------------------KAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQR 2116
Cdd:pfam12128 730 QLALLKAAIAARRSGAKaelkaletwykrdlaslgvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRR 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2117 QLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEevERLKAKVEEARRLRE-----RAEQESARQLQLAQEAAQKRLQ 2191
Cdd:pfam12128 810 PRLATQLSNIERAISELQQQLARLIADTKLRRAKLE--MERKASEKQQVRLSEnlrglRCEMSKLATLKEDANSEQAQGS 887
|
...
gi 1920237940 2192 AEE 2194
Cdd:pfam12128 888 IGE 890
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
318-418 |
1.46e-11 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 64.28 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 397
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1920237940 398 ED-VDVPQPDEKSIITYVSSLY 418
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2306-2662 |
1.64e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2306 ADAEMEKHKQFAEQA--LRQKA-QVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE 2382
Cdd:PRK02224 344 AESLREDADDLEERAeeLREEAaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2383 LGKLKARIEAENRALVLRDKDsAQRLLQE-EAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKM 2459
Cdd:PRK02224 424 LREREAELEATLRTARERVEE-AEALLEAgKCPECGQPVEGSPHVETIEEDRERVEELEAEleDLEEEVEEVEERLERAE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2460 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSraQ 2539
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN--S 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2540 ARAEEDARrfRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERL---REAIAELEHEKDklkqEAQLLQLKS 2616
Cdd:PRK02224 580 KLAELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLaekRERKRELEAEFD----EARIEEARE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1920237940 2617 EEMQTVR-QEQLLQETQALQQsflsEKDSLLQRERCIEQEKAKLEQL 2662
Cdd:PRK02224 654 DKERAEEyLEQVEEKLDELRE----ERDDLQAEIGAVENELEELEEL 696
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1862-2178 |
2.43e-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: 70.54 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1862 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElAKVRAEMEVLLASKARAEEESRSTSEKSkqrlEAEAGRFRE 1941
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEERKR----ELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1942 LAEEAARLRALaEEAKRQRQLAEEdAVRQRAEAERV--LAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA-- 2017
Cdd:pfam17380 370 IAMEISRMREL-ERLQMERQQKNE-RVRQELEAARKvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAre 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2018 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKglvedtlRQRRQVEEEilaLKGSFEKAAAGKAELELELGRIRGT 2097
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-------RDRKRAEEQ---RRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2098 AEDTLRSKEQAEQEAARQRQlaaeeerrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2177
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE---------AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
.
gi 1920237940 2178 Q 2178
Cdd:pfam17380 589 A 589
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1658-2194 |
2.70e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 70.66 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1658 AELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE-RARQVQVALETAQRSAEAELQSEHAS--------F 1728
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppaS 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1729 AEKTAQLERTLKEEHVAVVQLREEATRRAQQ--QAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQkslTQAEAE 1806
Cdd:COG3899 792 ARAYANLGLLLLGDYEEAYEFGELALALAERlgDRRLEARALFNLGFILHWLGPLREALELLREALEAGLE---TGDAAL 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1807 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA 1886
Cdd:COG3899 869 ALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1887 AAATQKRRELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1966
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1967 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 2046
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2047 SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRR 2126
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 2127 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2194
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1140-1695 |
2.86e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1140 EACETRTVHRLRLPLDKEPARECAQRITEQQKAqaevDGLGKGV--ARLSAEAEKVLAlPEPSPAAPTLRSELELTLGKL 1217
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAeeAKKKADAAKKKA-EEAKKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1218 EQVRSLS-AIYLEKLKTISLVIRSTQEAEEVLRAhEEQLKEAQAVPATLPELEATKAALKK---LRAQAEAQQPVfdalr 1293
Cdd:PTZ00121 1360 EAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKA----- 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1294 DELRGAQEvgERLQQRHGERDVEVERWRERVTLLLERwqavlaqtdvrQRELEQLGRQLRYYREsADPLGAWLRDAKQRQ 1373
Cdd:PTZ00121 1434 DEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEE-----------AKKADEAKKKAEEAKK-ADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1374 EQIQAVPLANSQAVREQLRQEKALLEDIERHGE--KVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1451
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1452 SESIIQEYVDLR----TRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERlaeveaalEKQRQLAEAHAQAKA 1527
Cdd:PTZ00121 1576 KNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--------KKVEQLKKKEAEEKK 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1528 QAEReaqgLQRRMQEEVARREEVAVEAQEQKRSIQEelqhLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEAT 1607
Cdd:PTZ00121 1648 KAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDE--------KKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1608 ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElalrvQAEAEAAREKQRALQALEELRLQ 1687
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK-----KEEEKKAEEIRKEKEAVIEEELD 1786
|
....*...
gi 1920237940 1688 AEEAERRL 1695
Cdd:PTZ00121 1787 EEDEKRRM 1794
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2872-2910 |
3.15e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.80 E-value: 3.15e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 2872 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPELHHKL 2910
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
205-300 |
3.81e-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: 62.99 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 205 EAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsSRLPrEKGRMRfhKLQNVQIALDYLRHRQV----KLVNIR 280
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSK-----LRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGIT 92
|
90 100
....*....|....*....|
gi 1920237940 281 NDDIADGNPKLTLGLIWTII 300
Cdd:cd21223 93 AKDIVDGHREKTLALLWRII 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2301-2503 |
3.88e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 68.25 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2301 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2380
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2381 EELGK---LKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2457
Cdd:COG4942 114 YRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237940 2458 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2503
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1475-2192 |
4.99e-11 |
|
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: 69.76 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1475 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1554
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1555 QEQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1624
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1625 --AEEAEAQKRQAQEEAERLRRQVQDET-QRKRQAEAELAlRVQAEAEAAREKQRALQAleelrlQAEEAERRLRQAEAE 1701
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRIeQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1702 RARQVQvALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAeaerelerwQLKA 1781
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ---------KLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1782 NEALRLRLQAEEVAQQKSLtqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1852
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1853 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRRELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1928
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1929 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAV----RQ----------------------RAEAERVLAEK 1981
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQqienmtqlvgqhgrtagamqveKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1982 LAAISEATRLKTEAEIALKEKEAE---------------NERLRRLAEDEAFQRRLLEEQAAQHK------ADIEARLAQ 2040
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARvsdlelekvklvnagSERLRAVKDIKQERDQLLNEVKTSRNelnslsEDYEVLKRN 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2041 LRKASE------SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG-KAELELELGRIrgtaeDTLRSK----EQAE 2109
Cdd:pfam15921 683 FRNKSEemetttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGmQKQITAKRGQI-----DALQSKiqflEEAM 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2110 QEAARQRQLAAEEERRRREAEERV---QKSLAAEEEAARQRKAALEE--------VERLKAKVEEARRLRERAEQESARq 2178
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEkvanmevaLDKASLQFAECQDIIQRQEQESVR- 836
|
810
....*....|....
gi 1920237940 2179 LQLAQEAAQKRLQA 2192
Cdd:pfam15921 837 LKLQHTLDVKELQG 850
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1502-2027 |
5.72e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.50 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1502 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1581
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1582 QVEAAERSRLRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDETQRKRQAEA 1658
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1659 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1738
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1739 LKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARR 1818
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1819 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA 1898
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1899 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1978
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920237940 1979 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQA 2027
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1824-2198 |
6.99e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1901
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1902 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVrQRAEAERVLAEK 1981
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1982 LAAISEATRLKTEAEIAL----------------KEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKAS 2045
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2046 ESELERQKGLVE-DTLRQRRQVEEEILALKGSFEKAAAGKAElelelgRIRGTAEDTLRSKEQAEQEAARQRQLAAEEER 2124
Cdd:COG4717 344 DRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2125 RRREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2198
Cdd:COG4717 418 LEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2398-2754 |
7.18e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2398 VLRDKDSAQRLLQEEA---EKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL---AEKMlkEKMQAVQEATRlKA 2470
Cdd:TIGR02168 149 IIEAKPEERRAIFEEAagiSKYKERRKETERKLERTRENlDRLEDILNELERQLKSLerqAEKA--ERYKELKAELR-EL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2471 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQET---QGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2547
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2548 RFRKQAEDIGERLYRtelatqekvmlvqtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL 2627
Cdd:TIGR02168 306 ILRERLANLERQLEE--------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2628 LQEtQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfqdeVAKAQALreeqQRQQQQMQQEKQQLAASMEEARRRQHEAE- 2706
Cdd:TIGR02168 372 SRL-EELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERL----EDRRERLQQEIEELLKKLEEAELKELQAEl 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237940 2707 EGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2754
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1555-1744 |
1.03e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 67.14 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1555 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL--EATERQRGGAEGELQALRARAEEAEAQK 1632
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQkkQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1633 RQAQEEAERLRRQV-QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1711
Cdd:PRK09510 147 AKAEAEAKRAAAAAkKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|...
gi 1920237940 1712 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHV 1744
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2398-2753 |
1.13e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2398 VLRDKDSAQRLLQEEAEKMKQ-----VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQAVQEA-TRLK 2469
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERykelkAELRELELALLVLRLEELREELEELQEELKEAEEELeeLTAELQELEEKlEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2470 AEAELLQQQKELAQE---QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2546
Cdd:TIGR02168 274 LEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2547 RRFRKQAEdigerlyrtelatqEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKSE-EMQTVRQE 2625
Cdd:TIGR02168 354 ESLEAELE--------------ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARlERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2626 QLLQETQALQQSFLSEKDSLLQRErcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHeA 2705
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAE--LEELEEELEEL-QEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-S 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237940 2706 EEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLqHLEEERRAALA 2753
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVDEGYEAAIE 540
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
320-420 |
1.15e-10 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 61.60 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 320 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 399
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1920237940 400 VdVPQPDEKSIITYVSSLYDA 420
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1488-1988 |
1.32e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 68.35 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1488 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-----EAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1562
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRhgnppASARAYANLGLLLLGDYEEAYEFGELALALA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1563 EELQHLRQSSEAEIqAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1642
Cdd:COG3899 821 ERLGDRRLEARALF-NLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1643 RRQVQDETQRKRQAEAELALRVQAEAEAAREkqRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1722
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAA--LALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1723 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQ 1802
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1803 AEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1882
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1883 QREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1962
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*.
gi 1920237940 1963 AEEDAVRQRAEAERVLAEKLAAISEA 1988
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRLL 1243
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
181-297 |
1.48e-10 |
|
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: 61.67 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 181 ERDRvQKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSgdslPRERDVIRSSRLPREKGRMRFHKLQ 260
Cdd:cd21300 4 EGER-EARVFTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDKVI----PGSVNWKKVNKAPASAEISRFKAVE 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 261 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 297
Cdd:cd21300 72 NTNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1824-2570 |
1.85e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1903
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1904 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1983
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1984 AISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRlleeqaaqhKADIEARLAQLRKAseseLERQKGLVEDTLR-- 2061
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELE--AEIASLERR---------KSNIPARLLALRDA----LAEALGLDEAELPfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2062 -QRRQVEEEILALKGSFEKAaagkaelelelgrIRGTAEDTLRSKEQAEQ--EAARQRQLAAEeerrrreaeerVQKSLA 2138
Cdd:COG4913 464 gELIEVRPEEERWRGAIERV-------------LGGFALTLLVPPEHYAAalRWVNRLHLRGR-----------LVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2139 AEEEAARQRKAALEE--VERLKAKVEEARrlrERAEQESARQLQLAQEAAQKRLQAEEKA--------HAFAVQQKEQEL 2208
Cdd:COG4913 520 RTGLPDPERPRLDPDslAGKLDFKPHPFR---AWLEAELGRRFDYVCVDSPEELRRHPRAitragqvkGNGTRHEKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2209 QQTLQqeqSVLerlrseaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEaeqe 2288
Cdd:COG4913 597 RIRSR---YVL---------------------------GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDA---- 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2289 aarraqaeqaaLRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQ 2368
Cdd:COG4913 643 -----------LQERREALQRLAEY-SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2369 VEEELFSLRvqmEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2448
Cdd:COG4913 711 LKGEIGRLE---KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2449 ALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLeterqrQLEMSAEAER 2527
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVADL------LSKLRRAIRE 861
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2528 LRLRVAEMSRA----------------QARAEEDARRFRKQAEDIGERLYRTELATQEK 2570
Cdd:COG4913 862 IKERIDPLNDSlkripfgpgrylrleaRPRPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1160-1748 |
1.94e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 67.67 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1160 RECAQRITEQQKAQaevdglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELEltlgkleqvrslsaiylEKLKTISLVI 1238
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELE-----------------ARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1239 RSTQEAEEVLRAHEEQLK-EAQAVPATLPELEATKAALKKLRAQAEaqqpvfdalrDELRGAQEVGERLQQrHGERDVEV 1317
Cdd:PRK04863 575 SEARERRMALRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSG----------EEFEDSQDVTEYMQQ-LLEREREL 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1318 ERWRERVTlllERWQAVLAQTD-VRQRELEQLGRQLRYyresADPLGAWL----------RDAKQRQ----EQIQAVPLA 1382
Cdd:PRK04863 644 TVERDELA---ARKQALDEEIErLSQPGGSEDPRLNAL----AERFGGVLlseiyddvslEDAPYFSalygPARHAIVVP 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1383 NSQAVREQLRQEKALLEDI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK----VQSG 1451
Cdd:PRK04863 717 DLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRAE 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1452 SESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1531
Cdd:PRK04863 795 REELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAD--PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1532 EAQGLQR-----------RMQEEVARREEVAVEAQEQKRSIQ---------EELQHLRQSSEAEIQAKARQVEAAE---- 1587
Cdd:PRK04863 873 GLSALNRllprlnlladeTLADRVEEIREQLDEAEEAKRFVQqhgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqr 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1588 --RSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDETQRKRQAEAELALR 1663
Cdd:PRK04863 953 daKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASLKSS 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1664 VQAEAEAAREKQRALQAL---------EELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQsehaSFAEKTAQ 1734
Cdd:PRK04863 1029 YDAKRQMLQELKQELQDLgvpadsgaeERARARRDELHARLSANRSRRN-----QLEKQLTFCEAEMD----NLTKKLRK 1099
|
650
....*....|....
gi 1920237940 1735 LERTLKEEHVAVVQ 1748
Cdd:PRK04863 1100 LERDYHEMREQVVN 1113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1350-2020 |
2.18e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1350 RQLRYYRESADPLGAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDY---- 1425
Cdd:PRK03918 111 SSVREWVERLIPYHVFLNAIYIRQGEIDA--ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikrt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1426 ---ELQLVTYKAQLEPVASPAKK-----PKVQSGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQ 1497
Cdd:PRK03918 189 eniEELIKEKEKELEEVLREINEisselPELREELEKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEER 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1498 RAEERERLAEVE---AALEKQRQLAEAHAQAK-----------------AQAEREAQGLQRRMQEEVARREEVAvEAQEQ 1557
Cdd:PRK03918 268 IEELKKEIEELEekvKELKELKEKAEEYIKLSefyeeyldelreiekrlSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1558 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1637
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1638 EAERLRRQVQDETQRKRQAEAELALRVQAEAEAarEKQRALQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQ- 1714
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEq 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1715 -RSAEAELQSEHASFAEKTAQLERTLKEEhvaVVQLREEATRRAQqqaeaeraraeaerelerwQLKANEALRLRLQAEE 1793
Cdd:PRK03918 505 lKELEEKLKKYNLEELEKKAEEYEKLKEK---LIKLKGEIKSLKK-------------------ELEKLEELKKKLAELE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1794 VAQQKsltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRaeteQGEQQRQ 1873
Cdd:PRK03918 563 KKLDE----------------------LEEELAELLKELEELGFESVEEL-EERLKELEPFYNEYLELK----DAEKELE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1874 LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLasKARAEEESRSTSEKskqrleaeagrFRELAEEAARLRALA 1953
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREE-----------YLELSRELAGLRAEL 682
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1954 EEAKRQRQLAEEDAvrqraeaeRVLAEKLAAISEATRLKTEAEIALKEKEAENERLRR---LAEDEAFQR 2020
Cdd:PRK03918 683 EELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKKykaLLKERALSK 744
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1678-2173 |
2.31e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1678 LQALEELRLQAEEAE---RRLRQAEAERARQVQVALE-TAQRSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEA 1753
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLKAQIEeKEEKDLHERLNGLESELAELDEEIER-YEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1754 TRRAQQQAEAERARAEAERELERWQLKANEALRLRLQ-AEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1832
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1833 AEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1912
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1913 SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE----------------DAVRQRAEAER 1976
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1977 VLAEKLAAIsEATRLKTEAEI----ALKEKEAENERLRRlaedeafQRRLLEEQAAQHKADIEA---RLAQLRKAS---E 2046
Cdd:PRK02224 479 ELEAELEDL-EEEVEEVEERLeraeDLVEAEDRIERLEE-------RREDLEELIAERRETIEEkreRAEELRERAaelE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2047 SELERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELElELGRIRgtaeDTLRSKEQAEQEAARQRQLAAEEERRR 2126
Cdd:PRK02224 551 AEAEEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIR----TLLAAIADAEDEIERLREKREALAELN 622
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920237940 2127 REAEERVQkslaaeeeAARQRKAALEEvERLKAKVEEARRLRERAEQ 2173
Cdd:PRK02224 623 DERRERLA--------EKRERKRELEA-EFDEARIEEAREDKERAEE 660
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1246-2065 |
2.54e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 67.29 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1246 EVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpvfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERvt 1325
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1326 llLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReQLRQEKALLE----DI 1401
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1402 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQY-- 1476
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLqq 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1477 IRFISETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1549
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1550 VAVEAQEQkRSIQEELQHLRQSSEAE----------IQAKARQVEAAERSRLRIEEEIRVVRLQLEATErQRGGAEGE-L 1618
Cdd:PRK04863 598 LAARAPAW-LAAQDALARLREQSGEEfedsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSEDPrL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1619 QALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDET-------------QRKRQA-----EA 1658
Cdd:PRK04863 676 NALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDSFDDSvfsveEL 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1659 ELALRVQ-AEAE--------------AAREKQralqaLEELRLQAEEAERRLRQAEAERaRQVQVALETAQR-------- 1715
Cdd:PRK04863 756 EKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAFSRfigshlav 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1716 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVA 1795
Cdd:PRK04863 830 AFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEA 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1796 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--------------LAEGTAQQRLAAEQEL-IR 1860
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahFSYEDAAEMLAKNSDLnEK 989
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1861 LRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRRELEAELAK--VRAEMEVLLASKARAEE----- 1919
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGAEERARARRDElharl 1069
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1920 ----ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAVRQRAEAERVLAEKLAAISeATRL 1991
Cdd:PRK04863 1070 sanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHRRELAYLS-ADEL 1147
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1992 KTEAEI---ALKEKEAENERLR---RLAEDEAFQ----------RRLLEEQAAQhkaDIeARLAQLRKASEsELERQKGL 2055
Cdd:PRK04863 1148 RSMSDKalgALRLAVADNEHLRdvlRLSEDPKRPerkvqfyiavYQHLRERIRQ---DI-IRTDDPVEAIE-QMEIELSR 1222
|
970
....*....|
gi 1920237940 2056 VEDTLRQRRQ 2065
Cdd:PRK04863 1223 LTEELTSREQ 1232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1835-2196 |
2.88e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1835 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR--EAAAATQKRRELEAELAKVRAEMEvlla 1912
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1913 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLK 1992
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1993 TEAEIALKEKEAENERLRRL---------------AEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVE 2057
Cdd:COG4717 229 LEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2058 DTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERrrreaeerVQKSL 2137
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAG 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2138 AAEEEAARQRKAALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQEAAQKRLQAEEKA 2196
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1093-1742 |
3.05e-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: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1093 DRLQAEREYgscSRHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRITEQQKA 1172
Cdd:TIGR02169 201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1173 QAEVDGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKL--------KTISLVIRS 1240
Cdd:TIGR02169 257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELedaeerlaKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1241 TQEAEEVLRAHEEQLKEAQAVPAtlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGE-------- 1312
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkreldrl 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1313 ------RDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ--------- 1377
Cdd:TIGR02169 412 qeelqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEkelsklqre 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1378 -----AVPLANSQAVREQLRQEKALLEDI--------------ERHGEKVE-------------------ECQRFAKQY- 1418
Cdd:TIGR02169 492 laeaeAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgERYATAIEvaagnrlnnvvveddavakEAIELLKRRk 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1419 --------INAIK---------------DYELQLVTYKAQLEPVASPAKKPKV-----QSGSESIIQ-----------EY 1459
Cdd:TIGR02169 572 agratflpLNKMRderrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLvvediEAARRLMGKyrmvtlegelfEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1460 VDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRR 1539
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1540 MQEEVARREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAAERSRLRIE-----EEIRVVRLQLEATERQRGGA 1614
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1615 EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK---RQAEAELALRVQAEAEAAREKQRALQALEE----LRLQ 1687
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLNGKKEELEEELEELEAALRDLESrlgdLKKE 890
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1688 AEEAERRLRQAEaERARQVQVALETAqRSAEAELQSEHASFAEKTAQLERTLKEE 1742
Cdd:TIGR02169 891 RDELEAQLRELE-RKIEELEAQIEKK-RKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1242-1693 |
3.10e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1242 QEAEEVLRAHEEQLK--EAQAVPATLPELEATKAALKKLRAQAEAQQPVFDAlrDELRGAQEVGERLQQRHGErdvEVER 1319
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEELKKAEEKKKAE---EAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1320 WRERVTLLLERWQavlaqtDVRQRELEQLGRQLRYYRESADPLGAWLRdaKQRQEQIQAvplansqavrEQLRQEKALLE 1399
Cdd:PTZ00121 1572 AEEDKNMALRKAE------EAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKA----------EELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1400 DIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESIIQEYVDLRtRYSELSTLTSQYIRF 1479
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK-KAAEALKKEAEEAKK 1703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1480 ISETLRRMEEEERLAEQQRAEERERLAEVEaalekqrqlaeahaQAKAQAEREaqglqRRMQEEVARREEVAVEAQEQKR 1559
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAE--------------EAKKEAEED-----KKKAEEAKKDEEEKKKIAHLKK 1764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1560 SIQEELQHLRQSSEAEIQAKARqvEAAERSRLRIEEEIRVVRLQLEATerQRGGAEGELQALRARAEEAEAQKRQAqEEA 1639
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELD--EEDEKRRMEVDKKIKDIFDNFANI--IEGGKEGNLVINDSKEMEDSAIKEVA-DSK 1839
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1640 ERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRaLQALEELRLQAEEAER 1693
Cdd:PTZ00121 1840 NMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDL-KEDDEEEIEEADEIEK 1892
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1913-2184 |
5.34e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 65.74 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1913 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARlralAEEAKRQRQLAEEDAVrqrAEAERVLAEKLAAISEATRL 1991
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREAR----HKKAAEARAAKDKDAV---AAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1992 KTEAEIALKEKEAEnERLRRLAEDEAFQRRLLEEQAAQHKADIEARL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 2069
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2070 ILALKGSFEKAAAGKAELELELgrirgTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2149
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQV-----AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237940 2150 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2184
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2411-2832 |
5.62e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2411 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2487
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2488 RLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQ-ARAEEDARRF---RKQAEDIGERLYRT 2563
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdAKKAEAVKKAeeaKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2564 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQllqlKSEEMQTVrqEQLLQETQALQQSFLSEKD 2643
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKA--DEAKKKAEEAKKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2644 SLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME-----------EARRRQHEAE---EGV 2709
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadaakkkaEEKKKADEAKkkaEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2710 RRQQEELQRLAQQQQQQEKLL--AEENQRLRERLQHLEEERRAalarseEIAPSRAAAARALPNGQDAADGPAAAAEPEH 2787
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKA------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1920237940 2788 AFDGLRRKVPAQRLQEVGVLSAEELQQLAQGRTTVAELAQREDVR 2832
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1387-1977 |
6.88e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1387 VREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDlrtRY 1466
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE---EY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1467 SELSTLTSQYIrfisETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLaeahaqakaqaeREAQGLQRRMQEEVAR 1546
Cdd:PRK03918 296 IKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELE---EKEERL------------EELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1547 REEvAVEAQEQKRSIQEELQHLRQS-SEAEIQAKARQVEAAERSRLRIEEEIRVV---RLQLEATERQRGGAEGELQALR 1622
Cdd:PRK03918 357 LEE-RHELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1623 ARA---------EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaEAEAAREKQRALQALEELRLQAEEAER 1693
Cdd:PRK03918 436 GKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKESELIKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1694 RLRQAEAERarqvqvaLETAQRSAEaELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERE 1773
Cdd:PRK03918 511 KLKKYNLEE-------LEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1774 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLA 1853
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1854 AEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlaSKARAEEESrstSEKSKQRLE 1933
Cdd:PRK03918 657 SEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER--EKAKKELEK---LEKALERVE 724
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1934 AEAGRFRELAEEAARlRALAEEAKRQRQLAEE------DAVRQRAEAERV 1977
Cdd:PRK03918 725 ELREKVKKYKALLKE-RALSKVGEIASEIFEEltegkySGVRVKAEENKV 773
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2300-2758 |
8.38e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 65.76 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILdeelqRLKAEVTEAARQRGQVEEELFSLRVQ 2379
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2380 MEELGKLKARIEA--ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---RLRQLAEE---DLAQQRALA 2451
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2452 EKMLKEKMQAVQEATRLKAEAELlQQQKELAQEQARRLQEDKEQMAQQLAQETQ-----------GFQKTLETERQRQ-- 2518
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihlqeSAQSLKEREQQLQtk 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2519 ---LEMSAEAERLRLRVAEMSRAQARAEEDARRF----RKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERL 2591
Cdd:TIGR00618 479 eqiHLQETRKKAVVLARLLELQEEPCPLCGSCIHpnpaRQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2592 REAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQRERCIE---------QEKAKLEQL 2662
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLrklqpeqdlQDVRLHLQQ 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2663 FQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEAR---------------------------------RRQHEAEEGV 2709
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmqsekeqltywkemlaqcqtllRELETHIEEY 716
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920237940 2710 RRQQEELQRLAQQQQQQeklLAEENQRLRERLQHLEEERRAALARSEEI 2758
Cdd:TIGR00618 717 DREFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVLKARTEA 762
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1239-1435 |
8.60e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 61.69 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1239 RSTQEAEEVLRAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVe 1318
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1319 rwRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLRDAKQRQEQIQavPLANSQAVREQLRQEKALL 1398
Cdd:cd00176 78 --QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELE 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237940 1399 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1435
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1863-2452 |
1.09e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1863 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAG--- 1937
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRele 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1938 --------RFRELAEEAARLRALAEEAKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKEAENERL 2009
Cdd:PRK03918 266 erieelkkEIEELEEKVKELKELKEKAEEYIKLSEF--YEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2010 RRLAEDEAFQRRLLEEQAAQHKA--DIEARLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEILAL---KGSFEKA 2080
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKItarIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2081 AAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLaaeeerrrrEAEERVQKSLAAEEEAARQRKAALEEVERLKAK 2160
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT---------AELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2161 VEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAeeaeaa 2239
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE------ 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2240 reraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2319
Cdd:PRK03918 563 ------------KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2320 ALRQKAQVEQELTALRLQLEETdhQKSILDEELQRLKAEVTEaarqrgqVEEELFSLRVQMEELGKLKARIEAEnralvL 2399
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKT-----L 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 2400 RDkdsaqrlLQEEAEKMKQVAEEAARLSVAAQEAARLRQ--LAEEDLAQQRALAE 2452
Cdd:PRK03918 697 EK-------LKEELEEREKAKKELEKLEKALERVEELREkvKKYKALLKERALSK 744
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1494-1692 |
1.10e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1494 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARReevavEAQEQKrsiQEELQHLRQSS 1572
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQ-----AALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1573 EAEIQAKARQVEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDETQR 1652
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237940 1653 KRQAEAELAL-RVQAEAEAAREKQRALQALEELRLQAEEAE 1692
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1840-2054 |
1.25e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1840 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEE 1919
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1920 ESRSTSEKSKQRLEA--EAGRFRELA--------EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEAT 1989
Cdd:COG4942 98 ELEAQKEELAELLRAlyRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1990 RLKTEAEIALKE----KEAENERLRRLAEDEAFQRRLLEEQAAQhKADIEARLAQLRKASESELERQKG 2054
Cdd:COG4942 178 ALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERTPA 245
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
187-300 |
1.40e-09 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 58.35 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 187 KKTFTKWVNKHL-----IKHWRAEAQRHiSDLYEDLRDGHNLISLLEVLSGDSLPrERdvirssRLPREKGRMRFHKLQN 261
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDG-DDLFEALRDGVLLCKLINKIVPGTID-ER------KLNKKKPKNIFEATEN 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237940 262 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 300
Cdd:cd21217 75 LNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1655-2022 |
1.47e-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: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1655 QAEAELALRVQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQvqvaletaqrsaeAELQSEHASFAEktaq 1734
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEK---AREVERRRKLEEAEKARQ-------------AEMDRQAAIYAE---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1735 lertlkEEHVAVVQLREeatrraqqqaeaeraraeaereLERWQLKANEALRLRLQAEEVAQQksLTQAEAEKQKEEAER 1814
Cdd:pfam17380 339 ------QERMAMERERE----------------------LERIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1815 EARRRGKAEEQAVRQRELAEQE-----LEKQRQLAEGTAQQRLAAEQELIRLraETEQGEQQRQLLEEELARLQReaaaa 1889
Cdd:pfam17380 389 QKNERVRQELEAARKVKILEEErqrkiQQQKVEMEQIRAEQEEARQREVRRL--EEERAREMERVRLEEQERQQQ----- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1890 TQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAvR 1969
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER-R 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1970 QRAEAER---VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRL 2022
Cdd:pfam17380 536 REAEEERrkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1636-2117 |
1.57e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1636 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQR 1715
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1716 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREeatrraqqqaeaeraraeaerelerwqlKANEALRLRLQAEEVA 1795
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEE----------------------------LEAELAELQEELEELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1796 QQKSLTQAeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1875
Cdd:COG4717 184 EQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1876 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEE 1955
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1956 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKAD 2033
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2034 IEARLAQLRKASESELERQKGLVEDTLRQR-RQVEEEILALKGSFEKAAAGKAELELELGRIRGtaEDTLRSKEQAEQEA 2112
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEEL 481
|
....*
gi 1920237940 2113 ARQRQ 2117
Cdd:COG4717 482 KAELR 486
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1342-1720 |
2.09e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 64.59 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1342 QRELEQLGRQLRYYRESADplgawlrDAKQRQEQIQA-VPLANSQAvREQLRQekaLLEDIERHGEKVEECQRFAKQYIN 1420
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKlLPQANLLA-DETLAD---RLEELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1421 AIkdyelqlvtykAQLEPVASPAKKPKVQSgsESIIQEYVDLRTRYSELStltsQYIRFISETLRRM------EEEERLA 1494
Cdd:COG3096 918 AL-----------AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRLK----QQIFALSEVVQRRphfsyeDAVGLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1495 EQQRAEE--RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEevarreevaveAQEQKRSIQEELQHLrqss 1572
Cdd:COG3096 981 ENSDLNEklRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL---- 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1573 eaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQ 1645
Cdd:COG3096 1046 --GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRL 1123
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1646 VQDETQRKRQAEAELalrvqaeaeaarekqrALQALEELRLQAEEAERRLRQAEAERArQVQVALETAQRSAEAE 1720
Cdd:COG3096 1124 ARDNDVERRLHRREL----------------AYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEDPRRPE 1181
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1832-2063 |
2.23e-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: 62.56 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1832 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAelakvraemevll 1911
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1912 askARAEEESRSTSEKSKQRLEAEAGRfrelAEEAARLRALAEEAKRQrqlAEEDAVRQRAEAervlAEKLAaisEATRL 1991
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1992 KTEAEiALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE----ARLAQLRKASESELERQKGLVEDTLRQR 2063
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1519-1742 |
2.90e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1519 AEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEE 1595
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1596 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1675
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1676 RALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQSEHASFAEKTAQLERTLKEE 1742
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2307-2757 |
3.10e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.83 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2307 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKaevtEAARQRGQVEEELFSLRVQMEELGKL 2386
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2387 KARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLSVAAQEAARLRQLA------EEDLAQQRALAEKMLKEKM 2459
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2460 QAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLaqetQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQ 2539
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2540 ARAEEDARRFRKQAEDIGER----------LYRTELATQEKVMLVQTLETQRQQSDR-----DAERLREAIAELEHEKDK 2604
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTaqceklekihLQESAQSLKEREQQLQTKEQIHLQETRkkavvLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2605 LKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQM 2684
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2685 QQEKQQLAASMEEARRR------QHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2757
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEdmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2397-2748 |
3.12e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.60 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2397 LVLRDKDSAQRLLQEEAEKM-----KQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaE 2471
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqerlRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------Q 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2472 AELLQQQKELAQEQARRL----QEDKEQMAQQLAQETQGFQKTLETERQR-QLEMSAEAERLRLRVAEMSRAQARAEEDA 2546
Cdd:pfam17380 333 AAIYAEQERMAMERERELerirQEERKRELERIRQEEIAMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2547 RRFRKQAEDIGERLYRTELATQEKVmlvQTLETQRQqsdRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQ 2626
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREV---RRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2627 LLQETQalqqsflsekdsllqRERCIEQEKAKLEQLFQDEVAKAQALREEqqrqqqqmqqekqqlaasMEEarRRQHEAE 2706
Cdd:pfam17380 487 KRAEEQ---------------RRKILEKELEERKQAMIEEERKRKLLEKE------------------MEE--RQKAIYE 531
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237940 2707 EGVRRQQEELQRlaqqqqqqEKLLAEENQRLRERLQHLEEER 2748
Cdd:pfam17380 532 EERRREAEEERR--------KQQEMEERRRIQEQMRKATEER 565
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
318-420 |
3.22e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.77 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 318 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 396
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1920237940 397 PEDVDVPQPDEKSIITYVSSLYDA 420
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1510-1734 |
3.23e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.52 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1510 AALEKQRQLAEAHAQAKAQAEREAQGLQRrmQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAK---ARQVEAA 1586
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKqaaLKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1587 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDETQRKRQAEAELALRVQ 1665
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1666 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1734
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1963-2496 |
3.70e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1963 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 2042
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2043 KASESELERQKGLVEDT--LRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAA 2120
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2121 EEERrrreaeerVQKSLAAEEEAArqrkaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfA 2200
Cdd:PRK03918 346 KLKE--------LEKRLEELEERH-------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-K 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2201 VQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEReaaqsRRQVEEAERLKQSAEEQAQAQAQAQAAAEK 2280
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELL-----EEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2281 LRKEAEQEAARraqaeqaaLRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA--- 2357
Cdd:PRK03918 485 LEKVLKKESEL--------IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkk 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2358 EVTEAARQRGQVEEELFSLRVQMEELG---------KLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLS 2427
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGfesveeleeRLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfEELA 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2428 VAAQEAARLR-QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2496
Cdd:PRK03918 637 ETEKRLEELRkELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1256-1677 |
3.80e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.22 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1256 KEAQAVPATLPELEA-----------------TKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERdVEVE 1318
Cdd:pfam17380 221 KEVQGMPHTLAPYEKmerrkesfnlaedvttmTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1319 RWR---ERVTLLLERWQAVLAQTDVRQRELEqlgRQLRYYRESAdplgawlRDAKQRQEQIQAVPLANSQAVREQLRQEK 1395
Cdd:pfam17380 300 RLRqekEEKAREVERRRKLEEAEKARQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEERKRELERIRQEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1396 ALLEDierhgEKVEECQRFakqyinaikdyelqlvtykaQLEPvaspakkpkvQSGSESIIQEYVDLRtrysELSTLTSQ 1475
Cdd:pfam17380 370 IAMEI-----SRMRELERL--------------------QMER----------QQKNERVRQELEAAR----KVKILEEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1476 YIRFISETLRRMEEEERLAEQQRAEERERLAEveaalEKQRQLAEAHAQakaQAEREAQGLQRRMQEEVARREEVAVEAQ 1555
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEE-----ERAREMERVRLE---EQERQQQVERLRQQEEERKRKKLELEKE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1556 EQKRSIQEELQhlRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleatERQRGGAEGElqalRARAEEAEAQKRQA 1635
Cdd:pfam17380 483 KRDRKRAEEQR--RKILEKELEERKQAMIEEERKRKLLEKEME---------ERQKAIYEEE----RRREAEEERRKQQE 547
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237940 1636 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRA 1677
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4530-4568 |
4.35e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.64 E-value: 4.35e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 4530 FLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTAQKL 4568
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
313-415 |
4.50e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 57.10 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 313 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 391
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1920237940 392 TRLLDPEDVDVPQPDEKSIITYVS 415
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1238-2175 |
4.54e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.43 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1238 IRSTQEAEEVLRAHEEQLKEAQAvpatlpeleatkaALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQ--RHGERdv 1315
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQY-------------RLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1316 eVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReqlrqek 1395
Cdd:COG3096 349 -IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1396 ALledierhgEKVEECQRFAKQYINAIKDYelqLVTYKAQLEpvaspakkpkvqsgseSIIQEYVDLRTRYSELSTLTSQ 1475
Cdd:COG3096 421 AL--------EKARALCGLPDLTPENAEDY---LAAFRAKEQ----------------QATEEVLELEQKLSVADAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1476 YIRFIsETLRRMEEE-ERLAEQQRAEERER-------LAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARR 1547
Cdd:COG3096 474 FEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1548 EEVAVEAQEQKRSIQEELQHLRQSSEAEIQakarqveaaersrlrieeeirvvrlqleaTERQRGGAEGELQALRARAEE 1627
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSE-----------------------------LRQQLEQLRARIKELAARAPA 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1628 AeaqkRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAeeaeRRLRQAE-AERARQV 1706
Cdd:COG3096 604 W----LAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQI----ERLSQPGgAEDPRLL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1707 Q----------------VALETAQR-------SAEAELQSEHASFAEKTAQLERTLkeEHVAVVQLREEATRRAQQQAEA 1763
Cdd:COG3096 676 AlaerlggvllseiyddVTLEDAPYfsalygpARHAIVVPDLSAVKEQLAGLEDCP--EDLYLIEGDPDSFDDSVFDAEE 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1764 ERARAEAERELERWQL-----------KANE--ALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQR 1830
Cdd:COG3096 754 LEDAVVVKLSDRQWRYsrfpevplfgrAAREkrLEELRAERDELAEQYA------------------------KASFDVQ 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1831 ELaeQELEKQ-RQLAEGTAQQRLAAEQElirlrAETEQGEQQRQLLEEELARL----QREAAAATQKRRELEAeLAKVRA 1905
Cdd:COG3096 810 KL--QRLHQAfSQFVGGHLAVAFAPDPE-----AELAALRQRRSELERELAQHraqeQQLRQQLDQLKEQLQL-LNKLLP 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1906 EMEVL----LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAKRQRQL---AEEDAVRQRAEAER 1976
Cdd:COG3096 882 QANLLadetLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpEQFEQLQADYLqakEQQRRLKQQIFALS 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1977 VLAEKLAAISEAtrlktEAEIALKEKEAENERLR---RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 2053
Cdd:COG3096 962 EVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2054 GLvedtlrQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG--TAEDTLRSKEQAEQEAARQRqlaaeeerrrreaEE 2131
Cdd:COG3096 1037 EL------EQELEELGVQADAEAEERARIRRDELHEELSQNRSrrSQLEKQLTRCEAEMDSLQKR-------------LR 1097
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1920237940 2132 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL--RERAEQES 2175
Cdd:COG3096 1098 KAERDYKQEREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSA 1143
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1484-1704 |
5.14e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1484 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1563
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1564 ---ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1640
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1641 RLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1704
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4452-4489 |
5.71e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 5.71e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1920237940 4452 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4489
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1490-1704 |
5.99e-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: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1490 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiQEELQHLR 1569
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQK-QAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1570 QSSEAEIQAKA-RQVEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE----AERLRR 1644
Cdd:TIGR02794 128 QAAEAKAKAEAeAERKAKEEAAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKA 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1645 QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1704
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2300-2756 |
8.58e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2374
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2375 SLRVQMEELG-----KLKARIEAENRALVLRDKDSAQrlLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2448
Cdd:COG4913 327 ELEAQIRGNGgdrleQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2449 ALAEKMLKEKMQAVQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM------------------------ 2496
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2497 ---AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyRTELATQEKVML 2573
Cdd:COG4913 485 ggfALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWL-EAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2574 VQTLE-------------------TQRQQSDRDAERL--------REAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQ-- 2624
Cdd:COG4913 564 VDSPEelrrhpraitragqvkgngTRHEKDDRRRIRSryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDal 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2625 EQLLQETQALQQSFLSEKDsLLQRERCIEQEKAKLEQL--FQDEVAKAQALREEqqrqqqqmqqekqqLAASMEEARRRQ 2702
Cdd:COG4913 644 QERREALQRLAEYSWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEE--------------LEAELEELEEEL 708
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 2703 HEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSE 2756
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1633-2153 |
1.02e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1633 RQAQEEAERLRRQVQD----ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARqvqv 1708
Cdd:COG4913 238 ERAHEALEDAREQIELlepiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1709 aLETAQRSAEAELQSEHASFAEKTAQLERTLKEEhvavvqlreeatrraqqqaeaeraraeaereLERWQLKANEALRLR 1788
Cdd:COG4913 314 -LEARLDALREELDELEAQIRGNGGDRLEQLERE-------------------------------IERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1789 LQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1868
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1869 EQQRQLLEEELARLQREAAAATQ-KRRELE--AELAKVRAE-------MEVLLASKAR---------------------- 1916
Cdd:COG4913 432 ERRKSNIPARLLALRDALAEALGlDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrlhlr 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1917 ------------AEEESRSTSEKS-KQRLEAEAGRFR-----ELAEEAARLRALAEEA-----------------KRQRQ 1961
Cdd:COG4913 512 grlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgnGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1962 LAEEDAVRQR----AEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEE-----QAAQHKA 2032
Cdd:COG4913 592 KDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvaSAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2033 DIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRirgtAEDTLRSKEQAEQEA 2112
Cdd:COG4913 672 ELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE----LQDRLEAAEDLARLE 746
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1920237940 2113 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2153
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
313-420 |
1.36e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 313 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 391
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1920237940 392 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 420
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
665-854 |
1.38e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 58.23 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 665 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQLSPATRGAY---RDCLGRLD 741
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 742 LQYAKLLSSSKARLRSLE---SLHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEI 818
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237940 819 QSTGDRLLREDHP-ARPTAESFQAALQTQWSWMLQLC 854
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1521-1980 |
1.62e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.19 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1521 AHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVV 1600
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLA---LAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1601 RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQA 1680
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1681 LEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1760
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1761 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1840
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1841 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1920
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1921 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1980
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1555-2095 |
1.71e-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: 60.81 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1555 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1632
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1633 RQAQEEAERLRRQVQDETQRKRQAEAELALrVQAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEAERAr 1704
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1705 QVQVALETAQRS-AEAELQSEHASFA--EKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKA 1781
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1782 NEALRLRLQAEEVAQQKSltqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1858
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1859 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1938
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1939 frelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEA--ENERLRRLAEDE 2016
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2017 AFQR----------------RLLEEQAaqhKADIEARLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKGSFEKA 2080
Cdd:pfam05701 466 DSPRgvtlsleeyyelskraHEAEELA---NKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKA 541
|
570
....*....|....*
gi 1920237940 2081 AAGKAELELELGRIR 2095
Cdd:pfam05701 542 KEGKLAAEQELRKWR 556
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1833-2035 |
2.13e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1833 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA--AATQKRRELEAELAKVRAEMEVL 1910
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1911 LASKARAEEESrstseksKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEdaVRQRAEAErvlAEKLAAISEATR 1990
Cdd:PRK09510 157 AAAAKKAAAEA-------KKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAE--AKKKAEAE---AKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1920237940 1991 LKTEAEIALKEKEAENErlrRLAEDEAFQRRLLEEQAAQHKADIE 2035
Cdd:PRK09510 219 AAAEAKAAAAKAAAEAK---AAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1243-1598 |
2.34e-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: 60.84 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1243 EAEEVLRAHEEQLKEAQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWR 1321
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1322 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLrDAKQRQEQIQAVPLANSQAVREQLRQEKALLED- 1400
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERr 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1401 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELstltsqyirfi 1480
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELE---------ALLNERASLEEALALLRSELEEL----------- 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1481 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ------------------LAEAHAQAKAQAEREAQGLQRRMQE 1542
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeysltleEAEALENKIEDDEEEARRRLKRLEN 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1543 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAErsrlRIEEEIR 1598
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE----EIDREAR 1031
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1505-1917 |
2.37e-08 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 61.03 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1505 LAEVEAALEKQRQLAEAHAQAkaqaeREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE----------- 1573
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1574 --------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1645
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1646 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEH 1725
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1726 ASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEA 1805
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1806 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1885
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 1920237940 1886 AAAATQKRRELEAELAKVRAEMEVLLASKARA 1917
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2309-2757 |
2.54e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2309 EMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEE--ELFSLRVQME----E 2382
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLdelrE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2383 LGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2460
Cdd:PRK03918 312 IEKRLSRLEEEINGIeeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2461 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQ-----RQLEMSAEAERLRLRVAEM 2535
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2536 SRAQ---ARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKL-KQEAQL 2611
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2612 LQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRER-----CIEQEKAKLEQL--FQDEVAKAQALREEQQRQQQQM 2684
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELepFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2685 QQEKQQLAASMEEARRRQHEAEEgVRRQQEELQRlaqqqqqqeKLLAEENQRLRERLQHLEEERRAALARSEE 2757
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEE-LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2318-2758 |
2.93e-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: 60.62 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2318 EQALRQKAQVEQELTALRLQL-EETDHQKSILDEELQRLKAEVTEAARQRGQV---EEELFSLRVQMEELGKLKARIEAE 2393
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2394 NRAlvlrdkdsaQRLLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAE 2473
Cdd:pfam12128 484 NAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2474 LLQQQ--KELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA-------QARAEE 2544
Cdd:pfam12128 546 DWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsarekQAAAEE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2545 DARRFRKQAE--DIGERLYRTELaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTV 2622
Cdd:pfam12128 626 QLVQANGELEkaSREETFARTAL-KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2623 RQEQLLQETQALQQSFL---SEKDSLLQR-----ERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAAS 2694
Cdd:pfam12128 705 QKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREIRTLERK 783
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 2695 MEEARRRQHEAEEGVRRQQE----ELQRLAQQQQQQEKLLAEENQRL-------RERLQHLEEERRAALARSEEI 2758
Cdd:pfam12128 784 IERIAVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLarliadtKLRRAKLEMERKASEKQQVRL 858
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2301-2747 |
3.17e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 60.61 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2301 RQKQAADAEMEKHKqfAEQAL-RQKAQVEQELTALRLQLEE-TDHQksildEELQRLKAEVTEAARQRGQVEEELFSLRV 2378
Cdd:NF041483 195 RQRLGSEAESARAE--AEAILrRARKDAERLLNAASTQAQEaTDHA-----EQLRSSTAAESDQARRQAAELSRAAEQRM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2379 QMEELGKLKARIEAEnRALVLRDKDSAQRLLQEEA---EKMKQVAEEAARL-SVAAQEAARLRQLAEEDLAQQRALAEKM 2454
Cdd:NF041483 268 QEAEEALREARAEAE-KVVAEAKEAAAKQLASAESaneQRTRTAKEEIARLvGEATKEAEALKAEAEQALADARAEAEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2455 LKEKMQAVQEATRLKAEAELlqqqkelaqEQARRLQEDKEQMAQQLAQETQGfQKTLETERQRQlEMSAEAERLRLRVAE 2534
Cdd:NF041483 347 VAEAAEKARTVAAEDTAAQL---------AKAARTAEEVLTKASEDAKATTR-AAAEEAERIRR-EAEAEADRLRGEAAD 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2535 MS-RAQARAEEDARRFRKQAEDIGE--RLYRTElATQEKVMLVQTLETQRQQSDRDA-ERLREAIAELEHEKDKLKQEA- 2609
Cdd:NF041483 416 QAeQLKGAAKDDTKEYRAKTVELQEeaRRLRGE-AEQLRAEAVAEGERIRGEARREAvQQIEEAARTAEELLTKAKADAd 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2610 QLLQLKSEEMQTVRQEQLLQETQALQQSflsekDSLLQRERCiEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQ 2689
Cdd:NF041483 495 ELRSTATAESERVRTEAIERATTLRRQA-----EETLERTRA-EAERLRAEAEEQAEEVRAAAERAARELREETERAIAA 568
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2690 QLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLR----ERLQHLEEE 2747
Cdd:NF041483 569 RQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLRteaaERIRTLQAQ 630
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1623-2074 |
3.42e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1623 ARAEEAEAQKRQAQEEAERLRRQVQD-ETQRKRQAEAELAL----RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQ 1697
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELeelrEELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1698 AEAERARQVQV-----ALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEaer 1772
Cdd:COG4717 151 LEERLEELRELeeeleELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1773 elerwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAvrqrELAEQELEKQRQLAEGTAQQRL 1852
Cdd:COG4717 228 -----ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA----GVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1853 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstsEKSKQRL 1932
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---EQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1933 EAEAGrfrelAEEAARLRALAEEAKRQRQLAEEdavrqRAEAERVLAEKLAAISEATRLKTEAEiaLKEKEAENERLRRL 2012
Cdd:COG4717 376 LAEAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2013 AEDEafqrrllEEQAAQHKADIEARLAQLrkASESELERQKGLVEDTLRQRRQVEEEILALK 2074
Cdd:COG4717 444 LEEE-------LEELREELAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1796-1991 |
4.53e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1796 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1875
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1876 EEELARLQREAAAATQKRRELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1955
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237940 1956 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1991
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1482-1742 |
4.91e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.39 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSI 1561
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1562 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1641
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1642 LR-RQVQDETQRK-RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1719
Cdd:pfam13868 206 LRaKLYQEEQERKeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR 285
|
250 260
....*....|....*....|...
gi 1920237940 1720 ELQSEHASFAEKTAQLERTLKEE 1742
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAA 308
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1190-1752 |
5.44e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1190 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEaqaVPATLPELE 1269
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1270 ATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLqqrhgerdvevERWRERvtllLERWQAVLAQTDVRQRELEQLG 1349
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-----------SRLEEE----INGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1350 RQLRYYRESADPLGAWLR---DAKQRQEQIqavplansqavrEQLRQEKALL--EDIERHGEKVEECQRFAKQYINAIKD 1424
Cdd:PRK03918 345 KKLKELEKRLEELEERHElyeEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1425 YELQLVTYKAQLEPVASPAKKPKVQS---GSESIIQEYVDLRTRYSElstltsqYIRFISETLRRMEEEERlaeqqraEE 1501
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1502 RERLAEVEAALEKQRQLAEAHAQAKaqaereaqglQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1581
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAE----------QLKELEE--KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1582 QVEAAERsrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1661
Cdd:PRK03918 547 ELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1662 lRVQAEAEAAREK-QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERtLK 1740
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK-LK 700
|
570
....*....|..
gi 1920237940 1741 EEHVAVVQLREE 1752
Cdd:PRK03918 701 EELEEREKAKKE 712
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2350-2618 |
5.52e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2350 EELQRLKAEVTEAARQRGQVE------EELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkQVAEEA 2423
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2424 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2503
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2504 TQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedigerlyrtelatqekvmlVQTLETQRQQ 2583
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE---------------------IASLERRKSN 437
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237940 2584 SDRDAERLREAIAE-LEHEKDKLKQEAQLLQLKSEE 2618
Cdd:COG4913 438 IPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1209-1657 |
5.60e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1209 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKA-------ALKKLRAQ 1281
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelaelpeRLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1282 AEAQQPVFDALRDELRGAQEVGERLQQrhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP 1361
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1362 LGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVeecqRFAKQYINAIkdyeLQLVTYKAQLEPVAS 1441
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV----LFLVLGLLAL----LFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1442 PAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRfiseTLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA 1521
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELL----ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1522 HAQAKAQAEREAQGLQRRmQEEVARREEVAVEAQEQKRSIQEELQHLRQSS-EAEIQAKARQVEAAERSRLRIEEEIRVV 1600
Cdd:COG4717 380 GVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 1601 RLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDETQRKRQAE 1657
Cdd:COG4717 459 EAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1574-1726 |
5.73e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.73 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1574 AEIQAKARQVEA-AERsrlriEEEIRVvrlqleaTERQRGGAEGELQALRARAE----EAEAQKRQAQEEAERlrrqvqd 1648
Cdd:COG2268 195 AEIIRDARIAEAeAER-----ETEIAI-------AQANREAEEAELEQEREIETariaEAEAELAKKKAEERR------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1649 ETQRKRqAEAELALRVQaEAEAAREKQRALQALE---ELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEH 1725
Cdd:COG2268 256 EAETAR-AEAEAAYEIA-EANAEREVQRQLEIAErerEIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR 333
|
.
gi 1920237940 1726 A 1726
Cdd:COG2268 334 A 334
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
181-305 |
6.62e-08 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 54.24 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 181 ERDRVQKKTFTKWVNKHLIkhwraeaQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQ 260
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1920237940 261 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 305
Cdd:cd21331 86 NCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1639-2098 |
6.94e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 59.26 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1639 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAleelRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1718
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1719 AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQK 1798
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1799 SLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1878
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1879 LARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1958
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1959 QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARL 2038
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2039 AQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTA 2098
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1543-1708 |
7.47e-08 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 59.00 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1543 EVARR----EEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegel 1618
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1619 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEtqrkrqaeaelalrvQAEAEAAREKQRALQALEElRLQAEEAERRLRQ 1697
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 1920237940 1698 AEAERARQVQV 1708
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1490-2117 |
8.10e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 59.04 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1490 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAQGLQRRMQEEVARREEV 1550
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1551 AVEAQEQKRSIQEELQHLRQ-SSEAEIQAKARQVEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1625
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1626 EEAEAQKRQAQEEAER-----LRRQVQDETQRKRQAEAelalrvqAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1700
Cdd:PRK10246 410 EVAAALAQHAEQRPLRqrlvaLHGQIVPQQKRLAQLQV-------AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1701 ERARQVQVALETAQRsaeAELQS----------EHASFAEKTAqLERTlkeehvaVVQLREEATRRAQQQAeaeraraea 1770
Cdd:PRK10246 483 ICEQEARIKDLEAQR---AQLQAgqpcplcgstSHPAVEAYQA-LEPG-------VNQSRLDALEKEVKKL--------- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1771 erelerwqlkANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQ 1850
Cdd:PRK10246 543 ----------GEEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1851 RLAAEQELIRLRAETEQGEQQRQLLEEELArLQREAAAATQKRRELEAELAKVRAEMEVLLASKA------RAEEESRST 1924
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLAT 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1925 SEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAVrqRAEAERVLAEKLAAISEATrLKTEAEIALKEKEA 2004
Cdd:PRK10246 670 RQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQD 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2005 ENERLR---------------RLAEDEAFQRRLLEEQAAQhkadieaRLAQLRKASESELERQKGLVEdtlrQRRQVEEE 2069
Cdd:PRK10246 741 VLEAQRlqkaqaqfdtalqasVFDDQQAFLAALLDEETLT-------QLEQLKQNLENQRQQAQTLVT----QTAQALAQ 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2070 ILALKGSFEKAAAGKAELELELGRIRGT-AEDTLRSKE---QAEQEA-ARQRQ 2117
Cdd:PRK10246 810 HQQHRPDGLDLTVTVEQIQQELAQLAQQlRENTTRQGEirqQLKQDAdNRQQQ 862
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
322-417 |
8.17e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 54.23 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 322 KLLL-WSQrMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNL-----------------------EN 377
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 378 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 417
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1245-1904 |
9.42e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.03 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1245 EEVLRAHEEQLKE-----AQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1319
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1320 WRERVT-------LLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAK-QRQEQIQAvPLANSQAVReQL 1391
Cdd:pfam01576 417 LQARLSeserqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQeLLQEETRQ-KLNLSTRLR-QL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1392 RQEKALLEdiERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESIIQEYVDLRTRY 1466
Cdd:pfam01576 495 EDERNSLQ--EQLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLEEKAAAY 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1467 SELS-------------TLTSQYIRFISETLRR-------MEEEERLAEQQRAEERERlAEVEAALEKQRQLAEAHA--- 1523
Cdd:pfam01576 569 DKLEktknrlqqelddlLVDLDHQRQLVSNLEKkqkkfdqMLAEEKAISARYAEERDR-AEAEAREKETRALSLARAlee 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1524 --QAKAQAEREAQGLQRRMQEEVARREEV------------AVEAQEQKRSIQEE-------------------LQHLRQ 1570
Cdd:pfam01576 648 alEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskrALEQQVEEMKTQLEeledelqatedaklrlevnMQALKA 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1571 SSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEAERLR 1643
Cdd:pfam01576 728 QFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQ 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1644 RQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERAR-QVQVALETAQRSA 1717
Cdd:pfam01576 805 AQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGASGKSA 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1718 eaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAE-----AERARAEAERELERWQL-KANEALRLRLQA 1791
Cdd:pfam01576 880 ---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelAAERSTSQKSESARQQLeRQNKELKAKLQE 956
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1792 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQELIRLR 1862
Cdd:pfam01576 957 MEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQLK 1036
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1920237940 1863 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR 1904
Cdd:pfam01576 1037 RQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4183-4219 |
9.67e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 9.67e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 4183 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 4219
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1854-2054 |
1.07e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1854 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1933
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1934 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEA 1995
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1996 EIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKG 2054
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1833-2085 |
1.16e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1833 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1912
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1913 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEK 1981
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1982 LAAISEATRLKteAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLR 2061
Cdd:COG3883 174 EAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|....
gi 1920237940 2062 QRRQVEEEILALKGSFEKAAAGKA 2085
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2301-2742 |
1.80e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.88 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2301 RQKQAADAEMEKHKQFAEQALRqkaqvEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV 2378
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLD-----EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2379 QMEE-------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMK----------QVAEEAARLS-VAAQEAARLRQLA 2440
Cdd:pfam01576 167 NLAEeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAeLRAQLAKKEEELQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2441 E-----EDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL--AQETQGFQKTLET 2513
Cdd:pfam01576 247 AalarlEEETAQKNNALKKIRELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEALKTELedTLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2514 ERQRQLEMSAEAERLRLRVAEMSRAQARaeedaRRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLRE 2593
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMR-----QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2594 AIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL-------------------------------------LQETQALQQ 2636
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAeklsklqselesvssllneaegkniklskdvsslesqLQDTQELLQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2637 SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQekqqLAASMEEARRRQHEAEEGVRRQQEEL 2716
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQREL 554
|
490 500 510
....*....|....*....|....*....|
gi 1920237940 2717 ----QRLAQQQQQQEKLlaeenQRLRERLQ 2742
Cdd:pfam01576 555 ealtQQLEEKAAAYDKL-----EKTKNRLQ 579
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1840-2040 |
2.01e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.19 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1840 QRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRqllEEELARLQREAAAATQKRRELEAELAKVraemevllaskaraEE 1919
Cdd:COG2268 191 RRKIAEIIRDARIAEAE--AERETEIAIAQANR---EAEEAELEQEREIETARIAEAEAELAKK--------------KA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1920 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA-----ERVLAEKLAAISEAtrlKTE 1994
Cdd:COG2268 252 EERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELeadvrKPAEAEKQAAEAEA---EAE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237940 1995 AEIALKEKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 2040
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1586-1706 |
2.05e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 56.21 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1586 AERSRLRIEEEIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------RQVQDETQRKR-Q 1655
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQQELDEARAALdA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 1656 AEAELAlRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1706
Cdd:COG1566 160 AQAQLE-AAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1869-2053 |
2.28e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1869 EQQRQLLEEELAR-LQREAAAATQKRRELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1947
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1948 RLRALAEeakrqrQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRrllEEQA 2027
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK--AEAEAKKK---AAAE 214
|
170 180
....*....|....*....|....*.
gi 1920237940 2028 AQHKADIEARLAQLRKASESELERQK 2053
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1821-2038 |
2.54e-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: 56.39 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRreleAEL 1900
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA----KEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1901 AKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDA---VRQRAEAERV 1977
Cdd:TIGR02794 148 AAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEA-----KAKAEAEAKAKAEEAKAKAEAAKAKAaaeAAAKAEAEAA 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 1978 LAEKLAAISEATRLKTEAEIAL-KEKEAENERLRRLAEDEAFQRRLleeqAAQHKADIEARL 2038
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAGSEVDKY----AAIIQQAIQQNL 276
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2306-2506 |
2.58e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2306 ADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE--- 2382
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2383 --------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2454
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2455 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQG 2506
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1893-2599 |
2.67e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1893 RRELEAELAKVRAEMEVLLASKARAEEESRStsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRA 1972
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQ--IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1973 EAERvlaeklaaiSEATRLKTEAEIALKEKEAENERLRRLaedeafqrrllEEQAAQHKADIEARLAQLRKASESELERQ 2052
Cdd:COG4913 298 EELR---------AELARLEAELERLEARLDALREELDEL-----------EAQIRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2053 KGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerrrreaeer 2132
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR--------------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2133 vqkSLAAEEEAARQRKAAL-EEVERLKAKVEEARRLRE------------RAEQES-------------------ARQLQ 2180
Cdd:COG4913 423 ---ELEAEIASLERRKSNIpARLLALRDALAEALGLDEaelpfvgelievRPEEERwrgaiervlggfaltllvpPEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2181 LAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAAREraereaaqSRRQVEEAERL 2260
Cdd:COG4913 500 AALRWVN-RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRF--------DYVCVDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2261 KQSAEEQAQAQaqaqaaaekLRKeaeqeaarraqaEQAALRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEE 2340
Cdd:COG4913 571 RRHPRAITRAG---------QVK------------GNGTRHEKDDRRRIRSRY-VLGFDNRAKLAALEAELAELEEELAE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2341 TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQmEELGKLKARIEAenralvLRDKDSAQRLLQEEAEKMKQVA 2420
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAELER------LDASSDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2421 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQ 2499
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlGDAVERELRENLEERIDALRAR 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2500 LAQETQGFQKTleterqrqleMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERL------YRTELATQEKVML 2573
Cdd:COG4913 782 LNRAEEELERA----------MRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYeerfkeLLNENSIEFVADL 851
|
730 740
....*....|....*....|....*.
gi 1920237940 2574 VQTLETQRQQSDRDAERLREAIAELE 2599
Cdd:COG4913 852 LSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1475-1736 |
2.72e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 57.27 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1475 QYIRFISETLRRMEEEERLAEQ--QRAEER-ERLAEVEAA-LEKQRQLAEAHAQAKAQA---------EREAQGLQRRMQ 1541
Cdd:PRK05035 429 QYYRQAKAEIRAIEQEKKKAEEakARFEARqARLEREKAArEARHKKAAEARAAKDKDAvaaalarvkAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1542 EEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEeirvvrlQLEATERQRGGAEGELQA 1620
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAiARAKAKKAA-------QQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1621 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAelalrvqaeAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1700
Cdd:PRK05035 582 VAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAA---------AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237940 1701 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLE 1736
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2418-2871 |
2.76e-07 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 57.29 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2418 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMA 2497
Cdd:COG4995 9 LLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2498 QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2577
Cdd:COG4995 89 LLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2578 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2657
Cdd:COG4995 169 ALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2658 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRL 2737
Cdd:COG4995 249 ALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2738 RERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLRRKVPAQRLQEVGVLSAEELQQLAQ 2817
Cdd:COG4995 329 ALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQL 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 2818 GRTTVAELAQREDVRHYLQGRSSIAGLL-LKPADEKLTIYAALRRQLLSPGTALI 2871
Cdd:COG4995 409 LRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2313-2616 |
3.03e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2313 HKQFAEQALRQKAQVEQ---ELTALRLQLEEtdhQKSILDEelqrLKAEVTEAARQRGQVEEELFSLRVQME-------- 2381
Cdd:PRK04863 336 HLNLVQTALRQQEKIERyqaDLEELEERLEE---QNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLAdyqqaldv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2382 ---------------------------ELGKLKARIEAenraLVLRDKDSAQRLLQEE-----AEKMKQVAEEAARL--- 2426
Cdd:PRK04863 409 qqtraiqyqqavqalerakqlcglpdlTADNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrk 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2427 ---SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2494
Cdd:PRK04863 485 iagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2495 QMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAE-MSRAQA--RAEEDARRFRKQAEDigerlyrtELATQEKV 2571
Cdd:PRK04863 565 ARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARAPAwlAAQDALARLREQSGE--------EFEDSQDV 629
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2572 M--LVQTLETQRQQSdRDAERLREAIAELEHEKDKLKQ-----EAQLLQLKS 2616
Cdd:PRK04863 630 TeyMQQLLERERELT-VERDELAARKQALDEEIERLSQpggseDPRLNALAE 680
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1485-1753 |
3.41e-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: 55.70 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1485 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVeaQEQKRSIQEE 1564
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM--DEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1565 LQHLRQSSEAEIQAKARQVEAAERSRLRI---------EEEIRVVRLQLEATERQRggAEGELQALRARAEEAEAQKRQA 1635
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1636 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQR 1715
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270
....*....|....*....|....*....|....*...
gi 1920237940 1716 SAEAELQSEhasfAEKTAQLERTLKEEHVAVVQLREEA 1753
Cdd:pfam13868 272 EDEEIEQEE----AEKRRMKRLEHRRELEKQIEEREEQ 305
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
186-302 |
3.86e-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: 51.73 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 186 QKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirSSRLPRekgRMRFHKLQNVQIA 265
Cdd:cd21299 5 EERCFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKH----ANKPPI---KMPFKKVENCNQV 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 266 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 302
Cdd:cd21299 71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1620-2018 |
3.97e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.88 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1620 ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAeaelalrvqaeAEAAREKQRALQAL---------EELRLQAEE 1690
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ-----------LDQLKEQLQLLNKLlpqanlladETLADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1691 AERRLRQAEAERA--RQVQVALETAQRSAEAeLQSEHASFAEktaqlertLKEEHVAVVQLREEATRRAQQQAEAERARA 1768
Cdd:COG3096 898 LREELDAAQEAQAfiQQHGKALAQLEPLVAV-LQSDPEQFEQ--------LQADYLQAKEQQRRLKQQIFALSEVVQRRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1769 EAERELERWQLKANEALRLRLQAeevaqqksltqaeaekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTA 1848
Cdd:COG3096 969 HFSYEDAVGLLGENSDLNEKLRA-------------------------------------RLEQAEEARREAREQLRQAQ 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1849 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA-----AAATQKRRELEAELAKVRAEmevllaskaraeeesRS 1923
Cdd:COG3096 1012 AQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaeERARIRRDELHEELSQNRSR---------------RS 1076
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1924 TSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAK----RQRQLAEEDAVRQRAEAERVL---AEKLAAISEatrlk 1992
Cdd:COG3096 1077 QLEKQLTRCEAEmdslQKRLRKAERDYKQEREQVVQAKagwcAVLRLARDNDVERRLHRRELAylsADELRSMSD----- 1151
|
410 420
....*....|....*....|....*....
gi 1920237940 1993 tEAEIALKEKEAENERLR---RLAEDEAF 2018
Cdd:COG3096 1152 -KALGALRLAVADNEHLRdalRLSEDPRR 1179
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1543-2170 |
4.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1543 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ----------LEATERQRG 1612
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkeleelkeeIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1613 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEaEAAREKQRALQALEELRLQAEEAE 1692
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1693 RRLRQAEAERARQVQValetaqRSAEAELQSEHASFaEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaer 1772
Cdd:PRK03918 328 ERIKELEEKEERLEEL------KKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKR-------------------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1773 elerwqLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREarrrgkaeEQAVRQRELAEQELEKqrqlAEGTAQ--Q 1850
Cdd:PRK03918 381 ------LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL--------KKEIKELKKAIEELKK----AKGKCPvcG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1851 RLAAEQELIRLRAEteqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVraEMEVLLASKARAE----EESRSTSE 1926
Cdd:PRK03918 443 RELTEEHRKELLEE----------YTAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLkelaEQLKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1927 KSK----QRLEAEAGRFRELAEEAARLRalaeeaKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEK 2002
Cdd:PRK03918 511 KLKkynlEELEKKAEEYEKLKEKLIKLK------GEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2003 --EAENERLRRLAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSF--- 2077
Cdd:PRK03918 583 gfESVEELEERLKELEPFYNEYLELKDAEK--ELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYsee 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2078 --EKAAAGKAELELELGRIRGTAEDTLRSKEQAEqeaarqrqlaaeeerrrreaeervqKSLAAEEEAARQRKAALEEVE 2155
Cdd:PRK03918 660 eyEELREEYLELSRELAGLRAELEELEKRREEIK-------------------------KTLEKLKEELEEREKAKKELE 714
|
650
....*....|....*
gi 1920237940 2156 RLKAKVEEARRLRER 2170
Cdd:PRK03918 715 KLEKALERVEELREK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2017-2506 |
4.34e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2017 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRg 2096
Cdd:COG4717 41 AFIRAMLLERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2097 tAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2176
Cdd:COG4717 116 -EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2177 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVL-ERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVE 2255
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2256 EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQA------LRQKAQVEQ 2329
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldrIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2330 ELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL-GKLKARIEAENRALVLRDKDSAQRL 2408
Cdd:COG4717 355 EAEELEEELQLEELEQEI-AALLAEAGVEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2409 LQEEAEKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRALAEKMLKEKMQ-AVQEATRLKAEAELLQQQKELAQEqa 2486
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELeAELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALELLEEAREEYRE-- 511
|
490 500
....*....|....*....|
gi 1920237940 2487 RRLQEDKEQMAQQLAQETQG 2506
Cdd:COG4717 512 ERLPPVLERASEYFSRLTDG 531
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1625-1742 |
4.49e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.03 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1625 AEEAEAQKRQAQEEAErLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAlQALEELRLQAEEAERRLRQA--EAER 1702
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARA-EAEAAYEIAEANAEREVQRQleIAER 288
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1920237940 1703 ARQVQVALETAQRsAEAELQSEHASFAEktAQLERTLKEE 1742
Cdd:COG2268 289 EREIELQEKEAER-EEAELEADVRKPAE--AEKQAAEAEA 325
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2399-2836 |
5.00e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.52 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2399 LRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2478
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2479 KELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRqLEMSAEAERLRLRVAEMSRAQARAEEdarrFRKQAEDI 2556
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQ----IEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2557 GERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS---EEMQTVRQEQLLQETQA 2633
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCqqhTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2634 LQQSFLSEKDSLLQRErciEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ 2713
Cdd:TIGR00618 393 QKLQSLCKELDILQRE---QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2714 EELQRLAQQQQQQEKlLAEENQRLRERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLR 2793
Cdd:TIGR00618 470 EREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2794 RKVPA-----QRLQEVGVLSAEELQQLAQGRTTVAELAQR-----EDVRHYLQ 2836
Cdd:TIGR00618 549 HQLTSerkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitVRLQDLTE 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2404-2620 |
6.23e-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: 55.16 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2404 SAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrqlAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQ 2483
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2484 EQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2563
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 2564 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2620
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
188-299 |
6.28e-07 |
|
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: 50.80 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 188 KTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNVQIALD 267
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEKV---EDI---NGCPRSQSQM----IENVDVCLS 69
|
90 100 110
....*....|....*....|....*....|..
gi 1920237940 268 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 299
Cdd:cd21286 70 FLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1622-1752 |
6.28e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 55.73 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1622 RARAEEAEAQ------KRQAQEEAerlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAER-- 1693
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1694 -RLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ----LERTLKEEHVAVVQLREE 1752
Cdd:pfam15709 411 rLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQrqkeLEMQLAEEQKRLMEMAEE 474
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2946-2982 |
7.49e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.49e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 2946 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 2982
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2310-2613 |
7.71e-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: 55.80 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2310 MEKHKQFAEQALRQKAQVEQELTAlrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKAR 2389
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2390 IEAENRALvlrdKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAarlRQLAEE--DLAQQRALaekmLKEKMQavqeatr 2467
Cdd:TIGR04523 466 LETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEK---KELEEKvkDLTKKISS----LKEKIE------- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2468 lKAEAELLQQQKELAQeqarrLQEDKEQMAQQLAQETqgfqktLETERQRQLEmsaEAERLRLRVAEMSRAQARAEEDAR 2547
Cdd:TIGR04523 528 -KLESEKKEKESKISD-----LEDELNKDDFELKKEN------LEKEIDEKNK---EIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2548 RFRKQAEDIGERLyrtelatQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQ 2613
Cdd:TIGR04523 593 QKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1821-2194 |
8.04e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.26 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1900
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1901 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAVRQRAEAERVL 1978
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1979 AEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRLLEEQAAQhkadiearlaqlrkASESELERQKGLVED 2058
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKSQ--------------NGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2059 TLRQRRQVEEEilalkgsfEKAAAGKAELELELGRIRGTAEDtlrsKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 2138
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRRRRQE----KESEEFEKLRQKQQEAELELEELKKKREERRKLL 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2139 AEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2194
Cdd:pfam02029 294 EEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1489-1673 |
8.59e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1489 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveaqEQKRSIQEELQhl 1568
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA------EAKKKAEAEAA-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1569 rQSSEAEIQAKARQVEAAersrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1648
Cdd:PRK09510 177 -KKAAAEAKKKAEAEAAA----------------KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 1920237940 1649 ETQRKRQAEAELALRVQAEAEAARE 1673
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2405-2732 |
8.78e-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: 54.54 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2405 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2484
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2485 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERlrlRVAEMSRAQARAEEDARRFRKQAEDIGERLYrte 2564
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREI--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2565 latqeKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqllqlksEEMQTVRQEQLLQETQALQQSFLSEKDS 2644
Cdd:pfam13868 187 -----ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKERE--------EAEKKARQRQELQQAREEQIELKERRLA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2645 LLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQ 2724
Cdd:pfam13868 254 EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
....*...
gi 1920237940 2725 QQEKLLAE 2732
Cdd:pfam13868 334 ERQKKLKE 341
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1386-2118 |
9.87e-07 |
|
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: 55.50 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1386 AVREQLRQEKALLEDierhGEKVEECQRFAKQyinaikdyELQLVTYKAQLepvaspakkpKVQSGsesiIQEYVDLRTR 1465
Cdd:pfam05483 96 SIEAELKQKENKLQE----NRKIIEAQRKAIQ--------ELQFENEKVSL----------KLEEE----IQENKDLIKE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1466 yselSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAQGLQRRMQEEva 1545
Cdd:pfam05483 150 ----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK---MILAFEELRVQAENARLEMHFKLKED-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1546 rreevaveaqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1625
Cdd:pfam05483 221 ----------------HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1626 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR----LQAEEAERRLRQAEaE 1701
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsFVVTEFEATTCSLE-E 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1702 RARQVQVALEtaqrSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaeaerarAEAERELERWQLKA 1781
Cdd:pfam05483 364 LLRTEQQRLE----KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK-------------ILAEDEKLLDEKKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1782 NEALRLRLQAEEvaQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR-QLAEGTAQ--------QRL 1852
Cdd:pfam05483 427 FEKIAEELKGKE--QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHcdklllenKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1853 AAEQE--LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLL---ASKARAEEESRST 1924
Cdd:pfam05483 505 TQEASdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreEFIQKGDEVKCKLdksEENARSIEYEVLK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1925 SEKSKQRLEAEAGRFRELAEEAAR-LRALAEEAKRQRQlaEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 2003
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKnIEELHQENKALKK--KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2004 AENERL--RRLAEdEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRrqvEEEILALKGSFEKAA 2081
Cdd:pfam05483 663 IEDKKIseEKLLE-EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQS 738
|
730 740 750
....*....|....*....|....*....|....*..
gi 1920237940 2082 AGKAELELELGRIRGtaeDTLRSKEQAEQEAARQRQL 2118
Cdd:pfam05483 739 SAKAALEIELSNIKA---ELLSLKKQLEIEKEEKEKL 772
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4286-4314 |
1.08e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.08e-06
10 20
....*....|....*....|....*....
gi 1920237940 4286 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4314
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2398-2751 |
1.10e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2398 VLRDKDSAQRLLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2471
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2472 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAQETQGFQKTLETER-------QRQLEMSAEAERLRLRVAEMSRAQAR 2541
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2542 AEEDARRFRKQAEDIGERlyrtelaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQT 2621
Cdd:PRK02224 340 HNEEAESLREDADDLEER-------AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2622 VRQEqllqetqalqqsFLSEKDSLLQRERCIEqekAKLEQLfQDEVAKAQALREE--------------QQRQQQQMQQE 2687
Cdd:PRK02224 413 FLEE------------LREERDELREREAELE---ATLRTA-RERVEEAEALLEAgkcpecgqpvegspHVETIEEDRER 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2688 KQQLAASMEEARRRQHEAEEGVRRQQE------ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2751
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1485-1746 |
1.14e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 54.27 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1485 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR--REEVAVEAQEQKRSIQ 1562
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1563 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleaterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1642
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1643 RRQVQDETQRKRQAEAELALRVQAEAEAAREK----QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1718
Cdd:pfam15558 168 KVQENNLSELLNHQARKVLVDCQAKAEELLRRlsleQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 1920237940 1719 AELQSEHASFAEKTAQLERTLKEEHVAV 1746
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
178-303 |
1.16e-06 |
|
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: 50.28 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 178 AADERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPrekgrmrfH 257
Cdd:cd21222 9 EAPEKLAEVKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDD--------E 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1920237940 258 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 303
Cdd:cd21222 76 KLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2310-2534 |
1.29e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2310 MEKHKQFAEQALR----QKAQVEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2383
Cdd:COG3206 166 LELRREEARKALEfleeQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2384 GKLKARIEAENRALVlrDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQ 2463
Cdd:COG3206 246 RAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS---LEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2464 EATRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLET--ERQRQLEMSAEAERLRLRVAE 2534
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESllQRLEEARLAEALTVGNVRVID 392
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1820-2040 |
1.31e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.57 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1820 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqreaaaATQKRREL 1896
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1897 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1976
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1977 VLAEKLAAISEATRLKTEAEIALkeKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 2040
Cdd:pfam15709 447 AEAEKQRQKELEMQLAEEQKRLM--EMAEEERLEYQRQkQEAEEKARLEAEERRQKEEEAARLAL 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1618-1892 |
1.34e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1618 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQA--------LEELRLQAE 1689
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQelaaleaeLAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1690 EAERRLRQAEAERARQVQVALETAQRSAEAELQSehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaeaerarae 1769
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRA----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1770 aerelerwQLKANEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgtaq 1849
Cdd:COG4942 158 --------DLAELAALRAELEAERAELEALL----------------------AELEEERAALEALKAERQKLLAR---- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237940 1850 qrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQK 1892
Cdd:COG4942 204 ----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1826-2568 |
1.49e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1826 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQrEAAAATQKrrelea 1898
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEK------ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1899 eLAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAVRQRAEAERvl 1978
Cdd:COG3096 349 -IERYQEDLEEL---TERLEEQEEVVEEAAEQLAEAEA-RLEAAEEEVDSLKS--QLADYQQAL---DVQQTRAIQYQ-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1979 aEKLAAISEATRLKTEAEIALKEKEAENERLRRlAEDEAFQRRLleeQAAQHKADIEARLAQLRKAseseLERQKGLVED 2058
Cdd:COG3096 417 -QAVQALEKARALCGLPDLTPENAEDYLAAFRA-KEQQATEEVL---ELEQKLSVADAARRQFEKA----YELVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2059 TLRQRR-QVEEEILALKGSFEKAAAGKAELELELGrirgtaedtlrskeQAEQEAARQRQLAAEEERRRREAEERVQKSL 2137
Cdd:COG3096 488 VERSQAwQTARELLRRYRSQQALAQRLQQLRAQLA--------------ELEQRLRQQQNAERLLEEFCQRIGQQLDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2138 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEA-----AQKRLQ--AEEKAHAFAVQQkeqelqQ 2210
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaAQDALErlREQSGEALADSQ------E 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2211 TLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeklrkeaeqeaa 2290
Cdd:COG3096 628 VTAAMQQLLERER----------------------EATVERDELAARKQ------------------------------- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2291 rraQAEQAALRQKQAADAEMEKHKQFAEQ----------------------AL--------------------------- 2321
Cdd:COG3096 655 ---ALESQIERLSQPGGAEDPRLLALAERlggvllseiyddvtledapyfsALygparhaivvpdlsavkeqlagledcp 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2322 ---------------------------------RQ-------------KAQVEQELTALRLQLEETD---HQKSILDEEL 2352
Cdd:COG3096 732 edlyliegdpdsfddsvfdaeeledavvvklsdRQwrysrfpevplfgRAAREKRLEELRAERDELAeqyAKASFDVQKL 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2353 QRL--------------------KAEVTEAARQRGQVEEELFSLRVQM----EELGKLKARIEAENRAL----VLRDKDS 2404
Cdd:COG3096 812 QRLhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADETL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2405 AQRL--LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlKEKMQAVQEATRLKAEA---------- 2472
Cdd:COG3096 892 ADRLeeLREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQ----ADYLQAKEQQRRLKQQIfalsevvqrr 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2473 -------------------ELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQkTLETERQRQLEMSAEAERlrlRVA 2533
Cdd:COG3096 968 phfsyedavgllgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ---ELE 1043
|
890 900 910
....*....|....*....|....*....|....*...
gi 1920237940 2534 EMS-RAQARAEEDA--RRFRKQAEDIGERLYRTELATQ 2568
Cdd:COG3096 1044 ELGvQADAEAEERAriRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1820-2102 |
1.58e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1820 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1899
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1900 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ----LAEEDAVRQRAEAE 1975
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1976 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL 2055
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1920237940 2056 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 2102
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1920-2761 |
1.58e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.74 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1920 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIAL 1999
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2000 KEKEAENERlrrlAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKASESELERQKGLVEDTLRQR--------RQVEEEIL 2071
Cdd:pfam15921 161 KEDMLEDSN----TQIEQLRKMMLSHEGVLQ--EIRSILVDFEEASGKKIYEHDSMSTMHFRSLgsaiskilRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2072 ALKGSF----EKAAAGKAELELELGRIRGTAEDTLrskEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR 2147
Cdd:pfam15921 235 YLKGRIfpveDQLEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2148 KAA----LEEVE----RLKAKVEEARRLRERAEQESARQLQLAQ----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2215
Cdd:pfam15921 312 NSMymrqLSDLEstvsQLRSELREAKRMYEDKIEELEKQLVLANseltEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2216 QSVLERlrseaeaarraaeeaeaareraereaAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2295
Cdd:pfam15921 392 ELSLEK--------------------------EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2296 EQAALRQKQAADAEMEKHKQFAEQALRQKA---QVEQELTALRLQLEETDHQKSILDEELQR----LKAEVTEAARQRGQ 2368
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEkeraIEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2369 VE---EELFSLRVQMEELGKLKAriEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ-EAArlrQLAEEDL 2444
Cdd:pfam15921 526 VDlklQELQHLKNEGDHLRNVQT--ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKA---QLEKEIN 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2445 AQQRALAE-KMLKEKMQAvqEATRLKAEAELLQQQK-ELAQEQARRLQEDKEqmaqqLAQETQGFQKTLETERQRQLEMS 2522
Cdd:pfam15921 601 DRRLELQEfKILKDKKDA--KIRELEARVSDLELEKvKLVNAGSERLRAVKD-----IKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2523 AEAERLRlrvaemsraqaraeedaRRFRKQAEDIGERLYRTELATQE-KVMLVQTLETQRQQSDRDAERLREA------I 2595
Cdd:pfam15921 674 EDYEVLK-----------------RNFRNKSEEMETTTNKLKMQLKSaQSELEQTRNTLKSMEGSDGHAMKVAmgmqkqI 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2596 AELEHEKDKLKQEAQLLQlksEEMQTVRQEQ-LLQEtqalqqsflsEKDSLLQRERCIEQEKAKLEQlfQDEVAKAQALR 2674
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLE---EAMTNANKEKhFLKE----------EKNKLSQELSTVATEKNKMAG--ELEVLRSQERR 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2675 eeqqrqqqqMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA----EENQRLRERLQhleeeRRA 2750
Cdd:pfam15921 802 ---------LKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQgpgyTSNSSMKPRLL-----QPA 867
|
890
....*....|.
gi 1920237940 2751 ALARSEEIAPS 2761
Cdd:pfam15921 868 SFTRTHSNVPS 878
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1552-2458 |
1.59e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1552 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAersrLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1631
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKA----CEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1632 KRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKqraLQALEELR-LQAEEAERRLRQAEAERARQVQVAL 1710
Cdd:TIGR00606 261 LSKIMKLDNEIKALKSRKKQMEKD-NSELELKMEKVFQGTDEQ---LNDLYHNHqRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1711 ETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL--R 1788
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLcaD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1789 LQAEEVAQQKSLTQAEAEKQKEEAEREArrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1868
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIEL----KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1869 EQQR--QLLEEELARLQREAAAATQKRRELEAELAKV------RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFR 1940
Cdd:TIGR00606 491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1941 ELAEEAARLRALAEEAKRQRQ-LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEI----ALKEKEAENERLRRLAED 2015
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2016 EAFQRRLLEEQAAQHKADIEAR---------LAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKaaagkaE 2086
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK------R 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2087 LELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRR--EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2164
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2165 RRLRERAEQESaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERA 2243
Cdd:TIGR00606 805 ERKIAQQAAKL-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2244 EREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKL----------RKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2313
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDqqekeelissKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2314 KQfaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVtEAARQRGQVEEELFSLRVQMEELGKLKarieae 2393
Cdd:TIGR00606 964 IQ--DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI-DTQKIQERWLQDNLTLRKRENELKEVE------ 1034
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2394 nRALVLRDKDSAQ-RLLQEEAEKMKqvAEEAARLSVAAQEAARLRQLAEEDlaqQRALAEKMLKEK 2458
Cdd:TIGR00606 1035 -EELKQHLKEMGQmQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEK---EIKHFKKELREP 1094
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2471-2757 |
1.65e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.74 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2471 EAELLQQQKELAQEQA----RRLQEDKEQMAQQ-LAQETQgfQKTLETERQRQLEMS-----AEAERLRLRVAEMSRAQA 2540
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQErLRQEKE--EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2541 RAEEDARRFRKQAEDI-GERLYRTELATQ-EKVMLVQTLETQRQQSDrdaERLREAIAELEHEKDKLKQEAQLLQLKSEE 2618
Cdd:pfam17380 345 ERERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2619 MQTVRQEQLLQETQALQQsflsekdslLQRERCIEQEKAKLEQLfqdevakaqalreeqqRqqqqMQQEKQQLAASMEEA 2698
Cdd:pfam17380 422 MEQIRAEQEEARQREVRR---------LEEERAREMERVRLEEQ----------------E----RQQQVERLRQQEEER 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2699 RRRQHEAEEGVRRQQ--EELQRLAQQQQQQEKLLAE-ENQRLRERLQHLEEERRAALARSEE 2757
Cdd:pfam17380 473 KRKKLELEKEKRDRKraEEQRRKILEKELEERKQAMiEEERKRKLLEKEMEERQKAIYEEER 534
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2349-2554 |
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 1920237940 2349 DEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSV 2428
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2429 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2500
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 2501 AQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2554
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3605-3641 |
1.79e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 1.79e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 3605 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEM 3641
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2031-2749 |
1.91e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2031 KADIEARLAQlRKASESELERQKGLVEDTLRQRrQVEEEILALKGSFEKAAAG-----KAELELELGRIRGTAEDTLRSK 2105
Cdd:pfam12128 199 KSMIVAILED-DGVVPPKSRLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEfntleSAELRLSHLHFGYKSDETLIAS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2106 EQAEQEA--ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQ 2183
Cdd:pfam12128 277 RQEERQEtsAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2184 EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQS 2263
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2264 AEEQAQaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDh 2343
Cdd:pfam12128 437 EEEYRL----------KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2344 qksildEELQRLKAEVTEAARQRGQVEEELFS--------LRVQM----EELGKLKARieaenrALVLR-------DKDS 2404
Cdd:pfam12128 506 ------EALRQASRRLEERQSALDELELQLFPqagtllhfLRKEApdweQSIGKVISP------ELLHRtdldpevWDGS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2405 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2484
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2485 QARRLQEDKEQMAQQLAQETQGFQKTLETERQrqlEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQA--EDIGERLYR 2562
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLN---SLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqVVEGALDAQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2563 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqLLQETQALQQSFLSEK 2642
Cdd:pfam12128 731 LALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE-VLRYFDWYQETWLQRR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2643 DSLLQRERCIEQEKAKLEQlfqdevakaqalreEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQ 2722
Cdd:pfam12128 810 PRLATQLSNIERAISELQQ--------------QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
730 740
....*....|....*....|....*..
gi 1920237940 2723 QQQQEKllAEENQRLRERLQHLEEERR 2749
Cdd:pfam12128 876 KEDANS--EQAQGSIGERLAQLEDLKL 900
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2322-2753 |
1.96e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 54.37 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2322 RQKAQVEQELTALRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALV 2398
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2399 LRDKDSAQRLLQEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2477
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2478 QKELAQEQA--RRLQEDKEQMAQQLAQETQGFQKTL----ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRK 2551
Cdd:pfam07111 347 VTSQSQEQAilQRALQDKAAEVEVERMSAKGLQMELsraqEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2552 QAEDIGERLYRTELATQE----------KVMLVQTLETQRQQSDRDAERLREAIAELEH---EKDKLKQEAQL-LQLKSE 2617
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKvhtikglmarKVALAQLRQESCPPPPPAPPVDADLSLELEQlreERNRLDAELQLsAHLIQQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2618 EMQTVRQE-------------QLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQ-LFQDEVAKAQALREEQQRQ 2680
Cdd:pfam07111 507 EVGRAREQgeaerqqlsevaqQLEQELQRAQESLASvgqQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEKVAEV 586
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 2681 QQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2753
Cdd:pfam07111 587 ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLA 663
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1488-1653 |
2.20e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.31 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1488 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQH 1567
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1568 LRQSSEAEIQAKARQVEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1636
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 1920237940 1637 EEAERLRRQVQDETQRK 1653
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2328-2757 |
2.36e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.41 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2328 EQELTALRLQLEETDHQKSILDEElQRLKAEvtEAARQRGQVEeelfslRVQMEelGKLKariEAENRALVLRDKDSaqR 2407
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLE-EQLDEE--EAARQKLQLE------KVTTE--AKIK---KLEEDILLLEDQNS--K 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2408 LLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK-EKMQAVQEATRLKAEAELLQqqkelAQEQA 2486
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKeEKGRQELEKAKRKLEGESTD-----LQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2487 RRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQA--RAEEDAR-RFRKQAEDIGERL--Y 2561
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEdlESERAARnKAEKQRRDLGEELeaL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2562 RTELA-TQEKVMLVQTLETQRQQsdrDAERLREAIaelehEKDKLKQEAQLLQLKSEEMQTVR--QEQLLQ--------- 2629
Cdd:pfam01576 305 KTELEdTLDTTAAQQELRSKREQ---EVTELKKAL-----EEETRSHEAQLQEMRQKHTQALEelTEQLEQakrnkanle 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2630 -ETQALQQSFL---SEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQalreEQQRQQQQMQQEKQQLAASMEEARRRQHEA 2705
Cdd:pfam01576 377 kAKQALESENAelqAELRTLQQAKQDSEHKRKKLEGQLQELQARLS----ESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 2706 EEGVRRQQEELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEE 2757
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQklnLSTRLRQLEDERNSLQEQLEE 507
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2302-2486 |
2.36e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2302 QKQAADAEMEKHKQFAEQA--LRQKAQVEQEltalRLQLEETDHQKSildeelQRLKAEVTEAARQRGQVEEELFSLRVQ 2379
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLEKERLAA------QEQKKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2380 MEELGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEK-----MKQVAEEAARLSVAAQEAARLRQLAEE---DLAQQRAL 2450
Cdd:PRK09510 141 AAAAAKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAKkaaaeAKKKAEAEAAAKAAAEAKKKAEAEAKKkaaAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237940 2451 AEKmlKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2486
Cdd:PRK09510 221 AEA--KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2350-2758 |
2.46e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2350 EELQRLKAEVteAARQRGQVEEELFSLRVQMEELGKLKARIEaENRALVLRDKDSAQRLLQEEAEKMKQ---VAEEAARL 2426
Cdd:PRK02224 187 GSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIERYE-EQREQARETRDEADEVLEEHEERREEletLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2427 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaqetQG 2506
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA----QA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2507 FQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2586
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI--------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2587 DAERLREAIAELEHEKDKLKQEAQLLQ--LKSEEMQTVRQEQLLQE------TQALQQSflSEKDSLLQRERCIEQEKAK 2658
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEatLRTARERVEEAEALLEAgkcpecGQPVEGS--PHVETIEEDRERVEELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2659 LEQL------FQDEVAKAQALREEQQR--QQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLL 2730
Cdd:PRK02224 484 LEDLeeeveeVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430
....*....|....*....|....*....|....
gi 1920237940 2731 AEENQRLRERLQHLEE------ERRAALARSEEI 2758
Cdd:PRK02224 564 EEEAEEAREEVAELNSklaelkERIESLERIRTL 597
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1482-1715 |
2.51e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 53.12 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQRAEERERLA--EVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvavEAQEQKR 1559
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGreERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQ---RKQCQEQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1560 SIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA------EAQKR 1633
Cdd:pfam15558 128 RLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlslEQSLQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1634 QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ----RALQALEELRL-QAEEAERRLRQAEAERARQVQV 1708
Cdd:pfam15558 208 RSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERqehkEALAELADRKIqQARQVAHKTVQDKAQRARELNL 287
|
....*..
gi 1920237940 1709 ALETAQR 1715
Cdd:pfam15558 288 EREKNHH 294
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1469-1724 |
2.56e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1469 LSTLTSQYIRFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAEREAQGLQRRMQEEVAR 1546
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1547 ReevaVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRieEEIRVVRLQLeATERQRGGAEG-ELQALRARA 1625
Cdd:COG3206 228 L----AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR--AQLAELEAEL-AELSARYTPNHpDVIALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1626 EEAEAQKRQaqeEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAeaeRARQ 1705
Cdd:COG3206 301 AALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL---LQRL 374
|
250
....*....|....*....
gi 1920237940 1706 VQVALETAQRSAEAELQSE 1724
Cdd:COG3206 375 EEARLAEALTVGNVRVIDP 393
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1515-1643 |
2.63e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 52.74 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1515 QRQLAEAHAQ-AKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRLRI 1593
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1594 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1643
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2302-2487 |
2.72e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.88 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2302 QKQAADAEMEKHKQFAEQALRQKAQvEQELTALRLQLEETDHQKSILDEELQRLKAEVTeaarqrgQVEEELFSLRVQME 2381
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSIK-------QVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2382 ELGK---LKARI-----EAENRALVLrdkdsaQRLLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALA 2451
Cdd:pfam05667 381 ELEKqykVKKKTldllpDAEENIAKL------QALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLE 454
|
170 180 190
....*....|....*....|....*....|....*....
gi 1920237940 2452 E-KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2487
Cdd:pfam05667 455 EiKELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2300-2746 |
2.82e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFAEQALRQ-----KAQVEQELTA---LRLQLEETDHQKSI-LDEELQRLKAEVTEAARQRGQVE 2370
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQvymdlNNNIEKMILAfeeLRVQAENARLEMHFkLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2371 EELFSLRVQM-EELGKLKARI----EAENRALVLRDKDSAQ-RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2444
Cdd:pfam05483 240 KQVSLLLIQItEKENKMKDLTflleESRDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2445 AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ--------KELAQEQARRLQEDKEQMaQQLAQETQgfQKTLETERQ 2516
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcslEELLRTEQQRLEKNEDQL-KIITMELQ--KKSSELEEM 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2517 RQLEMSAEAERLRLRVAeMSRAQARAEEdarrfRKQAEDIGERLYRTElatQEKVMLVQT-------LETQRQQSDRDAE 2589
Cdd:pfam05483 397 TKFKNNKEVELEELKKI-LAEDEKLLDE-----KKQFEKIAEELKGKE---QELIFLLQArekeihdLEIQLTAIKTSEE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2590 RLREAIAEL--EHEKDKLKQeaqlLQLKSE-EMQTVRQEQLLQETQALQQSFLSEKDSLLQrerCIEQEKAKLEQLfqde 2666
Cdd:pfam05483 468 HYLKEVEDLktELEKEKLKN----IELTAHcDKLLLENKELTQEASDMTLELKKHQEDIIN---CKKQEERMLKQI---- 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2667 vakaQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEE 2746
Cdd:pfam05483 537 ----ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1574-1753 |
2.94e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1574 AEIQAKARQVEAAERSRLRIEEEirvvrlQLEATERQRGGAEGELQALRARAEEAEAqKRQAQEEAERLRRQVQDETQRK 1653
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQ------QAEEAEKQRAAEQARQKELEQRAAAEKA-AKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1654 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1733
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170 180
....*....|....*....|
gi 1920237940 1734 QLERTLKEEHVAVVQLREEA 1753
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEA 225
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1523-1745 |
3.07e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1523 AQAKAQAEREAQGLQ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArqveaAERSRLRIEEEIRV 1599
Cdd:TIGR02794 46 GAVAQQANRIQQQKKpaaKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1600 vrlQLEATERQRggaegelqALRARAEEAEAqKRQAQEEAerlRRQVQDETQRKRQAEAelalrvQAEAEAAREKQRAL- 1678
Cdd:TIGR02794 121 ---AEEAKAKQA--------AEAKAKAEAEA-ERKAKEEA---AKQAEEEAKAKAAAEA------KKKAEEAKKKAEAEa 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1679 --QALEELRLQAEEAERRLRQAE----------AERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA 1745
Cdd:TIGR02794 180 kaKAEAEAKAKAEEAKAKAEAAKakaaaeaaakAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2407-2655 |
3.08e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.90 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2407 RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2482
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2483 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAE-AERLRLRVAEMSRAQARA----EEDARRFRKQAEDIG 2557
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2558 ERLYRTELATQEKVMLVQTLETQRQQ------SDRDAERLREAIAELEhEKDKLKQ----EAQLL--QLKSEEMQTvRQE 2625
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldteMAQLRvqRLRYEDLLN-KQP 360
|
250 260 270
....*....|....*....|....*....|
gi 1920237940 2626 QLLQETQALQQSFLSEKDSLLQRERCIEQE 2655
Cdd:PRK10929 361 QLRQIRQADGQPLTAEQNRILDAQLRTQRE 390
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1668-2199 |
3.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1668 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQS------EHASFAEKTAQLERTL 1739
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKlekevkELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1740 KEEHVAVVQLRE---EATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREA 1816
Cdd:PRK03918 248 ESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1817 RRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR--LQREA 1886
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeeIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1887 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQ-RQLAE 1964
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKElRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1965 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERlRRLAEDEAFQRRLLEEqaAQHKADIEARLAQLRKA 2044
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK-EKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2045 SEsELERQKGLVEDTLRQR-----RQVEEEILALKGSFEK---AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQR 2116
Cdd:PRK03918 565 LD-ELEEELAELLKELEELgfesvEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2117 QLAAEEERRrreaeervqKSLAAEEEAARQRKAALE---EVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQ 2191
Cdd:PRK03918 644 ELRKELEEL---------EKKYSEEEYEELREEYLElsrELAGLRAELEELEKRREEIKKtlEKLKEELEEREKAKKELE 714
|
....*...
gi 1920237940 2192 AEEKAHAF 2199
Cdd:PRK03918 715 KLEKALER 722
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1505-1599 |
3.89e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.42 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1505 LAEVEAALEKQRQLAEAHAQAKAQAEREAqglqRRMQEEVARREEVAVEAQEQKRSIQEELQHLR-QSSEAEIQAKARQV 1583
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 1920237940 1584 EAAERSRLRI---EEEIRV 1599
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3864-3899 |
3.93e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.93e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1920237940 3864 RQLLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPE 3899
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1497-2201 |
4.48e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 53.27 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1497 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-EAQGlqrrmqeevarrEEVAVEAQEQKRSIQEELQHLRQsseae 1575
Cdd:PRK10246 168 ERAELLEELTGTEIYGQISAMVFEQHKSARTELEKlQAQA------------SGVALLTPEQVQSLTASLQVLTD----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1576 iqakarqveaaersrlriEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvQDETQRKRQ 1655
Cdd:PRK10246 231 ------------------EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-------QPQLAALSL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1656 AEAELALRVQAEaeaarEKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQrsaeaELQSEHASFAEKTAql 1735
Cdd:PRK10246 286 AQPARQLRPHWE-----RIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLA-- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1736 ertlkeEHVAVVQLREE-----ATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLtqaeaekqke 1810
Cdd:PRK10246 354 ------EHDRFRQWNNElagwrAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQ---------- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1811 eaerearrrgKAEEQAVRQR--ELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqREAAA 1888
Cdd:PRK10246 418 ----------HAEQRPLRQRlvALHGQIVPQQKRLAQ-LQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-KTICE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1889 ATQKRRELEAELAKVRAEMEVLL--ASKARAEEESRS-TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1965
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQAlEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1966 DAvRQRAEAERVLAEKLAAISEA--TRLKTEAEIA--LKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKADIEARLA 2039
Cdd:PRK10246 566 EA-QSLRQEEQALTQQWQAVCASlnITLQPQDDIQpwLDAQEEHERQLRLLSQRHELQGQIAAhnQQIIQYQQQIEQRQQ 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2040 QLR----------------------KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 2097
Cdd:PRK10246 645 QLLtalagyaltlpqedeeaswlatRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2098 AEDTLRSK-----EQAEQEAARQRQLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEevERLKAKVEEARRLRER 2170
Cdd:PRK10246 725 QCLSLHSQlqtlqQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAAllDEETLTQLEQLK--QNLENQRQQAQTLVTQ 802
|
730 740 750
....*....|....*....|....*....|.
gi 1920237940 2171 AEQESARQLQLAQEAAQKRLQAEEKAHAFAV 2201
Cdd:PRK10246 803 TAQALAQHQQHRPDGLDLTVTVEQIQQELAQ 833
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4069-4106 |
5.12e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 5.12e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1920237940 4069 QRFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 4106
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1447-1661 |
5.19e-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: 52.07 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1447 KVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1521
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1522 --HAQAKAQAEREAQGLQRRMQeevARREEVaveaqEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrv 1599
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAP---ARREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 1600 vrlqleaTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1661
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1962-2662 |
5.20e-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: 53.13 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1962 LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQhkadiEARLAQL 2041
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQ-----LESSREI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2042 RKASESEL----ERQKGlVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ 2117
Cdd:TIGR00606 240 VKSYENELdplkNRLKE-IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2118 laaeeerrrrEAEERVQKSLAAEEEAAR---QRKAALE-EVERLKAKVE---EARRLRERAEQESARQLQLAQEAAQKRL 2190
Cdd:TIGR00606 319 ----------RELVDCQRELEKLNKERRllnQEKTELLvEQGRLQLQADrhqEHIRARDSLIQSLATRLELDGFERGPFS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2191 QAE-EKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQ 2269
Cdd:TIGR00606 389 ERQiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2270 AQAQAQAAAEKLRKEAE---------------QEAARRAQAEQAALRQKQAADAEME----------------KHKQFAE 2318
Cdd:TIGR00606 469 SSDRILELDQELRKAERelskaeknsltetlkKEVKSLQNEKADLDRKLRKLDQEMEqlnhhtttrtqmemltKDKMDKD 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2319 QALRQ-KAQVEQELTAL------RLQLEETDHQKS----ILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGklk 2387
Cdd:TIGR00606 549 EQIRKiKSRHSDELTSLlgyfpnKKQLEDWLHSKSkeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE--- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2388 ariEAENRALVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQeaaRLRQLAEED-----LAQQRALAEKMLKEKMQA 2461
Cdd:TIGR00606 626 ---DKLFDVCGSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQ---FITQLTDENqsccpVCQRVFQTEAELQEFISD 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2462 VQEATRLkAEAELLQQQKELAQEQARRlqEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSR--AQ 2539
Cdd:TIGR00606 700 LQSKLRL-APDKLKSTESELKKKEKRR--DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllGT 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2540 ARAEEDARRFRKQAEDIGERLYRtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEM 2619
Cdd:TIGR00606 777 IMPEEESAKVCLTDVTIMERFQM-ELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1920237940 2620 QTVRQeQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2662
Cdd:TIGR00606 856 QEQIQ-HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
313-420 |
6.61e-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: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 313 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 391
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1920237940 392 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 420
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2417-2633 |
7.19e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.77 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2417 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2496
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2497 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKvmlvQT 2576
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 2577 LETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA 2633
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1370-1689 |
7.39e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.75 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1370 KQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQ 1449
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1450 SGSESIIQEYVDLRTRYSELSTLTSQ---YIRFISETLRRMEeeerlaeQQRAEERERLAEVEAALEKQRQLAEAHAQAK 1526
Cdd:PRK10929 102 MSTDALEQEILQVSSQLLEKSRQAQQeqdRAREISDSLSQLP-------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1527 AQAereaqglqrrMQEEVARReevaveaqeqkRSIQEELQhLRQSSEAEIQAKAR-QVEAAERSRLRIEEEIRVVRLQLE 1605
Cdd:PRK10929 175 LTA----------LQAESAAL-----------KALVDELE-LAQLSANNRQELARlRSELAKKRSQQLDAYLQALRNQLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1606 aTERQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ-------AEAEAAREKQRAL 1678
Cdd:PRK10929 233 -SQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQrmdliasQQRQAASQTLQVR 299
|
330
....*....|.
gi 1920237940 1679 QALEELRLQAE 1689
Cdd:PRK10929 300 QALNTLREQSQ 310
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2318-2757 |
7.56e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2318 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenral 2397
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2398 vLRDKDSAQRLLQEEAEKMKQVAEEaarlsvaaqeaaRLRQLAEedlaqQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2477
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE------------KIRELEE-----RIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2478 QKELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMsRAQARAEEDARRFRKQAED 2555
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSrlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2556 IGERLyrTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKS---------EEMQTVRQEQ 2626
Cdd:PRK03918 377 LKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK--KAIEELKKakgkcpvcgRELTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2627 LLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEvAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAE 2706
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2707 EGVRRQQEELQRLAqQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2757
Cdd:PRK03918 532 EKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1533-2169 |
7.71e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1533 AQGLQR---RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATER 1609
Cdd:pfam05483 73 SEGLSRlysKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1610 QRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElaLRVQAEaeaarekqralQALEELRLQAE 1689
Cdd:pfam05483 153 TRHLCN-LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1690 EAERRLRQAEAERARQV-----QVALETAQrSAEAELQSEHASF-----AEKTAQLERTLKEEHVAVVQLREEATRRAqq 1759
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEIndkekQVSLLLIQ-ITEKENKMKDLTFlleesRDKANQLEEKTKLQDENLKELIEKKDHLT-- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1760 qaeaeraraeaerelerwqlKANEALRLRLQaEEVAQQKSLTQAEAEKQkeeaerearrrgKAEEQAVRQRELAEQELEK 1839
Cdd:pfam05483 296 --------------------KELEDIKMSLQ-RSMSTQKALEEDLQIAT------------KTICQLTEEKEAQMEELNK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1840 QR---QLAEGTAQQRLAAEQELIRLRAET-EQGEQQRQLLEEELARLQREAAAATQ----KRRELEaELAKVRAEMEVLL 1911
Cdd:pfam05483 343 AKaahSFVVTEFEATTCSLEELLRTEQQRlEKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1912 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1991
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1992 kteaeialkekeaENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL--VEDTLRQRR----- 2064
Cdd:pfam05483 500 -------------ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkc 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2065 ---QVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKsLAAEE 2141
Cdd:pfam05483 567 kldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELEL 645
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1920237940 2142 EAARQR-------------------KAALEEVERLKAKVEEARRLRE 2169
Cdd:pfam05483 646 ASAKQKfeeiidnyqkeiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2379-2759 |
8.11e-06 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 52.30 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2379 QMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2458
Cdd:COG5281 1 AAALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2459 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2538
Cdd:COG5281 81 AAALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2539 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2618
Cdd:COG5281 161 AAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2619 MQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEA 2698
Cdd:COG5281 241 SAAAQALAALAAAAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2699 R-RRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2759
Cdd:COG5281 321 AqALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWA 382
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2459-2604 |
8.40e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 52.33 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2459 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQ-QLAQetQGFQKTLETERQRQLEMSAEAERLR 2529
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2530 LRVAEMSRAQARAEEDARRFRKQAEdigerLYRTEL-ATQEKVMLVQTLETQRQQSDRDAERlREAIAELEHEKDK 2604
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1546-1899 |
8.58e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1546 RREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1625
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1626 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1705
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1706 VQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1785
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1786 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1865
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 1920237940 1866 EQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1899
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2300-2747 |
8.84e-06 |
|
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: 52.13 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTalrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVE-----EELF 2374
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2375 SLRVQMEELgklKARIEAENRALVLRDkDSAQRLL---QEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2451
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLemlQSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2452 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLAQETQgfqkTLETErqrqLEMSAEAERLRLR 2531
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQ----MLKTN----GLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2532 VAEMSRAQARaeedarrFRK-QAEDIGERLYRTE---LATQEKVmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQ 2607
Cdd:pfam10174 276 QMEVYKSHSK-------FMKnKIDQLKQELSKKEselLALQTKL---ETLTNQNSDCKQHIEVLKESLTAKEQRAAILQT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2608 EAQLLQLKSEEMQTV-----RQEQLLQETQALQQSFLSE-KDSLLQRERCIEQEKAKLEQL---FQDEVAKAQALREEQQ 2678
Cdd:pfam10174 346 EVDALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLqeqLRDKDKQLAGLKERVK 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2679 RQQQQMQQEKQQLAaSMEEARRrqhEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2747
Cdd:pfam10174 426 SLQTDSSNTDTALT-TLEEALS---EKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPE 490
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1519-1734 |
9.12e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1519 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrlRIEEEIR 1598
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1599 VVRLQLEATERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDETQRKRQAEA 1658
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1659 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1734
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4071-4109 |
9.51e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 9.51e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 4071 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 4109
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2468-2754 |
9.76e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2468 LKAEAELLQQQKELAQEQARRlqedkEQMAQQLAQETQGfQKTLETERQrqlemsAEAERLRLRVAEMsraqaRAEEDAR 2547
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRL-----VEMARELEELSAR-ESDLEQDYQ------AASDHLNLVQTAL-----RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2548 RFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEA----QLLQLKsEEMQTVR 2623
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQAL-EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2624 Q---------EQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQ------DEVAKAQA-------LREEQQRQQ 2681
Cdd:COG3096 430 GlpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiaGEVERSQAwqtarelLRRYRSQQA 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2682 QQMQQEKqqLAASMEEARRRQHEAEEgVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2754
Cdd:COG3096 510 LAQRLQQ--LRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1495-1649 |
9.84e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1495 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaqglQRRMQEEVARREEVAVEAQEQKRSIqeelqhlrqSSEA 1574
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNV---------RNNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1575 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1649
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1619-1883 |
1.01e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1619 QALRARAEEAEAQKRQAQEEAERLRRQVqDETQRKRQA--EAELALRVQAEAEAAREKQRALQA-LEELRLQAEEAERRL 1695
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1696 RQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerele 1775
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI---------------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1776 rwqlkanEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgKAEEQAVRQRelaEQELEKQRQLAEGTAQQRLAAE 1855
Cdd:COG3206 301 -------AALRAQLQQEAQRILASL--------------------EAELEALQAR---EASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*...
gi 1920237940 1856 QELIRLRAETeqgEQQRQLLEEELARLQ 1883
Cdd:COG3206 351 AELRRLEREV---EVARELYESLLQRLE 375
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1463-1604 |
1.08e-05 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 50.37 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1463 RTRYSELSTLTSQYIRFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaqakAQAEREAQglqR 1538
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKR----------YQDQLEAQ---R 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1539 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1604
Cdd:pfam12037 123 RRNEELLRKQEESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQ 188
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1986-2739 |
1.09e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1986 SEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQ 2065
Cdd:NF041483 22 AEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRNAQIQADQLRADAERELRDARA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2066 VEEEIlaLKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQ----------AEQEAARQRQLAAEEERRRREAEERVQK 2135
Cdd:NF041483 102 QTQRI--LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnenvAWAEQLRARTESQARRLLDESRAEAEQA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2136 SLAAEEEAARqrkAALEEVERLKAKVEEARRLRE----RAEQESARQLQLAQEAAQKRLQAEEKAHAF-------AVQQK 2204
Cdd:NF041483 180 LAAARAEAER---LAEEARQRLGSEAESARAEAEailrRARKDAERLLNAASTQAQEATDHAEQLRSStaaesdqARRQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2205 EQELQQTLQQEQSVLERLR-----SEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAE 2279
Cdd:NF041483 257 AELSRAAEQRMQEAEEALRearaeAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2280 KLRKEAEQEAARRAQAEQAALRQKQAAdAEMEKHKQFAEQALRQKAQVEQELTalRLQLEETDHQKSILDEELQRLKAEV 2359
Cdd:NF041483 337 ADARAEAEKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLTKASEDAKATT--RAAAEEAERIRREAEAEADRLRGEA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2360 TEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAAR-----LSVAAQEA 2433
Cdd:NF041483 414 ADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARtaeelLTKAKADA 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2434 ARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAQQLAQETQGFQKTLE 2512
Cdd:NF041483 494 DELRSTATAESERVRTEAiERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQ 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2513 TERQRQLE-MSAEAERlRLRVAEMSRAQARAEedARRFRKQAEDIGERLyRTELAtqekvmlvQTLETQRQQSDRDAERL 2591
Cdd:NF041483 571 AEAAEELTrLHTEAEE-RLTAAEEALADARAE--AERIRREAAEETERL-RTEAA--------ERIRTLQAQAEQEAERL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2592 R-EAIAELEHEkdKLKQEAQLLQLKSEEMQtvRQEQLLQETQALQQSFLSEKDSLLQRercIEQEKAKleqlfqdevaka 2670
Cdd:NF041483 639 RtEAAADASAA--RAEGENVAVRLRSEAAA--EAERLKSEAQESADRVRAEAAAAAER---VGTEAAE------------ 699
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2671 qalreeqqrqqqqmqqekqQLAASMEEARRRQHEAEEGVRRQQEEL-QRLAQQQQQQEKLLAEENQRLRE 2739
Cdd:NF041483 700 -------------------ALAAAQEEAARRRREAEETLGSARAEAdQERERAREQSEELLASARKRVEE 750
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1005-1655 |
1.09e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1005 NQEAQEAIARlEAQHQALVALWhQLHTEMKSLLAWQSLGRDMQlirsWSLATFRTLKPEE------------QRQALRsL 1072
Cdd:TIGR00618 223 VLEKELKHLR-EALQQTQQSHA-YLTQKREAQEEQLKKQQLLK----QLRARIEELRAQEavleetqerinrARKAAP-L 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1073 ELHYQAFLRDSQDAGGFGPEDRLQaEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRL 1152
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1153 PLDKEPARECAQRIT----EQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAptlRSELELTLGKLEQVRSLSAIYL 1228
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTtltqKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA---KKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1229 EKLKtisLVIRSTQEAEEVLRAHEEQLKEAQAVpaTLPELEATKAALKKLRAQAEAQQPVFDALR---------DELRGA 1299
Cdd:TIGR00618 452 QCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1300 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakqRQEQIQAV 1379
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1380 PLansqaVREQLRQEKALLEDIERHGEKVEECQRFAK--QYINAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESIIQ 1457
Cdd:TIGR00618 598 DL-----TEKLSEAEDMLACEQHALLRKLQPEQDLQDvrLHLQQCSQELALKLTALHALQ--LTLTQERVREHALSIRVL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1458 EYVDLRTRYSELSTLTSQY--IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQG 1535
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1536 LQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1615
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE 830
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1920237940 1616 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ 1655
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2580-2769 |
1.11e-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: 51.30 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2580 QRQQSDRDAERLREAIAELEHEKDKLKQEAQLL--QLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2657
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALlkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2658 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME------EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2731
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237940 2732 EENQRLRERLQHLEEERRAALARSEEIAPSRAAAARAL 2769
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1483-1699 |
1.24e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.41 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1483 TLRRMEEEERLAEQQRAEERERLAEVEAALEkqrqlaEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1562
Cdd:pfam02029 134 EIREKEYQENKWSTEVRQAEEEGEEEEDKSE------EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1563 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRV-VRLQLEATERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAE 1640
Cdd:pfam02029 208 KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLeAEQKLEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKRE 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1641 RLRRQVQDETQRKRQAEAELALRVQaeaeaaREKQRALQALEelRLQAEEAERRLRQAE 1699
Cdd:pfam02029 288 ERRKLLEEEEQRRKQEEAERKLREE------EEKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2300-2602 |
1.24e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.22 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHkqfAEQALRQKAQVEQELTALRLQLEETDHQksildeeLQRLKAEVTEAARQRGQVEEELFSLRVQ 2379
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2380 MEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2458
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2459 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLEterqrqlEMSAEAERLRLRVAEMSRA 2538
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRLA-------GLEADLERRTQQFQEMQRA 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 2539 QARAEEDARRFRKQAEDIGERLYRTE---LATQEKV-MLVQTLETQRQQSDRDAERLREaiaELEHEK 2602
Cdd:pfam19220 320 RAELEERAEMLTKALAAKDAALERAEeriASLSDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1883-2204 |
1.29e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1883 QREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRlEAEAGRFRELAEEAARLralaeEAKRQRQL 1962
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM-----AMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1963 AEEDAVRQRAEAERVLAEKLAAisEATRLKtEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 2042
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2043 KASESELERQ-KGLVEDTLRQRRQVEEEilalkgsfekaaagKAELELELGRIRGTAEDTLRSKEQAEQEaaRQRQLAAE 2121
Cdd:pfam17380 427 AEQEEARQREvRRLEEERAREMERVRLE--------------EQERQQQVERLRQQEEERKRKKLELEKE--KRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2122 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHA 2198
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRL 568
|
....*.
gi 1920237940 2199 FAVQQK 2204
Cdd:pfam17380 569 EAMERE 574
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1093-1663 |
1.36e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1093 DRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLRlpldkepaRECAQRITEQQK 1171
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLR--------RELDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1172 AQAEVDGL-----GKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEE 1246
Cdd:pfam15921 431 LEALLKAMksecqGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1247 VlraheeqlkeaqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRER 1323
Cdd:pfam15921 511 A--------------------IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1324 VTLLLE-------RWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLR--DAKQRQEQIQAVPLANSQAvrEQLRQE 1394
Cdd:pfam15921 571 IENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGS--ERLRAV 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1395 KALLEDIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesiiqeyvdLRTRYSELSTLTS 1474
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1475 qyirfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAHAQAKAqaereaqglqrrMQEEVARREEVAVEA 1554
Cdd:pfam15921 714 --------TLKSMEGSDGHA-------------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNA 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1555 QEQKRSIQEELQHLRQsseaeiqakarqveaaersrlrieeeirvvRLQLEATERQRggAEGELQALRA---RAEEAEAQ 1631
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQ------------------------------ELSTVATEKNK--MAGELEVLRSqerRLKEKVAN 808
|
570 580 590
....*....|....*....|....*....|..
gi 1920237940 1632 KRQAQEEAERLRRQVQDETQRKRQAEAELALR 1663
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1096-1534 |
1.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1096 QAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRITE 1168
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1169 QQKAQAEVDGLGKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVL 1248
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1249 R------AHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRE 1322
Cdd:COG4717 233 EneleaaALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1323 RVTLLLERWQAVLAQTDVRQREleqlgrQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIE 1402
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE-AGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1403 RHGEKVEECQRFaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEyvdLRTRYSELSTLTSQYIRFISE 1482
Cdd:COG4717 386 ELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE---LEELEEELEELREELAELEAE 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1483 tLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQ 1534
Cdd:COG4717 462 -LEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1098-1741 |
1.50e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1098 EREYGSCSRHYQQLLQSLEQGEQEEsrcqRCISELKDIRLQLEAcetrtvhrlRLPLDKEPARECAQRITEQQKAQAEVD 1177
Cdd:PRK04863 327 EQDYQAASDHLNLVQTALRQQEKIE----RYQADLEELEERLEE---------QNEVVEEADEQQEENEARAEAAEEEVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1178 GLGKGVA--------------------RLSAEAEKVLALPEPSPA-----APTLRSEL-ELTLGKLE---QVRSLSAIYL 1228
Cdd:PRK04863 394 ELKSQLAdyqqaldvqqtraiqyqqavQALERAKQLCGLPDLTADnaedwLEEFQAKEqEATEELLSleqKLSVAQAAHS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1229 EKLKTISLVIR-----STQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKK-LRAQAEAQQpvfdaLRDELRGAQEV 1302
Cdd:PRK04863 474 QFEQAYQLVRKiagevSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQrLRQQQRAER-----LLAEFCKRLGK 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1303 G-------ERLQQRHGER----DVEVERWRERVTLLlerwQAVLAQTDVRQRELEQLGRQLRYYRESADPL----GAWLR 1367
Cdd:PRK04863 549 NlddedelEQLQEELEARleslSESVSEARERRMAL----RQQLEQLQARIQRLAARAPAWLAAQDALARLreqsGEEFE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1368 DAKQRQEQIQ--AVPLANSQAVREQLRQEK-ALLEDIER----HGEKVEECQRFAKQ-------------------YINA 1421
Cdd:PRK04863 625 DSQDVTEYMQqlLERERELTVERDELAARKqALDEEIERlsqpGGSEDPRLNALAERfggvllseiyddvsledapYFSA 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1422 -------------IKDYELQLVT--------YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSelstltsqyiRFI 1480
Cdd:PRK04863 705 lygparhaivvpdLSDAAEQLAGledcpedlYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYS----------RFP 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1481 SETL-RRMEEEERLAEQQRaeERERLAEveaalekqrqlaeahaqAKAQAEREAQGLQRRMQ---EEVARREEVAVEAQE 1556
Cdd:PRK04863 775 EVPLfGRAAREKRIEQLRA--EREELAE-----------------RYATLSFDVQKLQRLHQafsRFIGSHLAVAFEADP 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1557 qkrsiqeelqhlrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGEL--------QALRARAEEA 1628
Cdd:PRK04863 836 ----------------EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLprlnlladETLADRVEEI 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1629 EAQKRQAQEEAERLRRQVQDETQRKRQA------EAELAlRVQAEAEAAREKQRALQ----ALEEL-------------R 1685
Cdd:PRK04863 900 REQLDEAEEAKRFVQQHGNALAQLEPIVsvlqsdPEQFE-QLKQDYQQAQQTQRDAKqqafALTEVvqrrahfsyedaaE 978
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 1686 LQAEEAE------RRLRQAEAERARQVQVALETAQRSAE-----AELQSEHASFAEKTAQLERTLKE 1741
Cdd:PRK04863 979 MLAKNSDlneklrQRLEQAEQERTRAREQLRQAQAQLAQynqvlASLKSSYDAKRQMLQELKQELQD 1045
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1228-1696 |
1.59e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.28 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1228 LEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraQAEAQQpVFDALRDELRGAQEVGERLQ 1307
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1308 QRHGERDVEVERWRERVTLLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLRDAKQRQEQIqavpl 1381
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1382 ANSQAVREQLRQEKALL----EDIERHGEKVEECQRFAKQYinaiKDYELQLVTYKAQLEPVASPAKK------------ 1445
Cdd:pfam05557 200 PELEKELERLREHNKHLneniENKLLLKEEVEDLKRKLERE----EKYREEAATLELEKEKLEQELQSwvklaqdtglnl 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1446 PKVQSGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL------ 1518
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREIVLKEENSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltke 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1519 ----------------AEAHAQAKAQAEREAQGLQRRMQ---EEVARREEVAVEA----QEQKRSIQEELQHLRQ----- 1570
Cdd:pfam05557 355 rdgyrailesydkeltMSNYSPQLLERIEEAEDMTQKMQahnEEMEAQLSVAEEElggyKQQAQTLERELQALRQqesla 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1571 ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1647
Cdd:pfam05557 435 dpsYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIE 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 1648 --DETQRKRQAEAELALRVQAEAEAAREKQralqaLEELRLQAEEAERRLR 1696
Cdd:pfam05557 515 rlKRLLKKLEDDLEQVLRLPETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1853-1948 |
1.61e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.49 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1853 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1932
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 1920237940 1933 EAEAGRFrELAEEAAR 1948
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1821-2043 |
1.77e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.05 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQAVRQRELAEQELEK-QRQLAEgtaqqrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRE-LEA 1898
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDmEEDLVE--------ARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1899 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1978
Cdd:COG1842 88 EALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1979 AEklaaiseatrlkteAEIALKEKEAENERLRRLAEDEAFQRRLLEeqaAQHKADIEARLAQLRK 2043
Cdd:COG1842 168 ER--------------MEEKIEEMEARAEAAAELAAGDSLDDELAE---LEADSEVEDELAALKA 215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1553-1690 |
1.94e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1553 EAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQA 1620
Cdd:COG1579 21 RLEHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1621 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEE 1690
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1412-1743 |
1.99e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.17 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1412 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESIIQEYVDLRTRY-SELSTLTSQyirfiSETLRRMEEE 1490
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1491 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ----RRMQEEVArreEVAVEAQEQKRSIQEELQ 1566
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPtntyKTLELEIA---ESDVEVKKAELELVKEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1567 HLRQSSEAEIQAKAR-QVEAAERSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRARAEEAEAQKRQA--------- 1635
Cdd:NF033838 198 KEPRDEEKIKQAKAKvESKKAEATRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlgepa 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1636 -----QEEAERLRRQVQDET-------QRKRQAEAE-LALRVQAEAEAAREKQR---ALQALEELRLQAEEAERRLRQAE 1699
Cdd:NF033838 275 tpdkkENDAKSSDSSVGEETlpspslkPEKKVAEAEkKVEEAKKKAKDQKEEDRrnyPTNTYKTLELEIAESDVKVKEAE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237940 1700 A----ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEH 1743
Cdd:NF033838 355 LelvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3940-3976 |
2.19e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.19e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 3940 LRLLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDT 3976
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2316-2547 |
2.21e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 50.46 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2316 FAEQALRQKAQ---VEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQrgqveeelfsLRVQMEELGKLKARIEA 2392
Cdd:PRK11637 38 FSAHASDNRDQlksIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRK----------LRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2393 ENRalvlrdkdSAQRLLQEEAEKMKqvaeeaarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA----VQEAtRL 2468
Cdd:PRK11637 108 LNA--------SIAKLEQQQAAQER---------LLAAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgyLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2469 KAEAELLQQQKELAQEqaRRLQEDKEQMAQQLAQETQGFQKTLETER-----------------QRQL-EMSAEAERLRL 2530
Cdd:PRK11637 170 ETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEQARnerkktltglesslqkdQQQLsELRANESRLRD 247
|
250
....*....|....*...
gi 1920237940 2531 RVAEMSR-AQARAEEDAR 2547
Cdd:PRK11637 248 SIARAEReAKARAEREAR 265
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1830-2542 |
2.21e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1830 RELAEQELEKQRQLAEGTAQQRLAAE---QELIRLRAETEQGEQQRQLLEEELARLQ-REAAAATQK-RRELEAELA--- 1901
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKiLRELDTEISylk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1902 ----KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1976
Cdd:pfam15921 238 grifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1977 VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQL-----RKASESELER 2051
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEK 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2052 QK-----------GLVEDTLRQR---RQVEEEIL-ALKGSFEKAAAGkaELELELGRIRGtaedtlrSKEQAEQEAARQR 2116
Cdd:pfam15921 398 EQnkrlwdrdtgnSITIDHLRRElddRNMEVQRLeALLKAMKSECQG--QMERQMAAIQG-------KNESLEKVSSLTA 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2117 QLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEEVER-LKAKVEEARRLRERAEQesarQLQLAQEaaqkrLQAE 2193
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLEssERTVSDLTASLQEKERaIEATNAEITKLRSRVDL----KLQELQH-----LKNE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2194 EKaHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraereaaqsrRQVEEAERLkqsaeeqaqaqaq 2273
Cdd:pfam15921 540 GD-HLRNVQTECEALKLQMAEKDKVIEILR----------------------------QQIENMTQL------------- 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2274 aqaaaeklrkeaeqeaarraqaeqaalrqkqaadaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQ 2353
Cdd:pfam15921 578 ------------------------------------VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2354 RLKAEVTEAARQRGQV----EEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEE-AARL 2426
Cdd:pfam15921 622 ELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKlKMQL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2427 SVAAQEAARLR---QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAqe 2503
Cdd:pfam15921 702 KSAQSELEQTRntlKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS-- 779
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1920237940 2504 tqgfqkTLETERQR---QLE-MSAEAERLRLRVAEMSRAQARA 2542
Cdd:pfam15921 780 ------TVATEKNKmagELEvLRSQERRLKEKVANMEVALDKA 816
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1494-1922 |
2.28e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1494 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1573
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1574 AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1653
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1654 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1733
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1734 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1813
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1814 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1893
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 1920237940 1894 RELEAELAKVRAEMEVLLASKARAEEESR 1922
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2300-2505 |
2.38e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADA-----EMEKHKQFAEQALRQKaqveqeltalrlQLEETDH---------QKSILDEELQRLKAEVTEAARQ 2365
Cdd:NF012221 1561 LADKERAEAdrqrlEQEKQQQLAAISGSQS------------QLESTDQnaletngqaQRDAILEESRAVTKELTTLAQG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2366 RGQVEEElfslRVQMEELGKlKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQ--------VAEEAARLSVAAQEAAR 2435
Cdd:NF012221 1629 LDALDSQ----ATYAGESGD-QWRNPFAGGLLdrVQEQLDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSEAGVAQGEQ 1703
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2436 LRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQ 2505
Cdd:NF012221 1704 NQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1680-2118 |
2.45e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 50.79 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1680 ALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQ---------LR 1750
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1751 EEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR 1830
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1831 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVL 1910
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1911 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATR 1990
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1991 LKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEI 2070
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1920237940 2071 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQL 2118
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
213-300 |
2.52e-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: 46.67 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 213 LYEDLRDGHNLISLLEvlsgDSLPRERDVIRSSRLPRE-KGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKL 291
Cdd:cd21294 38 LFDECKDGLVLSKLIN----DSVPDTIDERVLNKPPRKnKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHL 113
|
....*....
gi 1920237940 292 TLGLIWTII 300
Cdd:cd21294 114 ILGLIWQII 122
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1480-1685 |
2.63e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.67 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1480 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-REEVAVEAQEQK 1558
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1559 RSIQEELQHLRQsseaeiqakarQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKR----- 1633
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1634 ------QAQEEAERLRRQVqDETQRKRQAEAELALR--VQAEAEAAREKQRALQALEELR 1685
Cdd:COG1842 156 sgidsdDATSALERMEEKI-EEMEARAEAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1778-2196 |
2.75e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1778 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1857
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1858 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1937
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1938 RFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA 2017
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2018 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 2097
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2098 AEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2177
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 1920237940 2178 QLQLAQEAAQKRLQAEEKA 2196
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2300-2750 |
2.84e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFA--EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSL 2376
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTklQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTlDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2377 R----VQMEELGKLKARIEA-ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---------RLRQLAEE 2442
Cdd:pfam12128 307 NgelsAADAAVAKDRSELEAlEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKhqdvtakynRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2443 DLA------QQRALAEKMLKEKMQAVQEATRLKAEAEL---LQQQKELAQEQARRLQEDKEQMAQQLAQETQGfQKTLET 2513
Cdd:pfam12128 387 QNNrdiagiKDKLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2514 ERQRQLEMSAEAERLRLRVAEMSRAQaraeEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQ-RQQSDRDAERLR 2592
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQ----SELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2593 EAIAELEHEKDKLKQEAQL----LQLKSEEMQTVRQEQLLQETQALQQSflsEKDSLLQRERCIEQEKAKLEQLFQDEVA 2668
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLhrtdLDPEVWDGSVGGELNLYGVKLDLKRI---DVPEWAASEEELRERLDKAEEALQSARE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2669 KAQALreeqqrqqqqmQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLA----QQQQQQEKLLAEENQRLRERLQHL 2744
Cdd:pfam12128 619 KQAAA-----------EEQLVQANGELEKASREETFARTALKNARLDLRRLFdekqSEKDKKNKALAERKDSANERLNSL 687
|
....*.
gi 1920237940 2745 EEERRA 2750
Cdd:pfam12128 688 EAQLKQ 693
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1824-2534 |
2.88e-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: 50.49 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR-----LQREAAAATQKRRELEA 1898
Cdd:pfam05483 98 EAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1899 ELAKVR---AEMEVLLASKARAEEESRSTSEKSkqRLEAEAgrfrELAEEAARLRALAEEAKRQRQlaeedavrqraEAE 1975
Cdd:pfam05483 177 EREETRqvyMDLNNNIEKMILAFEELRVQAENA--RLEMHF----KLKEDHEKIQHLEEEYKKEIN-----------DKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1976 RVLAEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRLLEeQAAQHKADIEARLAQLRKASESELERQKGL 2055
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESR---DKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2056 VED---TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEerrrreaeer 2132
Cdd:pfam05483 316 EEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2133 VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEK-AHAFAVQqkeqeLQ 2209
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeIHDLEIQ-----LT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2210 QTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqea 2289
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM----------------------------- 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2290 arraqaeQAALRQKQAadaEMEKHKQFAEQALRQKAQVEQELTALRLQLE--------ETDHQKSILD---EELQRLKAE 2358
Cdd:pfam05483 512 -------TLELKKHQE---DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqKGDEVKCKLDkseENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2359 VTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRAlvLRDKDSAQRlLQEEAEKMKqVAEEAARLSVAAQEAARLRQ 2438
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKA--LKKKGSAEN-KQLNAYEIK-VNKLELELASAKQKFEEIID 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2439 LAEEDLAQQRALAEKMLKEKMQA---VQEATRLKAEAELLQQQK--------ELAQEQARRLQEDKEQ---MAQQLAQET 2504
Cdd:pfam05483 658 NYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIDKRCQHKiaemvalmEKHKHQYDKIIEERDSelgLYKNKEQEQ 737
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1920237940 2505 QGFQKTLETER----------QRQLEMS-AEAERLRLRVAE 2534
Cdd:pfam05483 738 SSAKAALEIELsnikaellslKKQLEIEkEEKEKLKMEAKE 778
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1480-1704 |
3.06e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.25 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1480 ISETLRRMEEEERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQglqRRMQEEVARREEVavEAQEQKR 1559
Cdd:pfam02029 100 VAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVRQAE---EEGEEEEDKSEEA--EEVPTEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1560 SIQEELQHLRQSSEAEIQAKARQVEaaERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEA 1639
Cdd:pfam02029 174 FAKEEVKDEKIKKEKKVKYESKVFL--DQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL-EAEQKL 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1640 ERLRRQVQD------ETQRKRQAEAELALrvqAEAEAAREKQRAL--------QALEELRLQAEEAERRLRQAEAERAR 1704
Cdd:pfam02029 251 EELRRRRQEkeseefEKLRQKQQEAELEL---EELKKKREERRKLleeeeqrrKQEEAERKLREEEEKRRMKEEIERRR 326
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1571-1784 |
3.10e-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: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1571 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1648
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1649 -ETQRKRQAEAELAL------------RVQAEAEAAREKQRALQALEELRLQAEEAerrlrQAEAERARQVQVALETAQR 1715
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1716 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEA 1784
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1451-1753 |
3.11e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1451 GSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQ--------RQLAEAH 1522
Cdd:pfam19220 63 AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA-LERQlaaeteqnRALEEEN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1523 AQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRsiqeeLQHLRQSSEAEIQAKARQVE------AAERSRLRIEEe 1596
Cdd:pfam19220 142 KALREEAQAAEKALQRAEGELATARERLALLEQENRR-----LQALSEEQAAELAELTRRLAeletqlDATRARLRALE- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1597 irvVRLQLEATERQRGGAEGELQALRARAEEAEaqkrqaqeeaerLRRQVQDETQRKRQAE---AELALRVQAEAEAARE 1673
Cdd:pfam19220 216 ---GQLAAEQAERERAEAQLEEAVEAHRAERAS------------LRMKLEALTARAAATEqllAEARNQLRDRDEAIRA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1674 KQRalqALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSE--HASFAEKTAQLERTlkEEHVAVVQLRE 1751
Cdd:pfam19220 281 AER---RLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEmlTKALAAKDAALERA--EERIASLSDRI 355
|
..
gi 1920237940 1752 EA 1753
Cdd:pfam19220 356 AE 357
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1790-1966 |
3.17e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1790 QAEEVAQQKsltQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1865
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1866 EQGEQQRQLLEEELArlQREAAAATQKRRELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1940
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 1920237940 1941 ELAEEAARLRALAEEAKRQRQLAEED 1966
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1635-1929 |
3.40e-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: 49.76 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1635 AQEEAERLRRQVQDETQRKRQAEAELAlrvqaeaEAAREKQRALQALEELRLQAEEAERRLRQAEAERArqvqvALETAQ 1714
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELA-----ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1715 RSAEAELQSEHASFAEKTAQLERTLKeehvavvqlreeatrraqqqaeaeraraeaerelERWQLKANEALRLRLQAEEV 1794
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLR----------------------------------ALYRLGRQPPLALLLSPEDF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1795 AQqksltqaeaekqKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL 1874
Cdd:COG4942 132 LD------------AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1875 LEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK 1929
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1530-1724 |
3.47e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 50.40 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1530 EREAQGLQRRMQEEVarreEVAVEAQEQKRSIQEELQhlrqsseaEIQAKARqveaAERSRL--RIE-EEIRVVRLQLEA 1606
Cdd:PTZ00491 643 ERTRDSLQKSVQLAI----EITTKSQEAAARHQAELL--------EQEARGR----LERQKMhdKAKaEEQRTKLLELQA 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1607 TerqrgGAEGELQAlRARAE-EAEAQKRQAQEEAErlrrqVQDETQRKRqaeaelALRVQAEAEAAREKQRALQALEELR 1685
Cdd:PTZ00491 707 E-----SAAVESSG-QSRAEaLAEAEARLIEAEAE-----VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQ 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237940 1686 LQAE---EAERRLRQAEAERARQVQVAL--ETAQRSAEA--ELQSE 1724
Cdd:PTZ00491 770 AQNEleiAKAKELADIEATKFERIVEALgrETLIAIARAgpELQAK 815
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1965-2443 |
3.51e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1965 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLleEQAAQHKADIEARLAQLRKA 2044
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2045 seselerqkglvedtLRQRRQVEEEILALKgsfEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEER 2124
Cdd:COG4717 155 ---------------LEELRELEEELEELE---AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2125 RRREAEervqKSLAAEEEAARQRKAALEEVERLKakveearRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQK 2204
Cdd:COG4717 217 EAQEEL----EELEEELEQLENELEAAALEERLK-------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2205 EQELQQTLQQEQSVLERLRseaeaarraaeeaEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKE 2284
Cdd:COG4717 286 LALLFLLLAREKASLGKEA-------------EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2285 AEQEAARRAQAEQAALRQKQAADaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQ-KSILDEELQRLKAEVTEAA 2363
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2364 RQR-GQVEEELFSLRVQMEELGKLKARIEAENRAlvLRDKDSAQRLLQEEAE---KMKQVAEEAARLSVAAQEAARLRQL 2439
Cdd:COG4717 431 EEElEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEElkaELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1920237940 2440 AEED 2443
Cdd:COG4717 509 YREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2319-2546 |
3.86e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2319 QALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKL--KARIEAENRA 2396
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2397 LVLRDKDSAQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2474
Cdd:COG3883 93 RALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2475 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2546
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3493-3528 |
4.26e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.26e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1920237940 3493 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3528
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3493-3531 |
4.35e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.47 E-value: 4.35e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 3493 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3531
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4279-4307 |
4.70e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.70e-05
10 20
....*....|....*....|....*....
gi 1920237940 4279 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4307
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1547-1707 |
5.02e-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: 49.75 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1547 REEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1626
Cdd:pfam07111 490 RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELT 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1627 EAEAQKRQAQEEA-----ERLRRQVQDETQ-----RKRQAEAELALRvQAEAEAAREKQRAlqalEELRLQAEEAerrlR 1696
Cdd:pfam07111 570 QQQEIYGQALQEKvaeveTRLREQLSDTKRrlneaRREQAKAVVSLR-QIQHRATQEKERN----QELRRLQDEA----R 640
|
170
....*....|..
gi 1920237940 1697 QAEAER-ARQVQ 1707
Cdd:pfam07111 641 KEEGQRlARRVQ 652
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1967-2178 |
5.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1967 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIeARLAQLRKASE 2046
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-AELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2047 SELERQKGLVEDTL----RQRRQVEEEILALKGSFEKAAAGKA-------ELELELGRIRGTAEDTLRSKEQAEQEAARQ 2115
Cdd:COG4942 97 AELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQylkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2116 RQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2178
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1494-1891 |
5.21e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1494 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEElqhlrqsse 1573
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1574 aeiqaKARQVEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1653
Cdd:COG3064 75 -----AAKKLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1654 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1733
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1734 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1813
Cdd:COG3064 224 RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAAL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 1814 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1891
Cdd:COG3064 304 AAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLA 381
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1615-1749 |
5.23e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.60 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1615 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDetqRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERR 1694
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1695 LRQAEAERARQ-VQVALETAQRSAEAELQSE-HA---SFAEKTAQLERTLKEEHVAVVQL 1749
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlHQlteTLIQKQTMLEALSTEKNSLVLQL 200
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
186-310 |
5.57e-05 |
|
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: 46.19 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 186 QKKTFTKWVNKHL-----IKHWRAEAQRHISdLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQ 260
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHVVPMNPTDES-LFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTISE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237940 261 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 310
Cdd:cd21323 96 NLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2412-2547 |
5.75e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.10 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2412 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2491
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2492 DKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2547
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1228-1705 |
5.91e-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: 49.66 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1228 LEKLKTISLVIRSTQEA-EEVLRAHEEQLKEAQAVPATLPELEATKAALKKL---RAQAEAQQPVFDALRDELRGA---- 1299
Cdd:TIGR00606 600 LASLEQNKNHINNELESkEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSskqRAMLAGATAVYSQFITQLTDEnqsc 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1300 --------------QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAW 1365
Cdd:TIGR00606 680 cpvcqrvfqteaelQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1366 LRDAKQRQEQIQAVplanSQAVREQLRQEKALLED---IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP 1442
Cdd:TIGR00606 760 IQRLKNDIEEQETL----LGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1443 AKKPKVQSGSE---SIIQEYVD-LRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR---------AEERERLAEVE 1509
Cdd:TIGR00606 836 HELDTVVSKIElnrKLIQDQQEqIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTevqslireiKDAKEQDSPLE 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1510 AALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERS 1589
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV---KNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKH 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1590 RLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALrvqaeae 1669
Cdd:TIGR00606 993 QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL------- 1065
|
490 500 510
....*....|....*....|....*....|....*.
gi 1920237940 1670 AAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1705
Cdd:TIGR00606 1066 IKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
181-306 |
5.92e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 45.36 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 181 ERDRVQKKTFTKWVNKHLIKHWraeaqrhISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQ 260
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237940 261 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 306
Cdd:cd21329 70 NCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1970-2360 |
5.97e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1970 QRAEAERVLAEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadIEARLAQLRKASESEL 2049
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAA-----IYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2050 ERQKglVEDTLRQRRQVEEEilalkgsfekaaagkaELELELGRIRGTaeDTLRSKEQAEQEAARQRqlaaeeerrrrea 2129
Cdd:pfam17380 351 ERIR--QEERKRELERIRQE----------------EIAMEISRMREL--ERLQMERQQKNERVRQE------------- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2130 EERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKeqel 2208
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK---- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2209 qqtlqqeqsvleRLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2288
Cdd:pfam17380 474 ------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2289 aarraqaeqaalRQKQaadAEMEKHKQFAEQALRqkaqVEQELTALRLQLEETDHQKSILDEELQRLKAEVT 2360
Cdd:pfam17380 542 ------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3274-3310 |
6.01e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 6.01e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 3274 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKET 3310
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
340-417 |
6.27e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.60 E-value: 6.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 340 DNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 417
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1844-2340 |
6.41e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.47 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1844 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV----------RAEMEVLLAS 1913
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1914 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKT 1993
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1994 EAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILAL 2073
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2074 KGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2153
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2154 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAA 2233
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2234 EEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2313
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 1920237940 2314 KQFAEQALRQKAQVEQELTALRLQLEE 2340
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2317-2706 |
7.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2317 AEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT--EAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2394
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2395 RALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKekmQAVQEATRLKAEAEL 2474
Cdd:COG4717 156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2475 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLET----------------------ERQRQLEMSAEAERLRLRV 2532
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlgllallfllLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2533 AEMSRAQARAEEDARRFRKQAEDIGER---LYRTELATQEKVMLVQTLETQRQQSDRDAER---LREAIAELEHEKDKLK 2606
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEElleLLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2607 QEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQ 2686
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|
gi 1920237940 2687 EKQQLAASMEEARRRQHEAE 2706
Cdd:COG4717 472 AELLQELEELKAELRELAEE 491
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1563-1937 |
7.44e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1563 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEAT----ERQRGGAEGELQALRARAEEAEAQKRQAQEE 1638
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1639 AERL---RRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAERRLRQAEAERaRQVQVALETAQ- 1714
Cdd:pfam07888 110 SEELseeKDALLAQRAAHEARIRELEEDIKTLTQRVLERE---TELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1715 --RSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLqaE 1792
Cdd:pfam07888 186 elRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV-EGLGEEL--S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1793 EVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1872
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 1873 QLLEEELArlqREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1937
Cdd:pfam07888 342 EKLEVELG---REKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1628-1753 |
7.66e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1628 AEAQKRQAQEEAERLRRQVQDETQRKRQAEaELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR----QAEAERA 1703
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAlkqkQAEEAAA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1704 RQVQVA----------LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1753
Cdd:PRK09510 140 KAAAAAkakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
186-311 |
8.23e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 45.82 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 186 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHK 258
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FII 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 311
Cdd:cd21325 94 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2323-2566 |
8.49e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2323 QKAQVEQELTALRLQleetdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2402
Cdd:TIGR02794 44 DPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2403 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAELLQ 2476
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2477 QQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedI 2556
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA---I 272
|
250
....*....|
gi 1920237940 2557 GERLYRTELA 2566
Cdd:TIGR02794 273 QQNLYDDPSF 282
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1855-2005 |
8.67e-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: 47.23 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1855 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1933
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1934 AE----AGRFRELAEEAARLRALAEEAKRQRQLAEEdavrQRAEAERVLAEKLAAISEATRlKTEAEIALKEKEAE 2005
Cdd:COG1579 96 KEieslKRRISDLEDEILELMERIEELEEELAELEA----ELAELEAELEEKKAELDEELA-ELEAELEELEAERE 166
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2410-2508 |
9.02e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 47.96 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2410 QEEAEKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKMQavQEATRLKAEAELLQQQKElaQ 2483
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKME--EERENLLKEQERALESKL--K 266
|
90 100
....*....|....*....|....*
gi 1920237940 2484 EQARRLQEDKEQMAQQLAQETQGFQ 2508
Cdd:cd16269 267 EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1092-1753 |
9.11e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1092 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQK 1171
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1172 AQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1251
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1252 EEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQE-------VGERLQQRHGERD----VEVERW 1320
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGriisAHGRLG 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1321 RERVTLLLERWQAVLAQTDVRQR-ELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLA---NSQAVREQLRQEKA 1396
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSAtADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleIDPILNLAQLDKAT 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1397 LLEDIERHGEKV----EECQRFAKQYINAiKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTL 1472
Cdd:pfam02463 613 LEADEDDKRAKVvegiLKDTELTKLKESA-KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1473 TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVA 1551
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSrLKKEEKEEEKSELSL 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1552 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrLQLEATERQRGGAEGELQALRARAEEAEAQ 1631
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1632 KRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1711
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1920237940 1712 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1753
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2317-2751 |
9.13e-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: 49.18 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2317 AEQALRQKAQVEQELTALRLQL-------EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLK-A 2388
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApA 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2389 RIEAENRALVLRD------KDSA------QRLLQEE----------AEKMKQVAEEAARLSVAA-QEAARLRQLAE---- 2441
Cdd:COG3096 604 WLAAQDALERLREqsgealADSQevtaamQQLLEREreatverdelAARKQALESQIERLSQPGgAEDPRLLALAErlgg 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2442 -------EDLAQQRA-LAEKMLKEKMQA--VQEATRLKAEAE----------LLQQQKELAQEQARRLQEDKEQMAQQLA 2501
Cdd:COG3096 684 vllseiyDDVTLEDApYFSALYGPARHAivVPDLSAVKEQLAgledcpedlyLIEGDPDSFDDSVFDAEELEDAVVVKLS 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2502 QETQGFQKTLE------TERQRQLE-MSAEAERLRLRVAEMS---RAQARAEEDARRFrkqaedIGERLYRTELATQEKV 2571
Cdd:COG3096 764 DRQWRYSRFPEvplfgrAAREKRLEeLRAERDELAEQYAKASfdvQKLQRLHQAFSQF------VGGHLAVAFAPDPEAE 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2572 MlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQsflsEKDSLLQRERC 2651
Cdd:COG3096 838 L--AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELRE----ELDAAQEAQAF 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2652 IEQEKAKLEQLfqdeVAKAQALReeqqrqqqQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2731
Cdd:COG3096 912 IQQHGKALAQL----EPLVAVLQ--------SDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLL 979
|
490 500
....*....|....*....|....
gi 1920237940 2732 EENQ----RLRERLQHLEEERRAA 2751
Cdd:COG3096 980 GENSdlneKLRARLEQAEEARREA 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2141-2754 |
9.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2141 EEAARQRKAALEEVERLKAKVEEARRlreraeqeSARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqSVLE 2220
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERYAAARERL--------------------AELE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2221 RLRSEAEAARRAAEEAEAARERAEREAAQSRRQvEEAERLKQsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2300
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAELEELRAELARLE-AELERLEA-----------------RLDALREELDELEAQIRGNGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2301 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETdhqKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2380
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2381 EELGKLKARIEAENRALVLRDKDSAQRLLQeeaekMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2455
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLLA-----LRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2456 ------KEKMQAVQEAT-RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETE--RQRQLEMSAEAE 2526
Cdd:COG4913 489 ltllvpPEHYAAALRWVnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgRRFDYVCVDSPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2527 RLRLRVAEMSRA-QARAeeDARRFRKQAEDIGERLYRTELATQEKvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKL 2605
Cdd:COG4913 569 ELRRHPRAITRAgQVKG--NGTRHEKDDRRRIRSRYVLGFDNRAK---LAALEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2606 KQEAQLLQ-LKSEEMQTVRQEQLLQETQALQQsflsekdsllQRERcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQM 2684
Cdd:COG4913 644 QERREALQrLAEYSWDEIDVASAEREIAELEA----------ELER-LDASSDDLAAL-EEQLEELEAELEELEEELDEL 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2685 QQEKQQLAASMEEARRRQHEAEEGVRRqQEELQRLAQQQQQQEKLLAEENQRLRERL-QHLEEERRAALAR 2754
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRAR 781
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2321-2761 |
9.22e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2321 LRQKAQVEQ-ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIeaenralvl 2399
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2400 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2479
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2480 ELAQEQARRLQEDKEQMAQQLAQET--QGFQKTLETERQRQLEMSAEAERLRlrvAEMSRAQARAEEDARRFRKQAEDIG 2557
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2558 ERL--YRTELAT--QEKVMLVQTLETQRQQSD----------------------------RDAERLREAIAELEHEKDKL 2605
Cdd:PRK01156 416 VKLqdISSKVSSlnQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeksnhiinhynEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2606 KQEAQLLQ-----LKSEEM-QTVRQEQLLQETQALQQSFLSE----KDSLLQRERCIEQEKA-KLEQLFQDEVAKAQALR 2674
Cdd:PRK01156 496 DEKIVDLKkrkeyLESEEInKSINEYNKIESARADLEDIKIKinelKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2675 EEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG-----------VRRQQEELQRLaqqqqQQEKLLAEENQRLRERLQH 2743
Cdd:PRK01156 576 VISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddksyidksIREIENEANNL-----NNKYNEIQENKILIEKLRG 650
|
490
....*....|....*...
gi 1920237940 2744 LEEERRAALARSEEIAPS 2761
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPD 668
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2142-2447 |
9.76e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2142 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2213
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2214 qeqsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArra 2293
Cdd:pfam17380 362 -----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEA--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2294 qaeqaalRQKQAADAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILD---------EELQRLKAEVTEAAR 2364
Cdd:pfam17380 433 -------RQREVRRLEEERAREM-ERVRLEEQERQQQVERLRQQEEERKRKKLELEkekrdrkraEEQRRKILEKELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2365 QRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEE--AEKMKQVAEEAARLSVAAQEAARLRQLAEE 2442
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRriQEQMRKATEERSRLEAMEREREMMRQIVES 584
|
....*
gi 1920237940 2443 DLAQQ 2447
Cdd:pfam17380 585 EKARA 589
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1453-1797 |
9.81e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1453 ESIIQEYVDLRTRYSELST---LTSQYIRFISETLRRMEEEERLAE-QQRAEE-RERLAEVEAALEKQRQLAEAHAQAKA 1527
Cdd:COG4717 98 EELEEELEELEAELEELREeleKLEKLLQLLPLYQELEALEAELAElPERLEElEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1528 QAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQ---- 1603
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE----ELEELEEELEQLENELEAAALEERLKEARllll 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1604 --------------LEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1665
Cdd:COG4717 254 iaaallallglggsLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1666 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV----------------------QVALETAQRSAEAELQS 1723
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraaleqaeeYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1724 -----EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLQAEEVAQQ 1797
Cdd:COG4717 414 llgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ-ELEELKAELRELAEE 491
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1490-1719 |
1.00e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.44 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1490 EERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELqhlr 1569
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1570 qsSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1649
Cdd:PRK07735 86 --TEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1650 TQRKRQAEAELALrvqaeaEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1719
Cdd:PRK07735 164 KAKAKAAAAAKAK------AAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGN 227
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1824-2019 |
1.07e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1900
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1901 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1965
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1966 DAVRQRAEAERVLAEKLAAIS-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 2019
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1626-1705 |
1.10e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.79 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1626 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE------AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1698
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvaleglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 1920237940 1699 EAERARQ 1705
Cdd:PRK11448 218 RKEITDQ 224
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1654-1938 |
1.15e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1654 RQAEAELALRVQAEAEAAREKQR--ALQAleelRLQAEEAER--RLRQAEAERARQVQVALETAQRSAEAELQSEHASFA 1729
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAReaRHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1730 EKTAQlertlKEEHVAVVQLREEATRRAQQQAEAERARAEAERelerwQLKANEALRLRLQAEEVAQQKSLTqaeAEKQK 1809
Cdd:PRK05035 508 IKAGA-----RPDNSAVIAAREARKAQARARQAEKQAAAAADP-----KKAAVAAAIARAKAKKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1810 EEAEREARRRGKAEEQAvrqRELAEQELEKQRQLAEGTAQQRLAAEQELIrLRAETEQGEQQRQLLEEElarlqreaaAA 1889
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAI-ARAKAKKAEQQANAEPEE---------PV 641
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1920237940 1890 TQKRRELEAELAKVRAEmevlLASKARAEEESRSTSEKSKQRLEAEAGR 1938
Cdd:PRK05035 642 DPRKAAVAAAIARAKAR----KAAQQQANAEPEEAEDPKKAAVAAAIAR 686
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2316-2482 |
1.16e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.92 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2316 FAEQALrqkAQVEQELTALRLQLEETDHQKSILDEElqrlkAEVTEAARQRGQVEEELFSLRVQMEELgklkarieaenR 2395
Cdd:COG3524 181 FAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAAL-----------R 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2396 AlVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEAE 2473
Cdd:COG3524 242 S-YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEAA 317
|
....*....
gi 1920237940 2474 llQQQKELA 2482
Cdd:COG3524 318 --RQQRYLA 324
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1453-1664 |
1.18e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1453 ESIIQEYVDLRTRYSelSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERL------AEVEAALEKQRQLAEAHAQAK 1526
Cdd:COG3206 155 NALAEAYLEQNLELR--REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlsEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1527 AQAeREAQGLQRRMQEEVARREEVAVEA-------------QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRI 1593
Cdd:COG3206 233 AEL-AEAEARLAALRAQLGSGPDALPELlqspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1594 EEEIRVVRLQLEATERQRGGAEGELQALRARAE---EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRV 1664
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1937-2183 |
1.21e-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: 48.35 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1937 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 2016
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2017 AFQRRLLEEQAAQHKADIE------ARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELE 2090
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIReleediKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2091 LGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2169
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 1920237940 2170 RAEQESAR-QLQLAQ 2183
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2017-2542 |
1.23e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 48.72 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2017 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEkAAAGKAELELELGRIRG 2096
Cdd:COG3321 867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA-LLALVALAAAAAALLAL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2097 TAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2176
Cdd:COG3321 946 AAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALA 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2177 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2256
Cdd:COG3321 1026 ALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAA 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2257 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2336
Cdd:COG3321 1106 LLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAAL 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2337 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEElgklkARIEAENRALVLRDKDSAQRLLQEEAEKM 2416
Cdd:COG3321 1186 AAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAA-----ALALLALAAAAAAVAALAAAAAALLAALA 1260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2417 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2496
Cdd:COG3321 1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1920237940 2497 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARA 2542
Cdd:COG3321 1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1821-2014 |
1.30e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.61 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1900
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1901 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1980
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 1920237940 1981 KLAAISEATRLKTEAEIALKEKEAENERLRRLAE 2014
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3237-3273 |
1.32e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.32e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 3237 KLLSAEKAVTGYKDPYSGQSVSLFQALKKGLIPREQG 3273
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1828-2544 |
1.35e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.64 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1828 RQRELAEQEleKQRQLAEGTAQQRLAAEQ-ELIRLRAeTEQGEQQRQLLEeelaRLQREAAAATQKRR---ELEAELAKV 1903
Cdd:PRK10246 251 RLDELQQEA--SRRQQALQQALAAEEKAQpQLAALSL-AQPARQLRPHWE----RIQEQSAALAHTRQqieEVNTRLQST 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1904 RAEMEVLLASKARAEEESRSTSEKSKQRLeAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQRAEAERvlaEKLA 1983
Cdd:PRK10246 324 MALRARIRHHAAKQSAELQAQQQSLNTWL-AEHDRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQLTHAE---QKLN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1984 AISEATRLKTEAEIAlkekeaenERLRRLAEDEAFQRRLLEEQaAQHkADIEARLAQLrKASESELERQKGLVEDTLRQR 2063
Cdd:PRK10246 398 ALPAITLTLTADEVA--------AALAQHAEQRPLRQRLVALH-GQI-VPQQKRLAQL-QVAIQNVTQEQTQRNAALNEM 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2064 RQVEEEilalkgsfekaaagKAElelELGRIRGTAEDTLRSKEQAEQEAarQRQLAAEEERRRREAEERVQKSLAAEEEA 2143
Cdd:PRK10246 467 RQRYKE--------------KTQ---QLADVKTICEQEARIKDLEAQRA--QLQAGQPCPLCGSTSHPAVEAYQALEPGV 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2144 ARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERL 2222
Cdd:PRK10246 528 NQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNITLQPQDDIQPWL 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2223 rseaeaarraaeeaeaareraereaaqsrrqvEEAERLKQsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaEQAALRQ 2302
Cdd:PRK10246 603 --------------------------------DAQEEHER---------------------------------QLRLLSQ 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2303 KQAADAEMEKH----KQFAEQALRQKAQVEQELTALRLQLEETDHQKSIL---DEELQRLKAEVTEAARQRGQVE--EEL 2373
Cdd:PRK10246 618 RHELQGQIAAHnqqiIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRIQqlTPL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2374 FSLRVQMEELGKLKARIEAEN------RALVLRDKDSA--QRLLQEEAEKMKQVAEEAARL--SVAAQEAARLRQLAEED 2443
Cdd:PRK10246 698 LETLPQSDDLPHSEETVALDNwrqvheQCLSLHSQLQTlqQQDVLEAQRLQKAQAQFDTALqaSVFDDQQAFLAALLDEE 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2444 LAQQralAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQK--TLETERQRQLEM 2521
Cdd:PRK10246 778 TLTQ---LEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLREntTRQGEIRQQLKQ 854
|
730 740
....*....|....*....|....
gi 1920237940 2522 SAEA-ERLRLRVAEMSRAQARAEE 2544
Cdd:PRK10246 855 DADNrQQQQALMQQIAQATQQVED 878
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4109-4143 |
1.45e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.45e-04
10 20 30
....*....|....*....|....*....|....*
gi 1920237940 4109 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4143
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1562-1920 |
1.46e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1562 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1641
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1642 LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAEL 1721
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1722 QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLT 1801
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1802 QAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1881
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340 350
....*....|....*....|....*....|....*....
gi 1920237940 1882 LQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1920
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1616-1838 |
1.66e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1616 GELQALRARAEEAEAQ-KRQAQEEAERLRRQVQDETQRKRQAEAElalRVQAEAEAAREKQRALQALEELRlQAEEAERR 1694
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQrKKKEQQQAEELQQKQAAEQERLKQLEKE---RLAAQEQKKQAEEAAKQAALKQK-QAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1695 LRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerel 1774
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA--------------------- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1775 erwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1838
Cdd:PRK09510 200 ---KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1824-2071 |
1.67e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.37 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRREL 1896
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1897 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEE--DAVRQRAE 1973
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEarNQLRDRDE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1974 AERVLAEKLaaiSEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 2053
Cdd:pfam19220 277 AIRAAERRL---KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSD 353
|
250
....*....|....*...
gi 1920237940 2054 GLveDTLRQRRQVEEEIL 2071
Cdd:pfam19220 354 RI--AELTKRFEVERAAL 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2520-2754 |
1.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2520 EMSAEAERLRLRVAEMSRAQARAEeDARRFRKQAEDIgERLYRTELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAE 2597
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALE-DAREQIELLEPI-RELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2598 LEHEKDKLKQEAQLLQLKSEEMQtvrqEQLLQETQALQQSFLSEKDSLlqrERCIEQEKAKLEQLFQdevaKAQALREEQ 2677
Cdd:COG4913 300 LRAELARLEAELERLEARLDALR----EELDELEAQIRGNGGDRLEQL---EREIERLERELEERER----RRARLEALL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 2678 QRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQqqqekllaeenQRLRERLQHLEEERRAALAR 2754
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL-----------RDLRRELRELEAEIASLERR 434
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4418-4451 |
1.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.97e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237940 4418 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4451
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2300-2474 |
1.98e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEE---LFSL 2376
Cdd:PRK09510 80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEakrAAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2377 RVQMEELGKLKARIEAENRALVLRDK----DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAE 2452
Cdd:PRK09510 160 AKKAAAEAKKKAEAEAAKKAAAEAKKkaeaEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAE 239
|
170 180
....*....|....*....|..
gi 1920237940 2453 KmlKEKMQAVQEATRLKAEAEL 2474
Cdd:PRK09510 240 K--AAAAKAAEKAAAAKAAAEV 259
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1007-1964 |
2.08e-04 |
|
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: 47.86 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1007 EAQEAIARLEAQHQALVAlwhQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQDA 1086
Cdd:pfam01576 219 DLQEQIAELQAQIAELRA---QLAKKEEELQAALARLEEETAQKNNALKKIRELE-AQISELQEDLESERAARNKAEKQR 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1087 GGFGPE-DRLQAEREYGSCSRHYQQLLQSleQGEQEESRCQRCISElkdirlqleacETRtVHRLRLPLDKEPARECAQR 1165
Cdd:pfam01576 295 RDLGEElEALKTELEDTLDTTAAQQELRS--KREQEVTELKKALEE-----------ETR-SHEAQLQEMRQKHTQALEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1166 ITEQQKaQAEVDGLGKGVARLSAEAEkVLALPEPSPAAPTLRSELELTLGKLE-QVRSLSAIYLEKLKtislvirstQEA 1244
Cdd:pfam01576 361 LTEQLE-QAKRNKANLEKAKQALESE-NAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESER---------QRA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1245 EEVLRAHEEQLkEAQAVPATLPELEATKAALKKLRAQAEAQ-QPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1323
Cdd:pfam01576 430 ELAEKLSKLQS-ELESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1324 VtlllerwqavlaqtdVRQRELEqlgRQLRyyresadPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIEr 1403
Cdd:pfam01576 509 E---------------EAKRNVE---RQLS-------TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE- 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1404 hgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK----VQSGSESIIQEYVDLRTRYS----ELSTLTSQ 1475
Cdd:pfam01576 563 --EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdqMLAEEKAISARYAEERDRAEaearEKETRALS 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1476 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglqrRMQEEVARREEVAVEAQ 1555
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE--------EMKTQLEELEDELQATE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1556 EQKRSIQEELQHLRQSSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEA 1628
Cdd:pfam01576 713 DAKLRLEVNMQALKAQFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1629 EAQKRQAQEEAERLRRQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERA 1703
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERD 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1704 R-QVQVALETAQRSAeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQqaeaeraraeaerelerwqlkaN 1782
Cdd:pfam01576 865 ElADEIASGASGKSA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQ----------------------V 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1783 EALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQRLAAeqELIRLR 1862
Cdd:pfam01576 920 EQLTTELAAERSTSQKS------------------------ESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALE 973
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1863 AETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAGRFREL 1942
Cdd:pfam01576 974 AKIAQ-------LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVE----DERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
970 980
....*....|....*....|..
gi 1920237940 1943 AEEAArlRALAEEAKRQRQLAE 1964
Cdd:pfam01576 1043 EEEAS--RANAARRKLQRELDD 1062
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2522-2770 |
2.16e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2522 SAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHE 2601
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2602 KDKLKQEAQLLQLKSEEMQTVRQEQLLqetqaLQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2681
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2682 QqmqqEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2761
Cdd:COG4942 174 A----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*....
gi 1920237940 2762 RAAAARALP 2770
Cdd:COG4942 250 ALKGKLPWP 258
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1912-2109 |
2.16e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1912 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAVRQRAEAERVLAEKLAAISEATRL 1991
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1992 KTEAEIALKEKEAENerlrrlAEDEAfQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 2071
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237940 2072 ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAE 2109
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1515-1694 |
2.23e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1515 QRQLAEAHAQAK---AQAEREAQglqrrmqeevARREEVAVEAqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERsRL 1591
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAE----------AIKKEALLEA-------KEEIHKLRNEFEKELRERRNELQKLEK-RL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1592 RIEEEIrvVRLQLEATERQRGGAEGELQALRARAEEAEAQKrqaqEEAERLRRQVQDETQR-----KRQAEAELALRVqa 1666
Cdd:PRK12704 92 LQKEEN--LDRKLELLEKREEELEKKEKELEQKQQELEKKE----EELEELIEEQLQELERisgltAEEAKEILLEKV-- 163
|
170 180
....*....|....*....|....*....
gi 1920237940 1667 EAEAAREKQRALQALEElrlQA-EEAERR 1694
Cdd:PRK12704 164 EEEARHEAAVLIKEIEE---EAkEEADKK 189
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1461-1741 |
2.32e-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: 47.20 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1461 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQrAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1540
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEEL-SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1541 QEEVARREEVAVEAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGE 1617
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1618 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE-KQRALQALEELRLQAE- 1689
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEa 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 1690 EAERRLRQAEAERARQVQVALETAQR-SAEAELQSEHASFAEKTAQLERTLKE 1741
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1513-1644 |
2.32e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 44.65 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1513 EKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1590
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1591 LRIEEEIRVVRLQLEATERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1644
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2315-2761 |
2.38e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2315 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2394
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2395 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2474
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2475 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2554
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2555 DIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL 2634
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2635 QQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2714
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1920237940 2715 ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2761
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1575-1742 |
2.38e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1575 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQvQDETQRKR 1654
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1655 QAEAelalrVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVQ--VALETAQRSAEAELQSEHASFAEK 1731
Cdd:COG1579 90 EYEA-----LQKEIESLKRRISDLeDEILELMERIEELEEELAELEAELAELEAelEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|.
gi 1920237940 1732 TAQLERTLKEE 1742
Cdd:COG1579 165 REELAAKIPPE 175
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2304-2627 |
2.42e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2304 QAADAEMEKHKQFAEQALRQKAQVEQELtalRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2383
Cdd:pfam13868 16 LAAKCNKERDAQIAEKKRIKAEEKEEER---RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2384 GKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2463
Cdd:pfam13868 93 YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE-FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2464 EATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGF---QKTLETERQRQLEMSAEAERLRLRVAEMSRA 2538
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRaqQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2539 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2618
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR-LEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRER 330
|
....*....
gi 1920237940 2619 MQTVRQEQL 2627
Cdd:pfam13868 331 IEEERQKKL 339
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2323-2662 |
2.46e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2323 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT-------EAARQRGQVEEELFSLRVQMEELGKLKARIEAENR 2395
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnnkynDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2396 AL-----VLRDKDSAQRLLQEEAEKMK----QVAEEAARLSVAAQEAARLRQLAEE---DLAQQRALAEKMLKEKMQAVQ 2463
Cdd:TIGR04523 198 KLelllsNLKKKIQKNKSLESQISELKkqnnQLKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2464 EATR-----------LKAEAELLQQQKE---------LAQEQARRLQEDKEQMAQ------QLAQETQGFQKTLETERQR 2517
Cdd:TIGR04523 278 QNNKkikelekqlnqLKSEISDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKELTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2518 QLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAE 2597
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 2598 LEHEKDKLKQEAQLLQLKSEEMQTVRqEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2662
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1824-2105 |
2.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1903
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1904 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1983
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1984 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 2063
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237940 2064 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSK 2105
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1235-1890 |
2.69e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1235 SLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPE-LEATKAALKKLRAQAEAQqpvfdalRDELR-GAQEVGERLQQRHGE 1312
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAENA-------RLEMHfKLKEDHEKIQHLEEE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1313 RDVEVERWRERVTLLLerwqavlAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakQRQEQIQAVPLANSQAVREQLR 1392
Cdd:pfam05483 231 YKKEINDKEKQVSLLL-------IQITEKENKMKDLTFLLEESRDKANQL--------EEKTKLQDENLKELIEKKDHLT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1393 QEkalLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYK-AQLEPVASPAK---------KPKVQSGSESIIQEYVDL 1462
Cdd:pfam05483 296 KE---LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAahsfvvtefEATTCSLEELLRTEQQRL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1463 RTRYSELSTLTSQYIRFISEtLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAEREAQGLQRRMQE 1542
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSE-LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-EKIAEELKGKEQELIFLLQAREK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1543 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEiqaKARQVEAAERSRLRIEEEIRVVR------LQLEATERQRGGAEG 1616
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE---KLKNIELTAHCDKLLLENKELTQeasdmtLELKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1617 ELQALRARAEEAEAQKRQAQEEAERLRR---QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAE 1692
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEnKCNNLKKQIENKN 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1693 RRLRQAEAE-RARQVQVALETAQRSA--------EAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaea 1763
Cdd:pfam05483 608 KNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKA------- 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1764 eraraeaerelerwQLKANEALRLRLQAEEVAQQKsltqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL 1843
Cdd:pfam05483 681 --------------KAIADEAVKLQKEIDKRCQHK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1920237940 1844 AEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1890
Cdd:pfam05483 736 EQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2400-2570 |
3.03e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2400 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR-LKAEAELLQQQ 2478
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAkAKAEAEAERKA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2479 KELAQEQARrlqEDKEQMAQQLAQetqgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGE 2558
Cdd:TIGR02794 145 KEEAAKQAE---EEAKAKAAAEAK-----KKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAE 216
|
170
....*....|..
gi 1920237940 2559 RLYRTELATQEK 2570
Cdd:TIGR02794 217 AAAAAAAEAERK 228
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1477-1741 |
3.08e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1477 IRFISETLRRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREaqglqrrmqeevarREEVAVEAQ 1555
Cdd:pfam00038 20 VRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1556 EQKRSIQEELQhLRQSSEAEIQAKARQVEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQA 1635
Cdd:pfam00038 86 DFRQKYEDELN-LRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1636 QEEAERLRRQVQDETQ-------RKRQAEAELA-LRVQAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEAERA 1703
Cdd:pfam00038 141 EEEVRELQAQVSDTQVnvemdaaRKLDLTSALAeIRAQYEEIAAKNREEAeewyQSKLEELQQAAARNGDALRSAKEEIT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1704 ---RQVQ-------------VALETAQRSAEAELQSEHASFAEKTAQLERTLKE 1741
Cdd:pfam00038 221 elrRTIQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQE 274
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1821-2033 |
3.13e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRRE 1895
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1896 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1952
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1953 AEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRlLEEQAAQHKA 2032
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ-ADAKGAKQDE 1776
|
.
gi 1920237940 2033 D 2033
Cdd:NF012221 1777 S 1777
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2307-2503 |
3.18e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2307 DAEMEKHKQFAEQALR---QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQR------GQVEEELFSLR 2377
Cdd:PRK11281 55 EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2378 VQMEELGklKARIEAENRALVLRDK--------DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAeedLAQQRA 2449
Cdd:PRK11281 135 DQLQNAQ--NDLAEYNSQLVSLQTQperaqaalYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL---LNAQND 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2450 LAEKMLK--EKMQAVQEATR--LKAEAELLQQQKELAQE--QARRLQEDKEQMAQQLAQE 2503
Cdd:PRK11281 210 LQRKSLEgnTQLQDLLQKQRdyLTARIQRLEHQLQLLQEaiNSKRLTLSEKTVQEAQSQD 269
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1553-1688 |
3.19e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.19 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1553 EAQEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRLRIEEEI-RVVRLQleateRQRGGAEGELQALRARAEEAE 1629
Cdd:COG1566 87 QAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEARAALDAAQ 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1630 AQKRQAQEEAERLRRQVQDETQrKRQAEAELAlrvQAEAEAAREKQRalqaLEELRLQA 1688
Cdd:COG1566 162 AQLEAAQAQLAQAQAGLREEEE-LAAAQAQVA---QAEAALAQAELN----LARTTIRA 212
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1546-1897 |
3.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1546 RREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1625
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1626 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA-- 1703
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1704 -RQVQVALETAQRSAEAELQSEHASF---AEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQL 1779
Cdd:COG4372 163 qEELAALEQELQALSEAEAEQALDELlkeANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1780 KANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1859
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350
....*....|....*....|....*....|....*...
gi 1920237940 1860 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELE 1897
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2145-2634 |
3.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2145 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2224
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2225 EAeaarraaeeaeaareraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArraqaeqaalRQKQ 2304
Cdd:COG4717 144 LP-------------------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLE----------QLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2305 AADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA-EVTEAARQRGQVEEELFSLRVQMEEL 2383
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2384 GKLKARI------EAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2457
Cdd:COG4717 269 LSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2458 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKtleTERQRQLEMSAEAERLRLRVAEMSR 2537
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL---KEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2538 AQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAER--LREAIAELEHEKDKLKQEAQLLQLK 2615
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELeeLKAELRELAEEWAALKLALELLEEA 505
|
490
....*....|....*....
gi 1920237940 2616 SEEMQTVRQEQLLQETQAL 2634
Cdd:COG4717 506 REEYREERLPPVLERASEY 524
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1821-1992 |
3.51e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLeeelarlqreaaaatqkrrELEAE 1899
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLL-------------------ELQAE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1900 LAKVRAemevllASKARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVL 1978
Cdd:PTZ00491 708 SAAVES------SGQSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAK 778
|
170
....*....|....
gi 1920237940 1979 AEKLAAIsEATRLK 1992
Cdd:PTZ00491 779 AKELADI-EATKFE 791
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3160-3197 |
3.59e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.59e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1920237940 3160 RRALRGSGVIAGVWLEEAGQKLSIYEALRKDLLQPEAA 3197
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1820-2001 |
3.60e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1820 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQREAAAATQKRRELEA 1898
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1899 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDavrqrAEAERV 1977
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 1920237940 1978 LAEKLAAISEATRLKTEAEIALKE 2001
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
186-310 |
3.71e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 43.84 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 186 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHK 258
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTI 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 259 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 310
Cdd:cd21324 94 QENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2300-2757 |
3.90e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2375
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2376 LRVQMEELGKLKARIEAENRALVLRDKDSaqrllqEEAEKMKqvaEEAARLSVAAQEAARLRqlaeEDLAQQRALAEKML 2455
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDS------EIVKNSK---SELARIPELEKELERLR----EHNKHLNENIENKL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2456 KEKMQAVQEATRLkaeaellqQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKT-------------LETERQRQLEMS 2522
Cdd:pfam05557 225 LLKEEVEDLKRKL--------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTglnlrspedlsrrIEQLQQREIVLK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2523 AEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE-----------LATQEKVMLVQTLE------TQRQQSD 2585
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKalvrrlqrrvlLLTKERDGYRAILEsydkelTMSNYSP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2586 RDAERLREA----------IAELEHEKDKLKQEA----QLLQLKSEEMQTVRQeqllQETQALQQSFLSEKDSLLQRERC 2651
Cdd:pfam05557 377 QLLERIEEAedmtqkmqahNEEMEAQLSVAEEELggykQQAQTLERELQALRQ----QESLADPSYSKEEVDSLRRKLET 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2652 IEQEKAKLEQlfQDEVAKAQALREEQQRQQQQMQQEKQQLaasmeearrRQHEAEEGVRRQQEELQRLAqqqqqqeklla 2731
Cdd:pfam05557 453 LELERQRLRE--QKNELEMELERRCLQGDYDPKKTKVLHL---------SMNPAAEAYQQRKNQLEKLQ----------- 510
|
490 500
....*....|....*....|....*.
gi 1920237940 2732 EENQRLRERLQHLEEERRAALARSEE 2757
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVLRLPET 536
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3568-3604 |
3.92e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.92e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 3568 KLLSAEKAVTGYRDPYSGSTISLFQAMKKGLVLREHG 3604
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1820-1942 |
4.01e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1820 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATQKR 1893
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1894 RELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1942
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1832-2117 |
4.16e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1832 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLL 1911
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1912 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedavrqraeAERVLAeKLAAISEAtRL 1991
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1992 KTEAEialkekeaenerLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVedtlrqrrqveeeil 2071
Cdd:PRK11637 170 ETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT--------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 2072 ALKGSFEKAAAGKAELELELGRIRGT-AEDTLRSKEQAEQEA-------ARQRQ 2117
Cdd:PRK11637 223 GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2352-2503 |
4.32e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2352 LQRLKAEVTEAARQR----GQVEEELfsLRVQMEELGKLKaRIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLS 2427
Cdd:PRK09510 67 QQQQQKSAKRAEEQRkkkeQQQAEEL--QQKQAAEQERLK-QLEKE-RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAA 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2428 VAAQEAARLRQLAEEDLAQQrALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAQE 2503
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAKKAaaeAKKKAEAEAAAKAAAEAKKKA---EAEAKKKAAAEAKK 217
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1811-1974 |
4.33e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.40 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1811 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREaaaat 1890
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAETARAE---AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE----- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1891 QKRRELEAELaKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEedAVRQ 1970
Cdd:COG2268 301 REEAELEADV-RKPAE-----AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEA 372
|
....
gi 1920237940 1971 RAEA 1974
Cdd:COG2268 373 AAKP 376
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2587-2717 |
4.48e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2587 DAERLREAIAELEHEKDKLKQEAQLLqlkseemqtvrqEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQDE 2666
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2667 V--AKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGV-------RRQQEELQ 2717
Cdd:PRK00409 579 IkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKekkkkkqKEKQEELK 638
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1821-2050 |
4.61e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEEL--------ARLQR 1884
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARpdnsaviaAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1885 EAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1959
Cdd:PRK05035 527 KAQARARQAEKQAAAaadpkKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1960 RQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAedeafqrrlleeqAAQHKAdiEARLA 2039
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVA-------------AAIARA--KARKA 660
|
250
....*....|.
gi 1920237940 2040 QLRKASESELE 2050
Cdd:PRK05035 661 AQQQANAEPEE 671
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3529-3564 |
5.06e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.06e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1920237940 3529 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3564
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1571-1705 |
5.07e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1571 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDET 1650
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1651 QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1705
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3200-3233 |
5.37e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.37e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237940 3200 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPE 3233
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1488-1753 |
5.43e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.57 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1488 EEEERLAEQQRAEERER----------LAEVEAALEKQR---QLAEAHAQAKAQAEREAQGLQRR----MQEEVARREEV 1550
Cdd:PRK10811 507 EEAMALPSEEEFAERKRpeqpalatfaMPDVPPAPTPAEpaaPVVAAAPKAAAATPPAQPGLLSRffgaLKALFSGGEET 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1551 AVEAQEQKRSIQEElqhlRQSSEaeiQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1630
Cdd:PRK10811 587 KPQEQPAPKAEAKP----ERQQD---RRKPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1631 QKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvQAEAEAarekqralQALEELRLQAEEAERRLRQAEAERAR------ 1704
Cdd:PRK10811 660 EVTEKARTQDEQQQAPRRERQRRRNDEKRQA---QQEAKA--------LNVEEQSVQETEQEERVQQVQPRRKQrqlnqk 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 1705 ---QVQVALETAQRSAEAELQSEHASfAEKTAQLERTLKEEHVAVVQLREEA 1753
Cdd:PRK10811 729 vriEQSVAEEAVAPVVEETVAAEPVV-QEVPAPRTELVKVPLPVVAQTAPEQ 779
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1745-2200 |
5.50e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.55 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1745 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEE 1824
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1825 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR 1904
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1905 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA 1984
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1985 ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRR 2064
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2065 QVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 2144
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2145 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2200
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1502-1753 |
5.68e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1502 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1581
Cdd:pfam13868 12 NSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1582 QVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1661
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1662 LRVQAEAEAAREKQRAlqaleELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELqsehasfAEKTAQLERTLKE 1741
Cdd:pfam13868 172 EAEREEIEEEKEREIA-----RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-------AEKKARQRQELQQ 239
|
250
....*....|..
gi 1920237940 1742 EHVAVVQLREEA 1753
Cdd:pfam13868 240 AREEQIELKERR 251
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
183-299 |
5.99e-04 |
|
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: 42.64 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 183 DRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNV 262
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDI---NGCPKNRSQM----IENI 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237940 263 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 299
Cdd:cd21285 75 DACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1477-1720 |
6.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1477 IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQE 1556
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1557 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR-------AraeEAE 1629
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1630 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVA 1709
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250
....*....|.
gi 1920237940 1710 LETAQRSAEAE 1720
Cdd:COG3883 255 AGAAAGSAGAA 265
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2427-2705 |
6.38e-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: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2427 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAqETQG 2506
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLA-AISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2507 FQKTLETERQRQLEMSAEAERlrlrvaemsraqARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2586
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR------------DAILEESRAVTKELTTLAQGL--------------DALDSQATYAGE 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2587 DAERLREAIAE--LEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSllqrerciEQEKAKLEQLFQ 2664
Cdd:NF012221 1642 SGDQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQDID 1713
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237940 2665 DEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRR-QHEA 2705
Cdd:NF012221 1714 DAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2303-2591 |
6.74e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2303 KQAADAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAaRQRGQVEEELfslRVQMEE 2382
Cdd:COG3096 402 QQALDVQQTRAIQY-QQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-EQKLSVADAA---RRQFEK 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2383 LGKLKARIEAEnralVLRDK--DSAQRLLQEEAEKMKQvaeeAARLSVAAQEAARLRQLAEEdlaQQRA--LAEKMLKEK 2458
Cdd:COG3096 477 AYELVCKIAGE----VERSQawQTARELLRRYRSQQAL----AQRLQQLRAQLAELEQRLRQ---QQNAerLLEEFCQRI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2459 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRA 2538
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL-EQLRARIKELAARAPAWLAAQDALERLR----EQSGE 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2539 QARAEEDARRFRKQAedigerLYRTELATQEKvmlvQTLETQRQQSDRDAERL 2591
Cdd:COG3096 621 ALADSQEVTAAMQQL------LEREREATVER----DELAARKQALESQIERL 663
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2514-2759 |
6.76e-04 |
|
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: 46.20 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2514 ERQRQLEMSAEA-ERLRLRVAEMSRAQARAEEDARRFRKQAEdigerlYRTELATQEKVMLVQTLETQRQQsdrdAERLR 2592
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERQLKSLERQAEKAERYKE------LKAELRELELALLVLRLEELREE----LEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2593 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQR-ERCIEQEKAKLEQLFQDEVAKAQ 2671
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKELYALANEISRlEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2672 ALREeqqrqqqqmqqekqqLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2751
Cdd:TIGR02168 324 QLEE---------------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
....*...
gi 1920237940 2752 LARSEEIA 2759
Cdd:TIGR02168 389 AQLELQIA 396
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
181-306 |
6.77e-04 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 42.67 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 181 ERDRVQKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQ 260
Cdd:cd21330 9 EGETREERTFRNWMNS-------LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237940 261 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 306
Cdd:cd21330 77 NCNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2163-2614 |
6.82e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.12 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2163 EARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2242
Cdd:COG4995 3 ALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2243 AEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALR 2322
Cdd:COG4995 83 AALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2323 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2402
Cdd:COG4995 163 AALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2403 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2482
Cdd:COG4995 243 LAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2483 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYR 2562
Cdd:COG4995 323 LLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2563 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2614
Cdd:COG4995 403 LAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQL 454
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1618-1742 |
7.11e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 43.24 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1618 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEtQRKRQAEAElALRVQAEAEAAREKQRALQALEelrlqaEEAERR 1694
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1920237940 1695 LRQAEAErarqvqvaLETAQRSAEAELQSEHASFAEKTAqlERTLKEE 1742
Cdd:COG0711 98 IAQAEAE--------IEQERAKALAELRAEVADLAVAIA--EKILGKE 135
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
762-854 |
7.41e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.93 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 762 HGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQA 841
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1920237940 842 ALQTQWSWMLQLC 854
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1486-1602 |
7.63e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1486 RMEEEERLAEQQRAEERERLAEVEA---ALEKQ-RQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-----REEVAVEAQE 1556
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKlkeELEEKkEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiikelRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237940 1557 QKRS-IQEELQHLRQSSEAEIQAKARQVEAAErsRLRIEEEIRVVRL 1602
Cdd:PRK00409 604 VKAHeLIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL 648
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1495-1622 |
7.65e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.88 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1495 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAqAEREaqglqRRMQEEVARREEVavEAQEQKRSIQEELQHLRQSSEA 1574
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEA-AEQE-----RKLLEEQQRELEQ--KLEDQERSYEEHLRQLKEKMEE 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1920237940 1575 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1622
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1485-1673 |
8.57e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1485 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEE 1564
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1565 LQHLRQSSEAEIQAKARQVEAAERSRLRieeeiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1644
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
170 180
....*....|....*....|....*....
gi 1920237940 1645 QVQDETQRKRQAEAELALRVQAEAEAARE 1673
Cdd:PRK12678 232 RRDRRDARGDDNREDRGDRDGDDGEGRGG 260
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1821-2202 |
8.91e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1900
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1901 AKVRAEMEVLLASKARAEEESRSTSEKSK--QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1978
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKaeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1979 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVED 2058
Cdd:COG3064 180 AALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2059 TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 2138
Cdd:COG3064 260 LGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEA 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 2139 AEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2202
Cdd:COG3064 340 ALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGL 403
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1562-1752 |
8.98e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 43.88 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1562 QEELQHLRQSSEAEIQakarqveaaersrlRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1641
Cdd:pfam15665 13 EAEIQALKEAHEEEIQ--------------QILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1642 LRRQVQDetqRKRQAEAELALRVQAEA----EAAREKQRALQALEELRLQAE-EAERRLRQAEAERARQVQVALETaqrs 1716
Cdd:pfam15665 79 YKRRVEE---RELKAEAEHRQRVVELSreveEAKRAFEEKLESFEQLQAQFEqEKRKALEELRAKHRQEIQELLTT---- 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237940 1717 aeaeLQSEHASFAEKTAQLERTLKEEhvaVVQLREE 1752
Cdd:pfam15665 152 ----QRAQSASSLAEQEKLEELHKAE---LESLRKE 180
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1820-2202 |
9.12e-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: 45.39 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1820 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1892
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1893 RRELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRqlaEEDA 1967
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPR---DEEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1968 VRQrAEAErVLAEKlaaiSEATRLKteaEIALKEKEAENERLRRLaedEAFQRRLLEEQAAQHKADIEARLAqlRKASES 2047
Cdd:NF033838 206 IKQ-AKAK-VESKK----AEATRLE---KIKTDREKAEEEAKRRA---DAKLKEAVEKNVATSEQDKPKRRA--KRGVLG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2048 ELERQKGLVEDTLRQRRQVEEEIL---ALKGSFEKAAAGKAELELElGRIRGTAEDTLR-----SKEQAEQEAARqrqla 2119
Cdd:NF033838 272 EPATPDKKENDAKSSDSSVGEETLpspSLKPEKKVAEAEKKVEEAK-KKAKDQKEEDRRnyptnTYKTLELEIAE----- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2120 aeEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA---KVEEARRLRERAEQESARQLQLAQEAAQKrlQAEEKA 2196
Cdd:NF033838 346 --SDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAeatRLEKIKTDRKKAEEEAKRKAAEEDKVKEK--PAEQPQ 421
|
....*.
gi 1920237940 2197 HAFAVQ 2202
Cdd:NF033838 422 PAPAPQ 427
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1490-1735 |
9.27e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1490 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQ----------EEVARREEVAVEAQEQKR 1559
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAelkeelrqsrEKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1560 SIQEE---LQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1636
Cdd:pfam07888 112 ELSEEkdaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1637 EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVAleTAQRS 1716
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA--AQRDR 269
|
250
....*....|....*....
gi 1920237940 1717 AEAELQSEHASFAEKTAQL 1735
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQL 288
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4528-4565 |
9.50e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 9.50e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1920237940 4528 QRFLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTA 4565
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1494-1655 |
9.90e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1494 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1573
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1574 AEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDETQRK 1653
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 1920237940 1654 RQ 1655
Cdd:PRK12678 216 EE 217
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2353-2547 |
1.02e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2353 QRLKAEVTEAARQRGQVEEElfslrvqmeelgklkarieaenralvlrdkdsaQRLLQEEAEKMKQVAEEAARLSVAAQE 2432
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQ---------------------------------RRLQQEQLERAEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2433 AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQQQKELAQEQARRLQEDKE---QMAQQLAQETQG 2506
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQrqkELEMQLAEEQKR 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237940 2507 FQKTLETERQRQLEMSAEAERLRLRVAEMSRaqARAEEDAR 2547
Cdd:pfam15709 468 LMEMAEEERLEYQRQKQEAEEKARLEAEERR--QKEEEAAR 506
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1625-2009 |
1.04e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1625 AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAR---EKQRALQALEELRLQAEEAERRLRQAEAE 1701
Cdd:PRK10929 104 TDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQLTALQAESA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1702 RARQVQVALETAQRSAE-----AELQSEhaSFAEKTAQLERTLkeehvavvqlreeatrraqqqaeaeraraeaereler 1776
Cdd:PRK10929 184 ALKALVDELELAQLSANnrqelARLRSE--LAKKRSQQLDAYL------------------------------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1777 wqlkanEALRLRLQAEevaqqksltqaeaekqkeeaerearrrgkaeeqavRQRElAEQELEKQRQLAEGTAQQRLAAEQ 1856
Cdd:PRK10929 225 ------QALRNQLNSQ-----------------------------------RQRE-AERALESTELLAEQSGDLPKSIVA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1857 ELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRREleaELAKVRAEMEVLLASKARAE----EESRSTSEKSKQRL 1932
Cdd:PRK10929 263 QFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQVRQ---ALNTLREQSQWLGVSNALGEalraQVARLPEMPKPQQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1933 EAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---------------ISEATRLK--- 1992
Cdd:PRK10929 339 DTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTqrellnsllsggdtlILELTKLKvan 413
|
410
....*....|....*...
gi 1920237940 1993 TEAEIALKE-KEAENERL 2009
Cdd:PRK10929 414 SQLEDALKEvNEATHRYL 431
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1857-2204 |
1.08e-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: 45.27 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1857 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA 1936
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE--RQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1937 GRFRELAEEAARLRAlAEEAKRQRQLAEEDAVrqRAEAERVLaeklaaiseatrlkteaeialkEKEAENERLRRLAEDE 2016
Cdd:pfam07888 108 ASSEELSEEKDALLA-QRAAHEARIRELEEDI--KTLTQRVL----------------------ERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2017 AFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG 2096
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLS-KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2097 TAE-------------------DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE----- 2152
Cdd:pfam07888 242 LQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrie 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 2153 ----EVERLKAKVEEARRLRERAEQESARQ--LQLAQEAAQKRLQAEEKAhAFAVQQK 2204
Cdd:pfam07888 322 klsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1488-1752 |
1.19e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1488 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA-----------QGL-----------QRRMQEEVA 1545
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELkpsgqggldeeEAFldrtakreerrQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1546 RREEVAVEAQEQKRSIQEELQHlRQSSEAEIQAKARQVEaAERSRLRIEEEIRVVRL---QLEATERQRGGAEGELQALR 1622
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKEN-NEEEENSSWEKEEKRD-SRLGRYKEEETEIREKEyqeNKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1623 ARAEEAEAQKRQAQEEAERLRRQVQDE---------------TQRKRQA--EAELALRVQAEAEAAREKQRALQALE-EL 1684
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKvkyeskvfldqkrghPEVKSQNgeEEVTKLKVTTKRRQGGLSQSQEREEEaEV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1685 RLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE--KTAQLERTLKEEHVAVVQLREE 1752
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREErrKLLEEEEQRRKQEEAERKLREE 312
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1491-1752 |
1.21e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1491 ERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAkaqaereaqgLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRq 1570
Cdd:pfam10174 453 ERLKEQREREDRERLEELE-SLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEHASSLASSGLKKDSKLK- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1571 SSEAEIQA-------------KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK----- 1632
Cdd:pfam10174 521 SLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1633 ----------RQAQEEAERLR--RQVQDETQRKRQAEAELALRVQ-AEAEAAREKQRA--LQALEELRLQAEEAERRLRQ 1697
Cdd:pfam10174 601 kiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDATKARLSS 680
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 1698 AE--------------AERARQVQVALETAQRSAEAELQSEHASFA--EKTAQLERTLKEEhvaVVQLREE 1752
Cdd:pfam10174 681 TQqslaekdghltnlrAERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE---VMALKRE 748
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1922-2070 |
1.25e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1922 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 2000
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2001 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 2070
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2909-2945 |
1.33e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.33e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 2909 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 2945
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1566-1854 |
1.35e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1566 QHLRQSsEAEIQAKARQVEAAERSRLRIEEeirvvrlqleateRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1645
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1646 VQDETQRKRQAEAELALRVQAEAEAAREK----------QRALQALEELR-LQAEEAERRLRQAEAERARQVQVALETAQ 1714
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKAKKAAATQPivikagarpdNSAVIAAREARkAQARARQAEKQAAAAADPKKAAVAAAIAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1715 RSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERElerwqlkANEALRLRLQAEEV 1794
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------AVAAAIARAKAKKA 629
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1795 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1854
Cdd:PRK05035 630 EQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2320-2753 |
1.37e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2320 ALRQKAQVEQ-ELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEaeNRALV 2398
Cdd:pfam10174 335 AKEQRAAILQtEVDALRLRLEE---KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE--NLQEQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2399 LRDKDsaqRLLQEEAEKMKQVAEEAARLSVA---AQEAARLRQLAEEDLAQQRALAEKMLKEKM-QAVQEATRLKAEAEL 2474
Cdd:pfam10174 410 LRDKD---KQLAGLKERVKSLQTDSSNTDTAlttLEEALSEKERIIERLKEQREREDRERLEELeSLKKENKDLKEKVSA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2475 LQQQKelaQEQARRLQEDKEQmAQQLAQ---ETQGFQKTLETERQRQLEmsaEAERLrlrVAEMSRAQaRAEEDARrfrk 2551
Cdd:pfam10174 487 LQPEL---TEKESSLIDLKEH-ASSLASsglKKDSKLKSLEIAVEQKKE---ECSKL---ENQLKKAH-NAEEAVR---- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2552 QAEDIGERLYRTELATQEKVMlvqtlETQRQQSDrdAERLREAIAELEHEK-DKLKQEAQLLQLKSEEMQTvrQEQLLQE 2630
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKE-----ESGKAQAE--VERLLGILREVENEKnDKDKKIAELESLTLRQMKE--QNKKVAN 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2631 TQALQQsflsekdsllqrercieQEKAKLEQLFQDevakaqALREEQQRQQQQMQQEKQQLAASMEEARRrqhEAEEGVR 2710
Cdd:pfam10174 623 IKHGQQ-----------------EMKKKGAQLLEE------ARRREDNLADNSQQLQLEELMGALEKTRQ---ELDATKA 676
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1920237940 2711 RQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2753
Cdd:pfam10174 677 RLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAIS 719
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2419-2662 |
1.50e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.71 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2419 VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--KEKMQAVQEATRLKAEAELLQQQKELAQEQAR--------- 2487
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlaKEEDLKRQNAVLQEAQVELDALQNQLALARAEmenikavat 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2488 ----RLQEDKEQMAQQLAQETQGFQKTL-ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfrkqaedigerlyR 2562
Cdd:pfam03528 86 vsenTKQEAIDEVKSQWQEEVASLQAIMkETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRR-------------R 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2563 TELATQEkvmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA--------- 2633
Cdd:pfam03528 153 LSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAekscrtdle 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237940 2634 -------LQQSFLSEKDSLLQRE-----RCIEQEKAKLEQL 2662
Cdd:pfam03528 228 myvavlnTQKSVLQEDAEKLRKElhevcHLLEQERQQHNQL 268
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2179-2614 |
1.56e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 44.96 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2179 LQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAE 2258
Cdd:COG4995 1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2259 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQL 2338
Cdd:COG4995 81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2339 EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQ 2418
Cdd:COG4995 161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2419 VAEEAARLSvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2498
Cdd:COG4995 241 LALAAAAAA-LAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2499 QLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEM-SRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2577
Cdd:COG4995 320 LAALLLLLAALALLALLLLLAAAALLAAALAAALALAaALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAA 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 1920237940 2578 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2614
Cdd:COG4995 400 LLALAAAQLLRLLLAALALLLALAAYAAARLALLALI 436
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1512-1718 |
1.57e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1512 LEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAaersrl 1591
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREEL-QREEERLVQKEEQLDA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1592 RIEEeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdETQRKRQAEAELALRVQAEAEaa 1671
Cdd:PRK12705 96 RAEK--------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237940 1672 REKQRALQALEelrlqaEEAerrlrQAEAERARQVQVAlETAQRSAE 1718
Cdd:PRK12705 157 EEKAQRVKKIE------EEA-----DLEAERKAQNILA-QAMQRIAS 191
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2330-2673 |
1.57e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2330 ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELG----KLKARIEA-ENralvlrDKDS 2404
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkynDLKKQKEElEN------ELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2405 AQRLLQEEAEKMKQVAEEAAR----LSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ 2478
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKlellLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2479 -KELAQEQarrlQEDKEQMAQQLAQETQGFQKTLETERQRQlEMSAEAERLRlrvaemsraqaraeedarrfRKQAEDIG 2557
Cdd:TIGR04523 255 lNQLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN--------------------NQKEQDWN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2558 ERLyRTELATQEKVmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlkseemqtvrqEQLLQETQALQQs 2637
Cdd:TIGR04523 310 KEL-KSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ-----------RELEEKQNEIEK- 374
|
330 340 350
....*....|....*....|....*....|....*.
gi 1920237940 2638 FLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQAL 2673
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1872-2184 |
1.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1872 RQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1951
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1952 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 2031
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2032 ADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 2111
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 2112 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2184
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2300-2464 |
1.59e-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: 43.37 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2300 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2379
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2380 mEELGKLKARIEAENRALVLRDkDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2459
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 1920237940 2460 QAVQE 2464
Cdd:COG1579 167 ELAAK 171
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1536-2201 |
1.60e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1536 LQRRMQeevARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRL---RIEEEIRVVR-LQLEATERQR 1611
Cdd:pfam07111 21 LERRLD---TQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQelrRLEEEVRLLReTSLQQKMRLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1612 GGA-EGELQALRARAEEAEAQK-RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKqralqALEELRLQAE 1689
Cdd:pfam07111 98 AQAmELDALAVAEKAGQAEAEGlRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE-----ALSSLTSKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1690 EAERRLRQAEAERARQVQvALETAQRsaEAELQSEHASFAEKTAQLERTLKEEHVAVV--QLREEATRRAQQQAEAERAR 1767
Cdd:pfam07111 173 GLEKSLNSLETKRAGEAK-QLAEAQK--EAELLRKQLSKTQEELEAQVTLVESLRKYVgeQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1768 AEAERELERWQLKAN-EALRLRLQaeevaqqkSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG 1846
Cdd:pfam07111 250 TMQHLQEDRADLQATvELLQVRVQ--------SLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1847 TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQReaaAATQKRRELEAELAKVRA-EMEVLLASKARAEEESRSTS 1925
Cdd:pfam07111 322 LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQR---ALQDKAAEVEVERMSAKGlQMELSRAQEARRRQQQQTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1926 EKSKQRLEAEAGRFRELAEEAARLRaLAEEAKRQRQLAEE--DAVRQRAEAERVLAEKLAAIS---EATRLKTEAEIALK 2000
Cdd:pfam07111 399 AEEQLKFVVNAMSSTQIWLETTMTR-VEQAVARIPSLSNRlsYAVRKVHTIKGLMARKVALAQlrqESCPPPPPAPPVDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2001 EKEAENERLRRlaedeafQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKA 2080
Cdd:pfam07111 478 DLSLELEQLRE-------ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2081 AAGKAELELELGRIRGTAEDTLRSKEQAEQEA-----ARQRQLAAEEERRRREAEERVQK---SLAAEEEAARQRKAALE 2152
Cdd:pfam07111 551 RQGQQESTEEAASLRQELTQQQEIYGQALQEKvaeveTRLREQLSDTKRRLNEARREQAKavvSLRQIQHRATQEKERNQ 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2153 EVERLK--AKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEKAHAFAV 2201
Cdd:pfam07111 631 ELRRLQdeARKEEGQRLARRVQElERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1482-1754 |
1.61e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.71 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAQGLQRRMQEevARREEVAVEAQEQKRSI 1561
Cdd:pfam03528 96 DEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQ-WNQYRESAEREIADLRRRLSE--GQEEENLEDEMKKAQED 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1562 QEELQHLRQSSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALraraeeaEAQKRQAQEEAE 1640
Cdd:pfam03528 173 AEKLRSVVMPMEKEIAAlKAKLTEAEDKIKELEASKMKELNHYLEAEKSCRTDLEMYVAVL-------NTQKSVLQEDAE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1641 RLRRQVQDETQRkrqaeaeLALRVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVqvalETAQRSAEA 1719
Cdd:pfam03528 246 KLRKELHEVCHL-------LEQERQQHNQLKHTWQKANdQFLESQRLLMRDMQRMESVLTSEQLRQV----EEIKKKDQE 314
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237940 1720 ELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAT 1754
Cdd:pfam03528 315 EHKRARTHKEKETLKSDREHTVSIHAVFSPAGVET 349
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2463-2541 |
1.64e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 44.32 E-value: 1.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2463 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAQETqgfqKTLETERQRQLEMSAEAERLRLRVAEMSRAQAR 2541
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQA----KALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
665-759 |
1.70e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.78 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 665 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQL---SPATRGAYRDCLGRLD 741
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1920237940 742 LQYAKLLSSSKARLRSLE 759
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1838-2111 |
1.75e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 44.08 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1838 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASK 1914
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1915 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAVRQRAEA 1974
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1975 ErvLAEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRLLE--EQAAQHKADIEARLAQLRKASES 2047
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 2048 ELERQKGLVEDTLRQRrqVEEeilalkgsFEKAaagKAELELELGRIRgtaedtlrsKEQAEQE 2111
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTL---------QEIAELE 278
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1603-2066 |
2.01e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1603 QLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE 1682
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1683 ELRLQAEEAERRLRQAEAERARQVQValETAQRSAE--AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1760
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKA--EEAKRKAEeeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1761 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1840
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1841 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1920
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1921 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 2000
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 2001 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQV 2066
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1618-1742 |
2.02e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1618 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEaarekqralQALEELRLQAEEAERRLRQ 1697
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ---------QAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1920237940 1698 AEAERARQVqvaletaqrsAEAELQSEHASFAEKTAQLERTLKEE 1742
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1603-1718 |
2.08e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1603 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAL 1681
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237940 1682 EELR---------LQAEEAERRLRQAE-AERARQVQVALetAQRSAE 1718
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKiADLGRRLNVAL--AQRVQE 191
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1263-1673 |
2.10e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.90 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1263 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerLQQRHGERDVEVERWRERvtllLERWQAVLAQTDVRQ 1342
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAG-------LTRRLSAAEGELEELVAR----LAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1343 RELEQLGRQLRYYRESADplgawlRDAKQRQEQIQAVPLANsQAVREQLRQEKALLEDIERHGEKVEECQRFAKQyinai 1422
Cdd:pfam19220 107 EELRIELRDKTAQAEALE------RQLAAETEQNRALEEEN-KALREEAQAAEKALQRAEGELATARERLALLEQ----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1423 kdyelqlvtykaqlepvaspaKKPKVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRA 1499
Cdd:pfam19220 175 ---------------------ENRRLQALSEEQAAELAELTRRLAELETQldaTRARLRALEGQLAAEQAERERAEAQLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1500 EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAK 1579
Cdd:pfam19220 234 EAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----EADLERR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1580 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaeAE 1659
Cdd:pfam19220 310 TQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQRER---AE 386
|
410
....*....|....
gi 1920237940 1660 LALrVQAEAEAARE 1673
Cdd:pfam19220 387 RAL-AQGALEIARE 399
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1824-1968 |
2.15e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1903
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 1904 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV 1968
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAI 356
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2461-2715 |
2.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2461 AVQEATRLKAEAELLQQQKEL--AQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2538
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2539 QARAEEDARRFRKQ------------AEDIGE---RLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKD 2603
Cdd:COG3883 85 REELGERARALYRSggsvsyldvllgSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2604 KLKQEAQLLQLKSEEmqtvrQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQ 2683
Cdd:COG3883 165 ELEAAKAELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 1920237940 2684 MQQEKQQLAASMEEARRRQHEAEEGVRRQQEE 2715
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1475-1669 |
2.31e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1475 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqakAQAEREAQgLQRRMQEEVARREEVAVEA 1554
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD---------EKAERDEL-RAKLYQEEQERKERQKERE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1555 QEQKRsiQEELQHLRQSSEAEIQAKARQvEAAERSRLRIEEEiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1634
Cdd:pfam13868 226 EAEKK--ARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 1920237940 1635 AQEEAERLRRQVQDETQRKRQAEAELALRVQAEAE 1669
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2417-2758 |
2.37e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2417 KQVAEEAARLSVAA--QEAARLRQLAEEDLAQQRALAEKmlkekmqavqEATRLKAEAELLQQQKELAQEQARR--LQED 2492
Cdd:PRK04863 260 KHLITESTNYVAADymRHANERRVHLEEALELRRELYTS----------RRQLAAEQYRLVEMARELAELNEAEsdLEQD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2493 KEQMA--QQLAQETQGFQKTLE------TERQRQLEMSAEAERLRLRVAEMSRAQAR-AEEDARRFRKQAEDIGERL--- 2560
Cdd:PRK04863 330 YQAASdhLNLVQTALRQQEKIEryqadlEELEERLEEQNEVVEEADEQQEENEARAEaAEEEVDELKSQLADYQQALdvq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2561 YRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqLLQLksEEMQTVRQEQLLQETQALQ--QSF 2638
Cdd:PRK04863 410 QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE--LLSL--EQKLSVAQAAHSQFEQAYQlvRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2639 LSEKDsllqRERCIEQEKAKLEQL--FQDEVAKAQALReeqqrqqqqmqqekqqlaASMEEARRRQHEAEEGVRRQQEEL 2716
Cdd:PRK04863 486 AGEVS----RSEAWDVARELLRRLreQRHLAEQLQQLR------------------MRLSELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237940 2717 QRLAQQQQQQEkLLAEENQRLRERLQHLEEERRAALARSEEI 2758
Cdd:PRK04863 544 KRLGKNLDDED-ELEQLQEELEARLESLSESVSEARERRMAL 584
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1592-1722 |
2.38e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.89 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1592 RIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAA 1671
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1672 REKQRAL-----QALEELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQ 1722
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKKD-----TLKARAKAAKAQEK 150
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2575-2758 |
2.44e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2575 QTLETQRQQSDR----DAERLREAIAELEHEKDKLKqeaqllqlKSEEMQTVRQEQLLQETQ--ALQQSFLSEKDSLLQR 2648
Cdd:pfam17380 281 QKAVSERQQQEKfekmEQERLRQEKEEKAREVERRR--------KLEEAEKARQAEMDRQAAiyAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2649 ERcIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEK 2728
Cdd:pfam17380 353 IR-QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190
....*....|....*....|....*....|.
gi 1920237940 2729 LLAEENQRL-RERLQHLEEERRAALARSEEI 2758
Cdd:pfam17380 432 ARQREVRRLeEERAREMERVRLEEQERQQQV 462
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1486-1840 |
2.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1486 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEEL 1565
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1566 QHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1645
Cdd:COG4372 83 EELNE----QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1646 VQDETQRKRQAEAELALRVQAEAEaaREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEH 1725
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAE--QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1726 ASFaEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEA 1805
Cdd:COG4372 237 ALL-DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350
....*....|....*....|....*....|....*
gi 1920237940 1806 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1840
Cdd:COG4372 316 ALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1461-1722 |
2.52e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 43.49 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1461 DLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQaKAQAEREAQGLQRRM 1540
Cdd:COG1538 77 EVAQAYFDLLAAQEQ-LALAEENLALAEELLELARARYEAGLASRLDVLQA---EAQLAQARAQ-LAQAEAQLAQARNAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1541 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA------EIQAKARQVEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1614
Cdd:COG1538 152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEalerrpDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1615 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1675
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1676 RALQALEEL-------RLQAEEAERRLRQAEAERarqvqVALETAQRSAEAELQ 1722
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1157-1754 |
2.55e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1157 EPARECAQRITEQQKAQAEVDGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIYlEKLKTISL 1236
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHTR-QQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1237 VIRSTQEAEEVLRAHeeQLKEAQAVPATLPELeatkaalkklrAQAEAQQPVFDALRDELRG-----AQEVGERLQQRhg 1311
Cdd:PRK10246 319 RLQSTMALRARIRHH--AAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1312 erdveveRWRERVTLLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLRDAKQRQEQIQAvplANSQA 1386
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1387 VREQLRQEKALLEDIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1439
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1440 ASPAKKPKVQSGSESIIQEYVDLRtrySELSTLTSQYIRFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1519
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1520 EAHAQ-AKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQV--EAAERSRL--RIE 1594
Cdd:PRK10246 596 DDIQPwLDAQEEHERQLRLLSQRHEL---QGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLpqEDEEASWLatRQQ 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1595 EEIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DETQRKRQAEA 1658
Cdd:PRK10246 673 EAQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1659 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLrqaeaERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1738
Cdd:PRK10246 753 QFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQI 827
|
650
....*....|....*.
gi 1920237940 1739 LKEEHVAVVQLREEAT 1754
Cdd:PRK10246 828 QQELAQLAQQLRENTT 843
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2318-2759 |
2.61e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2318 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRA 2396
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2397 LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE------DLAQQRALAEKMLKEKMQAVQEATRLKA 2470
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelkeELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2471 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQetqgFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFR 2550
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2551 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSdRDAERLREAIAELEHEKDK--LKQEAQLLQLKSE----------- 2617
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARAS-EERVRGGRAVEEVLKASIQgvHGTVAQLGSVGERyataievaagn 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2618 -------EMQTVRQE--QLLQETQALQQSFL-------SEKD-SLLQRERCI----------EQEKAKLEQLFQDEV--- 2667
Cdd:TIGR02169 548 rlnnvvvEDDAVAKEaiELLKRRKAGRATFLplnkmrdERRDlSILSEDGVIgfavdlvefdPKYEPAFKYVFGDTLvve 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2668 ----------------------------------------------AKAQALREEQQRQQQQMQQEKQQLA---ASMEEA 2698
Cdd:TIGR02169 628 dieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepAELQRLRERLEGLKRELSSLQSELRrieNRLDEL 707
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2699 RRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEenqrLRERLQHLEEERRAALARSEEIA 2759
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE----LEEDLSSLEQEIENVKSELKELE 764
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2460-2757 |
2.70e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2460 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRvaemsrAQ 2539
Cdd:pfam02029 6 EAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK------RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2540 ARAEEDARRFRKQAEDIGErlyrtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELE------------------HE 2601
Cdd:pfam02029 80 QEALERQKEFDPTIADEKE-----SVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEirekeyqenkwstevrqaEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2602 KDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2681
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2682 QQMQQEKQQLAA--SMEEARRRQHEAEEgvrrqqEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA-------AL 2752
Cdd:pfam02029 235 EREEEAEVFLEAeqKLEELRRRRQEKES------EEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRrkqeeaeRK 308
|
....*
gi 1920237940 2753 ARSEE 2757
Cdd:pfam02029 309 LREEE 313
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2249-2435 |
2.71e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2249 QSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKeaeqeaarraqaeqAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2328
Cdd:pfam15709 360 QRRLQQEQLERAEK-MREELELEQQRRFEEIRLRK--------------QRLEEERQRQEEEERKQRLQLQAAQERARQQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2329 QEltALRLQLEETDHQKsildeelQRLKAEVTEAARQRGQVEEElfslrvQMEELGKLKARIEAENRALVLRDKDSAQRL 2408
Cdd:pfam15709 425 QE--EFRRKLQELQRKK-------QQEEAERAEAEKQRQKELEM------QLAEEQKRLMEMAEEERLEYQRQKQEAEEK 489
|
170 180 190
....*....|....*....|....*....|..
gi 1920237940 2409 LQEEAEKMKQVAEEAARLSVA-----AQEAAR 2435
Cdd:pfam15709 490 ARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1328-1601 |
2.73e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1328 LERWQAVLAQTDVRQRELEQLGRQLryyrESADplgawlRDAKQRQEQIQAVPLANSQAVREQLrqEKALLEDIERhgeK 1407
Cdd:PRK11281 65 LEQTLALLDKIDRQKEETEQLKQQL----AQAP------AKLRQAQAELEALKDDNDEETRETL--STLSLRQLES---R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1408 VEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSelSTLTSQyiRFISETLR-R 1486
Cdd:PRK11281 130 LAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPSQRvL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1487 MEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAEREAQGLQRRM-QEEVARREEVAVEAQEQKRS-- 1560
Cdd:PRK11281 197 LQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQEAInSKRLTLSEKTVQEAQSQDEAar 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1561 ------IQEELQHLRQSSEAEIQAKAR-------------QVEAAERSRLRIEEEIRVVR 1601
Cdd:PRK11281 274 iqanplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1954-2203 |
2.76e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1954 EEAKRQRQLAEEDAVRQRAEAERVLAEKLAA-ISEATRLKTEAEIALKEKEAENerlrrlaedeafqrrlLEEQAAQHKA 2032
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGAeISKLEEENREKEKALPKNDDMT----------------IEEAKRRAAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2033 DIEARLAQLRKASESELERQkglvedtlrqrrqVEEEILALKGSFEKAAAGKAElELELGRIRGTAEDTLRSKEQAEQEA 2112
Cdd:PRK07735 66 AAKAKAAALAKQKREGTEEV-------------TEEEKAKAKAKAAAAAKAKAA-ALAKQKREGTEEVTEEEKAAAKAKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2113 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2192
Cdd:PRK07735 132 AAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAA 211
|
250
....*....|.
gi 1920237940 2193 EEKAHAFAVQQ 2203
Cdd:PRK07735 212 KAKAAALAKQK 222
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2425-2543 |
2.76e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2425 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2501
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 2502 ------QETQGFQKTLETERQRQLEMSAEAERLR-------LRVAEMSRAQARAE 2543
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKEI 158
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1569-1722 |
2.84e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.18 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1569 RQSSEAEIQAKARQVEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1646
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1647 QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1722
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1864-2086 |
2.88e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1864 ETEQGEQQRQLLEEELARLQ-----------REAAAATQKRRELEAELAKVRAEMevllASKARAEEESRSTSEKSKQRL 1932
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHgaeiskleeenREKEKALPKNDDMTIEEAKRRAAA----AAKAKAAALAKQKREGTEEVT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1933 EAEAGRFRELAEEAARLRAlAEEAKRQRQLAEEDAVRQRAEAERVLAE------------KLAAISEATRLKTEAEIAL- 1999
Cdd:PRK07735 87 EEEKAKAKAKAAAAAKAKA-AALAKQKREGTEEVTEEEKAAAKAKAAAaakakaaalakqKREGTEEVTEEEEETDKEKa 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2000 --KEKEAENERLRRLAEDEAFQRRLLEEQAAQH-KADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEE-ILALKG 2075
Cdd:PRK07735 166 kaKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEeKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKaIAAAKA 245
|
250
....*....|.
gi 1920237940 2076 SFEKAAAGKAE 2086
Cdd:PRK07735 246 KAAAAARAKTK 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2078-2560 |
2.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2078 EKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERvQKSLAAEEEAARQRKAALEEVERL 2157
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2158 KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaARRAAEEAE 2237
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-----LQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2238 AARERAEREAAQSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFA 2317
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2318 EQAL---------RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAArqrgqveEELFSLRVQMEELGKLKA 2388
Cdd:COG4717 282 VLGLlallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2389 RIE-AENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmqAVQEATR 2467
Cdd:COG4717 355 EAEeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2468 LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQ-ETQGFQKTLETERQRQLEMSAEAER--LRLRVAE--MSRAQARA 2542
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEewAALKLALelLEEAREEY 509
|
490
....*....|....*....
gi 1920237940 2543 EEDAR-RFRKQAEDIGERL 2560
Cdd:COG4717 510 REERLpPVLERASEYFSRL 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1209-1425 |
2.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1209 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraqaEAQQPV 1288
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1289 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDvrqrELEQLGRQLRYYResadpLGAWLRD 1368
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE----AAEDLARLELRAL-----LEERFAA 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 1369 AKQRqeqiqavplANSQAVREQLRQE-KALLEDIERHGEKVEEC-QRFAKQYINAIKDY 1425
Cdd:COG4913 758 ALGD---------AVERELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2414-2508 |
2.99e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 43.04 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2414 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2487
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 1920237940 2488 RLQEDKEQMAQQLAQETQGFQ 2508
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2378-2673 |
3.06e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.74 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2378 VQMEE---LGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAE 2452
Cdd:pfam15964 341 VQMTEeanFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2453 KMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAQETQgfqKTLETERQRQLEMS-AEAERLRL 2530
Cdd:pfam15964 421 KVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH---REYRTKTGRQLEIKdQEIEKLGL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2531 RVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE----LATQEKVMLVQTL----ETQRQQSDRDAERLREAIAELE--H 2600
Cdd:pfam15964 496 ELSESKQRLEQAQQDAARAREECLKLTELLGESEhqlhLTRLEKESIQQSFsneaKAQALQAQQREQELTQKMQQMEaqH 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2601 EKD----------------KLKQEAQLLQLKSEEM-QTVRQE--QLLQETQALQQSFLSEK-------DSLLQRERCIEQ 2654
Cdd:pfam15964 576 DKTvneqyslltsqntfiaKLKEECCTLAKKLEEItQKSRSEveQLSQEKEYLQDRLEKLQkrneeleEQCVQHGRMHER 655
|
330
....*....|....*....
gi 1920237940 2655 EKAKLEQLFQDEVAKAQAL 2673
Cdd:pfam15964 656 MKQRLRQLDKHCQATAQQL 674
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2252-2633 |
3.07e-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: 43.73 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2252 RQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAeQALRQKAQVEQEL 2331
Cdd:pfam07888 73 RQRRELES--------------------RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD-ALLAQRAAHEARI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2332 TALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLL 2409
Cdd:pfam07888 132 RELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2410 QEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ---- 2483
Cdd:pfam07888 212 QDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltlq 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2484 --EQARRLQEDKEQMaqqlAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEmsraqaraeedARRFRKQAEdigerly 2561
Cdd:pfam07888 288 laDASLALREGRARW----AQERETLQQSAEADKDRIEKLSAELQRLEERLQE-----------ERMEREKLE------- 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2562 rTELATQEKVMLVQTLETQRQQSDrdaerLREAIAELEHEKDKLKQEAQllqlksEEMQTVRQEQLLQETQA 2633
Cdd:pfam07888 346 -VELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAEKQ------ELLEYIRQLEQRLETVA 405
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
186-300 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 186 QKKTFTKWVNKHLIKHwrAEAQRHI------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKL 259
Cdd:cd21292 25 EKVAFVNWINKNLGDD--PDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTID-ERAINKKKLTV-------FTIH 94
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237940 260 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 300
Cdd:cd21292 95 ENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1566-2055 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1566 QHLRQSSEAEIQAKARqVEAAERSRLRIEEEIRVVRLQLEATERQRGGA--EGELQALRARAEEAEAQKRQAQEEAERLR 1643
Cdd:COG3064 2 QEALEEKAAEAAAQER-LEQAEAEKRAAAEAEQKAKEEAEEERLAELEAkrQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1644 RQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEELRLQAEEaerrlRQAEAERARQVQVALETAQRSAEAELQS 1723
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKA-KAAKEAEAAAAAEKAAAAAEKEKAEEAK-----RKAEEEAKRKAEEERKAAEAEAAAKAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1724 EHASFAEKTAQLERTLKEEhVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1803
Cdd:COG3064 155 EAARAAAAAAAAAAAAAAR-AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1804 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1883
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1884 REAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1963
Cdd:COG3064 314 EEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1964 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRK 2043
Cdd:COG3064 394 AAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDG 473
|
490
....*....|..
gi 1920237940 2044 ASESELERQKGL 2055
Cdd:COG3064 474 GAVLADLLLLGG 485
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2328-2758 |
3.13e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2328 EQELTALRLQLEETDHQKSILDEELQRLKAEVTeAARQRGQV-EEELFSLRVQMEElgklKARIEAEnRALVLRDKDSAQ 2406
Cdd:pfam10174 302 ESELLALQTKLETLTNQNSDCKQHIEVLKESLT-AKEQRAAIlQTEVDALRLRLEE----KESFLNK-KTKQLQDLTEEK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2407 RLLQEEAEKMKQVAEEAARLSVAAQEaaRLRQLAEEDLAQQRALAEkmLKEKMQAVQEATRLKAEAelLQQQKELAQEQA 2486
Cdd:pfam10174 376 STLAGEIRDLKDMLDVKERKINVLQK--KIENLQEQLRDKDKQLAG--LKERVKSLQTDSSNTDTA--LTTLEEALSEKE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2487 R---RLQEDKEQMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2563
Cdd:pfam10174 450 RiieRLKEQREREDRERLEE-------LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2564 ELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAelehekDKLKQEAQLLQLKSEEMQTVRqeqllqetqalqqsflSE 2641
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKkaHNAEEAVRTNPEIN------DRIRLLEQEVARYKEESGKAQ----------------AE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2642 KDSLLQRERCIEQEK-------AKLEQLFQDEVaKAQALREEQQRQQQQMQQEKQqlAASMEEARRRQHEAEEGVRRQQ- 2713
Cdd:pfam10174 581 VERLLGILREVENEKndkdkkiAELESLTLRQM-KEQNKKVANIKHGQQEMKKKG--AQLLEEARRREDNLADNSQQLQl 657
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2714 ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEE---ERRAALarsEEI 2758
Cdd:pfam10174 658 eelmGALEKTRQELDATKARLSSTQQSLAEKDGHLTNlraERRKQL---EEI 706
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1617-1751 |
3.18e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1617 ELQALRARAEEAEAQKRQAQEEAERLRRQVQdetqrkrqaE-AELALRVQAEAEAAREKQRaLQALEELRLQAEEAERRL 1695
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLE---------ElEAAALQPGEEEELEEERRR-LSNAEKLREALQEALEAL 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1696 RQAEAerarQVQVALETAQRSAEaELQSEHASFAEKTAQLERtlkeehvAVVQLRE 1751
Cdd:COG0497 236 SGGEG----GALDLLGQALRALE-RLAEYDPSLAELAERLES-------ALIELEE 279
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3903-3934 |
3.31e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.31e-03
10 20 30
....*....|....*....|....*....|..
gi 1920237940 3903 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLI 3934
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2872-2905 |
3.31e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.31e-03
10 20 30
....*....|....*....|....*....|....
gi 1920237940 2872 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPE 2905
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1849-2111 |
3.37e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1849 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstseKS 1928
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK----EL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1929 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQR--------------AEAERVLAEKLAaiseatRLKTE 1994
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGG--SIDKLRKEierlewrqqtevlsPEEEKELVEKIK------ELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1995 AEIALKEKEAENERLRRLAEDEAFQrrlleEQAAQHKADIEARLAQLRKASES------ELERQKGLVEDTLRQRRQVEE 2068
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELR-----KEAEEIHKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237940 2069 EILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 2111
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2355-2649 |
3.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2355 LKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRAlvlrdkdsAQRLLQEEAEKMKQVAEEAARLSVAAQEAA 2434
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ--------ARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2435 RLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETE 2514
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2515 RQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREA 2594
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 2595 IAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRE 2649
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2027-2203 |
3.40e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2027 AAQHKADIEARLAQLRKasesELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKE 2106
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2107 QAEQEAARQRQLAAEEERRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2172
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 1920237940 2173 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2203
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1486-1673 |
3.41e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.45 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1486 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQglqrrmQEEVARREEVAVEAQEQKRSIQEEL 1565
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ------QEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1566 QHLRQSSEAEIQAKARQVeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1645
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 1920237940 1646 VQDETQR-KRQAEAElalrVQAEAEAARE 1673
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2405-2538 |
3.49e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.85 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2405 AQRLLQE-----EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELL 2475
Cdd:PTZ00491 672 AELLEQEargrlERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRI 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2476 QQQKELAQEQARRLQEdkeqmaqqLAQETQgfQKTLETERQRQLeMSAEAERL--------RLRVAEMSRA 2538
Cdd:PTZ00491 749 EAEAELEKLRKRQELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFerivealgRETLIAIARA 808
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1506-1713 |
3.54e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1506 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ--RRMQEEVARREEVAVEAQEQKRSIQE-----------ELQHLRQSS 1572
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1573 EAE------IQAKARQVEAAERSRLRIEEEIRVVrLQLEATERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1639
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1640 ERLRRQVQDETQRKRQAEAELAL-RVQAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEAERARQVQVALETA 1713
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALAaTHGYNPRDFRKRAEQALAANAKTATLALEAA 1381
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1494-1747 |
3.57e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1494 AEQQRAEERERlaeVEAALEkqrqlaEAHAQAKAQAEREAQGL---------------------QRRMQEEVARREEVAV 1552
Cdd:PHA03247 1586 AKQQRAEATDR---VTAALR------EALAAHERRAQSEAESLanlktllrvaaipataaktldQARSVAEIVDQIELLL 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1553 EAQEQKRSIQEE----LQHLRQSSEAEIQAKARQVEAAERSRLRieeeirvVRLQLEATERQRggaegeLQALRARAEEA 1628
Cdd:PHA03247 1657 EQTEKAAELDVAavdwLEHARRVFEAHPLTAARGGGPDPLARLH-------ARLDALGETRRR------TEALRRSLEAA 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1629 EAQKRQAQEEAERLRRQvqdetqrkrqaeaelALRVQAEAEAAREKQRALQALEE--LRLQAEEAERRLrqaeAERARQV 1706
Cdd:PHA03247 1724 EAEWDEVWGRFGRVRGG---------------AWKSPEALRAAREQLRALQTATNtvLGLRADAHYERL----PAKYQGA 1784
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237940 1707 qVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVAVV 1747
Cdd:PHA03247 1785 -LGAKSAERAGAVE---ELGAAVARHDGLLARLREEVVARV 1821
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1518-1705 |
3.59e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1518 LAEAHAQAKAQAEREAQGLQRRMQEEVARreevaveAQEQKRSIQEELQHLRQ-----SSEAEIQAKARQVeaaersrlr 1592
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVER-------AEERLRDAREALLAFRNrngilDPEATAEALLQLI--------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1593 ieeeirvvrLQLEAterQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL-RVQAEaeaa 1671
Cdd:COG3524 224 ---------ATLEG---QLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLaSLLAE---- 287
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237940 1672 rekqralqaLEELRLQAEEAERRLRQAEA--ERARQ 1705
Cdd:COG3524 288 ---------YERLELEREFAEKAYTSALAalEQARI 314
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1941-2082 |
3.70e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1941 ELAEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 2019
Cdd:COG2268 196 EIIRDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 2020 RRLLEEQAAQHKADIEARLAQLRKA-SESELERQKGLVEDTLRQRRQVEEEiLALKGSFEKAAA 2082
Cdd:COG2268 276 EREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEAEAE-AEAEAIRAKGLA 338
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1612-1752 |
4.05e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1612 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQrkrqaEAELALRVQAEAEAAREKQralqaleelRLQAEEa 1691
Cdd:PRK12705 19 GVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK-----ELLLRERNQQRQEARRERE---------ELQREE- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 1692 ERRLRQAEAERARQVQVALETAQRS-AEAELQSEHASFAEKTAQLERTLKEehvaVVQLREE 1752
Cdd:PRK12705 84 ERLVQKEEQLDARAEKLDNLENQLEeREKALSARELELEELEKQLDNELYR----VAGLTPE 141
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1584-1701 |
4.06e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1584 EAAerSRLRIE-----EEIRVVRLQLEATERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1658
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA 461
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 1659 elalRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1701
Cdd:COG0542 462 ----RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2381-2509 |
4.13e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2381 EELGKLKARIEAENRALVLRDKDSAQrlLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2460
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237940 2461 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAQETQGFQK 2509
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1829-1922 |
4.16e-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: 40.29 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1829 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEME 1908
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 1920237940 1909 VLLASKARAEEESR 1922
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1640-2622 |
4.16e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1640 ERLRRQVQDETQRKRQAEAELALRVQAEAEAA--REKQRALQALEEL------RLQAEEAERRLRQAEAERARQVQVALE 1711
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACeiRDQITSKEAQLESsreivkSYENELDPLKNRLKEIEHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1712 ---TAQRSAEAELQSEHASFAEKTAQL----ERTLKE-EHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1783
Cdd:TIGR00606 269 neiKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDlYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1784 ALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQrelaEQELEKQRQLAEG-TAQQRLAAEQELIRLR 1862
Cdd:TIGR00606 349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN----FHTLVIERQEDEAkTAAQLCADLQSKERLK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1863 aeteqgEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKAR--AEEESRSTSEKSKQRLEAEAGRFR 1940
Cdd:TIGR00606 425 ------QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1941 ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLaaiseaTRLKTEA-EIALKEKEAENERLRRLAEDEAFQ 2019
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEML------TKDKMDKdEQIRKIKSRHSDELTSLLGYFPNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2020 RRLLE--EQAAQHKADIEARLAQLRKasesELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAElELELGRIRGT 2097
Cdd:TIGR00606 573 KQLEDwlHSKSKEINQTRDRLAKLNK----ELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-ESDLERLKEE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2098 AEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2177
Cdd:TIGR00606 648 IEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2178 QLQLAqEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEA 2257
Cdd:TIGR00606 728 MLGLA-PGRQSIIDLKEKE----------------------IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2258 ERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaADAEMEKHKQFAEQALRQKAQVEQEltalrlq 2337
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK-QEKQHELDTVVSKIELNRKLIQDQQ------- 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2338 lEETDHQKSILDeELQRLKAEVTEAARQRGQVEEELFSLRVQMEELgklkARIEAENRALVLRDKDSAQRLLQEEAEKMK 2417
Cdd:TIGR00606 857 -EQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL----IREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2418 QVAEEAARLSVAAQE-AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2496
Cdd:TIGR00606 931 SKETSNKKAQDKVNDiKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ 1010
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2497 AQQLAQETQGFQKTLETERQRQLEMSAE---AERLRLRVAEMSRAQARAEEDARRFRKQaedigERLYRTELATQEKVML 2573
Cdd:TIGR00606 1011 KIQERWLQDNLTLRKRENELKEVEEELKqhlKEMGQMQVLQMKQEHQKLEENIDLIKRN-----HVLALGRQKGYEKEIK 1085
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 2574 VQTLETQRQQSDRDAERLREAIAELEHEKDKLKQ--------EAQLLQLKSEEMQTV 2622
Cdd:TIGR00606 1086 HFKKELREPQFRDAEEKYREMMIVMRTTELVNKDldiyyktlDQAIMKFHSMKMEEI 1142
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1822-1922 |
4.18e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1822 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1901
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 1920237940 1902 KvRAEMEVLLaskarAEEESR 1922
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1463-1796 |
4.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1463 RTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQE 1542
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1543 EVARREEvaveAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR 1622
Cdd:COG4372 92 AQAELAQ----AQEELESLQEEAEELQE----ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1623 ARAEEAEAQ-----KRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQ 1697
Cdd:COG4372 164 EELAALEQElqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1698 AEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERW 1777
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|....*....
gi 1920237940 1778 QLKANEALRLRLQAEEVAQ 1796
Cdd:COG4372 324 LAKKLELALAILLAELADL 342
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1479-1695 |
4.37e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1479 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAqglqRRMQEEVARREEVAVEAQEQK 1558
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRL----EQQTEQAKKLEEKAQAALTKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1559 RsiqeelQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1638
Cdd:pfam04012 81 N------EELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 1639 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQaLEELRLQAEEAERRL 1695
Cdd:pfam04012 155 GSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1519-1707 |
4.55e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1519 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEir 1598
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1599 vvRLQLEATERQRGGAEGELQALRARAEEAEA--QKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKQR 1676
Cdd:PRK12678 145 --AGEGGEQPATEARADAAERTEEEERDERRRrgDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRREERGRR 221
|
170 180 190
....*....|....*....|....*....|.
gi 1920237940 1677 ALQALEELRLQAEEAERRLRQAEAERARQVQ 1707
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1614-1723 |
4.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1614 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE-ELRLQ 1687
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREeELEKK 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237940 1688 AEEAERRLRQAEAERARqvqvaLETAQRSAEAELQS 1723
Cdd:PRK12704 116 EKELEQKQQELEKKEEE-----LEELIEEQLQELER 146
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1482-1595 |
4.85e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVAVEAQEQKR 1559
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237940 1560 SIQEELQHLRQSSEAeiqAKARQVEAAERSRLRIEE 1595
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAERQRQEREK 123
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1503-1674 |
4.87e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.10 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1503 ERLAEVEAALEK-QRQLAEAHAQAKAQAEREAQGLQRRMQEEV-ARREEVAVEAQEQKRSIQEELQHLRQsseaeiQAKA 1580
Cdd:pfam01442 4 DSLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQKDLeEVRAKLEPYLEELQAKLGQNVEELRQ------RLEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1581 RQVEAAERSRLRIEEEIRVVRlqlEATERQRGGAEGELQALRARAEE-AEAQKRQAQEEAERLRRQVQDETQ----RKRQ 1655
Cdd:pfam01442 78 YTEELRKRLNADAEELQEKLA---PYGEELRERLEQNVDALRARLAPyAEELRQKLAERLEELKESLAPYAEevqaQLSQ 154
|
170
....*....|....*....
gi 1920237940 1656 AEAELALRVQAEAEAAREK 1674
Cdd:pfam01442 155 RLQELREKLEPQAEDLREK 173
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1630-2102 |
4.88e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1630 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQR--ALQALEELRLQAEEAERRLRQAEAERARQvQ 1707
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELeaKRQAEEEAREAKAEAEQRAAELAAEAAKK-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1708 VALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA----VVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1783
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAekekAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1784 ALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRA 1863
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1864 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1943
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1944 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 2023
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237940 2024 EEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 2102
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2317-2570 |
5.13e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2317 AEQALRQKAQVEQELTALRLQLEETDHQK----------SILDEELQRLKAEVTEAARQRGQVEEELF-SLRVQMEELGK 2385
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATEGLCVHSLSkELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2386 LKARIEAEnRALVLRDKDSAQRLLQEEAEKM---KQVAEEAARLSVAAQEAARLRQLAEED------------------- 2443
Cdd:PLN02939 238 LKDDIQFL-KAELIEVAETEERVFKLEKERSlldASLRELESKFIVAQEDVSKLSPLQYDCwwekvenlqdlldratnqv 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2444 ------LAQQRALAEK--MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTL---- 2511
Cdd:PLN02939 317 ekaalvLDQNQDLRDKvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLsklk 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 2512 ETERQRQLEMSAEA------ERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEK 2570
Cdd:PLN02939 397 EESKKRSLEHPADDmpsefwSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGK 461
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1935-2044 |
5.21e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1935 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAVRQRAEAERVLAEKLAAISEATRLKTEAEIA-LKEKEAE 2005
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237940 2006 NErlrrlAEDEAFQRRLLEEQAAQHKAD-IEARL---AQLRKA 2044
Cdd:PRK11448 210 TS-----QERKQKRKEITDQAAKRLELSeEETRIlidQQLRKA 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1321-1592 |
5.33e-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: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1321 RERVTLLLERWQAVLAQTDVR---QRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKAL 1397
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1398 LEDIERHGEKVEECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESIIQEYvdlrtRYSELSTLTSQYI 1477
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1478 RFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQ 1557
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237940 1558 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR 1592
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
188-417 |
5.42e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.01 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 188 KTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLSGDSLPRERDVIRSSRLPREKGRM-RFHKLQNVQIAL 266
Cdd:COG5069 382 RVFTFWLNSLDVSP-------EITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRFKAFENENYAV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 267 DYLRHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMV------EG 333
Cdd:COG5069 452 DLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGlkgdkeEG 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 334 CQGLRCDNFTTSWRDGRLFNAIIHrhkPTLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPd 406
Cdd:COG5069 524 IRSFGDPAGSVSGVFYLDVLKGIH---SELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP- 598
|
250
....*....|.
gi 1920237940 407 EKSIITYVSSL 417
Cdd:COG5069 599 RLDVLTFIESL 609
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1484-1867 |
5.44e-03 |
|
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: 43.09 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1484 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAveaqeqkrSIQ 1562
Cdd:pfam05701 228 LKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLkAELAAYMESKLKEEADGEGNEKKTSTSIQAALA--------SAK 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1563 EELQHLRQSSE-AEIQAKARQVeAAERSRLRIEEEIRVVrlqleATERQRGGA--------EGELQALRARAEEAEAQKR 1633
Cdd:pfam05701 300 KELEEVKANIEkAKDEVNCLRV-AAASLRSELEKEKAEL-----ASLRQREGMasiavsslEAELNRTKSEIALVQAKEK 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1634 QAQEEAERLRRQVQdetqrkrqaeaelalrvQAEAEAAREKQRALQALEELRLQAEEAErrlrQAEAErARQVQVALETA 1713
Cdd:pfam05701 374 EAREKMVELPKQLQ-----------------QAAQEAEEAKSLAQAAREELRKAKEEAE----QAKAA-ASTVESRLEAV 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1714 QRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaeaeraraeaerelerwqLKANEALRLRLQAEE 1793
Cdd:pfam05701 432 LKEIEAAKASEKLALAAIKALQESESSAESTNQEDSPRGVT------------------------LSLEEYYELSKRAHE 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1794 VAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1867
Cdd:pfam05701 488 AEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQELRKWRAEHEQ 561
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1480-1588 |
5.56e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.28 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1480 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEahaqakaqAEREAQGLQRRMQEEVARReevavEA 1554
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIE--------AEKDAEVAKIQMQQKIMEK-----EA 223
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237940 1555 QEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAER 1588
Cdd:cd03406 224 EKKISEIEDEMHLAREKAraDAEYYRALREAEANKL 259
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2314-2505 |
5.71e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2314 KQFAEQALRQKAQVEQELTALRlqleETDHQKSILDEELQRLkaevtEAARQRGQVEEELFSLRVQMEELGKLKARIEAE 2393
Cdd:pfam10174 568 ARYKEESGKAQAEVERLLGILR----EVENEKNDKDKKIAEL-----ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2394 NRALVLRD---KDSAQRLLQE---EAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2466
Cdd:pfam10174 639 EEARRREDnlaDNSQQLQLEElmgALEKTRQELDATkARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAI 718
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1920237940 2467 RLK----AEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQ 2505
Cdd:pfam10174 719 SEKdaniALLELSSSKKKKTQEEVMALKREKDRLVHQLKQQTQ 761
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1879-2016 |
5.73e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 42.99 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1879 LARLQREAAAATQKRRELEAELAKVRAEM--EVLLASKARAEEesrstseKSKQRLEAEAGRFR---ELAEEAARLRALA 1953
Cdd:pfam04147 139 LKRVRRAHFGGGEDDEEEEPERKKSKKEVmeEVIAKSKLHKYE-------RQKAKEEDEELREEldkELKDLRSLLSGSK 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237940 1954 EEAKRQRQLAEEDAVRQRAEAE-----RVLA-EKLAAISEatRLKTEAEIALKEKE----AENERLRRLAEDE 2016
Cdd:pfam04147 212 RPKPEQAKKPEEKPDRKKPDDDydklvRELAfDKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRMRGEE 282
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2379-2674 |
5.75e-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: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2379 QMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2458
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2459 MQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMS 2536
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2537 RAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS 2616
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237940 2617 EEMQTVRQEQLLQETQALQQSFLSEKDSLLQ----RERCIEQEKAKLEQLFQDEVAKAQALR 2674
Cdd:pfam13868 267 LRKQAEDEEIEQEEAEKRRMKRLEHRRELEKqieeREEQRAAEREEELEEGERLREEEAERR 328
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1488-1675 |
5.77e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1488 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER--------EAQGLQRRMQ-----EEVARREEVAVEA 1554
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegEIEAKEADHKgeteaEEVEHEGETEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1555 QEQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1629
Cdd:TIGR00927 726 TEDEGEIEtgEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237940 1630 AQKRQAQEEAERlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1675
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1485-1580 |
5.85e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.37 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1485 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAEREAQGLqrrmqeevaRREEVAV---EAQEQ 1557
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKL---------AAEALAEaqaEAQAS 102
|
90 100
....*....|....*....|...
gi 1920237940 1558 KRSIQEELQHLRQSSEAEIQAKA 1580
Cdd:PRK07353 103 KEKARREIEQQKQAALAQLEQQV 125
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1821-1961 |
6.07e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 41.89 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1821 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA-- 1898
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 1899 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1961
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1361-1561 |
6.27e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1361 PLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRfakqyinAIKDYELQLVTYKAQL-EPV 1439
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQIdELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1440 ASPAKKPKVQSGSESIIQEYVDLRTRYSE-------LSTLTSQ-------YIRFISE----------------TLRRMEE 1489
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAAFRQGEhtglqliLSGEESQrgerilaYFGYLNQarqetiaelkqtreelAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1490 EERLAEQQ----------------RAEERERLAEVEAALEK-QRQLAE--------------AHAQAKAQAEREAQGLQR 1538
Cdd:PRK11637 190 EEKQSQQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAAR 269
|
250 260
....*....|....*....|....
gi 1920237940 1539 -RMQEEVARREEVAVEAQEQKRSI 1561
Cdd:PRK11637 270 vRDKQKQAKRKGSTYKPTESERSL 293
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1485-1892 |
6.52e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1485 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1563
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1564 ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1643
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1644 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS 1723
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1724 EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1803
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1804 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1883
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*....
gi 1920237940 1884 REAAAATQK 1892
Cdd:COG3064 424 LALAGAAGA 432
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3828-3866 |
6.61e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.31 E-value: 6.61e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1920237940 3828 YLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVARQL 3866
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2567-2817 |
6.66e-03 |
|
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: 43.04 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2567 TQEKVMLVQTLETQRQQSDRDAERLREaIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLL 2646
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIID-LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2647 QRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQ 2726
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2727 EKLLAEENQRLRERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFD-GLRRKVPAQRLQEVG 2805
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSsAAKLKEEELELKSEE 403
|
250
....*....|..
gi 1920237940 2806 VLSAEELQQLAQ 2817
Cdd:pfam02463 404 EKEAQLLLELAR 415
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1574-1727 |
6.66e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.58 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1574 AEIQAKARQVEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElqALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1653
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA--AAATPAAPAAAARRAARAAAAARQAEQPAAEAAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237940 1654 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHAS 1727
Cdd:PRK12678 100 AKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERR 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1824-1989 |
6.80e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1824 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1903
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1904 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1983
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
....*.
gi 1920237940 1984 AISEAT 1989
Cdd:COG3883 275 GAAAAS 280
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1263-1706 |
6.84e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1263 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQ 1342
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1343 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAI 1422
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1423 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEER 1502
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1503 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQ 1582
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1583 VEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL 1662
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1920237940 1663 RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1706
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2063-2625 |
6.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2063 RRQVEEEILALKgSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlAAEEERRRREAEERVQKSLAAEEE 2142
Cdd:PRK03918 147 REKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK-ELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2143 AARQRKaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERL 2222
Cdd:PRK03918 225 KLEKEV---KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2223 RSEAEAARRAAEEAEAARERAEREAaqsRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ 2302
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGI---EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2303 KQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK----------AEVTEAARQRGQVE-- 2370
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKELLEEyt 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2371 EELFSLRVQMEELGKLKARIEAENRAL-VLRDKDSAQRLLQEEAEKMKQVAEE-----AARLSVAAQEAARLRQLAEEDL 2444
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELeKVLKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKLKEKLIKLK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2445 AQQRALAE-----KMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARRLQEDKEQMaqqlaQETQGFQK---TLETERQ 2516
Cdd:PRK03918 539 GEIKSLKKeleklEELKKKLAELEKKLD-ELEEELAELLKELEELGFESVEELEERL-----KELEPFYNeylELKDAEK 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2517 RQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLvqtletqrqQSDRDAERLREAIA 2596
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL---------ELSRELAGLRAELE 683
|
570 580
....*....|....*....|....*....
gi 1920237940 2597 ELEHEKDKLKQEAQLLQLKSEEMQTVRQE 2625
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1590-1707 |
7.00e-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: 39.52 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1590 RLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDETQR-KRQAEAELALRVQ 1665
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLeqkRQEAEEEKERlEESAEMEAEEKEQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237940 1666 AEAEAAREKQRALQALEELRLQAEEAERrlRQAEAERARQVQ 1707
Cdd:pfam20492 81 LEAELAEAQEEIARLEEEVERKEEEARR--LQEELEEAREEE 120
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2541-2720 |
7.09e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2541 RAEEDARRFRKQAEDIGERLYRTELATQEKvmlvqtlETQRQQSDRDAERLREAIAELEHEKDKLKQEAQL--------- 2611
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQ-------EEQRRLQQEQLERAEKMREELELEQQRRFEEIRLrkqrleeer 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2612 LQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQ-EKAKLEQLFQDEVaKAQALREEQQRQQQQMQQEKQQ 2690
Cdd:pfam15709 401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEaERAEAEKQRQKEL-EMQLAEEQKRLMEMAEEERLEY 479
|
170 180 190
....*....|....*....|....*....|
gi 1920237940 2691 LAASMEEARRRQHEAEEGvRRQQEELQRLA 2720
Cdd:pfam15709 480 QRQKQEAEEKARLEAEER-RQKEEEAARLA 508
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2348-2443 |
7.11e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2348 LDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALvlrdkdsAQRLLQEEAEKMKQVAEEAARLS 2427
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL-------EAQLEQLQEKAAETSQERKQKRK 219
|
90
....*....|....*.
gi 1920237940 2428 VAAQEAARLRQLAEED 2443
Cdd:PRK11448 220 EITDQAAKRLELSEEE 235
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1849-2260 |
7.19e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1849 QQRLAAEQELIRLRAETEQGEQQRQLL---EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS 1925
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLdelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1926 EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAE 2005
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2006 NERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKA 2085
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2086 ELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2165
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2166 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2245
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410
....*....|....*
gi 1920237940 2246 EAAQSRRQVEEAERL 2260
Cdd:COG5278 483 ALAEAEAAAALAAAA 497
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1470-1724 |
7.21e-03 |
|
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: 42.71 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1470 STLTSQYIRFISETLRRMEEEE---------RLAEQQ-RAEERERLaeVEAALEKQRQLAEAHAQAKAQAEREAQGLQRR 1539
Cdd:pfam05667 203 SVVPSLLERNAAELAAAQEWEEewnsqglasRLTPEEyRKRKRTKL--LKRIAEQLRSAALAGTEATSGASRSAQDLAEL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1540 MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsRLRIEEEIRVVRLQLEATERQRGGAEGELQ 1619
Cdd:pfam05667 281 LSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEEL-QQQREEELEELQEQLEDLESSIQELEKEIK 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1620 ALRARAEEAEAQKRQAQEEAERLrrqvQDETQRKRQAEAEL--------ALRVQAEAEAAR--------EKQRA--LQAL 1681
Cdd:pfam05667 360 KLESSIKQVEEELEELKEQNEEL----EKQYKVKKKTLDLLpdaeeniaKLQALVDASAQRlvelagqwEKHRVplIEEY 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1920237940 1682 EELRL----QAEEAERRLRQAEAERaRQVQVALETAQRSAE--AELQSE 1724
Cdd:pfam05667 436 RALKEaksnKEDESQRKLEEIKELR-EKIKEVAEEAKQKEElyKQLVAE 483
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2330-2720 |
7.26e-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: 42.64 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2330 ELTALRLQLEETDHQKSILdEELQRLKAEVTEAARQRGQVEEELFSLrvqmEELGKLKARIEAENRALVLRDKDSAQRLL 2409
Cdd:COG5185 174 QNLKKLEIFGLTLGLLKGI-SELKKAEPSGTVNSIKESETGNLGSES----TLLEKAKEIINIEEALKGFQDPESELEDL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2410 QEEAEKMKQVAEEAA--RLSVAAQEAARLRQLAEEDLAQQRALAEkmLKEKMQAVQEATRLKAEAELLQQQK---ELAQE 2484
Cdd:COG5185 249 AQTSDKLEKLVEQNTdlRLEKLGENAESSKRLNENANNLIKQFEN--TKEKIAEYTKSIDIKKATESLEEQLaaaEAEQE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2485 QARRLQEDKEQMAQQLAQETQGFQKTLE--TERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDigerlyr 2562
Cdd:COG5185 327 LEESKRETETGIQNLTAEIEQGQESLTEnlEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQN------- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2563 telATQEKVMLVQTLETQRQQSDRDAERLREAI----AELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSF 2638
Cdd:COG5185 400 ---QRGYAQEILATLEDTLKAADRQIEELQRQIeqatSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSV 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2639 LSEKDSLLQRERCIEQEKAKLEqlfqdevAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEgvrRQQEELQR 2718
Cdd:COG5185 477 RSKKEDLNEELTQIESRVSTLK-------ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHI---LALENLIP 546
|
..
gi 1920237940 2719 LA 2720
Cdd:COG5185 547 AS 548
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2415-2590 |
7.34e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.55 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2415 KMKQvAEEAARLSV--AAQEAARLRQLAEEDLAQQRALAEKMLKEK-----MQAVQEAT--RLKAEAELLQQQKELAQEQ 2485
Cdd:PRK00106 25 KMKS-AKEAAELTLlnAEQEAVNLRGKAERDAEHIKKTAKRESKALkkellLEAKEEARkyREEIEQEFKSERQELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2486 ARRLQE------------DKEQMAQQLAQETQGFQKTLEtERQRQLEMSAEAERLRL-RVAEMSRAQAR----------- 2541
Cdd:PRK00106 104 SRLTERatsldrkdenlsSKEKTLESKEQSLTDKSKHID-EREEQVEKLEEQKKAELeRVAALSQAEAReiilaetenkl 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1920237940 2542 AEEDARRFRKQAEDIGERLYRTelatqEKVMLVQTLetQRQQSDRDAER 2590
Cdd:PRK00106 183 THEIATRIREAEREVKDRSDKM-----AKDLLAQAM--QRLAGEYVTEQ 224
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1461-1754 |
7.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1461 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAQGLQRRM 1540
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1541 QEEVARREEVAvEAQEQKRSIQEELQHLR-QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ 1619
Cdd:COG4372 94 AELAQAQEELE-SLQEEAEELQEELEELQkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1620 ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE 1699
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237940 1700 AERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAT 1754
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1622-1892 |
7.60e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1622 RARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaeaELALRVQAEAEAAREKQRALQALEELRLQAEeAERRLRQAEAE 1701
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQER----EIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAEAN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1702 RARQVQVALETAQRSAEAELQsehasfaektaQLERTLKEEhvavvqlreeatrraqqqaeaeraraeaerelerwQLKA 1781
Cdd:COG2268 275 AEREVQRQLEIAEREREIELQ-----------EKEAEREEA-----------------------------------ELEA 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1782 NEALRLRLQAEEVAQqksltqaeaekqkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTAQQRLAAeqelirl 1861
Cdd:COG2268 309 DVRKPAEAEKQAAEA---------------------------------EAEAEAEAIRAKGLAEAEGKRALAE------- 348
|
250 260 270
....*....|....*....|....*....|..
gi 1920237940 1862 rAETEQGEQQRQL-LEEELARLQREAAAATQK 1892
Cdd:COG2268 349 -AWNKLGDAAILLmLIEKLPEIAEAAAKPLEK 379
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3827-3863 |
8.04e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 8.04e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237940 3827 RYLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVA 3863
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2463-2748 |
8.12e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2463 QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSA---EAERLRLRVAEMSRAQ 2539
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEkykELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2540 ARAEEDAR-RFRKQAEDIgerlyrtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2618
Cdd:pfam07888 121 LAQRAAHEaRIRELEEDI-------KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2619 MQTVRQEQLLQETQA--LQQSFLSEKDSLLQRERCIEQEKAKLEQL----------------FQDEVAKAQALREEQQRQ 2680
Cdd:pfam07888 194 FQELRNSLAQRDTQVlqLQDTITTLTQKLTTAHRKEAENEALLEELrslqerlnaserkvegLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237940 2681 QQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEER 2748
Cdd:pfam07888 274 LHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1453-1617 |
8.18e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1453 ESIIQEYVDLRTrysELSTLTSQYirfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQ 1528
Cdd:pfam09787 64 QKLRGQIQQLRT---ELQELEAQQ----QEEAESSREQLQELEEQLATERSARREAEAELERLQEelryLEEELRRSKAT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1529 aereaqgLQRRMQEEVARREEVA--VEAQEQKRSIQEEL-QHLRQSSEAEIQaKARQVEA--AERSRLRieeeirvvrLQ 1603
Cdd:pfam09787 137 -------LQSRIKDREAEIEKLRnqLTSKSQSSSSQSELeNRLHQLTETLIQ-KQTMLEAlsTEKNSLV---------LQ 199
|
170
....*....|....
gi 1920237940 1604 LEATERQRGGAEGE 1617
Cdd:pfam09787 200 LERMEQQIKELQGE 213
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1636-1960 |
8.40e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1636 QEEAERLRRQVQDETQRKRQAEAELALRVQ---------AEAEAAREKQRALQALEEL-----RLQAEEAERRLRQAEA- 1700
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTesvepnehnSYEEDSELKPSGQGGLDEEeafldRTAKREERRQKRLQEAl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1701 ERARQVQVALETAQ---RSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERw 1777
Cdd:pfam02029 84 ERQKEFDPTIADEKesvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1778 QLKANEALRLRLQAEEVAQQK-------SLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1850
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKikkekkvKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1851 RLAAEQELIRLRaeteqgeQQRQLLEEElarlqrEAAAATQKRRELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQ 1930
Cdd:pfam02029 243 FLEAEQKLEELR-------RRRQEKESE------EFEKLRQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAER 307
|
330 340 350
....*....|....*....|....*....|
gi 1920237940 1931 RLEAEAGRfRELAEEAARLRALAEEaKRQR 1960
Cdd:pfam02029 308 KLREEEEK-RRMKEEIERRRAEAAE-KRQK 335
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1482-1586 |
8.48e-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: 41.23 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1482 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQ-------AEREAQGLQRRMQEEVARR-EEVA 1551
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKqkaaesaSKSLAKPERKVSQEEAKEVlQEWE 148
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237940 1552 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAA 1586
Cdd:pfam13904 149 RKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2304-2757 |
8.51e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2304 QAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQ-----VEEELFSLRV 2378
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvareLLRRLREQRH 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2379 QMEELGKLKARI-EAENRalvLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2457
Cdd:PRK04863 511 LAEQLQQLRMRLsELEQR---LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2458 KMQAVQEATRLKAEAELLQQqkelAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSR 2537
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLA----AQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2538 AQARAEEDARRFRKQAEDIG-------------------ERLY---------------RTELATQEKVMLVQTLETQrqq 2583
Cdd:PRK04863 664 LSQPGGSEDPRLNALAERFGgvllseiyddvsledapyfSALYgparhaivvpdlsdaAEQLAGLEDCPEDLYLIEG--- 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2584 sdrDAERLREAIAEL-EHEKDKLKQEAQLlQLKSEEMQTV----------RQEQLLQETQALQQSF--LSEKDSLLQRer 2650
Cdd:PRK04863 741 ---DPDSFDDSVFSVeELEKAVVVKIADR-QWRYSRFPEVplfgraarekRIEQLRAEREELAERYatLSFDVQKLQR-- 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2651 cieqekakLEQLFQDEVAKAQALreeqqRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLL 2730
Cdd:PRK04863 815 --------LHQAFSRFIGSHLAV-----AFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLL 881
|
490 500
....*....|....*....|....*..
gi 1920237940 2731 AEENQRLRERLQHLEEERRAALARSEE 2757
Cdd:PRK04863 882 PRLNLLADETLADRVEEIREQLDEAEE 908
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2304-2556 |
8.93e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2304 QAADAEMEKHKQFAEQALRQKAQVEQEL------------TALRLQLEETDHQKSILDEELQRLKAEV----TEAARQRG 2367
Cdd:pfam09787 3 ESAKQELADYKQKAARILQSKEKLIASLkegsgvegldssTALTLELEELRQERDLLREEIQKLRGQIqqlrTELQELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2368 QVEEELFSLRvqmEELGKLKARIEAENRAlvlrdKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQ 2447
Cdd:pfam09787 83 QQQEEAESSR---EQLQELEEQLATERSA-----RREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2448 raLAEKMLKEKMQAVQEAtRLKAEAELLQQQkelaQEQARRLQEDKEQMAQQLAQ-ETQGFQKTLETERQRQLEMSA--- 2523
Cdd:pfam09787 155 --LTSKSQSSSSQSELEN-RLHQLTETLIQK----QTMLEALSTEKNSLVLQLERmEQQIKELQGEGSNGTSINMEGisd 227
|
250 260 270
....*....|....*....|....*....|....
gi 1920237940 2524 -EAERLRLRVAEMSRAQARAEEDARRFRKQAEDI 2556
Cdd:pfam09787 228 gEGTRLRNVPGLFSESDSDRAGMYGKVRKAASVI 261
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1626-1689 |
9.49e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 9.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237940 1626 EEAEAQKRQAQEEAERLRrqvQDETQRKRQAE--AELALRVQAEAEAAREKQRALQALEELRLQAE 1689
Cdd:PLN02316 253 EKRRELEKLAKEEAERER---QAEEQRRREEEkaAMEADRAQAKAEVEKRREKLQNLLKKASRSAD 315
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1869-2044 |
9.61e-03 |
|
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: 40.89 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1869 EQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAA- 1947
Cdd:cd00176 18 EKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1948 RLRALAEEAKRQRQLAEEDAVRQRAEAervlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED----EAFQRRLL 2023
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADDLEQWLEE----KEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRlkslNELAEELL 173
|
170 180
....*....|....*....|.
gi 1920237940 2024 EEQAAQHKADIEARLAQLRKA 2044
Cdd:cd00176 174 EEGHPDADEEIEEKLEELNER 194
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1614-1753 |
9.75e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 1614 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQdetqrKRQAEAELALRVQAEA---EAAREKQ--------------R 1676
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLEQQTEQAK-----KLEEKAQAALTKGNEElarEALAEKKslekqaealetqlaQ 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237940 1677 ALQALEELRLQAEEAERRLRQAEAERaRQVQVALETAQRSAEAELQSEHASFAEKTAQLERTlkEEHVAVVQLREEA 1753
Cdd:pfam04012 109 QRSAVEQLRKQLAALETKIQQLKAKK-NLLKARLKAAKAQEAVQTSLGSLSTSSATDSFERI--EEKIEEREARADA 182
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2080-2581 |
9.80e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2080 AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 2159
Cdd:COG3899 736 PPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGEL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2160 KVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ-----KEQELQQTLQQEQSVLERLRSEAEAARRAAE 2234
Cdd:COG3899 816 ALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAgletgDAALALLALAAAAAAAAAAAALAAAAAAAAR 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2235 EAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHK 2314
Cdd:COG3899 896 LLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2315 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2394
Cdd:COG3899 976 AAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAA 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2395 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2474
Cdd:COG3899 1056 AAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAAL 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237940 2475 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2554
Cdd:COG3899 1136 LLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALL 1215
|
490 500
....*....|....*....|....*..
gi 1920237940 2555 DIGERLYRTELATQEKVMLVQTLETQR 2581
Cdd:COG3899 1216 ALEAAALLLLLLLAALALAAALLALRL 1242
|
|
| |
