|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
318-423 |
1.08e-71 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 235.69 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 318 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 397
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1046896947 398 PEDVDVPQPDEKSIITYVSSLYDAMP 423
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
184-305 |
2.01e-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: 234.99 E-value: 2.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 184 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsvrlprekGRMRFHKLQNV 263
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNV 63
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046896947 264 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 305
Cdd:cd21188 64 QTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
181-316 |
3.28e-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: 226.44 E-value: 3.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirsvrlpreKGRMRFHKL 260
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 261 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 316
Cdd:cd21235 64 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
179-314 |
2.60e-66 |
|
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: 221.40 E-value: 2.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 179 ATDERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirsvrlpreKGRMRFH 258
Cdd:cd21236 10 YKDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRFH 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 259 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 314
Cdd:cd21236 73 RLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
319-423 |
1.26e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.41 E-value: 1.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 398
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1046896947 399 EDVDVPQPDEKSIITYVSSLYDAMP 423
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
181-315 |
7.04e-59 |
|
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: 199.49 E-value: 7.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsVRLPREKGRMRFHKL 260
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 261 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 315
Cdd:cd21237 64 QNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
319-423 |
9.90e-58 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 195.59 E-value: 9.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 398
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1046896947 399 EDVDVPQPDEKSIITYVSSLYDAMP 423
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
317-423 |
4.13e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 176.77 E-value: 4.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 317 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 396
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1046896947 397 DPEDVDVPQPDEKSIITYVSSLYDAMP 423
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
319-419 |
2.55e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.97 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 398
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1046896947 399 EDVDVPQPDEKSIITYVSSLY 419
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-99 |
9.85e-46 |
|
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: 160.76 E-value: 9.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 7 MPLDQLRAIYEVLFREGVMVAKKDRRPrSLHPHVpGVTNLQVMRAMTSLKARGLVRETFAWCHFYWYLTNEGIDHLRQYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKDFNL-PKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 1046896947 87 HLPPEIVPASLQR 99
Cdd:pfam03501 79 HLPAEIVPATLKR 91
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
186-306 |
1.38e-45 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 161.01 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 186 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDslprerdvirsvRLPREKGRMRFHKLQNVQI 265
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTGK------------KLKPEKGRMRVHHLNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046896947 266 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21186 66 ALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
319-419 |
1.88e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 157.94 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 398
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1046896947 399 EDVDVPQPDEKSIITYVSSLY 419
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
181-302 |
6.25e-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: 156.76 E-value: 6.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirsvrlprEKGRMRFHKL 260
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKMRIHCL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046896947 261 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 302
Cdd:cd21246 75 ENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
185-530 |
1.93e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 170.89 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 185 RVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsvrlprEKGRMRFHKLQNVQ 264
Cdd:COG5069 8 KVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYN----------ETPETRIHVMENVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 265 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNF 343
Cdd:COG5069 74 GRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 344 TTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS---- 416
Cdd:COG5069 151 FRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyii 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 417 --SLYD----AMPRVPGAQDGVRANElQLRwQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETE-- 488
Cdd:COG5069 231 rfGLLEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsr 308
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1046896947 489 LPAKEAD-KNRSKGIYQSLEgAVQAGQLKIPPGYHPLDVEKEW 530
Cdd:COG5069 309 APLETTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
182-306 |
1.02e-41 |
|
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: 150.22 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 182 ERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDslprerdvirsvRLPREKGRM--RFHK 259
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHF 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1046896947 260 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21241 66 LSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
306-421 |
3.09e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 149.05 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 306 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 385
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 386 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 421
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
182-306 |
4.91e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 148.49 E-value: 4.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 182 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDslprerdvirsvRLPREKGRM--RFHK 259
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHK 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1046896947 260 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21190 66 LSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
318-423 |
6.30e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 147.85 E-value: 6.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 318 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 397
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1046896947 398 PEDVDVPQPDEKSIITYVSSLYDAMP 423
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
181-302 |
6.02e-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: 145.13 E-value: 6.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirsvrlprEKGRMRFHKL 260
Cdd:cd21193 11 EERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRLRVQKI 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046896947 261 QNVQIALDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 302
Cdd:cd21193 75 ENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1508-2131 |
2.00e-39 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 162.03 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1508 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAElEARELQRRMQEevtrreeaavdaqqqkRSIQEELQHLRQSs 1586
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAE-RYRELKEELKE----------------LEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1587 EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1666
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1667 KRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALEtaQRSAEVELQSKRASFAEKT 1746
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1747 AQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA 1826
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1827 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQHEATAA 1903
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1904 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA-----LAEEAKRQRQLAE 1978
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtlLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1979 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 2058
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2059 SESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKE-------LAEQEAARQRQ 2131
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEalgpvnlLAIEEYEELEE 795
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
315-419 |
1.67e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 141.35 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 315 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 394
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1046896947 395 LLDPEDVDVPQPDEKSIITYVSSLY 419
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
315-419 |
2.84e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.53 E-value: 2.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 315 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 394
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1046896947 395 LLDPEDVDVPQPDEKSIITYVSSLY 419
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1635-2218 |
8.16e-38 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 157.02 E-value: 8.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1635 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQR---KRQAE-AELALRVKAEAEaAREKQRALQALDELKLQAEEAER 1707
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLeplERQAEkAERYRELKEELK-ELEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1708 RLRQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERE 1787
Cdd:COG1196 247 ELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1788 LERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1867
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAE-----------AELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1868 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1947
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1948 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALkEKEAENERLRRLA 2027
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-EAALEAALAAALQ 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2028 EDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGR 2107
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2108 IRSNAEDTMRSK---ELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRER 2184
Cdd:COG1196 630 ARLEAALRRAVTlagRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
570 580 590
....*....|....*....|....*....|....
gi 1046896947 2185 AEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQR 2218
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
318-419 |
6.94e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.15 E-value: 6.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 318 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 397
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1046896947 398 PEDVDVPQPDEKSIITYVSSLY 419
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
171-302 |
8.39e-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: 137.46 E-value: 8.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 171 RPGPEPTPA------------TDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR 238
Cdd:cd21318 11 RPWDEPAATaklfecsrikalADEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 239 ErdvirsvrlprEKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 302
Cdd:cd21318 86 P-----------TRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
182-306 |
1.39e-36 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 135.34 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 182 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDslprerdvirsvRLPREKGRMRFHKLQ 261
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1046896947 262 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21242 66 NIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1606-2206 |
2.18e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.40 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1606 RIEEEIRVVRLQLETTERQRGGAEdELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1685
Cdd:COG1196 190 RLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1686 REKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLre 1765
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1766 eaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1845
Cdd:COG1196 347 ---------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1846 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL 1925
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1926 ASKARAEEESRST---SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEA 2002
Cdd:COG1196 498 EAEADYEGFLEGVkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2003 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQkglVEDTLRQRRQVEE 2082
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT---LAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2083 EIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRK 2162
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1046896947 2163 VALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2206
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
322-423 |
4.96e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 133.71 E-value: 4.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 322 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 400
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1046896947 401 VDVPQPDEKSIITYVSSLYDAMP 423
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
181-302 |
9.76e-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: 134.03 E-value: 9.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirsvrlprEKGRMRFHKL 260
Cdd:cd21317 26 DEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMRIHCL 89
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046896947 261 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 302
Cdd:cd21317 90 ENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
303-419 |
1.42e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 133.26 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 303 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 382
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 383 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 419
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1837-2399 |
2.21e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.93 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1837 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK 1916
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1917 VRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKL 1996
Cdd:COG1196 300 LEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1997 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQ 2076
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2077 RRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEE 2156
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2157 AARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERL 2236
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2237 RSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ 2316
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2317 KQAADAEMEKHKKFAE-QTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQME 2395
Cdd:COG1196 698 ALLAEEEEERELAEAEeERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
....
gi 1046896947 2396 ELGK 2399
Cdd:COG1196 778 ALGP 781
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
184-302 |
2.93e-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: 131.36 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 184 DRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirsvrlPREKGRMRFHKLQNV 263
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANV 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046896947 264 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 302
Cdd:cd21214 67 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
186-304 |
1.45e-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: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 186 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdvirSVRLPRekgrMRFHKLQNVQI 265
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGR------YNKNPK----MRVQKLENVNK 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046896947 266 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 304
Cdd:cd21215 69 ALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1471-2058 |
1.60e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 146.24 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1471 QEYVDLRTRYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ-------LAEAHAQAKAQ 1542
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1543 AELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTE 1622
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1623 RQRGGAEDELQALRARAE------------------EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1684
Cdd:COG1196 373 ELAEAEEELEELAEELLEalraaaelaaqleeleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1685 AREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLR 1764
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1765 EEAERRAQQQAEAERAREEAERELERWQ-----LKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQ 1839
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1840 AVRQRELAEQELEKQRQLAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRA 1919
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1920 EMEVLLASKARAEEESRSTSEKSKQRleaeagrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI 1999
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2000 SEATRLKTEAEIALKEKEAENERlrrlAEDE-AFQRRRLEEQAAQHkADIEERLAQLRKA 2058
Cdd:COG1196 763 EELERELERLEREIEALGPVNLL----AIEEyEELEERYDFLSEQR-EDLEEARETLEEA 817
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
181-306 |
5.35e-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: 125.42 E-value: 5.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHISDLYEDLRDGHNLISLLEVLSGDslprerdvirsvRLPREKGRMRFHKL 260
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHAL 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1046896947 261 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21231 65 NNVNKALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
319-419 |
5.54e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 125.21 E-value: 5.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 398
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1046896947 399 EDVDVPQPDEKSIITYVSSLY 419
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-115 |
7.04e-33 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 125.52 E-value: 7.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 5 MLMPLDQLRAIYEVLFREGVMVAKKDRrPRSLHPHVpGVTNLQVMRAMTSLKARGLVRETFAWCHFYWYLTNEGIDHLRQ 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKDP-KGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90 100 110
....*....|....*....|....*....|.
gi 1046896947 85 YLHLPPEIVPASLQRVRRPVAMVMPARRRSP 115
Cdd:PTZ00034 80 YLHLPPDVFPATHKKKSVNFERKTEEEGSRG 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1502-2208 |
7.88e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 141.82 E-value: 7.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1502 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELqrrmqeEVTRREEAAVDAQQQKRSiqEELQH 1581
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA------EEARKAEDAKRVEIARKA--EDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1582 LRQSSEAEiqaKAQQVEAAERS-RMRIEEEIRvvrlqletterqrgGAEDELQALRARAEEAEAQKRQAQ--EEAERLRR 1658
Cdd:PTZ00121 1166 AEEARKAE---DAKKAEAARKAeEVRKAEELR--------------KAEDARKAEAARKAEEERKAEEARkaEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1659 QVQDESQRKRQAEAELALRVKaEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVA--LETAQRSAEVELQ 1736
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1737 SKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEAlrlRLQAEEVAQQKSLAQ 1816
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---EKKKEEAKKKADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1817 ADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELAR 1895
Cdd:PTZ00121 1385 KKAEEKKKADEAKK----KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKK 1458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1896 LQHEATAATQKRQeleAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEaEAGRFRELAEEAARLRAlAEEAKRQRQ 1975
Cdd:PTZ00121 1459 AEEAKKKAEEAKK---ADEAKKKAE-------EAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK-AEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1976 LAEEDAARQRAEAERVLTEKLA-AISEATRLKT-----EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE 2049
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKAdELKKAEELKKaeekkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2050 ERLAQLRKASESEL--------ERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDtMRSKEL 2121
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIkaeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2122 AEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2201
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
....*..
gi 1046896947 2202 KRLQAEE 2208
Cdd:PTZ00121 1766 EEKKAEE 1772
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
318-416 |
5.87e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 122.15 E-value: 5.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 318 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 397
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1046896947 398 PEDVDVPQPDEKSIITYVS 416
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
306-421 |
9.65e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 121.87 E-value: 9.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 306 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 385
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 386 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 421
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
322-423 |
1.18e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 121.22 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 322 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 400
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1046896947 401 VDVPQPDEKSIITYVSSLYDAMP 423
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
324-419 |
1.31e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 118.22 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 324 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 402
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1046896947 403 VPQPDEKSIITYVSSLY 419
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
322-424 |
1.97e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.11 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 322 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 399
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1046896947 400 DVDVPQPDEKSIITYVSSLYDAMPR 424
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
318-416 |
2.39e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 117.63 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 318 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 397
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1046896947 398 PEDVDVPQPDEKSIITYVS 416
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
304-431 |
3.03e-30 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 117.88 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 304 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 383
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1046896947 384 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQDG 431
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF---SGAQKA 123
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
186-306 |
3.37e-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: 117.00 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 186 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdVIRsvrlpreKGRMRFHKLQNVQI 265
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIK-------KPLNQHQKLENVTL 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046896947 266 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21227 69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1940-2623 |
6.75e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.21 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1940 EKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedaaRQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 2019
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2020 NERLRRLAEDEAFQRRRLEEQAAqhkadiEERLAQLRKASESELERQkglvEDTLRQRRQVEEEIMALKASFEKAAAGKA 2099
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYEL------LAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2100 ELELELgrIRSNAEDTMRSKELAEQEAARQRQLAAEEEQrrreaeervqrsLAAEEEAARQRKVALEEVERLKAKVEEAR 2179
Cdd:COG1196 341 ELEEEL--EEAEEELEEAEAELAEAEEALLEAEAELAEA------------EEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2180 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAER 2259
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2260 EAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAE--MEKHKKFAEQTLRQ 2337
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2338 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRsqvEEELFSVRVQMEELGKLKARIEAENRALILRDKD 2417
Cdd:COG1196 567 KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR---EADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2418 NTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2497
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2498 EQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQL----EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgek 2573
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL--- 800
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2574 lhrtelaTQEKVTLVQTLeiqrqqsdqdaERLREAIAELEREKEKLKQEA 2623
Cdd:COG1196 801 -------SEQREDLEEAR-----------ETLEEAIEEIDRETRERFLET 832
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1471-2187 |
8.66e-30 |
|
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: 131.33 E-value: 8.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1471 QEYVDLRTRYSELT-TLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQ-AKAQAEL-E 1546
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeELRLEVSELEEEiEELQKELyA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1547 ARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSE---AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTER 1623
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1624 QRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQD-ESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQA 1702
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1703 EEAERRLRQAEaERARQVQVALETAQRSAEVELQSKRASFAektaqLERTLQEEHVTVTQLREEAERRAQQQAEAERARE 1782
Cdd:TIGR02168 453 QEELERLEEAL-EELREELEEAEQALDAAERELAQLQARLD-----SLERLQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1783 EAERELERWQLKANEALRLRLQA---EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQ---------E 1850
Cdd:TIGR02168 527 ELISVDEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNiegflgvakD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1851 LEKQR------------------QLAEGTAQQRLAAEQELI---------------RLRAETEQGEQQRQL----LEEEL 1893
Cdd:TIGR02168 607 LVKFDpklrkalsyllggvlvvdDLDNALELAKKLRPGYRIvtldgdlvrpggvitGGSAKTNSSILERRReieeLEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1894 ARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAE--EAARLRALAEEAK 1971
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAqlSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1972 RQRQLAEEDAARQRAEAERVLTEKLAAisEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 2051
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIE--QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2052 LAQLRKASEsELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELgrirSNAEDTMRSKELAEQEAARQRQ 2131
Cdd:TIGR02168 844 EEQIEELSE-DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EELSEELRELESKRSELRRELE 918
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2132 LAAEEEQRRREAEERVQRSLAAEEEAARQR-KVALEEVERLKAKVE-EARRLRERAEQ 2187
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEdDEEEARRRLKR 976
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1556-2345 |
8.91e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 131.80 E-value: 8.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1556 EEVTrrEEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQAL 1635
Cdd:PTZ00121 1030 EELT--EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1636 RARAEEA----EAQKRQaqEEAERLRRQVQDESQRK----RQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAER 1707
Cdd:PTZ00121 1108 TGKAEEArkaeEAKKKA--EDARKAEEARKAEDARKaeeaRKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1708 RLRQAE----AERARQVQVAletaqRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREE 1783
Cdd:PTZ00121 1186 EVRKAEelrkAEDARKAEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1784 AERELERWQ--LKANEALR---LRlQAEEVAQQKSLAQADaEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1858
Cdd:PTZ00121 1261 RMAHFARRQaaIKAEEARKadeLK-KAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1859 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQEL-EAELAKVRAEMEVLLASKARAEEESRS 1937
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1938 TSEKSKQRLEA-----EAGRFRELAEEAARLRALAEEAKRQRQL---AEE----DAARQRAEAERVLTEKLAAISEATRL 2005
Cdd:PTZ00121 1419 KADEAKKKAEEkkkadEAKKKAEEAKKADEAKKKAEEAKKAEEAkkkAEEakkaDEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2006 KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ---HKADIEERLAQLRKASESELERQKGLVEDtlrQRRQVEE 2082
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKADELKKAEELKKAEEKKKAEE---AKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2083 EIMALKASFEKAAAGKAELELELGRIRSnaEDTMRSKELAEQEAARQRqlaaeeeqrrreaeervQRSLAAEEEaarQRK 2162
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIK-----------------AEELKKAEE---EKK 1633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2163 VALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEA 2242
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2243 ARRAAEEAEEAREQAEREAAQSRKQVEEAERlkqsaeeqaqaqaqaqaAAEKLRKEAEqeaarraqaeqaalKQKQAADA 2322
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKK-----------------KAEEAKKDEE--------------EKKKIAHL 1762
|
810 820
....*....|....*....|...
gi 1046896947 2323 EMEKHKKFAEQTLRQKAQVEQEL 2345
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1051-1128 |
1.15e-29 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 114.62 E-value: 1.15e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1051 LAWQSLNRDIQLIRSWSLVTFRTLKPEEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLVAEREYGSCSRHYQQLLQS 1128
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1879-2726 |
1.20e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 131.42 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1879 TEQGEQQRQLLEEELARLQHEATAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1956
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1957 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlTEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 2034
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2035 RRLEEQaaqHKADIEERLAQLRKASESelerqkglvedtlrqrRQVEEeimalkasfekaaAGKAELELELGRIRsNAED 2114
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2115 TMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERlkaKVEEARRLRERAEQESARQLQ 2194
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2195 LAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERlrseaeaarraaeeaeeareqaereaaqsRKQVEEAERL 2274
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2275 KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2354
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2355 TDHQksildEELQRLKAEVTEAARQRSQVEEelfsvRVQMEELGKlkaRIEAENRALILRDKDNTQRFLEE---EAEKMK 2431
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEAK 1496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2432 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDK 2507
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2508 eQMAQQLVEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVTL 2587
Cdd:PTZ00121 1577 -NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKK 1648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2588 VQTL-------EIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ-----EQILQETQALQKSFLSE 2655
Cdd:PTZ00121 1649 AEELkkaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAEELKKAEEEN 1728
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 2656 KDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRK 2726
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
185-307 |
1.34e-29 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 116.01 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 185 RVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsvrlprEKGRMRFHKLQNVQ 264
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFN----------KRPTFRSQKLENVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1046896947 265 IALDYLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 307
Cdd:cd21311 79 VALKFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
186-306 |
3.46e-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: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 186 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsvrlprekGRMRFHKLQNVQI 265
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046896947 266 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21232 66 VLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
182-308 |
9.24e-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: 113.44 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 182 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsvrlprEKGRMRFHKLQ 261
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEY----------KPSSHRIFRLN 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1046896947 262 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 308
Cdd:cd21191 68 NIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
181-302 |
9.61e-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: 114.76 E-value: 9.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirsvrlprEKGRMRFHKL 260
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMRIHCL 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046896947 261 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 302
Cdd:cd21316 112 ENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
322-421 |
2.26e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.99 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 322 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 400
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1046896947 401 VDVPQPDEKSIITYVSSLYDA 421
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1851-2663 |
3.06e-28 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 126.79 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1851 LEKQRQLAEGTAQQRLAAEQELIRLRAE------TEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmEVL 1924
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDgnhegkAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAE-EAK 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1925 LASKARAEEESRStsEKSKQRLEaEAGRFREL--AEEAARlralAEEAKRQRQLAEEDAARQRAEAERVlteKLAAISEA 2002
Cdd:PTZ00121 1105 KTETGKAEEARKA--EEAKKKAE-DARKAEEArkAEDARK----AEEARKAEDAKRVEIARKAEDARKA---EEARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2003 TRLKTEAEIALKEKEAEN----ERLRRLAEDEAFQRRRLEEQAaqHKADIEERLAQLRKASES---ELERQKGLVEDTLR 2075
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEElrkaEDARKAEAARKAEEERKAEEA--RKAEDAKKAEAVKKAEEAkkdAEEAKKAEEERNNE 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2076 QRRQVEEEIMALKAsfEKAAAGKAELELELGRIRsNAEDTMRSKELAEQEAARQrqlaaeeeqrrreaeervQRSLAAEE 2155
Cdd:PTZ00121 1253 EIRKFEEARMAHFA--RRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKKK------------------ADEAKKKA 1311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2156 EAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfvvqqreeelqqtlqqeqnmLER 2235
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA--------------------AEK 1371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2236 LRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKlRKEAEQEAARRAQAEQAALK 2315
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAK 1450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2316 QKQAADAEMEKHKKFAEQT-----LRQKAQVEQELTTLRLQLEETDHQKsildEELQRlKAEVTEAARQRSQVEEelfsv 2390
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAkkadeAKKKAEEAKKADEAKKKAEEAKKKA----DEAKK-AAEAKKKADEAKKAEE----- 1520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2391 RVQMEELGKLKARIEAEN--RALILRDKDNTQRFLE----EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAL 2464
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEakKAEEKKKADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2465 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ--EQARRLQEDKEQMAQQL--VEETQGFQRTLEA----ERQRQLEMS 2536
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKkvEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAkkaeEDKKKAEEA 1680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2537 AEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigEKLHRTELATQEKVTLVQTLEIQRQQsDQDAERLREAIAElEREK 2616
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEA-EEDKKKAEEAKKD-EEEK 1756
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1046896947 2617 EKLKQEAKLLQLKSEEmqtvqqeqILQETQALQKSFLSEKDSLLQRE 2663
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEE--------IRKEKEAVIEEELDEEDEKRRME 1795
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
306-430 |
5.59e-28 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 111.33 E-value: 5.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 306 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 385
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1046896947 386 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQD 430
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF---SGAQK 119
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1789-2380 |
8.68e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1789 ERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1868
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----LELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1869 EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRLEA 1948
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1949 EAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAE 2028
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2029 DEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFE-KAAAGKAELELELGR 2107
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyEAALEAALAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2108 IRSNAEDTMRSKELAEQEAARQR---QLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRER 2184
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRAtflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2185 AEQESARQLQLAQEAAQKRLQAEEkahafvvqqREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQS 2264
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEG---------GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2265 RKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQ---- 2340
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpv 782
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1046896947 2341 ---VEQELTTLRLQLEETDHQKSILDEELQRLK---AEVTEAARQR 2380
Cdd:COG1196 783 nllAIEEYEELEERYDFLSEQREDLEEARETLEeaiEEIDRETRER 828
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1499-2543 |
1.04e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 124.55 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1499 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAELEARELQRRMQEEVTRR-EEAAVDAQQQKRSIQ 1576
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIARLvGEATKEAEALKAEAE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1577 EELQhlrqssEAEIQAKAQQVEAAERSRMRIEEEIRVvrlQLETTERQrggAEDelqALRARAEEAEAQKRQAQEEAERL 1656
Cdd:NF041483 334 QALA------DARAEAEKLVAEAAEKARTVAAEDTAA---QLAKAART---AEE---VLTKASEDAKATTRAAAEEAERI 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1657 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqalDELKLQaEEAeRRLRqAEAERARQVQVA----LETAQRSAE 1732
Cdd:NF041483 399 RREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLRAEAVAegerIRGEARREA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1733 VELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerraqqqaeaerAREEAERELERWQLKANE-ALRLRLQAEEVAQQ 1811
Cdd:NF041483 472 VQQIEEAARTAEELLTKAKADADE-----------------------LRSTATAESERVRTEAIErATTLRRQAEETLER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1812 kslAQADAEKQKeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAEteqGEQQRQLLE 1890
Cdd:NF041483 529 ---TRAEAERLR----------AEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTE---AEERLTAAE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1891 EELARLQHEataATQKRQELEAELAKVRAEM-EVLLASKARAEEEsrstSEKSKQRLEAEAGRFRELAEEAA-RLRA-LA 1967
Cdd:NF041483 593 EALADARAE---AERIRREAAEETERLRTEAaERIRTLQAQAEQE----AERLRTEAAADASAARAEGENVAvRLRSeAA 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1968 EEAKRQRQLAEEDAARQRAE----AERVLTEKL----AAISEATRLKTEAEIALKEKEAENERLRRLAEDE-----AFQR 2034
Cdd:NF041483 666 AEAERLKSEAQESADRVRAEaaaaAERVGTEAAealaAAQEEAARRRREAEETLGSARAEADQERERAREQseellASAR 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2035 RRLEEQAAQHKADIEE---RLAQLRKASESELERQKGLVEDTlrqRRQVEEEIMALKASFEKAAA-GKAELELELGRIRS 2110
Cdd:NF041483 746 KRVEEAQAEAQRLVEEadrRATELVSAAEQTAQQVRDSVAGL---QEQAEEEIAGLRSAAEHAAErTRTEAQEEADRVRS 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2111 naeDTMRSKELAEQEAARQRQlaaeeeqrrreaeERVQRSLAAEEEAARQRKVALEEVERLKAKVEE-ARRLRERA---- 2185
Cdd:NF041483 823 ---DAYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEAsdtl 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2186 ---EQESARQLQLAQEAAQK-RLQAEEKAHAFVVQQREEELQQTLQQEQNMlERLRSEAEAARRAAEEAEEAREQAEREA 2261
Cdd:NF041483 887 asaEQDAARTRADAREDANRiRSDAAAQADRLIGEATSEAERLTAEARAEA-ERLRDEARAEAERVRADAAAQAEQLIAE 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2262 AQS---RKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQA------------ADAEMEK 2326
Cdd:NF041483 966 ATGeaeRLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKdankrrseaaeqADTLITE 1045
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2327 HKKFAEQtLRQKAQVEQELTTLRLQlEETDHQKSILDEELQRLKAEVT-----EAARQRSQVEEELFSVRVQM----EEL 2397
Cdd:NF041483 1046 AAAEADQ-LTAKAQEEALRTTTEAE-AQADTMVGAARKEAERIVAEATvegnsLVEKARTDADELLVGARRDAtairERA 1123
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2398 GKLKARIEAENRALilrdkdnTQRFLEEEAEKMKQVAEEAARLSVAAQEaarlrQLAEEDLAQQRALAE---KMLKEKMQ 2474
Cdd:NF041483 1124 EELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEE-----QLAEAEAKAKELVSDansEASKVRIA 1191
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 2475 AVQEATRLKAEAEllqQQKELAQEQARRLQEDKEQMAQQLVEETqgfQRTLEAERQRQLEMSAEAERLK 2543
Cdd:NF041483 1192 AVKKAEGLLKEAE---QKKAELVREAEKIKAEAEAEAKRTVEEG---KRELDVLVRRREDINAEISRVQ 1254
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1641-2623 |
1.62e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 123.78 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1641 EAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALDELKLQAE-EAERRLR 1710
Cdd:NF041483 73 QAEQLLRNAQIQADQLRadaerelRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1711 QAEAERARQVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvtqlreEAERRAQQQAEAERAREEAERE 1787
Cdd:NF041483 153 WAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE---------AESARAEAEAILRRARKDAERL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1788 LERWQLKANEALRlrlQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQRLA 1867
Cdd:NF041483 224 LNAASTQAQEATD---HAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKVVAEAKEAAAKQLA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1868 AeqelirlrAETeQGEQQRQLLEEELARLQHEATA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSK 1943
Cdd:NF041483 298 S--------AES-ANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1944 QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI---------------SEATRLKTE 2008
Cdd:NF041483 369 AARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2009 AEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIEErlaqLRKASESELERQKG-LVEDTLRQRRQVEE 2082
Cdd:NF041483 449 AEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADE----LRSTATAESERVRTeAIERATTLRRQAEE 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2083 eimALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLA------AEEE 2156
Cdd:NF041483 525 ---TLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAeealadARAE 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2157 AARQRKVALEEVERLKAKV-EEARRLRERAEQESAR-QLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqNMLE 2234
Cdd:NF041483 602 AERIRREAAEETERLRTEAaERIRTLQAQAEQEAERlRTEAAADASAARAEGE-----------------------NVAV 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2235 RLRSEAEaarraaeeaeeareqaereaaqsrkqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2314
Cdd:NF041483 659 RLRSEAA---------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEAL 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 kqkQAADAEMEKHKKFAEQTL------------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ 2382
Cdd:NF041483 702 ---AAAQEEAARRRREAEETLgsaraeadqereRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2383 -VEEELFSVRVQM-EELGKLkaRIEAENRAlilrdkDNTQRFLEEEAEKMKqvAEEAARLSVAAQEAARLRQLAEEDLAQ 2460
Cdd:NF041483 779 qVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SDAYAERERASEDANRLRREAQEETEA 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2461 QRALAEKMLKEkmqAVQEATRLKAEAELLQQQ-------------------KELAQEQARRLQEDKEQMAQQLVEETQGF 2521
Cdd:NF041483 849 AKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAQADRLIGEATSE 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2522 QRTLEAE-----RQRQLEMSAEAERLKLRMAEMS-RAQARAEEDAQRFRKQAEEIgeklhrTELATQEKVTLVQTLEIQR 2595
Cdd:NF041483 926 AERLTAEaraeaERLRDEARAEAERVRADAAAQAeQLIAEATGEAERLRAEAAET------VGSAQQHAERIRTEAERVK 999
|
1050 1060
....*....|....*....|....*....
gi 1046896947 2596 QQSDQDAERLR-EAIAELEREKEKLKQEA 2623
Cdd:NF041483 1000 AEAAAEAERLRtEAREEADRTLDEARKDA 1028
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
185-304 |
1.93e-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: 109.49 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 185 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirsvrlprEKGRMRFHKLQNVQ 264
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1046896947 265 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 304
Cdd:cd21183 69 TALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1498-2188 |
5.09e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 122.09 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1498 LRRMEEEERLAEQQRaEERERLAEVEAAL------EKQRQLAEAHAQAKAqAELEARELQRRMQEEVTRREEAaVDAQQQ 1571
Cdd:TIGR02168 202 LKSLERQAEKAERYK-ELKAELRELELALlvlrleELREELEELQEELKE-AEEELEELTAELQELEEKLEEL-RLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1572 KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQE 1651
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1652 EAERLRRQVQDESQRKRQAEAELaLRVKAEAEAAREKQRALQAldelklQAEEAERRLRQAEAERARQVQVALETAQRSA 1731
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQL-ETLRSKVAQLELQIASLNN------EIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1732 EVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAEREL----------------------- 1788
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslerlqenlegfsegvkal 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1789 ---------------------ERWQLKANEALRLRLQA---EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQR 1844
Cdd:TIGR02168 512 lknqsglsgilgvlselisvdEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1845 ELAEQE-------------------------------------LEKQRQL-----------------------AEGTAQQ 1864
Cdd:TIGR02168 592 EILKNIegflgvakdlvkfdpklrkalsyllggvlvvddldnaLELAKKLrpgyrivtldgdlvrpggvitggSAKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1865 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK--- 1941
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaq 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1942 -SKQRLEAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAeialKEKEAEN 2020
Cdd:TIGR02168 752 lSKELTELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2021 ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEIMALKASFEKAAAGKAE 2100
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2101 LELELGRIRSNAEDTMRSKE-----LAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvalEEVERLKAKV 2175
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAqlelrLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKI 981
|
810
....*....|...
gi 1046896947 2176 EEARRLRERAEQE 2188
Cdd:TIGR02168 982 KELGPVNLAAIEE 994
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1495-2211 |
7.09e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 121.86 E-value: 7.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1495 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAELEARELQRRMQEEVTR-REEA 1564
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1565 AVDAQQQKRSIQEELQHLRqsSEAEiQAKAQQVEAAERSRMRIEEEIRVVRLQLE-TTERQRGGAEDELQALRARAEE-- 1641
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1642 --AEAQKRQAQEEAERLRRQVQDESQRKRqaeaelalrvkaeAEAArEKQRALQAldelklQAEEAERRLRQAEAERARQ 1719
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLR-------------TEAA-ERIRTLQA------QAEQEAERLRTEAAADASA 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1720 VQVALEtaqrSAEVELQSKrasfaektaqlertlqeehvtvtqlreeaerraqqqaeaerareeaerelerwqlKANEAL 1799
Cdd:NF041483 649 ARAEGE----NVAVRLRSE-------------------------------------------------------AAAEAE 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1800 RLRLQAEEVAQQ-KSLAQADAEKqkeEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI---RL 1875
Cdd:NF041483 670 RLKSEAQESADRvRAEAAAAAER---VGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1876 RAETEQGEQQRqLLEEELARLQHEATAATQKRQELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAEAG 1951
Cdd:NF041483 747 RVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSDAY 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1952 RFRELA-EEAARLRALA-EEAKRQRQLAEEDAARQRAEAERVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAED 2029
Cdd:NF041483 826 AERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADARE 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2030 EAFQRRrlEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAElelelgRIR 2109
Cdd:NF041483 903 DANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------RLR 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2110 SNAEDTMRSkelAEQEAARQRQLAAEEEQRrreaeervqrslaAEEEAARQRKVALEEVERL--KAKVEEARRLRERAEQ 2187
Cdd:NF041483 975 AEAAETVGS---AQQHAERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAAEQ 1038
|
730 740
....*....|....*....|....
gi 1046896947 2188 ESARQLQLAQEAAQKRLQAEEKAH 2211
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
306-421 |
7.77e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 108.27 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 306 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 385
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 386 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 421
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
306-421 |
2.36e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 104.00 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 306 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 385
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 386 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 421
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
324-419 |
2.77e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.00 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 324 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 402
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1046896947 403 VPQPDEKSIITYVSSLY 419
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1838-2676 |
4.60e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.92 E-value: 4.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1838 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1917
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1918 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKla 1997
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1998 aiseatrlkTEAEIALKEKEAENERLRRLAEDeafqrrrLEEQAAQHKADIEERLAQLRKASeSELERQKGLVEDTLRQR 2077
Cdd:TIGR02168 354 ---------ESLEAELEELEAELEELESRLEE-------LEEQLETLRSKVAQLELQIASLN-NEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2078 RQVEEEIMALKASFEKAAagKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRReaeervqrSLAAEEEA 2157
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD--------AAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2158 ARQRKVALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQAEEKAHAFVVQQREEELQ 2223
Cdd:TIGR02168 487 LQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAVVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2224 QTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEA 2303
Cdd:TIGR02168 567 QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2304 ARRAQAEQAALKQKQAAdaemeKHKKFAEQTLRQKaqveQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV 2383
Cdd:TIGR02168 647 IVTLDGDLVRPGGVITG-----GSAKTNSSILERR----REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2384 EEELFSVRVQMEELGKLKARIEAENRALiLRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA 2463
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2464 LAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLVEETQgfqrtleaerqrqlEMSAEAERL 2542
Cdd:TIGR02168 797 ELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------------ELSEDIESL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2543 KLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQE 2622
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2623 -AKLLQLKSEEMQTVQQEqilqetqALQKSFLSEKDSLLQRERfIEQEKAKLEQL 2676
Cdd:TIGR02168 938 iDNLQERLSEEYSLTLEE-------AEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
318-424 |
5.55e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 102.36 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 318 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 394
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1046896947 395 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 424
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1508-2764 |
1.05e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 114.54 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1508 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAELEARELQRRM---QEEVTRRE--EAAVD-----AQQQKRSIQ 1576
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAELHTEAVQRRQqldQELAERRQtvESHVNenvawAEQLRARTE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1577 EELQHLRQSSEAEiqakAQQVEAAERSRM-RIEEEirvvrlqlettERQRGGAEDElqalRARAEeAEAQKRQAQEEAER 1655
Cdd:NF041483 163 SQARRLLDESRAE----AEQALAAARAEAeRLAEE-----------ARQRLGSEAE----SARAE-AEAILRRARKDAER 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1656 LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQaeEAERRLRQAEAERARQVQVALETAqrsaevel 1735
Cdd:NF041483 223 LLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA-------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1736 qSKRASFAEKT-AQLERTLQEEHVTVTQlrEEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1814
Cdd:NF041483 293 -AKQLASAESAnEQRTRTAKEEIARLVG--EATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1815 AQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEEL 1893
Cdd:NF041483 370 ARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1894 ARLQHEATaatQKRQELEAELAKVRAEmevllaskARAE-----EESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALA 1967
Cdd:NF041483 443 RRLRGEAE---QLRAEAVAEGERIRGE--------ARREavqqiEEAARTAEELLTKAKADADELRSTATaESERVRTEA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1968 -EEAKRQRQLAEEDAARQRAEAERVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR-RRLEEQAAQHK 2045
Cdd:NF041483 512 iERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQAEAAEElTRLHTEAEERL 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2046 ADIEERLAQLRkaSESELERQKGlVEDTLRQRRQVEEEIMALKAsfekaaagKAELELElgRIRSNA-EDTMRSKELAEQ 2124
Cdd:NF041483 589 TAAEEALADAR--AEAERIRREA-AEETERLRTEAAERIRTLQA--------QAEQEAE--RLRTEAaADASAARAEGEN 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2125 EAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkVALEEVERLKAKVEEARRLRERAEQ--ESARQlqlaqEAAQK 2202
Cdd:NF041483 656 VAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAER-VGTEAAEALAAAQEEAARRRREAEEtlGSARA-----EADQE 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2203 RLQAEEKAHAFVVQQREEELQQTLQQEqnmleRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQA 2282
Cdd:NF041483 730 RERAREQSEELLASARKRVEEAQAEAQ-----RLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEH 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2283 QAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQkAQVEQElttlRLQLEETDHQKSIL 2362
Cdd:NF041483 805 AAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE-AIAEAE----RLRSDASEYAQRVR 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2363 DEELQRLKAEVTEAARQRSQVEEELFSVR----VQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAA 2438
Cdd:NF041483 880 TEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQA 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2439 R--LSVAAQEAARLRQLAEEDLAQQRALAEKMLKE----KMQAVQEATRLKAEA--ELLQQQKELAQEQARRLQEDKEQM 2510
Cdd:NF041483 960 EqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEaervKAEAAAEAERLRTEAreEADRTLDEARKDANKRRSEAAEQA 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2511 AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARaeedaqrfRKQAEEIGEKLHRTELATQEKVTLvqt 2590
Cdd:NF041483 1040 DTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAE--------RIVAEATVEGNSLVEKARTDADEL--- 1108
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2591 LEIQRQQSDQDAERLREAIAELEREKEKLKQEAKllQLKSEEMQTVQQ---------EQILQETQALQKSFLSEKDSLLQ 2661
Cdd:NF041483 1109 LVGARRDATAIRERAEELRDRITGEIEELHERAR--RESAEQMKSAGErcdalvkaaEEQLAEAEAKAKELVSDANSEAS 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2662 RERFIEQEKAklEQLFQDEVAKAKQLqeeqqrqqqqmeqekqelvasMEEARRRQREAEEGVRRkqeelqrleqqrqqqe 2741
Cdd:NF041483 1187 KVRIAAVKKA--EGLLKEAEQKKAEL---------------------VREAEKIKAEAEAEAKR---------------- 1227
|
1290 1300
....*....|....*....|...
gi 1046896947 2742 klLAEENQRLRERLQRLEEEHRA 2764
Cdd:NF041483 1228 --TVEEGKRELDVLVRRREDINA 1248
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
185-304 |
3.53e-24 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 99.87 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 185 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirsvrlprEKGRMRFHKLQNVQ 264
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1046896947 265 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 304
Cdd:cd21228 69 VALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1508-2212 |
5.56e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.07 E-value: 5.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1508 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQA-KAQAELEARELQRRMQEEV-TRREEAAVDAQQQKRSIQEELQHLRQ 1584
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILnELERQLKSLERQAeKAERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1585 SSEAEIQAKAQQVEAAERSRMRIEEEIRVvrlqletterqrggAEDELQALRARAEEAEAQKRQAQEEAERLRR------ 1658
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEE--------------LQKELYALANEISRLEQQKQILRERLANLERqleele 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1659 -QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLR--QAEAERARQVQVALETAQRSAEVEL 1735
Cdd:TIGR02168 323 aQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEelEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1736 QSKRASFAEKTAQLERTLQEehvtvtqlreEAERRAQQQAEAERAREEAERELERWQLKANEALRlRLQAEEVAQQKSLA 1815
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQE----------IEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1816 QADAEKQKEeaerearrrgKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQ---------ELIRLRAETEQG--- 1882
Cdd:TIGR02168 472 EAEQALDAA----------ERELAQLQARlDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAiea 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1883 --------------EQQRQ----LLEEELARL----------------QHEATAATQKRQELEAELAKVRAEMEVLLA-- 1926
Cdd:TIGR02168 542 alggrlqavvvenlNAAKKaiafLKQNELGRVtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSyl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1927 --------SKARAEEESRSTSEK-----------------SKQRLEAEAGRF---RELAEEAARLRALAEEAKRQRQlAE 1978
Cdd:TIGR02168 622 lggvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggviTGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK-AL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1979 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKA 2058
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2059 SESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQlaaeeeq 2138
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------- 852
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 2139 rrreAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLqlaQEAAQKRLQAEEKAHA 2212
Cdd:TIGR02168 853 ----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL---RELESKRSELRRELEE 919
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
320-419 |
5.77e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 99.17 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 320 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 399
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1046896947 400 D-VDVPQPDEKSIITYVSSLY 419
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
322-422 |
1.06e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 98.31 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 322 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 401
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1046896947 402 DVPQPDEKSIITYVSSLYDAM 422
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
319-419 |
1.18e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 98.27 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 398
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1046896947 399 EDVDVPQ-PDEKSIITYVSSLY 419
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2013-2763 |
2.37e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 110.62 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2013 LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESE-LERQKGLVEDTLRQRRQVEEEimalkASF 2091
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEaTEEAFGKAEEAKKTETGKAEE-----ARK 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2092 EKAAAGKAELELELGRIRsNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKV-------A 2164
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrkaeelrK 1195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2165 LEEVERLKA--KVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEA 2242
Cdd:PTZ00121 1196 AEDARKAEAarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2243 ARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAeqaalKQKQAADA 2322
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK-----KAAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2323 EMEKHKKFAEQTLRQKAQVEQElttlrlqlEETDHQKSildEELQRLKAEVTEAARQRSQVEEElfsvRVQMEELgklKA 2402
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKK--------KEEAKKKA---DAAKKKAEEKKKADEAKKKAEED----KKKADEL---KK 1412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2403 RIEAENRALILRDKDNTQRfleeEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRL 2482
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2483 KAEAEllqQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAErlKLRMAEMSRaqaRAEEdaqr 2562
Cdd:PTZ00121 1489 KKKAE---EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE--EKKKADELK---KAEE---- 1556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2563 fRKQAEEIgEKLHRTELATQEKVTLVQTLEIQRQqsdqdAERLR-EAIAELEREKEKLKQEakllQLKSEEMQTVQQEQI 2641
Cdd:PTZ00121 1557 -LKKAEEK-KKAEEAKKAEEDKNMALRKAEEAKK-----AEEARiEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2642 LQETQalqksflsEKDSLLQRERFIEQEKAKLEQlfqdeVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEE 2721
Cdd:PTZ00121 1626 KKAEE--------EKKKVEQLKKKEAEEKKKAEE-----LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1046896947 2722 GVRRKQEELQRLEQQRQQQekllaEENQRLRERLQRLEEEHR 2763
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKE-----AEEKKKAEELKKAEEENK 1729
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
185-307 |
2.41e-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: 98.18 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 185 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirsvrlPREKgrMRFHKLQNVQ 264
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1046896947 265 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 307
Cdd:cd21310 81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
181-306 |
2.78e-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: 97.91 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirsvrlprEKGRMRFHKL 260
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRVHFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1046896947 261 QNVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21247 81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
319-423 |
7.84e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.01 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 398
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1046896947 399 EDVDVPQPDEKSIITYVSSLYDAMP 423
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
189-303 |
9.74e-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: 9.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 189 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVirsvrlprEKGRMRFHKLQNVQIALD 268
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALS 67
|
90 100 110
....*....|....*....|....*....|....*
gi 1046896947 269 YLRHRQVKLVNIRNDDIADGnPKLTLGLIWTIILH 303
Cdd:smart00033 68 FAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1698-2577 |
1.23e-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: 107.83 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1698 LKLQAEEAERRLRQAEAERARqVQVALETAQRSAE-VELQSKRAS-FAEKTAQLERTlqEEHVTVTQLREEAERRAQQQA 1775
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDR-LEDILNELERQLKsLERQAEKAErYKELKAELREL--ELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1776 eaerareeaerelerwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAE-----QE 1850
Cdd:TIGR02168 247 ----------------ELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYAlaneiSR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1851 LEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllaskar 1930
Cdd:TIGR02168 300 LEQQKQILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1931 aeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK-LAAISEATRLKTEA 2009
Cdd:TIGR02168 369 ---ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2010 EIALKEKEAENERLRRLAEdEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDT---LRQRRQVEEEIMA 2086
Cdd:TIGR02168 446 EEELEELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkalLKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2087 LKASFEKAAAGKAELELELGRIRSNAedTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALE 2166
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2167 EVERLKAKVEEARRL----------RERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERL 2236
Cdd:TIGR02168 603 VAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEEL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2237 RSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ 2316
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2317 KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEE 2396
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2397 LGKLKARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAV 2476
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2477 QEATRLKAEAEL----LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQLEMS------------AEAE 2540
Cdd:TIGR02168 918 EELREKLAQLELrlegLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR-RRLKRLENKikelgpvnlaaiEEYE 996
|
890 900 910
....*....|....*....|....*....|....*..
gi 1046896947 2541 RLKLRMAEMSRAQaraeEDAQRFRKQAEEIGEKLHRT 2577
Cdd:TIGR02168 997 ELKERYDFLTAQK----EDLTEAKETLEEAIEEIDRE 1029
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
186-306 |
1.83e-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: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 186 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirsvrlPREKGRMRFHKLQNVQI 265
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046896947 266 ALDYLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:pfam00307 68 ALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
319-417 |
2.52e-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: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 397
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1046896947 398 PEDVDVPQPDEKSIITYVSS 417
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1595-2411 |
3.88e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 106.29 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1595 QQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAED-----------ELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1663
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1664 SQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERAR--QVQVALETAQRSAEVELQSKRAS 1741
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1742 FAEKTAQLERtLQEEHvtvtqlreeaerraqqqaeaerarEEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEK 1821
Cdd:TIGR02168 339 LAELEEKLEE-LKEEL------------------------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1822 QKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAT 1901
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1902 AATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA-- 1977
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvv 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1978 --EEDAARQRAEAERVLTEKLAAISEATRLKteaeialkEKEAENERLRRLAEDEAFQR--RRLEEQAAQHKADIEERLA 2053
Cdd:TIGR02168 552 veNLNAAKKAIAFLKQNELGRVTFLPLDSIK--------GTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2054 QLRKASEselerqkglVEDTLRQRRQVEEEIMALKASFEKAAAG----KAELELELGRI-RSNAEDTMRSK-ELAEQEAA 2127
Cdd:TIGR02168 624 GVLVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTNSSILeRRREIEELEEKiEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2128 RQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAE 2207
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2208 EKAHAfvVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQ 2287
Cdd:TIGR02168 775 EELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2288 AQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQ 2367
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1046896947 2368 RLKAEVteaARQRSQVEEElfsVRVQMEELGKLKARIEAENRAL 2411
Cdd:TIGR02168 933 GLEVRI---DNLQERLSEE---YSLTLEEAEALENKIEDDEEEA 970
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-112 |
5.87e-22 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 93.45 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 5 MLMPLDQLRAIYEVLFREGVMVAKKDRRpRSLHPHVpGVTNLQVMRAMTSLKARGLVRETFAWCHFYWYLTNEGIDHLRQ 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|....*...
gi 1046896947 85 YLHLPPEIVPASLQRVRRPVAmvMPARR 112
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQ--RPQRR 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1173-1718 |
6.84e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.02 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1173 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1252
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1253 RSTQGAEEVLKTHEEHLKEAQAvpATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE 1332
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1333 RWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALL 1412
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1413 EEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRyseLTTLTSQYIK 1492
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA---LAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1493 FISETLRRMEEEERLAEQQRAEER--ERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQ 1570
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1571 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggAEDELQALRARAEEAEAQKRQAQ 1650
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER---LAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1651 EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERAR 1718
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1258-2058 |
2.12e-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: 103.60 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1258 AEEVLKTHEEHLKEAQAvpatlqELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1337
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1338 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIER 1417
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1418 hgekveecqkfAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISET 1497
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1498 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAE------------LEARE---------LQRRMQE 1556
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlselISVDEgyeaaieaaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1557 EVTRREEAAVDAQqqkrSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALR 1636
Cdd:TIGR02168 550 VVVENLNAAKKAI----AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1637 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAeaeLALRVKAEAEAAREKQRalQALDELKLQAEEAERRLRQAEAE- 1715
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGG---VITGGSAKTNSSILERR--REIEELEEKIEELEEKIAELEKAl 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1716 -RARQVQVALETAQRSAEVELQSKRASFAEKTAQLERtLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERwQLK 1794
Cdd:TIGR02168 701 aELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1795 ANEALRLRLQAeEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELaEQELEKQRQLAEGTAQQRLAAEQELIR 1874
Cdd:TIGR02168 779 EAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIES 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1875 LRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEAEAG 1951
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEGLEV 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1952 RFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLTEKLAAISEATRLkteaeiALKEKEAENERLRRLaede 2030
Cdd:TIGR02168 937 RIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL---- 1005
|
810 820
....*....|....*....|....*...
gi 1046896947 2031 afqrrrleeqaAQHKADIEERLAQLRKA 2058
Cdd:TIGR02168 1006 -----------TAQKEDLTEAKETLEEA 1022
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1847-2724 |
5.87e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.21 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1847 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQHEA-TAATQKRQELEAELAKVRAEMEV 1923
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1924 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLtekLAAISE 2001
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2002 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR----LEEQAAQHKADIEERLAQLRKASESELE-------RQKGLV 2070
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARRqaaeLSRAAEQRMQEAEEALREARAEAEKVVAeakeaaaKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2071 EDTLRQR-RQVEEEIMALKASFEK-AAAGKAELELELG-------RIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRR 2141
Cdd:NF041483 300 ESANEQRtRTAKEEIARLVGEATKeAEALKAEAEQALAdaraeaeKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2142 EAEERVQRSLAAEEEAARQRKVALEEVERLKAKV--------------------------EEARRLRERAEQ-------- 2187
Cdd:NF041483 380 ASEDAKATTRAAAEEAERIRREAEAEADRLRGEAadqaeqlkgaakddtkeyraktvelqEEARRLRGEAEQlraeavae 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2188 ------ESARQ-LQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERL----RSEAEAARRAAEEAEEAREQ 2256
Cdd:NF041483 460 gerirgEARREaVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERAttlrRQAEETLERTRAEAERLRAE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2257 AEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlkqkqAADAEMEK-HKKFAEQTL 2335
Cdd:NF041483 540 AEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALA-----DARAEAERiRREAAEETE 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2336 RQKAQVEQELTTLRLQLEetdhqksildEELQRLKaevTEAARQRSQVEEELFSVRVqmeelgKLKARIEAENRALILRD 2415
Cdd:NF041483 615 RLRTEAAERIRTLQAQAE----------QEAERLR---TEAAADASAARAEGENVAV------RLRSEAAAEAERLKSEA 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2416 KDNTQRFLEEEAEKMKQVAEEAAR-LSVAAQEAARLRQLAEEDLAQQRALAEkmlKEKMQAVQEATRLKAEAellQQQKE 2494
Cdd:NF041483 676 QESADRVRAEAAAAAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA---RKRVE 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2495 LAQEQARRLQED-----------KEQMAQQLVEETQGFQRTLE-------------AERQRQlEMSAEAERLKlrmAEMS 2550
Cdd:NF041483 750 EAQAEAQRLVEEadrratelvsaAEQTAQQVRDSVAGLQEQAEeeiaglrsaaehaAERTRT-EAQEEADRVR---SDAY 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2551 RAQARAEEDAQRFRKQAEEIGEKLHrtELATQEKVTLVQTLEIQRQQSDQDAERLR----EAIAELEREKEKLKQEAKLL 2626
Cdd:NF041483 826 AERERASEDANRLRREAQEETEAAK--ALAERTVSEAIAEAERLRSDASEYAQRVRteasDTLASAEQDAARTRADARED 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2627 QLKSEEMQTVQQEQILQEtqALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELV 2706
Cdd:NF041483 904 ANRIRSDAAAQADRLIGE--ATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETV 981
|
970
....*....|....*...
gi 1046896947 2707 ASMEEARRRQREAEEGVR 2724
Cdd:NF041483 982 GSAQQHAERIRTEAERVK 999
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1636-2524 |
7.04e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 101.97 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1636 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEA 1714
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1715 ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHvtvtqlreeaeRRAQQQAEAERAREEAERELERWQLK 1794
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL-----------AKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1795 ANEALRLRLQAEEVAQQKSLAQAdaEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1874
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1875 LRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKvRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFR 1954
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1955 ELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAER--------VLTEKLAAISEATRLKTEAEIALKEKEAEN---ERL 2023
Cdd:pfam02463 475 KETQLVKLQEQLELLLSRQKL--EERSQKESKARSGlkvllaliKDGVGGRIISAHGRLGDLGVAVENYKVAIStavIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2024 RRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRqrrqveeEIMALKASFEKAAAGKAELEL 2103
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN-------LAQLDKATLEADEDDKRAKVV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2104 ELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEverlkAKVEEARRLRE 2183
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL-----AKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2184 RAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQ 2263
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2264 SRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2343
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2344 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFL 2423
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2424 EEEAEKMKQVAEEAarlsvaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL 2503
Cdd:pfam02463 941 LLEEADEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
890 900
....*....|....*....|.
gi 1046896947 2504 QEDKEQMAQQLVEETQGFQRT 2524
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSI 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2033-2622 |
7.20e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2033 QRRRLEEQAA---QHKADIEERLAQLRKASE---------SELERQKGLVEdtlRQRRQVEE-----------EIMALKA 2089
Cdd:COG1196 156 ERRAIIEEAAgisKYKERKEEAERKLEATEEnlerledilGELERQLEPLE---RQAEKAERyrelkeelkelEAELLLL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2090 SFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVE 2169
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2170 RLKakvEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafvvQQREEELQQTLQQEQNMLERLRSEAEAARRAAEE 2249
Cdd:COG1196 313 ELE---ERLEELEEELAELEEELEELEEELEELEEELEEA------EEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2250 AEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKK 2329
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2330 FAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENR 2409
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2410 AL-----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKA 2484
Cdd:COG1196 544 LAaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2485 EAELLQQQKELAQEQARRLQEDKE------QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEE 2558
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLRevtlegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 2559 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREA--------IAELEREKEKLKQE 2622
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppdLEELERELERLERE 775
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
323-420 |
9.56e-21 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 90.49 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 323 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 401
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1046896947 402 DVPQPDEKSIITYVSSLYD 420
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
950-1016 |
1.12e-20 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 88.47 E-value: 1.12e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 950 QLKPRNpaHPVRGHVPLLAVCDYKQVEVTVHKGDQCQLVGPAQPFHWKVLGGSSSEAAVPSVCFLVP 1016
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1500-2238 |
2.13e-20 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 100.67 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1500 RMEEEERlAEQQRAEERERLAEVEAALEKQRQLAEAHAQA-KAQAELEARELqrrmqeevtrREEAAVDAQQQKRSIQEE 1578
Cdd:NF041483 508 RTEAIER-ATTLRRQAEETLERTRAEAERLRAEAEEQAEEvRAAAERAAREL----------REETERAIAARQAEAAEE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1579 LQHLRQSSEAEIQAKAQQVEAA--ERSRMRIEEEIRVVRLQLETTERQR---GGAEDELQALRARA-EEAEAQKRQAQEE 1652
Cdd:NF041483 577 LTRLHTEAEERLTAAEEALADAraEAERIRREAAEETERLRTEAAERIRtlqAQAEQEAERLRTEAaADASAARAEGENV 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1653 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQrALQALDELKLQAEEAERRLRQAE----AERARQVQvALETAQ 1728
Cdd:NF041483 657 AVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERV-GTEAAEALAAAQEEAARRRREAEetlgSARAEADQ-ERERAR 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1729 RSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERElerwqlkanEALRLRLQAEEV 1808
Cdd:NF041483 735 EQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEE---------EIAGLRSAAEHA 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1809 AQQ-KSLAQADAEKQKEEAEREARrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRLRAETeqGEQQRQ 1887
Cdd:NF041483 806 AERtRTEAQEEADRVRSDAYAERE---RASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDA--SEYAQR 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1888 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRAL 1966
Cdd:NF041483 878 VRTEASDTLASAEQDAARTRADAREDANRIRSDAA---AQADRLIGEATSEAERLTAEARAEAERLRdEARAEAERVRAD 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1967 A-EEAKRQRQLAEEDAARQRAEAERVLTeklAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ---------RRR 2036
Cdd:NF041483 955 AaAQAEQLIAEATGEAERLRAEAAETVG---SAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRtldearkdaNKR 1031
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2037 LEEQAAQHKADIEERLAQ----LRKASE------SELERQKGLVEDTLRQR--RQVEEEIMALKASFEKAAAGKAELELE 2104
Cdd:NF041483 1032 RSEAAEQADTLITEAAAEadqlTAKAQEealrttTEAEAQADTMVGAARKEaeRIVAEATVEGNSLVEKARTDADELLVG 1111
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2105 LGR----IRSNAEDtMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLK-------- 2172
Cdd:NF041483 1112 ARRdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANseaskvri 1190
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 2173 AKVEEARRLRERAEQESARQLQLAQ------EAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRS 2238
Cdd:NF041483 1191 AAVKKAEGLLKEAEQKKAELVREAEkikaeaEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEALES 1262
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1494-2125 |
3.58e-20 |
|
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: 99.76 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1494 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAELEARELQRRMqEEVTRREEAAVDAQQQKR 1573
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1574 SIQEELQHLRQSSEAEIQAKAQQVEAaersrmrIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKR------ 1647
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1648 --------QAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQA-LDELKLQAEEAERRLRQAEAER-- 1716
Cdd:TIGR02169 388 kdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLsk 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1717 ARQVQVALETAQRSAEVELQSKRA--SFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREeaerelERWQLK 1794
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG------ERYATA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1795 ANEALRLRLQA-----EEVAQQ--KSLAQADAE----------KQKEEAEREARRRG------------KAEEQAVR--- 1842
Cdd:TIGR02169 541 IEVAAGNRLNNvvvedDAVAKEaiELLKRRKAGratflplnkmRDERRDLSILSEDGvigfavdlvefdPKYEPAFKyvf 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1843 QRELAEQELEKQRQL--------------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1896
Cdd:TIGR02169 621 GDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1897 QHEATAATQKRQELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQRLEAEAgrfrELAEEAARLRALaEEAKR 1972
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEIENVKS----ELKELEARIEEL-EEDLH 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1973 QRQLAEEDAARQRAEAE--------RVLTEKLAAISEATRlktEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQH 2044
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2045 KADIEERLAQLRKAsESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQ 2124
Cdd:TIGR02169 853 EKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
.
gi 1046896947 2125 E 2125
Cdd:TIGR02169 932 E 932
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
319-418 |
4.61e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 88.31 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 398
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1046896947 399 ED-VDVPQPDEKSIITYVSSL 418
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1471-2065 |
8.23e-20 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 98.45 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1471 QEYVDLRTRYSELTTLTSQY-IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEL 1545
Cdd:COG4913 262 ERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1546 EARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1625
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1626 GGAEDELQALRARA---EEAEAQKRQAQEEAERLRR----------QVQDESQRKRQAeAELALR-------VKAEAEAA 1685
Cdd:COG4913 422 RELEAEIASLERRKsniPARLLALRDALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLGgfaltllVPPEHYAA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1686 rekqrALQALDELK----LQAEEAERRLRQAEAER------ARQVQVALETAQRSAEVELQsKRASFA--EKTAQLERTl 1753
Cdd:COG4913 501 -----ALRWVNRLHlrgrLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELG-RRFDYVcvDSPEELRRH- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1754 qEEHVTVTQLREEAERRAQQQAEAERAreeaerelERWQL-KANEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearr 1832
Cdd:COG4913 574 -PRAITRAGQVKGNGTRHEKDDRRRIR--------SRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL-------- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1833 rgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEATAATQKRQE 1909
Cdd:COG4913 637 --EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1910 LEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1989
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 1990 RVLTE-KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELER 2065
Cdd:COG4913 791 RAMRAfNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
319-419 |
1.49e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 86.63 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 398
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1046896947 399 EDVDV--PQPDEKSIITYVSSLY 419
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1488-2419 |
1.54e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 97.73 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1488 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAELEARELQRRMQEEVTRREEAAVD 1567
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1568 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELqalraraEEAEAQKR 1647
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE-------EELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1648 QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAarEKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETA 1727
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1728 QRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAeaerareeaerelerwqLKANEALRLRLQAEE 1807
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL-----------------EILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1808 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1887
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1888 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL--EAEAGRFRELAEEAARLRA 1965
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLipKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1966 LAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaaQHK 2045
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ--ELQ 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2046 ADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQE 2125
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2126 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQ 2205
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2206 AEEKahaFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQ 2285
Cdd:pfam02463 840 LELK---EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2286 AQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEE 2365
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2366 LQRLKAEVTEAARQRSQVEEELF------SVRVQMEELGKLKARIEAENRALILRDKDNT 2419
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQRLkeflelFVSINKGWNKVFFYLELGGSAELRLEDPDDP 1056
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
315-420 |
2.67e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 86.15 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 315 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 394
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1046896947 395 LLDPEDV-DVPQPDEKSIITYVSSLYD 420
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
185-307 |
3.31e-19 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 86.68 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 185 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirsvrlprEKGRMRFHKLQNVQ 264
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVS 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1046896947 265 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 307
Cdd:cd21308 85 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2099-2762 |
3.89e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2099 AELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQrslAAEEEAARQRKVALEEVERLKAKVEEA 2178
Cdd:COG1196 196 GELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELE---AELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2179 RRLRERAEQEsARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQtlqqeqnmLERLRseaeaarraaeeaeeareqae 2258
Cdd:COG1196 273 RLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRRELEER--------LEELE--------------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2259 reaaqsrkqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKhkkfAEQTLRQK 2338
Cdd:COG1196 323 ----------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2339 AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDN 2418
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2419 TQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA-- 2496
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAal 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2497 QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHR 2576
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2577 TELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEK 2656
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2657 DS-LLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRkqeelqrleq 2735
Cdd:COG1196 709 LAeAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpv------ 782
|
650 660
....*....|....*....|....*..
gi 1046896947 2736 qrqqqekllAEENQRLRERLQRLEEEH 2762
Cdd:COG1196 783 -----nllaIEEYEELEERYDFLSEQR 804
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
322-418 |
3.89e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.45 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 322 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 397
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1046896947 398 PEDVDVPQPDEKSIITYVSSL 418
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1220-1994 |
4.28e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 96.28 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1220 LRSELELTLGKLEQVRSLSaiylEKLKTISLVIRSTQGAEEVLKTHEEHlKEAQAVPATLQELEVTKASLKKLRAQAEAQ 1299
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKA----ERYKELKAELRELELALLVLRLEELR-EELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1300 qpvFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSW 1379
Cdd:TIGR02168 269 ---LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1380 LQDAKSRQEQIQA--------VPIANS--QAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQ 1449
Cdd:TIGR02168 346 LEELKEELESLEAeleeleaeLEELESrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1450 LEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ 1529
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1530 RQLAEAHAQAKAQAE------------LEARE---------LQRRMQEEVTRREEAAVDAQQ---QKRSIQEELQHLRQS 1585
Cdd:TIGR02168 502 EGFSEGVKALLKNQSglsgilgvlselISVDEgyeaaieaaLGGRLQAVVVENLNAAKKAIAflkQNELGRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1586 SEAEIQAKAQQVEAAERSRMRI-------EEEIRVV------------------RLQLETTERQR--------------- 1625
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVakdlvkfDPKLRKAlsyllggvlvvddldnalELAKKLRPGYRivtldgdlvrpggvi 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1626 -GGAEDE---LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQ 1701
Cdd:TIGR02168 662 tGGSAKTnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1702 AEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAR 1781
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1782 EEAERELERWQlkaNEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGT 1861
Cdd:TIGR02168 820 ANLRERLESLE---RRIAATERRLEDLEEQIEELSEDIESLA-----------AEIEELEELIEELESELEALLNERASL 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1862 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA--------KVRAEMEVLLASKARAEE 1933
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerlseEYSLTLEEAEALENKIED 965
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 1934 ESRSTSEKSKQ--RLEAEAGRFRELAEEAARlralaEEAKRQRQLAE--EDAARQRAEAERVLTE 1994
Cdd:TIGR02168 966 DEEEARRRLKRleNKIKELGPVNLAAIEEYE-----ELKERYDFLTAqkEDLTEAKETLEEAIEE 1025
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
185-307 |
4.62e-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: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 185 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDslprerdviRSVRLPREKGRMRFHKLQNVQ 264
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQK---------RMYRKYHQRPTFRQMQLENVS 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1046896947 265 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 307
Cdd:cd21309 82 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1883-2772 |
1.85e-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: 94.27 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1883 EQQRQLLEEELARLQH-----EATAAT-QKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRF-RE 1955
Cdd:pfam02463 152 PERRLEIEEEAAGSRLkrkkkEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYlDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1956 LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTE-KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEafQR 2034
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVlKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER--RK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2035 RRLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRirsNAED 2114
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL---ESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2115 TMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLREraEQESARQLQ 2194
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE--KQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2195 LAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERL 2274
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2275 KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQ 2351
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaqlDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2352 LEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEelgklkarieaenralilrDKDNTQRFLEEEAEKMK 2431
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKAS-------------------LSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2432 QVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKELAQEQARRLQEDKEQM 2510
Cdd:pfam02463 685 AESELAkEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD--KINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2511 AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAE--EDAQRFRKQAEEIGEKLHRTELATQEKVTLV 2588
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEElkEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2589 QTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKS----EEMQTVQQEQILQETQALQKSFLSEKDSllQRER 2664
Cdd:pfam02463 843 KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLkdelESKEEKEKEEKKELEEESQKLNLLEEKE--NEIE 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2665 FIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRkqeelqrleqqrqqQEKLL 2744
Cdd:pfam02463 921 ERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE--------------EFEEK 986
|
890 900
....*....|....*....|....*...
gi 1046896947 2745 AEENQRLRERLQRLEEEHRAALAHSEEI 2772
Cdd:pfam02463 987 EERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2332-2676 |
1.89e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2332 EQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVtEAARQRSQVEEELFsvrvqmeelgklkariEAENRAL 2411
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGE-------LERQLEPLERQA-EKAERYRELKEELK----------------ELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2412 ILRDKDntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQ 2491
Cdd:COG1196 231 LLKLRE-----LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---LLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2492 QKELAQEQARRLQEDKEQMAQQLVEETQ---GFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2568
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2569 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQAL 2648
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE-EEAELEEEEEAL 461
|
330 340
....*....|....*....|....*...
gi 1046896947 2649 QKSFLSEKDSLLQRERFIEQEKAKLEQL 2676
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1496-2110 |
2.01e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.57 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1496 ETLRRMEEEERLA-EQQRAEERERLAEVEAALEkQRQLAEAHAQ--------AKAQAELEARELQRRMQEEvtrREEAAV 1566
Cdd:PRK02224 165 EEYRERASDARLGvERVLSDQRGSLDQLKAQIE-EKEEKDLHERlngleselAELDEEIERYEEQREQARE---TRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1567 DAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQK 1646
Cdd:PRK02224 241 EVLEEHEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1647 RQAQEEAERLRRQVQDESQRKRQAEaelalrvkAEAEAAREKQRALQA-LDELKLQAEEAERRLRQAEAERARQvqvalE 1725
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHN--------EEAESLREDADDLEErAEELREEAAELESELEEAREAVEDR-----R 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1726 TAQRSAEVELQSKRASFAEKTAQLERtLQEEHVTVTQlreeaerraqqqaeaerareeaerelERWQLKANEA-LRLRLQ 1804
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGN-AEDFLEELRE--------------------------ERDELREREAeLEATLR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1805 AEEVAQQKSLAQADAEK-----QKEEAEREARRRGKAEEqavrQRELAEQELEKQRqLAEGTAQQRLAAEQELIRLRAET 1879
Cdd:PRK02224 437 TARERVEEAEALLEAGKcpecgQPVEGSPHVETIEEDRE----RVEELEAELEDLE-EEVEEVEERLERAEDLVEAEDRI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1880 EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLEAEAGRFRELAEE 1959
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1960 AARLRALAEeakrqrQLAEEDAARQRAEAERvltEKLAAISEatrLKTEAEIALKEKeaeNERLRRLAEDeaFQRRRLEE 2039
Cdd:PRK02224 588 IESLERIRT------LLAAIADAEDEIERLR---EKREALAE---LNDERRERLAEK---RERKRELEAE--FDEARIEE 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2040 ------QAAQHKADIEERLAQLRkASESELERQKGLVE------DTLRQRR-QVEEEIMALKASFEKAaagkAELELELG 2106
Cdd:PRK02224 651 aredkeRAEEYLEQVEEKLDELR-EERDDLQAEIGAVEneleelEELRERReALENRVEALEALYDEA----EELESMYG 725
|
....
gi 1046896947 2107 RIRS 2110
Cdd:PRK02224 726 DLRA 729
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
319-418 |
9.16e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 81.82 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 398
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1046896947 399 ED-VDVPQPDEKSIITYVSSL 418
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
323-420 |
5.01e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.54 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 323 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 401
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1046896947 402 DVPQPDEKSIITYVSSLYD 420
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1978-2675 |
5.57e-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: 89.26 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1978 EEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA------QHKADIEER 2051
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyyQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2052 LAQLRKASESELERQKGLVEDTLRQRRQVEEEIMA--LKASFEKAAAGKAELELELgRIRSNAEDTMRSKELAEQEAARQ 2129
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKqeIEKEEEKLAQVLKENKEEE-KEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2130 RQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLA------QEAAQKR 2203
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLeqleeeLLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2204 LQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAE------RLKQS 2277
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKeelekqELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2278 AEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKK--FAEQTLRQKAQVEQELTTLRLQLEET 2355
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLalIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2356 DHQKSILDEELQRLKAEVTEAARQRSQVEEELF----SVRVQMEELGKLKARIEAENRALILR----DKDNTQRFLEEEA 2427
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPlgarKLRLLIPKLKLPLKSIAVLEIDPILNlaqlDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2428 EKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDK 2507
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2508 EQMAQQLVEETQ---GFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2584
Cdd:pfam02463 702 KKKEQREKEELKklkLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2585 VTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSF--LSEKDSLLQR 2662
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEE 861
|
730
....*....|...
gi 1046896947 2663 ERFIEQEKAKLEQ 2675
Cdd:pfam02463 862 EITKEELLQELLL 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1946-2801 |
5.89e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.35 E-value: 5.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1946 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLTEKLAAISEATRlKTEAE 2010
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2011 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMAL 2087
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2088 KASFEKAAAGKAELELELGRIRSnaedtmRSKELAEQEAARQRQLAAEEEQRRreaeervqrSLAAEEEAARqrkvalEE 2167
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELES------KLDELAEELAELEEKLEELKEELE---------SLEAELEELE------AE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2168 VERLKAKVEEARRLRERAEQESArQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRA 2246
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVA-QLELQIASLNNEIErLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2247 AEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADaemek 2326
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG----- 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2327 hkkfAEQTLRQKAQVEQElttLRLQLEETdhqksiLDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEA 2406
Cdd:TIGR02168 521 ----ILGVLSELISVDEG---YEAAIEAA------LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQ 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2407 ENRALILRDKDNTQRF---LEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEED------------------LAQQRAL 2464
Cdd:TIGR02168 588 GNDREILKNIEGFLGVakdLVKFDPKLRKALSYLlGGVLVVDDLDNALELAKKLRpgyrivtldgdlvrpggvITGGSAK 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2465 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKL 2544
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2545 RMAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAK 2624
Cdd:TIGR02168 748 RIAQLSKELTELEA-------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2625 LLQLKSEEMQTvQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQQQQMEQEKQE 2704
Cdd:TIGR02168 821 NLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2705 LVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEhraALAHSEEIATSQAAA---TK 2781
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEArrrLK 975
|
890 900
....*....|....*....|
gi 1046896947 2782 ALPNGRDALDGPSMEAEPEY 2801
Cdd:TIGR02168 976 RLENKIKELGPVNLAAIEEY 995
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2315-2783 |
1.65e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2394
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2395 EELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEkmLKEKMQ 2474
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAELEEEEEEEEEALEEAAEEEAELEEE--EEALLE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2475 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMS-------AEAERLKLRMA 2547
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligvEAAYEAALEAA 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2548 EMSRAQARAEEDAQRFRKQAEEIgeKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQ 2627
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYL--KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2628 LKSEEMQTVQQEQ---ILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQlfqdEVAKAKQLQEEQQRQQQQMEQEKQE 2704
Cdd:COG1196 622 LLGRTLVAARLEAalrRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA----ALLEAEAELEELAERLAEEELELEE 697
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 2705 LVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKAL 2783
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
187-304 |
1.69e-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: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 187 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdvirsvrlPREKGRMRFHKLQNVQIA 266
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQAC 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046896947 267 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 304
Cdd:cd21212 68 LQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1078-1755 |
1.76e-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: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1078 EQRQALRNLELHYQA----FLRDSQDAGgfgPEDRLVAEREYGSCSRHYQQLLQSLEQGEQE----ESRCQRCISELKDI 1149
Cdd:TIGR02168 217 ELKAELRELELALLVlrleELREELEEL---QEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1150 RLQLEACETRTVH---RLRlPLDKDPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELEL 1226
Cdd:TIGR02168 294 ANEISRLEQQKQIlreRLA-NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1227 TLGKL-EQVRSLSAIYLEKLKTISLvIRSTQgaeEVLKTHEEHLKEAQAVpatlQELEVTKASLKKLRAQAEAQQPVFNT 1305
Cdd:TIGR02168 373 RLEELeEQLETLRSKVAQLELQIAS-LNNEI---ERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1306 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQL---LERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQD 1382
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1383 AKSR---------------QEQIQAVPIANSQAAR---EQLRQEK----ALLEEIERHGEKVEECQKFAKQYINAIKDYE 1440
Cdd:TIGR02168 525 LSELisvdegyeaaieaalGGRLQAVVVENLNAAKkaiAFLKQNElgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1441 LQLITYKAQLEPVASP---------------AKKPKVQSGSESVIQEYVDLRTRYS--------ELTTL-TSQYIKFISE 1496
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1497 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQ 1576
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1577 EELQHLRQSSEAEIQAKAQQVEAaersrmriEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERL 1656
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEEL--------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1657 RRQVQDESQRKRQAE---AELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRsaev 1733
Cdd:TIGR02168 837 ERRLEDLEEQIEELSediESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE---- 912
|
730 740
....*....|....*....|..
gi 1046896947 1734 elqskrasfaektaqLERTLQE 1755
Cdd:TIGR02168 913 ---------------LRRELEE 919
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
188-302 |
2.37e-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: 77.38 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 188 KKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirsvrlpREKGRMRFHKLQNVQIAL 267
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFL 66
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 268 DYLRHRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 302
Cdd:cd00014 67 NACKKLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1570-2513 |
2.86e-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: 87.05 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1570 QQKRSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEdELQALRARAEEAEA----- 1644
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1645 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAARE-KQRALQALDELKLQAEEAERRLRQAEAERA---RQV 1720
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEEQLRVKEKIGELEAEIAsleRSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1721 QVALETAQRSAE--VELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQaeaerareeaerelerwqlkanEA 1798
Cdd:TIGR02169 311 AEKERELEDAEErlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------------------ED 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1799 LRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRA 1877
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1878 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAGRFR 1954
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1955 ELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLTEKLAAiseatrlktEAEIALKEKEAENER---LRRLAEDEA 2031
Cdd:TIGR02169 529 QLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2032 FQRRRLEEQAAQHKADIEERLAQLRKASESELeRQKGLVEDTLRQRRQVEEEIMALKAS--FEKAAAGKAELELELGRIR 2109
Cdd:TIGR02169 589 DLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRMVTLEGelFEKSGAMTGGSRAPRGGIL 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2110 SNAEDTMRSKELAEQEaarqrqlaaeeeqrrreaeervqrslaaeEEAARQRKVALEEVERLKAKVEEARRLRERAEQE- 2188
Cdd:TIGR02169 668 FSRSEPAELQRLRERL-----------------------------EGLKRELSSLQSELRRIENRLDELSQELSDASRKi 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2189 ---SARQLQLAQEAAQKRLQAEEkahafvVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSR 2265
Cdd:TIGR02169 719 geiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2266 KQVEEAERLKQsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQEL 2345
Cdd:TIGR02169 793 IPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2346 TTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENraliLRDKDNTQRfLEE 2425
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSELKAK-LEA 928
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2426 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQE 2505
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
....*...
gi 1046896947 2506 DKEQMAQQ 2513
Cdd:TIGR02169 1008 RIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1325-2087 |
3.41e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.66 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1325 GERDVEVERWRE---RVTQLLERWQAVLAQTdvrqreLEQLGRqLRYYRESADPLsswlQDAKSRQEQIQAVPIANS-QA 1400
Cdd:TIGR02169 166 AEFDRKKEKALEeleEVEENIERLDLIIDEK------RQQLER-LRREREKAERY----QALLKEKREYEGYELLKEkEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1401 AREQLRQEKALLEEIERHGEKVEEcqkfakqyinAIKDYELQLITYKAQLEPVASPAKKpkvqSGSESVIQEYVDLRTRY 1480
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELNKKIKD----LGEEEQLRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1481 SELTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTR 1560
Cdd:TIGR02169 301 AEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1561 REEAaVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAE 1640
Cdd:TIGR02169 380 FAET-RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1641 EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALDELKLQAEEAE----RRLRQAEAER 1716
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVhgtvAQLGSVGERY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1717 ARQVQVAL------------ETAQRSAEV--ELQSKRASFA--EKTAQLERTLQEEH----------------------- 1757
Cdd:TIGR02169 538 ATAIEVAAgnrlnnvvveddAVAKEAIELlkRRKAGRATFLplNKMRDERRDLSILSedgvigfavdlvefdpkyepafk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1758 ------VTVTQLREEAERRAQQQAEAER-------------AREEAERELERWQLKAnEALRLRLQAEEVAQQKSLAQAD 1818
Cdd:TIGR02169 618 yvfgdtLVVEDIEAARRLMGKYRMVTLEgelfeksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1819 AEKQKEEAEREARRRGKAEEQAV---RQRELAEQELEKQRQLAEG-------TAQQRLAAEQELIRLRAETEQGEQQRQL 1888
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGeieKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHK 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1889 LEEELARLqhEATAATQKRQELEAELAKVRAEmevllaskaRAEEESRSTS-EKSKQRLEAEAGRFRELAEEAARLRALA 1967
Cdd:TIGR02169 777 LEEALNDL--EARLSHSRIPEIQAELSKLEEE---------VSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1968 EEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 2047
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1046896947 2048 IE---ERLAQLRKASESELE-RQKGLVEDTLRQRRQ-VEEEIMAL 2087
Cdd:TIGR02169 926 LEaleEELSEIEDPKGEDEEiPEEELSLEDVQAELQrVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1299-2177 |
3.55e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 86.38 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1299 QQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1368
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1369 YRESADPLSSWLQDAKSR-QEQIQAVP--IANSQAAREQLRQEKALLE-EIERHGEKVEECQKFAKQYINAIKDYELQLI 1444
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKmQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1445 TYKAQLEPVASPAKK-PKVQSGSESVIQEyVDLRTRYSELTTLTSQYIKfisetlRRMEEEERLAEQQRAEERERLAEVE 1523
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEEKGRQELEKAK------RKLEGESTDLQEQIAELQAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1524 AAL-EKQRQLAEAHAQ------AKAQAELEARELQRR---MQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAK 1593
Cdd:pfam01576 236 AQLaKKEEELQAALARleeetaQKNNALKKIRELEAQiseLQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1594 AQQVEAaersRMRIEEEIRVVRLQLETTERQRggaEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE 1673
Cdd:pfam01576 316 AAQQEL----RSKREQEVTELKKALEEETRSH---EAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1674 LALRVK----AEAEAAREKQRALQALDELKLQAEEAErRLRQAEAERARQVQVALETAQRSAEvELQSKRASFAEKTAQL 1749
Cdd:pfam01576 389 LQAELRtlqqAKQDSEHKRKKLEGQLQELQARLSESE-RQRAELAEKLSKLQSELESVSSLLN-EAEGKNIKLSKDVSSL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1750 ERTLQE----------EHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL-RLRLQAEEVA-------QQ 1811
Cdd:pfam01576 467 ESQLQDtqellqeetrQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLsDMKKKLEEDAgtlealeEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1812 KSLAQADAEKQKEEAEREARRRGKAEEQAVR-QRELAEQ--ELEKQRQLAEGTAQQ-----RLAAEQELIRLRAETEQGE 1883
Cdd:pfam01576 547 KKRLQRELEALTQQLEEKAAAYDKLEKTKNRlQQELDDLlvDLDHQRQLVSNLEKKqkkfdQMLAEEKAISARYAEERDR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1884 QQRQLLEEE--LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAeEESRSTSEKSKQRLEAEAGRFRELAEEA- 1960
Cdd:pfam01576 627 AEAEAREKEtrALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDV-GKNVHELERSKRALEQQVEEMKTQLEELe 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1961 --------ARLR------ALAEEAKRQRQLAEEDA-------ARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 2019
Cdd:pfam01576 706 delqatedAKLRlevnmqALKAQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQ 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2020 NERLRRLAEDEAFQRRRLEEQAAQHKADIEE-RLAQ---LRKASESElERQKGLVEDTL----------RQRRQVEEEIM 2085
Cdd:pfam01576 786 IDAANKGREEAVKQLKKLQAQMKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedlaaseRARRQAQQERD 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2086 ALKASFEKAAAGKAELELELGRIrsnaEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL 2165
Cdd:pfam01576 865 ELADEIASGASGKSALQDEKRRL----EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESAR 940
|
970
....*....|....*.
gi 1046896947 2166 EEVER----LKAKVEE 2177
Cdd:pfam01576 941 QQLERqnkeLKAKLQE 956
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1121-1878 |
5.51e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.88 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1121 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkdpaRECAQRIAEQQK----AQAEVEGLGK 1195
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1196 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTH-----EEHL 1269
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeleEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1270 KEAQAVPATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQ-QRHGERDVEVERWRERVTQLLERWQAV 1348
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1349 LAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAvPIANSQAAREQLRQEKALLEEIERHGEKVEEC--- 1425
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE-GVKALLKNQSGLSGILGVLSELISVDEGYEAAiea 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1426 -------------QKFAKQYINAIKDYELQLITYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTL 1486
Cdd:TIGR02168 542 alggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1487 TSQYikFISETLrrmEEEERLAEQQRAEER-----ERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRR 1561
Cdd:TIGR02168 622 LGGV--LVVDDL---DNALELAKKLRPGYRivtldGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1562 EEAAVDAQQQKRSIQEELQHLR---QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRAR 1638
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1639 AEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERAr 1718
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE- 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1719 qvqvaletaqrSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAeaerareeaerelerwQLKANEA 1798
Cdd:TIGR02168 856 -----------SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE----------------ELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1799 LRLRLQAEEVAQQKSLAQADAEKQKeeaerearRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAE 1878
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEG--------LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1792-2652 |
6.70e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1792 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1867
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1868 --AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1945
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1946 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLTEKLAAISEatrlKTEAEIALKEKEAENERLRR 2025
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINELEEE----KEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2026 LAEDEAFQRRRLEEQAAQhkadIEERLAQLRKaSESELERQKGLVEDTLRQRRQVEEEImalkasfEKAAAGKAELELEL 2105
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDR----VEKELSKLQR-ELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2106 GRIRsnaedtmRSKELAEQEAARQRqlaaeeeqrrreaeervQRSLAAEEEAarqrkVALEEVERLKA------------ 2173
Cdd:TIGR02169 531 GSVG-------ERYATAIEVAAGNR-----------------LNNVVVEDDA-----VAKEAIELLKRrkagratflpln 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2174 KVEEARRLRERAEQESARQLQLAQEAAQKRLqaeEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEA 2253
Cdd:TIGR02169 582 KMRDERRDLSILSEDGVIGFAVDLVEFDPKY---EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2254 REQAEREAAQSRKQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKF 2330
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2331 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVteAARQRSQVEEELFSVRVQMEELGKLKARIEAENRA 2410
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2411 L--ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAEL 2488
Cdd:TIGR02169 817 IeqKLNRLTLEKEYLEKEIQELQEQRIDL-----KEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGD 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2489 LQQQKELAQEQARRLQEDKEQMAQQlVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2568
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2569 EIgeklhrtelatqekvtlvQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2648
Cdd:TIGR02169 966 EI------------------RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
....
gi 1046896947 2649 QKSF 2652
Cdd:TIGR02169 1028 NENF 1031
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
321-419 |
7.26e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 76.57 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 321 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 400
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1046896947 401 -VDVPQPDEKSIITYVSSLY 419
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1471-1980 |
1.36e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 84.05 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1471 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERL---AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEL-- 1545
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyq 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1546 EARELQRRMQEEVTRREEAavdaQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1625
Cdd:COG4717 133 ELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1626 GGAEDELQALRARAEEAEAQKRQAQEEAER--LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAE 1703
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1704 EAERRLRQAEAERARQVQVALETAQRSAEvelqskrasfaekTAQLERTLQEEHVtvtqlreeaeRRAQQQAEAERAREE 1783
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELE-------------EEELEELLAALGL----------PPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1784 AERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEkqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEgtAQ 1863
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVE---------------DEEELRAALEQAEEYQELKEELEE--LE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1864 QRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlaskaraeEESRSTSEKSK 1943
Cdd:COG4717 409 EQLEELLGELEELLEALDEEE----LEEELEELEEELEELEEELEELREELAELEAELEQL--------EEDGELAELLQ 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 1046896947 1944 QRLEAEAgRFRELAEEAARLRALAEEAKRQRQLAEED 1980
Cdd:COG4717 477 ELEELKA-ELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3621-3659 |
1.65e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.75 E-value: 1.65e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 3621 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 3659
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
324-419 |
1.96e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.09 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 324 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 402
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1046896947 403 VPQPDEKSIITYVSSLY 419
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
321-420 |
2.20e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.00 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 321 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 400
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1046896947 401 VDV--PQPDEKSIITYVSSLYD 420
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1258-1756 |
2.32e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.55 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1258 AEEVLKTHEEhlkeaqavpaTLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1337
Cdd:PRK02224 239 ADEVLEEHEE----------RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1338 VTQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLSSWLQDAKSRQEQIQavpiANSQAAREQLRQEKA 1410
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1411 LLEEIERHGEKVEECQKFAkqyinaikdyelqlitykaqlepvasPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqy 1490
Cdd:PRK02224 385 EIEELEEEIEELRERFGDA--------------------------PVDLGNAEDFLEELREERDELREREAELEAT---- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1491 ikfISETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAKAQAELEAR- 1548
Cdd:PRK02224 435 ---LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEDLVEAEDRi 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1549 ----ELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvRLQLETTERQ 1624
Cdd:PRK02224 512 erleERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1625 RGGAEDELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDESQRKRQAEAELAlrvKAEAEAARE-KQRALQALDEL- 1698
Cdd:PRK02224 590 SLERIRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYLEQVe 666
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 1699 -KLQAEEAERRLRQAEAERARQVQVALEtaqrsaevELQSKRASFAEKTAQLErTLQEE 1756
Cdd:PRK02224 667 eKLDELREERDDLQAEIGAVENELEELE--------ELRERREALENRVEALE-ALYDE 716
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4199-4237 |
2.83e-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: 2.83e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 4199 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4237
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
321-424 |
3.30e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 74.70 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 321 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 400
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1046896947 401 VDV--PQPDEKSIITYVSSLYDAMPR 424
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2489-2779 |
3.79e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2489 LQQQKELAqEQARRLQEDKEQM-AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQA 2567
Cdd:COG1196 205 LERQAEKA-ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2568 EEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2647
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2648 LQKSFLSEKDSLLQRERFIEQEKAKLEQLfqdevaKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQ 2727
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 2728 EELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAA 2779
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2962-3000 |
3.83e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.83e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 2962 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEMNRVL 3000
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1545-2058 |
7.92e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.27 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1545 LEARELQ---RRMQEEVT---RREEAAVDAQQQKRSiqeeLQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQL 1618
Cdd:COG4913 218 LEEPDTFeaaDALVEHFDdleRAHEALEDAREQIEL----LEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1619 ETTERQRggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKRQAEAELALRVKAEAEAAREKQRALQALDE 1697
Cdd:COG4913 293 LEAELEE--LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1698 LKLQAEEAERRLrQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTlqeehvtvtqlreeaerraqqqaea 1777
Cdd:COG4913 371 LGLPLPASAEEF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL------------------------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1778 erareeaERELERwqLKAN--------EALRLRLQAE---------------EVAQ-----------------------Q 1811
Cdd:COG4913 425 -------EAEIAS--LERRksniparlLALRDALAEAlgldeaelpfvgeliEVRPeeerwrgaiervlggfaltllvpP 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1812 KSLAQA----DAEKQKEEAEREARRRGKAEEQAVR--QRELAEqELEKQRQLAEGTAQQRLAA---------EQELIRL- 1875
Cdd:COG4913 496 EHYAAAlrwvNRLHLRGRLVYERVRTGLPDPERPRldPDSLAG-KLDFKPHPFRAWLEAELGRrfdyvcvdsPEELRRHp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1876 RAETEQG---------------------------EQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK 1928
Cdd:COG4913 575 RAITRAGqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1929 ARAEEESRSTS--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLTEKLA 1997
Cdd:COG4913 655 EYSWDEIDVASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1998 AISEATRLKTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 2058
Cdd:COG4913 735 RLEAAEDLARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
775-953 |
9.39e-15 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 76.33 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 775 LHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQ 854
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 855 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLQKLQETLRRKYSCDrsiTVTRLEDLLQDAQDEKEQLNEY 934
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 1046896947 935 KGHLSGLAKRAKAIVQLKP 953
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3880-3918 |
1.11e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.11e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 3880 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3918
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1289-1738 |
3.11e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.43 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1289 LKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWR--ERVTQLLERWQAVLAQTDVRQRELEQLGRQL 1366
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1367 RYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQekaLLEEIERHGEKVEECQKFAKQYINAIKDYELQLITY 1446
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1447 KAQLEPVASPAK--KPKVQSGSESVI-------QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEE 1515
Cdd:COG4717 233 ENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1516 RERL--AEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKrsIQEELQHLRQSSEAEIQAK 1593
Cdd:COG4717 313 LEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1594 AQQVEAAErsrmRIEEEIRVVRLQLettERQRGGAEDELQALraRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE 1673
Cdd:COG4717 391 LEQAEEYQ----ELKEELEELEEQL---EELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 1674 LalrvkAEAEAAREKQRALQALDELKLQAEEAERRLRqaeaeRARQVQVALETAQRSAEVELQSK 1738
Cdd:COG4717 462 L-----EQLEEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYREERLPP 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1123-2032 |
3.62e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.11 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1123 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKDPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1200
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1201 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEEVLKTHEEHLKE 1271
Cdd:TIGR02169 250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1272 AQAVPATLQ-ELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1350
Cdd:TIGR02169 320 AEERLAKLEaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1351 qtdvRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAvpiansqaareqlrqekalleEIERHGEKVEECQKFAK 1430
Cdd:TIGR02169 390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1431 QYINAIKDYELQLITYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQ 1510
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1511 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEArelQRRMQEEVTRREEAAVDAQQQKRS-------------IQE 1577
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAA---GNRLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1578 ELQHLRQSSEAEIQAKA-------QQVEAA--------------ERSRmRIEEEIRVVRLQLETTERQ---RGGAEDEL- 1632
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAvdlvefdPKYEPAfkyvfgdtlvvediEAAR-RLMGKYRMVTLEGELFEKSgamTGGSRAPRg 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1633 QALRARAEEAEAQKRQAQEEA-ERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDElklqaeeaerrlrq 1711
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------------- 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1712 aEAERARQVQVALETAQRSAEVELQSKRASFAE---KTAQLERTLQEEHVTVTQLREEAERraqqqaeaerareeaerel 1788
Cdd:TIGR02169 731 -EEEKLKERLEELEEDLSSLEQEIENVKSELKEleaRIEELEEDLHKLEEALNDLEARLSH------------------- 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1789 ERWQLKANEALRLRlqAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAvRQRELAEQELEKQRQLAEGTAQQRlAA 1868
Cdd:TIGR02169 791 SRIPEIQAELSKLE--EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEIENLNGKKE-EL 866
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1869 EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE- 1947
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEi 946
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1948 -AEAGRFRELAEE----AARLRALAEEAKRQRQLAEEDAARQRAeaervLTEKLAaiseatRLKTEAEiALKEKEAENER 2022
Cdd:TIGR02169 947 pEEELSLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILERIEEYEK 1014
|
970
....*....|
gi 1046896947 2023 LRRLAEDEAF 2032
Cdd:TIGR02169 1015 KKREVFMEAF 1024
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
321-422 |
5.91e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 71.27 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 321 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 400
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1046896947 401 -VDVPQPDEKSIITYVSSLYDAM 422
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
319-419 |
7.56e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 70.87 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 398
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1046896947 399 ED-VDVPQPDEKSIITYVSSLY 419
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
319-416 |
7.73e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.49 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 394
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 1046896947 395 LLDPEDVDVPQPDEKSIITYVS 416
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
187-304 |
8.25e-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: 70.40 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 187 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerDVIRSvrlPREKGRMRfhklQNVQIA 266
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKV 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046896947 267 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 304
Cdd:cd21213 68 LQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2025-2845 |
1.22e-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: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2025 RLAEDEAFQRRRLEEQAA---QHKADIEERLAQLRKASESeLERQKGLVEDTLRQ----RRQVEEeimALKASFEKAAAG 2097
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKETERKLERTREN-LDRLEDILNELERQlkslERQAEK---AERYKELKAELR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2098 KAELELELGRIRSnAEDTMRSKELAEQEAARQRqlaaeeeqrrreaeervqrslaaeEEAARQRKVALEEVERLKAKVEE 2177
Cdd:TIGR02168 224 ELELALLVLRLEE-LREELEELQEELKEAEEEL------------------------EELTAELQELEEKLEELRLEVSE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2178 arrLRERAEQESARQLQLAQEaaQKRLQAEEKAHafvvQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQA 2257
Cdd:TIGR02168 279 ---LEEEIEELQKELYALANE--ISRLEQQKQIL----RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2258 EREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKkfAEQTLRQ 2337
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ--QEIEELL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2338 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALilRDKD 2417
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL--EGFS 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2418 NTQRFLEEEAEKMKQV---------AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQ--------AVQEAT 2480
Cdd:TIGR02168 506 EGVKALLKNQSGLSGIlgvlselisVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGrvtflpldSIKGTE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2481 RLKAEAELLQQQKELAQEQARRLQEDKE------------------QMAQQLVEETQGFQR--TLEAERQR--------- 2531
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddlDNALELAKKLRPGYRivTLDGDLVRpggvitggs 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2532 ------QLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERL 2605
Cdd:TIGR02168 666 aktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2606 REAIAELEREKEKLKQEAKLLQLK-----------SEEMQTVQQ--EQILQETQALQKSFLSEKDSLLQRERFIEQEKAK 2672
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERleeaeeelaeaEAEIEELEAqiEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2673 LEQLfQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQ---EELQRLEQQRQQQEKLLAEENQ 2749
Cdd:TIGR02168 826 LESL-ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASLEEALALLRSELEELSEELR 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2750 RLRERLQRLEEEHRAALAHSEEIATSQAAATKALPNGRDAL---------DGPSMEAEPEYTFEGLRQKVPA--QQLQEA 2818
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeysltleEAEALENKIEDDEEEARRRLKRleNKIKEL 984
|
890 900 910
....*....|....*....|....*....|
gi 1046896947 2819 G---ILSMEELQRLTQGHTTVAEltQREDV 2845
Cdd:TIGR02168 985 GpvnLAAIEEYEELKERYDFLTA--QKEDL 1012
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
180-303 |
1.50e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 70.00 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 180 TDERDrvqKKTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLsgDSLprERDVIRSVRLPREKGRMRFHK 259
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKK 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1046896947 260 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 303
Cdd:cd21219 64 VENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3214-3252 |
1.53e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.35 E-value: 1.53e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 3214 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEMHEKL 3252
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1154-1709 |
1.57e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1154 EACETRTVHRLRLPLDKDPARECAQRIAEQQKA---QAEVEGLGKGVARLSAEAEkvlalpEPSPAAPTLRSELELTLGK 1230
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKKAE------EAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1231 LEQVRslsaiylEKLKTISLVIRSTQGAEEVLKTHEEHLKEAQAVPATLQELEVTKASLKKlRAQAEAQQPVFNTLRDEL 1310
Cdd:PTZ00121 1359 AEAAE-------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1311 RGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQlgrqlryyRESADPLSSWLQDAKSRQEQI 1390
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--------AKKADEAKKKAEEAKKKADEA 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1391 QAVPIANSQAAREQLRQEKALLEEIERHGE--KVEECQKFAKQYinaiKDYELQLITYKAQLEPVASPAKKPKVQSGSES 1468
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1469 VIQEYVDLR----TRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERER--LAEVEAALEKQRQLAEAHAQAKAQ 1542
Cdd:PTZ00121 1579 ALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkVEQLKKKEAEEKKKAEELKKAEEE 1658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1543 AELEARELQRRMQEEvTRREEAAVDAQQQKRSIQEELQhlrqsSEAEIQAKAQQVEAAERSRMRIEEEIRvvrlqlette 1622
Cdd:PTZ00121 1659 NKIKAAEEAKKAEED-KKKAEEAKKAEEDEKKAAEALK-----KEAEEAKKAEELKKKEAEEKKKAEELK---------- 1722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1623 rqrgGAEDElqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElalrvKAEAEAAREKQRALQALDELKLQA 1702
Cdd:PTZ00121 1723 ----KAEEE------NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK-----KEEEKKAEEIRKEKEAVIEEELDE 1787
|
....*..
gi 1046896947 1703 EEAERRL 1709
Cdd:PTZ00121 1788 EDEKRRM 1794
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1482-1901 |
1.67e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 77.47 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1482 ELTTLTSQYI-----------KFISETLRRMEEEERLAEQQRAEERERLAEveaalEKQRQlaeahaqakaQAELEAREL 1550
Cdd:pfam17380 248 DVTTMTPEYTvryngqtmtenEFLNQLLHIVQHQKAVSERQQQEKFEKMEQ-----ERLRQ----------EKEEKAREV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1551 QRRMQ-EEVTRREEAAVDAQqqkrsiqeelqhlrqsseAEIQakaqqveaAERSRMRIEEEIRVVRLQLEttERQRggae 1629
Cdd:pfam17380 313 ERRRKlEEAEKARQAEMDRQ------------------AAIY--------AEQERMAMERERELERIRQE--ERKR---- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1630 dELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEAELALRVK-AEAEAAREKQRALQALDELKLQAEEA-ER 1707
Cdd:pfam17380 361 -ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEEERQRKIQQQKVEMEQIRAEQEEArQR 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1708 RLRQAEAERARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerraqqqaEAERAREEAERE 1787
Cdd:pfam17380 436 EVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE-------------------EERKRKKLELEK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1788 LERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQavrQRELAEQELEKQRQLAE--GTAQQR 1865
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE---RRREAEEERRKQQEMEErrRIQEQM 558
|
410 420 430
....*....|....*....|....*....|....*.
gi 1046896947 1866 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAT 1901
Cdd:pfam17380 559 RKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1570-2211 |
1.91e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 77.70 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1570 QQKRSIQEELQHLRQSSEAEIQAKAQQVEAaersrmRIEEEIRVVRLQLET--TERQRGGAEDELQALRARAEEAEAQKR 1647
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSL------HGKAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1648 QAQEEAERLRRQvqDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEA-ERARQVQVALET 1726
Cdd:TIGR00618 237 QTQQSHAYLTQK--REAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAvTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1727 AQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAE 1806
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1807 EVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA-EGTAQQRLAAEQELIRLR---AETEQG 1882
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAqslKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1883 EQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllaskarAEEESRSTSEKSKQRLEAEAGRFRELAEEAAR 1962
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN--------PARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1963 LRALAEEAKRQRQLAEEDAARQRAEaERVLTEKLAAISE-ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 2041
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEdIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2042 -----AQHKADIEERLAQLRKASES-ELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDT 2115
Cdd:TIGR00618 626 dlqdvRLHLQQCSQELALKLTALHAlQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2116 MRSKELAEQEAARQRQlaaeeeqRRREAEERVQRSLAAEEEAARQRKVALEEVER--LKAKVEEARRLRERA---EQESA 2190
Cdd:TIGR00618 706 LRELETHIEEYDREFN-------EIENASSSLGSDLAAREDALNQSLKELMHQARtvLKARTEAHFNNNEEVtaaLQTGA 778
|
650 660
....*....|....*....|.
gi 1046896947 2191 RQLQLAQEAAQKRLQAEEKAH 2211
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTH 799
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1305-2132 |
2.20e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 77.69 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1305 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQRelEQLGRqlryYRESADPLSSW 1379
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQ--EKIER----YQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1380 LqdaksrQEQIQAVPIANSQAAREQLRQEKAlLEEIER-------HGEKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1451
Cdd:PRK04863 364 L------EEQNEVVEEADEQQEENEARAEAA-EEEVDElksqladYQQALDVQQTRAIQYQQAVQALErAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1452 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERlaeveaALEKQRQ 1531
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR------RLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1532 LAEAHAQAKAQ-AELEARELQRRMQEevtRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEE 1610
Cdd:PRK04863 511 LAEQLQQLRMRlSELEQRLRQQQRAE---RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1611 IrvvrlqletterqrggaeDELQALRARAEEAEAQKRQAQEEAERLRRQVQDE--------SQRKRQAEAELALRVkAEA 1682
Cdd:PRK04863 588 L------------------EQLQARIQRLAARAPAWLAAQDALARLREQSGEEfedsqdvtEYMQQLLERERELTV-ERD 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1683 EAAREKQRALQALDELkLQAEEAERRLRQAEAERARQV-------QVALETA---------QRSAEVELQSKRAsfAEKT 1746
Cdd:PRK04863 649 ELAARKQALDEEIERL-SQPGGSEDPRLNALAERFGGVllseiydDVSLEDApyfsalygpARHAIVVPDLSDA--AEQL 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1747 AQLERTLQEEHVT---VTQLREEAERRAQQQAEAERAREEAERELERWQL------KANEAL--RLRLQAEEVAQQksLA 1815
Cdd:PRK04863 726 AGLEDCPEDLYLIegdPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEvplfgrAAREKRieQLRAEREELAER--YA 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1816 QADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1895
Cdd:PRK04863 804 TLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQLN-------RRRVELERALADHESQEQQQRSQLEQAKEGLSA 876
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1896 L-QHEATAATQKRQELEAELAKVRAEMEvllaskaRAEEESRSTSEKSKQ--RLEAEAGRFRELAEEAARLRALAEEAKR 1972
Cdd:PRK04863 877 LnRLLPRLNLLADETLADRVEEIREQLD-------EAEEAKRFVQQHGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQAQQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1973 QRQlaeedAARQRAEAervLTEklaAISEATRLKTEAEIALKEKEAE-NERLR-RLAEDEAfQRRRLEEQAAQHKADIEE 2050
Cdd:PRK04863 950 TQR-----DAKQQAFA---LTE---VVQRRAHFSYEDAAEMLAKNSDlNEKLRqRLEQAEQ-ERTRAREQLRQAQAQLAQ 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2051 -------------RLAQLRKASESELE----RQKGLVEDTLRQRRqvEEEIMALKASFEKaaagKAELELELGRIRSNAE 2113
Cdd:PRK04863 1018 ynqvlaslkssydAKRQMLQELKQELQdlgvPADSGAEERARARR--DELHARLSANRSR----RNQLEKQLTFCEAEMD 1091
|
890
....*....|....*....
gi 1046896947 2114 DTMRSKELAEQEAARQRQL 2132
Cdd:PRK04863 1092 NLTKKLRKLERDYHEMREQ 1110
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1266-1989 |
2.24e-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: 77.69 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1266 EEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQPVfntlrdeLRGAQEVGERLQQRHGERDVEVERWRervTQLLERW 1345
Cdd:COG3096 333 SDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEV-------VEEAAEQLAEAEARLEAAEEEVDSLK---SQLADYQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1346 QAVlaqtDVRQRE----------LEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIAN------SQAAREQLRQEK 1409
Cdd:COG3096 403 QAL----DVQQTRaiqyqqavqaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELeqklsvADAARRQFEKAY 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1410 ALLEEIERHGEKVEECQKfAKQYINAIKDYELQLitykAQLEPVAspakkpkvqsgsesviQEYVDLRTRYS---ELTTL 1486
Cdd:COG3096 479 ELVCKIAGEVERSQAWQT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRLRqqqNAERL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1487 TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ-AELEARELQ-RRMQEEVTRREEA 1564
Cdd:COG3096 538 LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARiKELAARAPAwLAAQDALERLREQ 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1565 AVDAQQQKRSIQEELQHLrqsSEAEIQAKAQQVEAAERsRMRIEEEIRvvRLQletterQRGGAED-ELQALRAR----- 1638
Cdd:COG3096 618 SGEALADSQEVTAAMQQL---LEREREATVERDELAAR-KQALESQIE--RLS------QPGGAEDpRLLALAERlggvl 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1639 ------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQRKRQaEAELALRVKAE- 1681
Cdd:COG3096 686 lseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVFDAE-ELEDAVVVKLSd 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1682 --------------AEAAREKQralqaLDELKLQAEE-----AERRLRQAEAER---------ARQVQVALETaqrSAEV 1733
Cdd:COG3096 765 rqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvGGHLAVAFAP---DPEA 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1734 ELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRA-------QQQAEAERAREEAERELERWQLKANEALR-LRLQA 1805
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELREELDAAQEAQAfIQQHG 916
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1806 EEVAQQKSLAQA-DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLAAEQELI-RLRAETEQG 1882
Cdd:COG3096 917 KALAQLEPLVAVlQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQA 996
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1883 EQQRQLLEEELARLQHEATAATQKRQELEA-------ELAKVRAEMEVL-LASKARAEEESRSTSEKSKQRLEAEAGRFR 1954
Cdd:COG3096 997 EEARREAREQLRQAQAQYSQYNQVLASLKSsrdakqqTLQELEQELEELgVQADAEAEERARIRRDELHEELSQNRSRRS 1076
|
810 820 830
....*....|....*....|....*....|....*
gi 1046896947 1955 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1989
Cdd:COG3096 1077 QLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
184-300 |
2.72e-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: 69.10 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 184 DRVQKKTFTKWVNKHLIKhwRAEAQrhISDLYEDLRDGHNLISLLEVLSGDSLPRERDVirsvrlpreKGRMRFHKLQNV 263
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKFDL---------EPKNRIQMIQNL 68
|
90 100 110
....*....|....*....|....*....|....*...
gi 1046896947 264 QIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTI 300
Cdd:cd21225 69 HLAMLFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
319-419 |
6.29e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 68.13 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 398
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1046896947 399 ED-VDVPQPDEKSIITYVSSLY 419
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1145-1745 |
1.01e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.34 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1145 ELKDIRLQLEAcETRTVHRLRlpldkdPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1224
Cdd:COG4913 236 DLERAHEALED-AREQIELLE------PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1225 ELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEvlktheEHLKEAqavpatLQELEVTKASLKKLRAQAEAQqpvFN 1304
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLERE------IERLERELEERERRRARLEAL---LA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1305 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLSSWLQDAk 1384
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLAL- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1385 sRQEQIQAVPIANS---------QAAREQLRQEKAlleeIER--HGEKV-----EECQKFAKQYINAIKDyELQLITYKA 1448
Cdd:COG4913 446 -RDALAEALGLDEAelpfvgeliEVRPEEERWRGA----IERvlGGFALtllvpPEHYAAALRWVNRLHL-RGRLVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1449 QLEPVASPAKKPKVQSGSEsviqeyvdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-E 1521
Cdd:COG4913 520 RTGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1522 VEAALEK--QRQLAEAH------AQAKAQAELEARELQRRMQEEVTRREEAAvDAQQQKRSIQEELQHLRQSSEAEIqak 1593
Cdd:COG4913 586 NGTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEI--- 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1594 aqQVEAAERSRMRIEEEIRvvrlQLETterqrggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE 1673
Cdd:COG4913 662 --DVASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 1674 LAlRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEK 1745
Cdd:COG4913 729 LD-ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4468-4506 |
1.39e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.66 E-value: 1.39e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 4468 LLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMVDRI 4506
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
321-420 |
1.53e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 66.59 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 321 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 396
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1046896947 397 DPEDVdVPQPDEKSIITYVSSLYD 420
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3290-3328 |
3.15e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.15e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 3290 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETNRAL 3328
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3545-3583 |
3.41e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.41e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 3545 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3583
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1500-2623 |
3.42e-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: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1500 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHA----QAKAQAEL--EARELQRRMQ------EEVTRREE 1563
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNalqeQLQAETELcaEAEEMRARLAarkqelEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1564 AAVDaQQQKRSIQeeLQHLRQSSEAEIQAKAQQVEAAERSRMrieeeirvvRLQLE--TTERQRGGAEDELQALRARAEE 1641
Cdd:pfam01576 82 SRLE-EEEERSQQ--LQNEKKKMQQHIQDLEEQLDEEEAARQ---------KLQLEkvTTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1642 AEAQKRQAQEEAERLRRQVQDESQRKRQaeaelalrvkaeAEAAREKQRALQALDELKLQAEEAERRlrqaEAERARQVQ 1721
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKS------------LSKLKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1722 VALETAQRSAEVELQskrASFAEKTAQLERtlQEEHVTVTQLreeaerraqqqaeaerareeaerELERWQLKANEALRl 1801
Cdd:pfam01576 214 EGESTDLQEQIAELQ---AQIAELRAQLAK--KEEELQAALA-----------------------RLEEETAQKNNALK- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1802 rlQAEEVAQQKSLAQADAEKQKEeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTaQQRLAAEQELiRLRAETEQ 1881
Cdd:pfam01576 265 --KIRELEAQISELQEDLESERA-----------ARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQEL-RSKREQEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1882 GEQQRQLLEEEL---ARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEAGRfR 1954
Cdd:pfam01576 330 TELKKALEEETRsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlQQAKQDSEHKR-K 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1955 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-------------LTEKLAAIS-----------EATRLKTEAE 2010
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaegknikLSKDVSSLEsqlqdtqellqEETRQKLNLS 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2011 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdieeRLAQLRKASESELERQKGLVEDtlrqRRQVEEEIMALKAS 2090
Cdd:pfam01576 489 TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQ 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2091 FEKAAAGKAELELELGRIRSNAEDTMrskelaeQEAARQRQLAAEEEQRRREAEErvqrsLAAEEEAARQRKVALEEVER 2170
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAE 628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2171 LKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqnmLERLRSEAEAARRAAEEA 2250
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHEL 683
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2251 EEAREQAEREAAQSRKQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalKQKQAADAEMEKHKKf 2330
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR- 745
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2331 aeQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRA 2410
Cdd:pfam01576 746 --QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDE 823
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2411 LILRDKDNTQRFLEEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQ 2490
Cdd:pfam01576 824 ILAQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQ 902
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2491 QQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQrqleMSAEAERLKLRMAEMSRAQ---------------AR 2555
Cdd:pfam01576 903 SNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ----LERQNKELKAKLQEMEGTVkskfkssiaaleakiAQ 978
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2556 AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEA 2623
Cdd:pfam01576 979 LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1835-2051 |
3.67e-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: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1914
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1915 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1990
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1991 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 2051
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
321-416 |
3.92e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 65.49 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 321 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 399
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1046896947 400 DVDVPQPDEKSIITYVS 416
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1330-2039 |
3.99e-12 |
|
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: 73.33 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1330 EVERWRERVtQLLERWQAVLAQTDVRQRELEQLgrqlryyrESAD----PLSSWLQDAKSRQEQIQAVPIANSQAAREQL 1405
Cdd:pfam12128 222 QVEHWIRDI-QAIAGIMKIRPEFTKLQQEFNTL--------ESAElrlsHLHFGYKSDETLIASRQEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1406 RQEKALLEEI--ERHGEKVEECQKFAK--QYINAIKDYELQ-----LITYKAQLEpvaspaKKPKVQSGSESVIQEYVDL 1476
Cdd:pfam12128 293 RTLDDQWKEKrdELNGELSAADAAVAKdrSELEALEDQHGAfldadIETAAADQE------QLPSWQSELENLEERLKAL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1477 RTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEERERlAEVEAALEKQ-RQLAEAHAQAKAQAELEARELQRR 1553
Cdd:pfam12128 367 TGKHQDVTAKYNRRRSKIKEQNNRDIAgiKDKLAKIREARDRQL-AVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1554 MQEEVTRREEAAVDaqqqkrsiQEELQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQ 1633
Cdd:pfam12128 446 LGELKLRLNQATAT--------PELLLQLENFDE-RIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1634 ALRARAEEAEAQ-KRQAQEEAERLRRQVQDESQR-KRQAEAELALRVKAEAEAAREKQRALQALDELKLQ---------- 1701
Cdd:pfam12128 517 ERQSALDELELQlFPQAGTLLHFLRKEAPDWEQSiGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDlkridvpewa 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1702 --AEEAERRLRQAE----AERARQVQVALETAQRSAEVELQSKRASFAektaqlERTLQEEHVTVTQLREEAERRAQQQA 1775
Cdd:pfam12128 597 asEEELRERLDKAEealqSAREKQAAAEEQLVQANGELEKASREETFA------RTALKNARLDLRRLFDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1776 EAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA--------EREARRRGKAEEQAVRQRELA 1847
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvvegaldaQLALLKAAIAARRSGAKAELK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1848 EQELEKQRQLAE-GTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEataATQKRQELEAELAKVRAEMEVLL 1925
Cdd:pfam12128 751 ALETWYKRDLASlGVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQET---WLQRRPRLATQLSNIERAISELQ 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1926 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlaeeakRQRQLAEEDAARQRAEAERVLTEKLAAISEaTRL 2005
Cdd:pfam12128 828 QQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATLKEDANSEQAQGSIGERLAQLED-LKL 900
|
730 740 750
....*....|....*....|....*....|....*....
gi 1046896947 2006 KTEAEIALKEKEAEN-----ERLRRLAEDEAFQRRRLEE 2039
Cdd:pfam12128 901 KRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2886-2924 |
6.06e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 6.06e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 2886 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2924
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1583-2209 |
6.68e-12 |
|
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: 72.56 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1583 RQSSEAEIQAKAQQVEA--AERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAE----RL 1656
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1657 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVeLQ 1736
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1737 SKRASFAEKTAQLERTLQEEHVT-VTQLREEAERRAQQQAEAERAREEAERELE---RWQLKAN------EALRLRLQAE 1806
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALEselREQLEAGklefneEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1807 EVAQQKSLAQADAEK--QKEEAEREARRRGKAEEQAVRQRELAEQELekqrqlaegtAQQRLAAEQELIRLRAETEQGEQ 1884
Cdd:pfam12128 448 ELKLRLNQATATPELllQLENFDERIERAREEQEAANAEVERLQSEL----------RQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1885 QRQLLEEelARLQHEATAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAE 1958
Cdd:pfam12128 518 RQSALDE--LELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1959 EAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE 2038
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2039 EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEE--------IMALKASFEKAAAGKAELELELGRiRS 2110
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqaywqvvEGALDAQLALLKAAIAARRSGAKA-EL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2111 NAEDTMRSKELAEQEAARQR--QLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQE 2188
Cdd:pfam12128 750 KALETWYKRDLASLGVDPDViaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQ 829
|
650 660
....*....|....*....|.
gi 1046896947 2189 SARQlqlaQEAAQKRLQAEEK 2209
Cdd:pfam12128 830 LARL----IADTKLRRAKLEM 846
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
189-307 |
7.20e-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: 65.33 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 189 KTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsVRLPREKGRMRFHKLQNVQIALD 268
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVDWSR-----VNKPFKKLGANMKKIENCNYAVE 76
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046896947 269 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 307
Cdd:cd21298 77 LGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4123-4161 |
7.67e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.67e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 4123 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4161
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
321-421 |
7.80e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 64.68 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 321 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 400
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1046896947 401 VdVPQPDEKSIITYVSSLYDA 421
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3956-3994 |
8.54e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 8.54e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 3956 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3994
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
206-301 |
9.53e-12 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 64.54 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 206 EAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSVRLPRekgrmrfhKLQNVQIALDYLRHRQV----KLVNIR 281
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQ--------KLHNVEVALKALKEAGVlrggDGGGIT 92
|
90 100
....*....|....*....|
gi 1046896947 282 NDDIADGNPKLTLGLIWTII 301
Cdd:cd21223 93 AKDIVDGHREKTLALLWRII 112
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1611-1993 |
9.56e-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: 71.69 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1611 IRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKrqaqeEAERlRRQVQdESQRKRQAEAELALRVKAEAE-AAREKQ 1689
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR-----EVER-RRKLE-EAEKARQAEMDRQAAIYAEQErMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1690 RALQaldelKLQAEEAERrlrqaEAERARQVQVALETaQRSAEVElqskrasfaekTAQLERTLQEEHVtvtqlreeaer 1769
Cdd:pfam17380 348 RELE-----RIRQEERKR-----ELERIRQEEIAMEI-SRMRELE-----------RLQMERQQKNERV----------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1770 rAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEvAQQKSLAQADAEKQKeeaerearrrgkaEEQAVRQRELA-E 1848
Cdd:pfam17380 395 -RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE-ARQREVRRLEEERAR-------------EMERVRLEEQErQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1849 QELEKQRQLAEGTAQQRLAAEQE-LIRLRAEteqgEQQRQLLEEELARLQHEATAATQKRQELEAELAKvRAEMEVLLAS 1927
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEkRDRKRAE----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEE-RQKAIYEEER 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1928 KARAEEESRSTSEKSKQRLEAEagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLT 1993
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQE--QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPIT 598
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1876-2192 |
1.17e-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: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1876 RAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAElAKVRAEMEVLLASKARAEEESRSTSEKSkqrlEAEAGRFRE 1955
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEERKR----ELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1956 LAEEAARLRALaEEAKRQRQLAEEdAARQRAEAERV--LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA-- 2031
Cdd:pfam17380 370 IAMEISRMREL-ERLQMERQQKNE-RVRQELEAARKvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAre 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2032 FQRRRLEEQAAQHKAdieERLAQlrkaSESELERQKGLVEDTLRQRRQVEEEimaLKASFEKAAAGKAELELELGRIRSN 2111
Cdd:pfam17380 448 MERVRLEEQERQQQV---ERLRQ----QEEERKRKKLELEKEKRDRKRAEEQ---RRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2112 AEDTMRSKELAEQEAARQRQlaaeeeqrrREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESAR 2191
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE---------AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
.
gi 1046896947 2192 Q 2192
Cdd:pfam17380 589 A 589
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1810-2019 |
1.56e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 69.84 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1810 QQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAegtaQQRLAAeQELIRLRAETEQGEQQRQLL 1889
Cdd:PRK09510 68 QQQQKSAKRAEEQRKK---------KEQQQAEELQQKQAAEQERLKQLE----KERLAA-QEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1890 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1969
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAE---AKKKAEAEAAKKAAAEAKKKAEAEA---AAKAAAEAKKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1970 AKRQRQLAEEDAARQ-RAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 2019
Cdd:PRK09510 208 KKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1849-2212 |
2.22e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1849 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH--EATAATQKRQELEAELAKVRAEMEVLLA 1926
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1927 S--------------KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERvL 1992
Cdd:COG4717 154 RleelreleeeleelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ-L 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1993 TEKLAAISEATRLKTEAEIAL--------------------------------------------KEKEAENERLRRLAE 2028
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllarekASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2029 DEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEIMALKASFEKAAAGKAElelelgR 2107
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------E 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2108 IRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAE-EEAARQRKVALEEVERLKAKVEEAR-RLRERA 2185
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLE 466
|
410 420
....*....|....*....|....*..
gi 1046896947 2186 EQESARQLQLAQEAAQKRLQAEEKAHA 2212
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEWA 493
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1482-2076 |
2.25e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 70.55 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1482 ELTTLTSQYIKFIS---ETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQ---AELEARELQRRMQ 1555
Cdd:pfam07111 56 EGSQALSQQAELISrqlQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEglrAALAGAEMVRKNL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1556 EEVTRREeaavdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSrmrieeeirvvrlqLETTERQRGGAEDELQal 1635
Cdd:pfam07111 135 EEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQLA-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1636 raraeeaeaqkrQAQEEAERLRRQVqdeSQRKRQAEAELALrvkaeAEAAReKQRALQALDELKLQAEEAERRLRQAEAE 1715
Cdd:pfam07111 194 ------------EAQKEAELLRKQL---SKTQEELEAQVTL-----VESLR-KYVGEQVPPEVHSQTWELERQELLDTMQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1716 RARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLreeaerraqqqaeaeraREEAERELERWQLKA 1795
Cdd:pfam07111 253 HLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEF-----------------PKKCRSLLNRWREKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1796 NeALRLRLQAEEVAQQKSLAQADAEkqkeEAEREARRRGKAEEQAVRQRELAEQ--ELEKQRQLAEGTAQQRLAAEQELI 1873
Cdd:pfam07111 316 F-ALMVQLKAQDLEHRDSVKQLRGQ----VAELQEQVTSQSQEQAILQRALQDKaaEVEVERMSAKGLQMELSRAQEARR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1874 RLRAETEQGEQQRQL------------------LEEELAR---LQHEATAATQKRQELEA------ELAKVRAE------ 1920
Cdd:pfam07111 391 RQQQQTASAEEQLKFvvnamsstqiwlettmtrVEQAVARipsLSNRLSYAVRKVHTIKGlmarkvALAQLRQEscpppp 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1921 ------MEVLLASKARAEEESRSTSE--KSKQRLEAEAGRFRELAE-EAARLRALAEEAKRQRQLAEEDAARQRAEAERV 1991
Cdd:pfam07111 471 pappvdADLSLELEQLREERNRLDAElqLSAHLIQQEVGRAREQGEaERQQLSEVAQQLEQELQRAQESLASVGQQLEVA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1992 LTEKLAAISEATRLKTE----AEI---ALKEKEAENErlRRLAEDEAFQRRRLEEQAAQH-KADIEERLAQLRKASESEL 2063
Cdd:pfam07111 551 RQGQQESTEEAASLRQEltqqQEIygqALQEKVAEVE--TRLREQLSDTKRRLNEARREQaKAVVSLRQIQHRATQEKER 628
|
650
....*....|...
gi 1046896947 2064 ERQKGLVEDTLRQ 2076
Cdd:pfam07111 629 NQELRRLQDEARK 641
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1511-2041 |
2.33e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 70.66 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1511 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAR----ELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSS 1586
Cdd:COG3899 713 RRALARGAYAEALRYLERALELLPPDPEEEYRLALLLElaeaLYLAGRFEEAEALLERALAARALAALAALRHGNPPASA 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1587 EAEIQAKAQQVEAAERSRMRIEEEIRVV-RLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERL--RRQVQDE 1663
Cdd:COG3899 793 RAYANLGLLLLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLA 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1664 SQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFA 1743
Cdd:COG3899 873 LAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAA 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1744 EKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQK 1823
Cdd:COG3899 953 ALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAA 1032
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1824 EEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAA 1903
Cdd:COG3899 1033 AAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALA 1112
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1904 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR 1983
Cdd:COG3899 1113 ALALAAALAALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAA 1186
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1984 QRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 2041
Cdd:COG3899 1187 AAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1873-2679 |
2.90e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.38 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1873 IRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1950
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1951 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdE 2030
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2031 AFQRRRLEEQAAQHKADIEERLAQLRKASESELERQkglvedtlrQRRQVEEeimalkasfeKAAAGKAELELELGRIRS 2110
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2111 NAEdtMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESA 2190
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2191 RQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEE 2270
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2271 AERLKQSAEEQAQAQAQAQAAAEKlRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRL 2350
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2351 QLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLkARIEAENRALILRDKDNTQRFLEEEAEKM 2430
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2431 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQR----ALAEKMLKEKMQAVQEATRLKAEAELLQ---QQKELAQEQ-ARR 2502
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQLT-LTQERvrehALSIRVLPKELLASRQLALQKMQSEKEQltyWKEMLAQCQtLLR 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2503 LQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlKLRMAEMSRAQARAEEDAQRFrkqaeeigEKLHRTELATQ 2582
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK-ELMHQARTVLKARTEAHFNNN--------EEVTAALQTGA 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2583 EKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKL--LQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLL 2660
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLqcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
810
....*....|....*....
gi 1046896947 2661 QRERFIEQEKAKLEQLFQD 2679
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLSDK 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1990-2726 |
6.43e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1990 RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaaqhKADIEERLAQLRKASESELERQKGL 2069
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2070 VEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAED-TMRSKELAEQEAARQRQLAAEEEQRRREAEERVQ 2148
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2149 RSLAAEEEAARQRKVALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAA---------QKRLQAEEKAHAFVVQQRE 2219
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAelkeeledlRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2220 EELQQTLQQEQNMLERLRSEaeaarraaeeaeeareqaereaaqsRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEa 2299
Cdd:TIGR02169 389 DYREKLEKLKREINELKREL-------------------------DRLQEELQRLSEELADLNAAIAGIEAKINELEEE- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2300 eqeaarraqaeqaalkqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAE---VTEA 2376
Cdd:TIGR02169 443 -----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraSEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2377 ARQRSQVEEELFS----VRVQMEELGKLKAR------IEAENR--ALILRDKDNTQR---FLEEEA---------EKMKQ 2432
Cdd:TIGR02169 506 VRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2433 VAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAEA 2486
Cdd:TIGR02169 586 ERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2487 ELLQQQKElaqEQARRLQEDKEQMAQQLveetQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2566
Cdd:TIGR02169 666 ILFSRSEP---AELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2567 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELER-----------------EKEKLKQEAKLLQLK 2629
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiqaelsklEEEVSRIEARLREIE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2630 SEEMQTVQQEQILQ-ETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQQQQMEQEKQELVAS 2708
Cdd:TIGR02169 819 QKLNRLTLEKEYLEkEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
810
....*....|....*...
gi 1046896947 2709 MEEARRRQREAEEGVRRK 2726
Cdd:TIGR02169 898 LRELERKIEELEAQIEKK 915
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1805-2187 |
6.57e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1805 AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQ 1884
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1885 QRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR 1964
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1965 ALAEEAKRQRQLAEE----DAARQRAEAERV--LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAF------ 2032
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRierlee 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2033 QRRRLEEQAAQHKADIEE---RLAQLRKAS---ESELERQKglvEDTLRQRRQVEEEIMALKASFEKAAAGKAELElELG 2106
Cdd:PRK02224 517 RREDLEELIAERRETIEEkreRAEELRERAaelEAEAEEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2107 RIRS------NAEDTM-----RSKELAEQEAARQRQLaaeeeqrrreaeervqrslaaeeEAARQRKVALEEvERLKAKV 2175
Cdd:PRK02224 593 RIRTllaaiaDAEDEIerlreKREALAELNDERRERL-----------------------AEKRERKRELEA-EFDEARI 648
|
410
....*....|..
gi 1046896947 2176 EEARRLRERAEQ 2187
Cdd:PRK02224 649 EEAREDKERAEE 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1494-1965 |
6.91e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1494 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaqakaqaelEARELqrrmqeevtrREEAAVDaqqqkr 1573
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE-----------RAEEL----------REEAAEL------ 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1574 siqeelqhlrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEaqkrqaQEEA 1653
Cdd:PRK02224 369 -------------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR------EREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1654 ErLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARqVQVALETAQRSAEV 1733
Cdd:PRK02224 430 E-LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEE-VEERLERAEDLVEA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1734 E-----LQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQaeaerareeaerelERWQLKANEAlrlRLQAEEV 1808
Cdd:PRK02224 508 EdrierLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA--------------EEKREAAAEA---EEEAEEA 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1809 AQqkslAQADAEKQKEEAEREARRRGKAEEQAVRqRELAEQEL----EKQRQLAEGTAQQR--LAAEQELIRLRAET--- 1879
Cdd:PRK02224 571 RE----EVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIerlrEKREALAELNDERRerLAEKRERKRELEAEfde 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1880 ---EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlaskaRAEEESRSTSEKSKQRLEAEAGRFREL 1956
Cdd:PRK02224 646 ariEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL-----EELRERREALENRVEALEALYDEAEEL 720
|
....*....
gi 1046896947 1957 AEEAARLRA 1965
Cdd:PRK02224 721 ESMYGDLRA 729
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1470-1968 |
7.58e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.22 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1470 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaqakaqaelearE 1549
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLV--------------E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1550 LQRRMQEEVTRREEAAVDAQQQKrsiqeelQHLRQSSEAEIQAKA--QQVEAAERSRMRIEEEIRVVRLQLEtterqrgg 1627
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEEADE-------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1628 aedelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQR----------KRQAEAELAlRVKA-------EAEAAREKQR 1690
Cdd:PRK04863 377 ----------QQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALE-RAKQlcglpdlTADNAEDWLE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1691 ALQA-LDELKLQAEEAERRLRQAEAERaRQVQVALETAQR-SAEVElqskRASFAEKTAQLERTLQEEHVTVTQLreeae 1768
Cdd:PRK04863 446 EFQAkEQEATEELLSLEQKLSVAQAAH-SQFEQAYQLVRKiAGEVS----RSEAWDVARELLRRLREQRHLAEQL----- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1769 rraqqqaeaerareeaerelerwqlkanEALRLRLQAeevAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAE 1848
Cdd:PRK04863 516 ----------------------------QQLRMRLSE---LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1849 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQHEATAATQKRQELEAELAKvraemevlL 1925
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------L 636
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1046896947 1926 ASKARAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1968
Cdd:PRK04863 637 LERERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2315-2517 |
8.97e-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: 67.10 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2394
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2395 EEL----------GKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAL 2464
Cdd:COG4942 107 AELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2465 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2517
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1633-2029 |
9.67e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.83 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1633 QALRARAEEAEAQKRQA--QEEAERLRRQVQDESQRKRQAEAELA-----LRVKAEAEAAREK-QRALQALDELKLQAEE 1704
Cdd:PRK04863 287 EALELRRELYTSRRQLAaeQYRLVEMARELAELNEAESDLEQDYQaasdhLNLVQTALRQQEKiERYQADLEELEERLEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1705 A--------------ERRLRQAEAERAR------QVQVALETAQRSAEVELQSKRAsfAEKTAQLertLQEEHVTVTQLR 1764
Cdd:PRK04863 367 QnevveeadeqqeenEARAEAAEEEVDElksqlaDYQQALDVQQTRAIQYQQAVQA--LERAKQL---CGLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1765 EEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEevaQQKSLAQADAEKQKEEAEREARRRG---------- 1834
Cdd:PRK04863 442 DW---------------------LEEFQAKEQEATEELLSLE---QKLSVAQAAHSQFEQAYQLVRKIAGevsrseawdv 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 --KAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAAtqkRQELEA 1912
Cdd:PRK04863 498 arELLRRLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR---LESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1913 ELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVL 1992
Cdd:PRK04863 573 SVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE-YMQQLLEREREL 643
|
410 420 430
....*....|....*....|....*....|....*...
gi 1046896947 1993 TEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAED 2029
Cdd:PRK04863 644 TVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1271-1763 |
9.86e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1271 EAQAVPATLQELEVTKASLKKLRAQAEAQQPV------FNTLRDELRGAQEVGERLQQRHGERdvEVERWRERVTQLLER 1344
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1345 WQAVLAQTDVRQRELEQLGRQLRYYREsadplsswlqdaksrqeqiqavpiansQAAREQLRQEKALLEEIERHGEKVEE 1424
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEA---------------------------QIRGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1425 CQKFAKQYINAIKDYELQLITYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSELT------------------ 1484
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDLRrelreleaeiaslerrks 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1485 TLTSQYIKF---ISETLRRMEEEER-LAE--QQRAEERE-RLAeVEAALEKQRQ--LAEAHAQAKAQAELEARELQRRMQ 1555
Cdd:COG4913 437 NIPARLLALrdaLAEALGLDEAELPfVGEliEVRPEEERwRGA-IERVLGGFALtlLVPPEHYAAALRWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1556 -EEVTRREEAAVDAQQQKRSIQEEL------------QHLRQSSEAEIQAKAQQVEAAERS------------RMRIEEE 1610
Cdd:COG4913 516 yERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawleAELGRRFDYVCVDSPEELRRHPRAitragqvkgngtRHEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1611 IRVVRLQL--ETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR-VKAEAEAARE 1687
Cdd:COG4913 596 RRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1688 KQRALQA----LDELKLQAEEAERRLRQAEAERArqvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQL 1763
Cdd:COG4913 676 ELERLDAssddLAALEEQLEELEAELEELEEELD-----ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1810-2005 |
1.07e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 67.14 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1810 QQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1889
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1890 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1969
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 1046896947 1970 AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRL 2005
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1513-2001 |
1.79e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.06 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1513 AEERERLaeVEAALEKQRQLAEAHAQ-AKAQAELE--ARELqrrmqEEVTRREEAAVDAQQQKRsiqeelQHLrqsseAE 1589
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQlAEEQYRLVemAREL-----EELSARESDLEQDYQAAS------DHL-----NL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1590 IQAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEDELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrKRQ 1669
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1670 AEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVElqSKRASFAEKTAQL 1749
Cdd:COG3096 404 ALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD--AARRQFEKAYELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1750 ERTLQEehvtvtqlreeaerraqqqaeaerareeaERELERWQlKANEALR----LRLQAEEVAQ-QKSLAQAdaekqke 1824
Cdd:COG3096 482 CKIAGE-----------------------------VERSQAWQ-TARELLRryrsQQALAQRLQQlRAQLAEL------- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1825 eaerearrrgkaeEQAVRQRELAEQELEkqrQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQHEATAAT 1904
Cdd:COG3096 525 -------------EQRLRQQQNAERLLE---EFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1905 QKRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR 1974
Cdd:COG3096 585 QQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
490 500
....*....|....*....|....*..
gi 1046896947 1975 QLAEEDAARQRAEAERVLTEKLAAISE 2001
Cdd:COG3096 665 QPGGAEDPRLLALAERLGGVLLSEIYD 691
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1510-2131 |
2.14e-10 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 67.52 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1510 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQeevtrreeAAVDAQQQKRSIQEELQHLRQSSEAE 1589
Cdd:PRK10246 219 QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ--------ALQQALAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1590 I-----QAKAQQVEAAERSRMRIEEEirVVRLQLETTERQ--RGGAEDELQALRA------------------RAEEA-- 1642
Cdd:PRK10246 291 QlrphwERIQEQSAALAHTRQQIEEV--NTRLQSTMALRAriRHHAAKQSAELQAqqqslntwlaehdrfrqwNNELAgw 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1643 EAQKRQAQEEAERLRRQVQ--DESQRKRQAEAELALRVKA-EAEAAREKQRALQALDE--LKLQAEEAERRLRQAEAERA 1717
Cdd:PRK10246 369 RAQFSQQTSDREQLRQWQQqlTHAEQKLNALPAITLTLTAdEVAAALAQHAEQRPLRQrlVALHGQIVPQQKRLAQLQVA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1718 RQvqvALETAQRSAEVELQSKRASFAEKTAQLE--RTLQEEHVTVTQLREEAERRAQQQAEAE--RAREEAERELERWQL 1793
Cdd:PRK10246 449 IQ---NVTQEQTQRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQALEP 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1794 KANEALRLRLQaEEVAQQKS-----LAQADAEKQKEEaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAA 1868
Cdd:PRK10246 526 GVNQSRLDALE-KEVKKLGEegaalRGQLDALTKQLQ---------RDESEAQSLRQ-EEQALTQQWQAVCASLNITLQP 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1869 EQELIRLRAETEQGEQQRQLLEEELArLQHEATAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKS 1942
Cdd:PRK10246 595 QDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1943 KQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLTEKLAAISEATrLKTEAEIALKEKEAENER 2022
Cdd:PRK10246 674 AQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2023 lRRLAE-----DEAFQRRRLEEQAAQHKADIEE----RLAQLRKASESELERQKGLVE---DTLRQRRQVEEEIMALKAS 2090
Cdd:PRK10246 745 -QRLQKaqaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVTqtaQALAQHQQHRPDGLDLTVT 823
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1046896947 2091 FEKAAAGKAELELELgrirsnAEDTMRSKELAEQ----EAARQRQ 2131
Cdd:PRK10246 824 VEQIQQELAQLAQQL------RENTTRQGEIRQQlkqdADNRQQQ 862
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4544-4582 |
2.15e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.49 E-value: 2.15e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 4544 FLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTAQKL 4582
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1077-1697 |
2.49e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1077 EEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLV----AEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQ 1152
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1153 LEacetrtvhrlrlpldkdparecaQRIAEQqkaqaeveglgkGVARLSAeaekvlalpepspaaptLRSELELTLGKLE 1232
Cdd:COG4913 328 LE-----------------------AQIRGN------------GGDRLEQ-----------------LEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1233 QVRSLSAIYLEKLKTISLVIRSTqgAEEVLKTHEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQqpvFNTLRDELrg 1312
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPAS--AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE---LRELEAEI-- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1313 aqevgERLQQRHGERDVEVERWRERVTQLL--------------------ERWQAVLaqtdvrQRELEQLGRQL----RY 1368
Cdd:COG4913 429 -----ASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeERWRGAI------ERVLGGFALTLlvppEH 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1369 YREsadpLSSWLQDAKSRQE-QIQAVPIANSQAAREQLrQEKALLEEIERhgeKVEECQKFAKQYINAIKDYELqlityk 1447
Cdd:COG4913 498 YAA----ALRWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLDF---KPHPFRAWLEAELGRRFDYVC------ 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1448 aqlepVASPAkkpkvqsgsesviqeyvDLRtRYSELTTLTSQyIKFiSETLRRMEEEERL---------AEQQRAEERER 1518
Cdd:COG4913 564 -----VDSPE-----------------ELR-RHPRAITRAGQ-VKG-NGTRHEKDDRRRIrsryvlgfdNRAKLAALEAE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1519 LAEVEAALEKQRQLAEAHAQAKAQaeLEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKAQQVE 1598
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDA--LQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1599 AAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEE--AERLRRQVQDESQRKRQAEAElAL 1676
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERELRENLE-ER 774
|
650 660
....*....|....*....|.
gi 1046896947 1677 RVKAEAEAAREKQRALQALDE 1697
Cdd:COG4913 775 IDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1532-1756 |
4.38e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1532 LAEAHAQAKAQAELEARelQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEI 1611
Cdd:COG4942 12 ALAAAAQADAAAEAEAE--LEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1612 RVVRLQLETTERQRGGAEDELQALRARAEEAEAQKR-------QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1684
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 1685 AREKQRALQALDELKLQAEEAERRLRQAEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1756
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
182-298 |
4.54e-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: 60.13 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 182 ERDRvQKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSgdslPRERDVIRSVRLPREKGRMRFHKLQ 261
Cdd:cd21300 4 EGER-EARVFTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDKVI----PGSVNWKKVNKAPASAEISRFKAVE 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 262 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 298
Cdd:cd21300 72 NTNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
188-301 |
4.60e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 59.89 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 188 KKTFTKWVNKHL-----IKHWRAEAQRHiSDLYEDLRDGHNLISLLEVLSGDSLPrerdvIRSVRLPREKGRmrFHKLQN 262
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDG-DDLFEALRDGVLLCKLINKIVPGTID-----ERKLNKKKPKNI--FEATEN 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046896947 263 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 301
Cdd:cd21217 75 LNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1498-1714 |
4.62e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1498 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQE 1577
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1578 ---ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAE 1654
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 1655 RLRRQVqdesQRKRQAEAELALRVKAEAEAAREKQRALQALDEL--KLQAEEAERRLRQAEA 1714
Cdd:COG4942 189 ALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1257-1753 |
4.98e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1257 GAEEVLKTHEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELrgAQEVGERLQQRHGERDVEVERWRE 1336
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1337 RVTQLLER--------WQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQE 1408
Cdd:COG4913 317 RLDALREEldeleaqiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1409 KALLEEIErhgekveecqkfakqyiNAIKDYELQLITYKAQLEPVAspAKKPKVQSGSESVIQEYVDLRTRYSELTTLTS 1488
Cdd:COG4913 397 EEELEALE-----------------EALAEAEAALRDLRRELRELE--AEIASLERRKSNIPARLLALRDALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1489 QYIKFISETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAELEAR 1548
Cdd:COG4913 458 AELPFVGELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1549 ELQRRM-----------QEEVTRREEAA-VDAQQQ----KRSIQEELQ--------------HLRQ------SSEAEIQA 1592
Cdd:COG4913 535 SLAGKLdfkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1593 KAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGG---------AEDELQALRARAEEAEAQKRQAQE---EAERLRRQV 1660
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDAssdDLAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1661 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQV--QVALETAQRSAEVELQSK 1738
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEER 774
|
570
....*....|....*
gi 1046896947 1739 RASFAEKTAQLERTL 1753
Cdd:COG4913 775 IDALRARLNRAEEEL 789
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1482-1699 |
5.47e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 65.28 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1482 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAELEA 1547
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1548 RELQRRMQEEVTRRE-EAAVDAQQQKRSIQEELQhlrqsseAEIQAKAQQVEAAERSRMRIEEEirvvrlqLETTERQRg 1626
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANAEREVQRQ-------LEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 1627 gAEDELQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELK 1699
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1508-1719 |
5.77e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1508 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEevtrREEAAVDAQQQKRSIQEEL-------Q 1580
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA----LARRIRALEQELAALEAELaelekeiA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1581 HLRQSSEAEIQAKAQQVEAAERSRMR-----------IEEEIRVVRLQLETTERQRggaeDELQALRARAEEAEAQKRQA 1649
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARR----EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1650 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQ 1719
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1489-2128 |
6.71e-10 |
|
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: 65.91 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1489 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDA 1568
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1569 QQQKRSIQEELQHLRQ---SSEAEIQA-KAQQVEAAERSRMRIEEEIRVVRLQLetteRQRGGA--------EDELQALR 1636
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHF----RSLGSAiskilrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1637 AR----AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEAELAlRVKAEAEAAREKQRALQAldelklQAEEAERRLRQ 1711
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1712 AEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQlreeaerraqqqaeaerareeaeRELERW 1791
Cdd:pfam15921 311 QNSMYMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE-----------------------ARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1792 QLKANEA-LRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRqRELAEQELEKQRQLA---------EGT 1861
Cdd:pfam15921 367 QFSQESGnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR-RELDDRNMEVQRLEAllkamksecQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1862 AQQRLAAEQ----ELIRLRAETEQGEQQRQLLEEELARLqheataaTQKRQELEAELAKVrAEMEVLLASKARAEEESRS 1937
Cdd:pfam15921 446 MERQMAAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1938 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLTEKLAAISEATRL-KTEAEI 2011
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLEK 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2012 ALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASESELERQKGL--VEDTLRQRRQVEEEIM 2085
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDYE 677
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2086 ALKASF----EKAAAGKAELELELGRIRSNAE---DTMRSKELAEQEAAR 2128
Cdd:pfam15921 678 VLKRNFrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMK 727
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1364-1979 |
8.67e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1364 RQLRYYRESADPLSSWLQDAKSRQEQIQAvpIANSQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDY---- 1439
Cdd:PRK03918 111 SSVREWVERLIPYHVFLNAIYIRQGEIDA--ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikrt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1440 ---ELQLITYKAQLEPVASPAKK-----PKVQSGSESVIQEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEERLAEQQ 1511
Cdd:PRK03918 189 eniEELIKEKEKELEEVLREINEisselPELREELEKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEER 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1512 RAEERERLAEVEaalEKQRQLAEAHAQAKAQAEL-----------------------EARELQRRMqEEVTRREEAAVDA 1568
Cdd:PRK03918 268 IEELKKEIEELE---EKVKELKELKEKAEEYIKLsefyeeyldelreiekrlsrleeEINGIEERI-KELEEKEERLEEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1569 QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQ 1648
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1649 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAarEKQRALQALDELKLQAEEAERRLRQAEAERARQ--VQVALET 1726
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKEL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1727 AQ--RSAEVELQSKRASFAEKTAQLERTLQEEHVTVT--------------QLREEAERRAQQQAEAERAREEAERELER 1790
Cdd:PRK03918 502 AEqlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeikslkkelekleELKKKLAELEKKLDELEEELAELLKELEE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1791 WQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQ 1870
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEE 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1871 ELIRLRAETEQgeqqrqlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlaSKARAEEESrstSEKSKQRLEAEA 1950
Cdd:PRK03918 660 EYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER--EKAKKELEK---LEKALERVEELR 727
|
650 660
....*....|....*....|....*....
gi 1046896947 1951 GRFRELAEEAARlRALAEEAKRQRQLAEE 1979
Cdd:PRK03918 728 EKVKKYKALLKE-RALSKVGEIASEIFEE 755
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1843-2716 |
9.01e-10 |
|
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: 65.58 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1843 QRELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAe 1920
Cdd:pfam01576 109 EEQLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1921 MEVLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervLTEKLAAIS 2000
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2001 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRrrleEQAAQHKADIEErlaqlrkasesELERQKGLVEDTLRQRRQV 2080
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGE-----------ELEALKTELEDTLDTTAAQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2081 EEEimalkasfekaaagKAELELELGRIRSNAEDTMRSKELAEQEAaRQRQLaaeeeqrrreaeervqrslAAEEEAARQ 2160
Cdd:pfam01576 319 QEL--------------RSKREQEVTELKKALEEETRSHEAQLQEM-RQKHT-------------------QALEELTEQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2161 rkvaLEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFV--VQQREEELQQTLQQEQNMLERLRS 2238
Cdd:pfam01576 365 ----LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLqeLQARLSESERQRAELAEKLSKLQS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2239 EAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQ 2318
Cdd:pfam01576 441 ELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2319 AADAEMEKHKKFAEQTL-------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAA----RQRSQVEeel 2387
Cdd:pfam01576 521 TLQAQLSDMKKKLEEDAgtlealeEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldHQRQLVS--- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2388 fsvrvQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKmkqvAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEK 2467
Cdd:pfam01576 598 -----NLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK----ETRALSLARALEEALEAKEELERTNKQLRAEMED 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2468 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqEDKEQMAQ----QLVEETQG----FQRTLEA------ERQRQL 2533
Cdd:pfam01576 669 LVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEEL-EDELQATEdaklRLEVNMQAlkaqFERDLQArdeqgeEKRRQL 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2534 -----EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKlhRTELATQEKVTLVQTLEIQRQQSDQDAERLREA 2608
Cdd:pfam01576 748 vkqvrELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEIL 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2609 IAELEREKEKLKQEAKLLQLKSE----EMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 2684
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDlaasERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNT 905
|
890 900 910
....*....|....*....|....*....|..
gi 1046896947 2685 KQLQEEQQRQQQQMEQEKQELVASMEEARRRQ 2716
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQLTTELAAERSTSQKSE 937
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4466-4503 |
1.28e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 55.95 E-value: 1.28e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1046896947 4466 QRLLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMV 4503
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1577-1951 |
1.37e-09 |
|
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: 64.15 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1577 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETT----ERQRGGAEDELQALRARAEEAEAQKRQAQEE 1652
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1653 AERL---RRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALDELKLQAEEAERRLRQAEAERaRQVQVALETAQ- 1728
Cdd:pfam07888 110 SEELseeKDALLAQRAAHEARIRELEEDIKTLTQRVLERE---TELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1729 --RSAEVELQSKRASFAEKTAQLERtLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKAnEALRLRLqaE 1806
Cdd:pfam07888 186 elRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV-EGLGEEL--S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1807 EVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1886
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1887 QLLEEELARlqhEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1951
Cdd:pfam07888 342 EKLEVELGR---EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1591-1823 |
1.38e-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: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1591 QAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1670
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1671 EAELALRVKAEAEAAREKQRA-LQALDELKLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1748
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1749 LERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQKSLAQADAEKQK 1823
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1527-1748 |
1.48e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 63.67 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1527 EKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEaavdaQQQKRSIQEELQhlRQSSEAEIQAKAQQVEAAERsrmr 1606
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ-----LEKERLAAQEQK--KQAEEAAKQAALKQKQAEEA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1607 ieeeirvvrlQLETTERQRGGAEDELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEAELALRVKAEAEAA 1685
Cdd:PRK09510 138 ----------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 1686 REKQRALQAldelklqAEEAErrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1748
Cdd:PRK09510 203 AEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1623-2161 |
1.89e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 64.49 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1623 RQRGGAEDELQALRaRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQA 1702
Cdd:COG3899 716 LARGAYAEALRYLE-RALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARA 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1703 EEAERRLRQAEAERARQV-QVALETAQRSAEVELQskrasfaektAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAR 1781
Cdd:COG3899 795 YANLGLLLLGDYEEAYEFgELALALAERLGDRRLE----------ARALFNLGFILHWLGPLREALELLREALEAGLETG 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1782 EEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGT 1861
Cdd:COG3899 865 DAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAA 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1862 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1941
Cdd:COG3899 945 LAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAAL 1024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1942 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENE 2021
Cdd:COG3899 1025 AALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAA 1104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2022 RLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAEL 2101
Cdd:COG3899 1105 LALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLA 1184
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2102 ELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR 2161
Cdd:COG3899 1185 AAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1499-1732 |
1.92e-09 |
|
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: 62.63 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1499 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKrsIQEE 1578
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER--IQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1579 LQHLRQSSEAEIQAKAQQVEAAERSRMRI---------EEEIRVVRLQLETTERQRggAEDELQALRARAEEAEAQKRQA 1649
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1650 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQR 1729
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
...
gi 1046896947 1730 SAE 1732
Cdd:pfam13868 272 EDE 274
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1524-1756 |
1.96e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 64.20 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1524 AALEKQRQLAEAHAQAKAQaeLEARelQRRMQEEVTRREE-----AAVDAQQQKRSIQEELQHLR--QSSEAEIQAKAQQ 1596
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKAR--FEAR--QARLEREKAAREArhkkaAEARAAKDKDAVAAALARVKakKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1597 VEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL 1676
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKA 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1677 RVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEE 1756
Cdd:PRK05035 592 KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK-ARKAAQQQANAEPE 670
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1259-1749 |
2.49e-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: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1259 EEVLKTHEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQpvfnTLRDELRGAQEVGERL--QQRHGERDVEVERWRE 1336
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT----SIREISCQQHTLTQHIhtLQQQKTTLTQKLQSLC 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1337 RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIE 1416
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1417 RHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyI 1491
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-R 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1492 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQ 1571
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1572 K----------------------------RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTER 1623
Cdd:TIGR00618 639 QelalkltalhalqltltqervrehalsiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDR 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1624 QRggaEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAE 1703
Cdd:TIGR00618 719 EF---NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1046896947 1704 EAERRLRQAEAE---RARQVQVALETAQRSAEVELQSKRASFAEKTAQL 1749
Cdd:TIGR00618 796 EDTHLLKTLEAEigqEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATL 844
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1538-2774 |
2.54e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.04 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1538 QAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQhlrqsSEAEIQAKAqqveaaersrmrieEEIRVvRLQ 1617
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEA--------------EEMRA-RLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1618 LETTErqrggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEAElalrvkaeaEAAREKqralqalde 1697
Cdd:pfam01576 68 ARKQE-----LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEE---------EAARQK--------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1698 LKLQAEEAERRLRQAEAErarqvqVALETAQRSaevELQSKRASFAEKTAQLERTLQEEHVTV---TQLREEAERRAQQQ 1774
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEED------ILLLEDQNS---KLSKERKLLEERISEFTSNLAEEEEKAkslSKLKNKHEAMISDL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1775 AEAERAREEAERELERWQLKAN--------EALRLRLQAEEVAQQksLAQADAEKQkeeaereaRRRGKAEEQAVRQREL 1846
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKLEgestdlqeQIAELQAQIAELRAQ--LAKKEEELQ--------AALARLEEETAQKNNA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1847 AEQELEKQRQLAEgtAQQRLAAEqelirlRAETEQGEQQRQLLEEELARLQHEA-----TAATQkrQELEAelakvRAEM 1921
Cdd:pfam01576 263 LKKIRELEAQISE--LQEDLESE------RAARNKAEKQRRDLGEELEALKTELedtldTTAAQ--QELRS-----KREQ 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1922 EVLLASKArAEEESRSTSEKSKQRLEAEAGRFRELAEEAarlralaEEAKRQRQLAEEdaARQRAEAERV-LTEKLAAIS 2000
Cdd:pfam01576 328 EVTELKKA-LEEETRSHEAQLQEMRQKHTQALEELTEQL-------EQAKRNKANLEK--AKQALESENAeLQAELRTLQ 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2001 EAtrlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE-------------RLAQLRKASESELERQK 2067
Cdd:pfam01576 398 QA---KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESvssllneaegkniKLSKDVSSLESQLQDTQ 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2068 GLVEDTLRQR-------RQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTmrsKELAEQEAARQRQLAAEEEQrr 2140
Cdd:pfam01576 475 ELLQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM---KKKLEEDAGTLEALEEGKKR-- 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2141 reaeervqrsLAAEEEAARQRkvaLEEVERLKAKVEEAR-RLRERAE-----QESARQLQLAQEAAQKR---LQAEEKA- 2210
Cdd:pfam01576 550 ----------LQRELEALTQQ---LEEKAAAYDKLEKTKnRLQQELDdllvdLDHQRQLVSNLEKKQKKfdqMLAEEKAi 616
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2211 HAFVVQQREEELQQTLQQEQNMLERLRSEAEAarraaeeaeeareqaereaaqsRKQVEEAERLKQSAEEQAQAQAQAQA 2290
Cdd:pfam01576 617 SARYAEERDRAEAEAREKETRALSLARALEEA----------------------LEAKEELERTNKQLRAEMEDLVSSKD 674
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2291 AAEKLRKEAEQEAARRAQAEQAALKQKQAADAEM---EKHKKFAEQTLRQ-KAQVEQELTTLRLQLEEtdhQKSILDEEL 2366
Cdd:pfam01576 675 DVGKNVHELERSKRALEQQVEEMKTQLEELEDELqatEDAKLRLEVNMQAlKAQFERDLQARDEQGEE---KRRQLVKQV 751
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2367 QRLKAEVTEAARQRSQveeeLFSVRVQME-ELGKLKARIEAENRAlilRDkdntqrfleeeaEKMKQVAEEAARLSVAAQ 2445
Cdd:pfam01576 752 RELEAELEDERKQRAQ----AVAAKKKLElDLKELEAQIDAANKG---RE------------EAVKQLKKLQAQMKDLQR 812
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2446 EAARLRQLAEEDLAQQRAlAEKMLKekmqavqeatrlKAEAELLQQQKELA-QEQARR-LQEDKEQMAQQLVEETQGfqR 2523
Cdd:pfam01576 813 ELEEARASRDEILAQSKE-SEKKLK------------NLEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--K 877
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2524 TLEAERQRQLEmsaeaERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDQDAE 2603
Cdd:pfam01576 878 SALQDEKRRLE-----ARIAQLEEELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNK 948
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2604 RLREAIAELERE-KEKLKQEAKLLQLKSEEMQtvqqEQILQETQALQKSflsekdsllqrERFIEQEKAKLEQLfqdeva 2682
Cdd:pfam01576 949 ELKAKLQEMEGTvKSKFKSSIAALEAKIAQLE----EQLEQESRERQAA-----------NKLVRRTEKKLKEV------ 1007
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2683 kakqlqeeqqrqqqqmeqekqelVASMEEARRRQreaeEGVRRKQEELQRLEQQRQQQEKLLAEENQRL---RERLQR-L 2758
Cdd:pfam01576 1008 -----------------------LLQVEDERRHA----DQYKDQAEKGNSRMKQLKRQLEEAEEEASRAnaaRRKLQReL 1060
|
1290
....*....|....*.
gi 1046896947 2759 EEEHRAALAHSEEIAT 2774
Cdd:pfam01576 1061 DDATESNESMNREVST 1076
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1492-1734 |
2.63e-09 |
|
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: 62.24 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1492 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQ 1571
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1572 KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEDELQALRARAEEaEAQKRQAQE 1651
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE----LRAKLYQEEQERKERQKEREEAEKKARQ-RQELQQARE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1652 EAERLRRQVQDESQRKRQAEAELALRVKAEAE------AAREKQRALQALDELKLQAEEAER-RLRQAEAERARQVQVAL 1724
Cdd:pfam13868 243 EQIELKERRLAEEAEREEEEFERMLRKQAEDEeieqeeAEKRRMKRLEHRRELEKQIEEREEqRAAEREEELEEGERLRE 322
|
250
....*....|
gi 1046896947 1725 ETAQRSAEVE 1734
Cdd:pfam13868 323 EEAERRERIE 332
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1259-1449 |
2.72e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.54 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1259 EEVLKTHEEHLKEAQaVPATLQELEVTKASLKKLRAQAEAQQPVFNTLrdelrgaQEVGERLQQRHGERDVEVerwRERV 1338
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1339 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLSSWLQDAKSRQEQIQavPIANSQAAREQLRQEKALLEEIERH 1418
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 1046896947 1419 GEKVEECQKFAKQYINAIKDYELQLITYKAQ 1449
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
679-868 |
2.85e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.54 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 679 LRYLHDLLAWVEENQRRIDGAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQLSPATRGAY---RDCLGRLD 755
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 756 LQYAKLLNSSKARLRSLE---SLHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEI 832
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1046896947 833 QNTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 868
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1808-2042 |
2.88e-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: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1808 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1887
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1888 LLEEELARLQHEAtaatqKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRAL 1966
Cdd:COG4942 94 ELRAELEAQKEEL-----AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1967 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 2042
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1846-2077 |
4.09e-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: 61.79 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1846 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAelakvraemevll 1925
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1926 askARAEEESRSTSEKSKQRLEAEAGRfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAERvlteklaAISEATRL 2005
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAEAK-------KKAEEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 2006 KTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE----ERLAQLRKASESELERQKGLVEDTLRQR 2077
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1885-2216 |
4.11e-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: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1885 QRQLLEEELARLQHEATAATQKRQEL--EAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRlEAEAGRFRELAEEAAR 1962
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKE----EKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1963 LralaeEAKRQRQLAEEDAARQRAEAERVLTEKLAAisEATRLKtEAEIALKEKEAENERLRRlaEDEAFQRRRLEEQAA 2042
Cdd:pfam17380 342 M-----AMERERELERIRQEERKRELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQ--ELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2043 QHKADIEER-LAQLRKASESELERQ-KGLVEDTLRQRRQVEEEIMalkasfekaaagkaELELELGRIRSNAEDTMRSKE 2120
Cdd:pfam17380 412 QRKIQQQKVeMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQ--------------ERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2121 LAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEeaaRQRKVALEEVE-RLKAKVEEARR------LRERAEQESARQL 2193
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE---RKRKLLEKEMEeRQKAIYEEERRreaeeeRRKQQEMEERRRI 554
|
330 340
....*....|....*....|....*.
gi 1046896947 2194 QLAQEAA---QKRLQAEEKAHAFVVQ 2216
Cdd:pfam17380 555 QEQMRKAteeRSRLEAMEREREMMRQ 580
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1258-2038 |
4.22e-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: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1258 AEEVLKTHEEHLKEAQAvpatlqELEVTKASLKKLRAQ-AEAQQP--VFNTLRDELRGAQEVGERLQQRHGERDVEVERW 1334
Cdd:COG3096 366 QEEVVEEAAEQLAEAEA------RLEAAEEEVDSLKSQlADYQQAldVQQTRAIQYQQAVQALEKARALCGLPDLTPENA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1335 RERvtqlLERWQAVLAQTDVRQRELEQ---LGRQLRYYRESADPLSSWLQDAKSR-------QEQIQAVPIANSQAAR-E 1403
Cdd:COG3096 440 EDY----LAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERsqawqtaRELLRRYRSQQALAQRlQ 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1404 QLRQEKALLEEIERHGEKVEE-----CQKFAKQYINAIkDYELQLITYKAQLEPVAspAKKPKVQSGSESVIQEYVDLRT 1478
Cdd:COG3096 516 QLRAQLAELEQRLRQQQNAERlleefCQRIGQQLDAAE-ELEELLAELEAQLEELE--EQAAEAVEQRSELRQQLEQLRA 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1479 RYSELTTLTSQYIKfISETLRRMEEE---------------ERLAEQQRA--EERERLAEVEAALEKQ------------ 1529
Cdd:COG3096 593 RIKELAARAPAWLA-AQDALERLREQsgealadsqevtaamQQLLEREREatVERDELAARKQALESQierlsqpggaed 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1530 ---RQLAEA-----------------------------HAQAKAQAELEARELQRR---------MQEEVTRREEAAVDA 1568
Cdd:COG3096 672 prlLALAERlggvllseiyddvtledapyfsalygparHAIVVPDLSAVKEQLAGLedcpedlylIEGDPDSFDDSVFDA 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1569 QQQKRSI--QEELQHLRQSSEAEI-----QAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDEL-----QALR 1636
Cdd:COG3096 752 EELEDAVvvKLSDRQWRYSRFPEVplfgrAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVgghlaVAFA 831
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1637 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAeaelalrvkaeAEAAREKQRALQAL---------DELKLQAEEAER 1707
Cdd:COG3096 832 PDPEAELAALRQRRSELERELAQHRAQEQQLRQQ-----------LDQLKEQLQLLNKLlpqanlladETLADRLEELRE 900
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1708 RLRQAEAERA--RQVQVALETAQRSAEVeLQSKRASFAEKTAQLERTLQEEHVTVTQLreeaerraqqqaeaerareeae 1785
Cdd:COG3096 901 ELDAAQEAQAfiQQHGKALAQLEPLVAV-LQSDPEQFEQLQADYLQAKEQQRRLKQQI---------------------- 957
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1786 relerwqlkanEALrlrlqaEEVAQQKS-LAQADAEKQkeeaereaRRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQ 1863
Cdd:COG3096 958 -----------FAL------SEVVQRRPhFSYEDAVGL--------LGENSDLNEKLRARlEQAEEARREAREQLRQAQA 1012
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1864 QRLAAEQELIRLRAETEQGEQQRQLLEEELA----RLQHEATA-ATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1938
Cdd:COG3096 1013 QYSQYNQVLASLKSSRDAKQQTLQELEQELEelgvQADAEAEErARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1939 SEKSKQrLEAEAGRFRELAEEA----ARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKlaaiseatrlkteAEIALK 2014
Cdd:COG3096 1093 QKRLRK-AERDYKQEREQVVQAkagwCAVLRLARDNDVERRLHRRELAYLSADELRSMSDK-------------ALGALR 1158
|
890 900
....*....|....*....|....*..
gi 1046896947 2015 EKEAENERLR---RLAEDEAFQRRRLE 2038
Cdd:COG3096 1159 LAVADNEHLRdalRLSEDPRRPERKVQ 1185
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
319-421 |
4.28e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.39 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 319 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 397
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1046896947 398 PEDVDVPQPDEKSIITYVSSLYDA 421
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1305-2130 |
4.40e-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: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1305 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQREleQLGRqlryYRESADPLSSW 1379
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1380 LQdaksrqEQIQAVPIANSQAAREQLRQEKALlEEIERHG-------EKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1451
Cdd:COG3096 363 LE------EQEEVVEEAAEQLAEAEARLEAAE-EEVDSLKsqladyqQALDVQQTRAIQYQQAVQALEkARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1452 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIsETLRRMEEE-ERLAEQQRAEER-ERLAEVEAALEK- 1528
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEvERSQAWQTARELlRRYRSQQALAQRl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1529 ---QRQLAEAHAQAKAQAELE--ARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAER- 1602
Cdd:COG3096 515 qqlRAQLAELEQRLRQQQNAErlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARi 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1603 SRMRIEEEI-RVVRLQLETTERQRGGAEDELQALRA-------RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1674
Cdd:COG3096 595 KELAARAPAwLAAQDALERLREQSGEALADSQEVTAamqqlleREREATVERDELAARKQALESQIERLSQPGGAEDPRL 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1675 A--------------------------------LR---VKAEAEAAREKQRAL--------------QALDELKLQAEEA 1705
Cdd:COG3096 675 LalaerlggvllseiyddvtledapyfsalygpARhaiVVPDLSAVKEQLAGLedcpedlyliegdpDSFDDSVFDAEEL 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1706 ERRL------RQAEAER----------ARQVQVALETAQRSAEVELQSKRASFAEKtaqLERTLQEEHVTVTQlreeaer 1769
Cdd:COG3096 755 EDAVvvklsdRQWRYSRfpevplfgraAREKRLEELRAERDELAEQYAKASFDVQK---LQRLHQAFSQFVGG------- 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1770 raqqqAEAERAREEAERELERWQLKANEALR-LRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAE 1848
Cdd:COG3096 825 -----HLAVAFAPDPEAELAALRQRRSELEReLAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELR 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1849 QELEKQRQLAEGTAQQRLAAEQ---ELIRLRAETEQGEQqrqlleeelarLQHEATAATQKRQELEAE---LAKVRAEME 1922
Cdd:COG3096 900 EELDAAQEAQAFIQQHGKALAQlepLVAVLQSDPEQFEQ-----------LQADYLQAKEQQRRLKQQifaLSEVVQRRP 968
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1923 VLLASKARAE-EESRSTSEKSKQRLEAeagrfrelaeeaarlralAEEAKRQRQLAEEDAARQRAEAERVLTeklaaiSE 2001
Cdd:COG3096 969 HFSYEDAVGLlGENSDLNEKLRARLEQ------------------AEEARREAREQLRQAQAQYSQYNQVLA------SL 1024
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2002 ATRLKTEAEIaLKEKEAENERLRRLAEDEAfqrrrlEEQAAQHKADIEERLAQLRkASESELERQKGLVE---DTLRQR- 2077
Cdd:COG3096 1025 KSSRDAKQQT-LQELEQELEELGVQADAEA------EERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSLQKRl 1096
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2078 RQVEEEIMALKASFEKAAAGKAELeLELGRiRSNAEDTMRSKELAEQEAARQR 2130
Cdd:COG3096 1097 RKAERDYKQEREQVVQAKAGWCAV-LRLAR-DNDVERRLHRRELAYLSADELR 1147
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1402-1691 |
5.03e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.83 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1402 REQLRQEKA-LLEEIERHgEKVEECQKFAKQYINA----IKDYELQLITYKAQLEPVASPAKKPKVQsgsesviqeyvdl 1476
Cdd:pfam17380 298 QERLRQEKEeKAREVERR-RKLEEAEKARQAEMDRqaaiYAEQERMAMERERELERIRQEERKRELE------------- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1477 RTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELqRRMQE 1556
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV-RRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1557 EVTR-----REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQV-----------EAAERSRMRIEEEIRVVRLQLET 1620
Cdd:pfam17380 443 ERARemervRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkilekELEERKQAMIEEERKRKLLEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1621 TERQRGGAEDElqalRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRA 1691
Cdd:pfam17380 523 EERQKAIYEEE----RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1371-2188 |
5.53e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.14 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1371 ESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKalleeierhGEKVEECQ---KFAKQYINAIKDYELQLITYK 1447
Cdd:TIGR00606 160 DSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQ---------GQKVQEHQmelKYLKQYKEKACEIRDQITSKE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1448 AQLEPVASPAKK------------PKVQSGSESVIQ---EYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQR 1512
Cdd:TIGR00606 231 AQLESSREIVKSyeneldplknrlKEIEHNLSKIMKldnEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1513 A----EERERLAEVEAALEKQRQLAEAHAQAKAqaELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEA 1588
Cdd:TIGR00606 311 QrtvrEKERELVDCQRELEKLNKERRLLNQEKT--ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1589 EIQAKaqqveaaersrmrieeeiRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1668
Cdd:TIGR00606 389 ERQIK------------------NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1669 QAEAELALRVKAEAEAAREKQRALQALDELKlqaeEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1748
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILELDQELR----KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1749 LER---------TLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERW-QLKANEALRLRLQAEEVaqQKSLAQAD 1818
Cdd:TIGR00606 527 LNHhtttrtqmeMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAKL--NKELASLE 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1819 AEKQKEEAerearrrgkaeeqavRQRELAEQELEKQRQLAEGTAQQrlAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1898
Cdd:TIGR00606 605 QNKNHINN---------------ELESKEEQLSSYEDKLFDVCGSQ--DEESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1899 EATAATQKRQ----------ELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1968
Cdd:TIGR00606 668 FITQLTDENQsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1969 EAKRQRQLAEEDAARQR---AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAE----------DEAFQRR 2035
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKndiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQqaaklqgsdlDRTVQQV 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2036 RLEEQAAQHKAD------------IEERLAQLR--KASESELERQKGLVEDTLRQRRQVEE-------EIMALKASFEKA 2094
Cdd:TIGR00606 828 NQEKQEKQHELDtvvskielnrklIQDQQEQIQhlKSKTNELKSEKLQIGTNLQRRQQFEEqlvelstEVQSLIREIKDA 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2095 AAGKAELELELGRIRSNAEDTMRSKELAEQEAarQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 2174
Cdd:TIGR00606 908 KEQDSPLETFLEKDQQEKEELISSKETSNKKA--QDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQ 985
|
890
....*....|....
gi 1046896947 2175 VEEARRLRERAEQE 2188
Cdd:TIGR00606 986 LEECEKHQEKINED 999
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
314-416 |
6.59e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 314 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 392
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1046896947 393 TRLLDPEDVDVPQPDEKSIITYVS 416
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2431-2651 |
7.59e-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: 61.32 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2431 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQED 2506
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARriraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2507 KEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2586
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2587 LVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKS 2651
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1499-1760 |
8.37e-09 |
|
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: 61.21 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1499 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTR--REEAAVDAQQQKRSIQ 1576
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1577 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrlqletterqRGGAEDELQALRARAEEAEaQKRQAQEEAERL 1656
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1657 RRQVQDESQR-KRQA-EAELALRVKAEAEAARE--KQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1732
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 1046896947 1733 VELQSKRASFAEKTAQLERTLQEEHVTV 1760
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
323-418 |
8.74e-09 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.93 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 323 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 378
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 379 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 418
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1840-2212 |
1.23e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1840 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEATAATQK----RQ 1908
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1909 ELEAELAKVRAEMEVLLA---SKARAEEESRSTSEKSK----------QRLEAE---AGRFR------ELAEEAARLRAL 1966
Cdd:COG3096 355 DLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEVDslksqladyqQALDVQqtrAIQYQqavqalEKARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1967 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERlrrlaeDEAFQR-RRLEEQAAQHK 2045
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER------SQAWQTaRELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2046 AdIEERLAQLRkASESELERQkglvedtLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQE 2125
Cdd:COG3096 509 A-LAQRLQQLR-AQLAELEQR-------LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2126 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQ 2205
Cdd:COG3096 580 RSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
....*..
gi 1046896947 2206 AEEKAHA 2212
Cdd:COG3096 660 IERLSQP 666
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1535-1990 |
1.45e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.57 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1535 AHAQAKAQAELEARELQRRMQEEVTRReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVV 1614
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1615 RLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA 1694
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1695 LDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQ 1774
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1775 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1854
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1855 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1934
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1935 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1990
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAA 927
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1683-2186 |
1.55e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1683 EAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvtq 1762
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1763 lreeaerraqqqaeaerareeaereLERW-QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRgKAEEQAV 1841
Cdd:COG4717 145 -------------------------PERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE-EELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1842 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEM 1921
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1922 EVLLASKARAeeeSRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISE 2001
Cdd:COG4717 279 LFLVLGLLAL---LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2002 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR-R 2078
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2079 QVEEEIMALKASFEKAAAGKAELELELgrirsnaEDTMRSKELAEQEAARQRQLAAeeeqrrreaeervqrsLAAEEEAA 2158
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAEL-------EQLEEDGELAELLQELEELKAE----------------LRELAEEW 492
|
490 500 510
....*....|....*....|....*....|
gi 1046896947 2159 RQRKVALEEVERLKAKVEEAR--RLRERAE 2186
Cdd:COG4717 493 AALKLALELLEEAREEYREERlpPVLERAS 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1112-1717 |
1.56e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1112 EREYGSCSRHYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETRtVHRLRLPLDKDPARECAQRIAEQQKAQAEVE 1191
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEE---ELEKLTEEISELEKR-LEEIEQLLEELNKKIKDLGEEEQLRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1192 GLGKGVARL-SAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSlsAIYLEKLKTISLvirsTQGAEEVLKTHEEHLK 1270
Cdd:TIGR02169 298 ELEAEIASLeRSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER--EIEEERKRRDKL----TEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1271 EAQAVPATLQElevTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLA 1350
Cdd:TIGR02169 372 ELEEVDKEFAE---TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1351 QTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQ---AVPIANSQAAREQLRQEKALLEEIERHGEKV----- 1422
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtva 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1423 --------------------------------EECQKFAKQY---------INAIK---------------DYELQLITY 1446
Cdd:TIGR02169 529 qlgsvgeryataievaagnrlnnvvveddavaKEAIELLKRRkagratflpLNKMRderrdlsilsedgviGFAVDLVEF 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1447 KAQLEPVASPA-------------------------------KKPKVQSGSESVIQEYVDLRTRYSELTTLtSQYIKFIS 1495
Cdd:TIGR02169 609 DPKYEPAFKYVfgdtlvvedieaarrlmgkyrmvtlegelfeKSGAMTGGSRAPRGGILFSRSEPAELQRL-RERLEGLK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1496 ETLRRMEEEERLAEQQRAEERERLAEVEAALE----KQRQLAEAHAQAKAQAELEARELQRRMQE-EVTRREEAAVDA-- 1568
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEiENVKSELKELEAri 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1569 ---QQQKRSIQEELQHLRQS-SEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEA 1644
Cdd:TIGR02169 768 eelEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1645 QK---RQAQEEAERLRRQVQDESQRKRQAEAELALR---VKAEAEAAREKQRALQ-ALDELKLQAEEAERRLRQAEAERA 1717
Cdd:TIGR02169 848 QIksiEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELErKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1499-1706 |
1.59e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.21 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1499 RRMEEEERLAEQQRAEERErlaEVEAALEKQRQLAEAHAQAkaqaelearelqrrmQEEVTRREEAAVDAQQQKRsiQEE 1578
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQ---KQAAEQERLKQLEKERLAA---------------QEQKKQAEEAAKQAALKQK--QAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1579 LQHLRQSSEAEIQAKAQQVEAAERSRmRIEEEIRvVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERlrr 1658
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK--- 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1046896947 1659 qVQDESQRKRQAEAELAL-RVKAEAEAAREKQRALQALDELKLQAEEAE 1706
Cdd:PRK09510 211 -AAAEAKKKAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1867-2676 |
1.63e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1867 AAEQELIRLRAETEQGEQQRQLLEEElaRLQHEataatqKRQELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRL 1946
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRRE--REKAE------RYQALLKEKREYEGY---ELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1947 EAEAGRFRELAEE-----AARLRALAEEAKRQRQLAEEDAARQRAEAERVlteklaaisEATRLKTEAEIALKEKEAEnE 2021
Cdd:TIGR02169 250 EEELEKLTEEISElekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGEL---------EAEIASLERSIAEKERELE-D 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2022 RLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESELERQKglVEDTLRQRrqVEEEIMALKASFEKAAAGKAEL 2101
Cdd:TIGR02169 320 AEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE--ELEDLRAE--LEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2102 ELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvalEEVERLKAKVEEARRl 2181
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE----WKLEQLAADLSKYEQ- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2182 RERAEQESARQLQLAQEAAQKRLqAEEKAHAFVVQQREEELQQTLQqeqnMLERLRSEAEAARRAAEEAEEAREQAEREA 2261
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQREL-AEAEAQARASEERVRGGRAVEE----VLKASIQGVHGTVAQLGSVGERYATAIEVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2262 AQSRKQ--VEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAqaeqaaLKQKQAADAEM------EKHKKFAEQ 2333
Cdd:TIGR02169 545 AGNRLNnvVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSI------LSEDGVIGFAVdlvefdPKYEPAFKY 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2334 TLRQKAQVEQELTTLRLQLEetdHQKSILDEELQRLKAEVTEAARQRS-------QVEEELFSVRVQMEELGKLKARIEA 2406
Cdd:TIGR02169 619 VFGDTLVVEDIEAARRLMGK---YRMVTLEGELFEKSGAMTGGSRAPRggilfsrSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2407 ENRALILRDKDNTQRFLEEEaekmKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmqavQEATRLkaEA 2486
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK----SELKEL--EA 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2487 ELLQQQKELAQEQARrLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlklrmAEMSRAQARAEEDAQRFRKQ 2566
Cdd:TIGR02169 766 RIEELEEDLHKLEEA-LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-----KLNRLTLEKEYLEKEIQELQ 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2567 AEEIGEKLHRTELATQekvtlVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQ------ 2640
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKE-----IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqiek 914
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1046896947 2641 ------ILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQL 2676
Cdd:TIGR02169 915 krkrlsELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV 956
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1204-1756 |
1.64e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1204 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEHLKEaqaVPATLQELE 1283
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1284 VTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLqqrhgerdveverwrERVTQLLERWQAVLAQTDVRQRELEQLG 1363
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---------------SRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1364 RQLRYYRESADPLSSW---LQDAKSRQEQIqavpiansqaarEQLRQEKALL--EEIERHGEKVEECQKFAKQYINAIKD 1438
Cdd:PRK03918 345 KKLKELEKRLEELEERhelYEEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1439 YELQLITYKAQLEPVASPAKKPKVQ---SGSESVIQEYVDLRTRYSElttltsqYIKFISETLRRMEEEERlaeqqraEE 1515
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1516 RERLAEVEAALEKQRQLAEAHAQAKAQAELEaRELQRRMQEEVTRREEAAvdaqqqkRSIQEELQHLrqssEAEIQAKAQ 1595
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEY-------EKLKEKLIKL----KGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1596 QVEAAErsrmRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1675
Cdd:PRK03918 547 ELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1676 lRVKAEAEAAREK-QRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERtLQ 1754
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK-LK 700
|
..
gi 1046896947 1755 EE 1756
Cdd:PRK03918 701 EE 702
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1174-1758 |
1.67e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.51 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1174 RECAQRIAEQQKAQAEVEGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEQVRslsaiyleklktislvir 1253
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------------ELEELLAELEAQL------------------ 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1254 stqgaeevlKTHEEHLKEAQAVPATL-QELEVTKASLKKLRAQAEA---QQPVFNTLRDE----LRGAQEVGERLQQR-H 1324
Cdd:COG3096 567 ---------EELEEQAAEAVEQRSELrQQLEQLRARIKELAARAPAwlaAQDALERLREQsgeaLADSQEVTAAMQQLlE 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1325 GERDVEVER-----WRERVTQLLERWQAVLAQTDVRQREL-EQLGRQLryYRESADPLSswLQDAK--------SRqeqi 1390
Cdd:COG3096 638 REREATVERdelaaRKQALESQIERLSQPGGAEDPRLLALaERLGGVL--LSEIYDDVT--LEDAPyfsalygpAR---- 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1391 QAVPIANSQAAREQLRQEKALLEE---IERH----GEKVEECQKFAKQYINAIKDYELQLITYKAqlEPV----ASPAKK 1459
Cdd:COG3096 710 HAIVVPDLSAVKEQLAGLEDCPEDlylIEGDpdsfDDSVFDAEELEDAVVVKLSDRQWRYSRFPE--VPLfgraAREKRL 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1460 PKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQR----QLAEA 1535
Cdd:COG3096 788 EELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRaqeqQLRQQ 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1536 HAQAKAQAELEARELQRRM-------QEEVTRREEAAVDAQQQKRSIQEELQHLR---------QSSEAEIQAKAQQVEA 1599
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQANlladetlADRLEELREELDAAQEAQAFIQQHGKALAqleplvavlQSDPEQFEQLQADYLQ 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1600 AERSRMRIEEEI--------RVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR----- 1666
Cdd:COG3096 946 AKEQQRRLKQQIfalsevvqRRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVlaslk 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1667 -----KRQAEAEL-----ALRVKAEAEAArekQRALQALDELKLQAEEAERRLRQAEAERARQvqvaletaqrSAEVELQ 1736
Cdd:COG3096 1026 ssrdaKQQTLQELeqeleELGVQADAEAE---ERARIRRDELHEELSQNRSRRSQLEKQLTRC----------EAEMDSL 1092
|
650 660
....*....|....*....|..
gi 1046896947 1737 SKRASFAEKTAQLERTLQEEHV 1758
Cdd:COG3096 1093 QKRLRKAERDYKQEREQVVQAK 1114
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1909-2773 |
1.88e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1909 ELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRleaeaGRFRELAEEAARLRALAEEaKRQRQLAEEDAARQRAEA 1988
Cdd:TIGR02169 167 EFDRKKEKALEELEEV---EENIERLDLIIDEKRQQL-----ERLRREREKAERYQALLKE-KREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1989 ERVLTEKlaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRL-EEQAAQHKADIEErlaqlrkaSESELERQK 2067
Cdd:TIGR02169 238 QKEAIER--QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGE--------LEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2068 GLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTM-RSKELAEQEAARQRQLAAEEEqrrreaeer 2146
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTeEYAELKEELEDLRAELEEVDK--------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2147 vqrSLAAEEEAARQRKVALEEVERLKAKVE-EARRLRERAEQESARQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQ 2224
Cdd:TIGR02169 379 ---EFAETRDELKDYREKLEKLKREINELKrELDRLQEELQRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2225 TLQQEQNMLERLRSEAEAARRAAEEAEEAREqaereaaQSRKQVEEAERLKQSAEEQAQAQAqaqaaaeklrkeaeqeaa 2304
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELS-------KLQRELAEAEAQARASEERVRGGR------------------ 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2305 rraqaeqaalkqkqAADAEMEKHKKFAEQTLRQKAQVEQELTTL-------RLQL----EETDHQKSIldEELQRLKA-E 2372
Cdd:TIGR02169 511 --------------AVEEVLKASIQGVHGTVAQLGSVGERYATAievaagnRLNNvvveDDAVAKEAI--ELLKRRKAgR 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2373 VTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENR-----ALILRDKDNTQRfLEEEAEKMKQV-------------- 2433
Cdd:TIGR02169 575 ATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTLVVED-IEAARRLMGKYrmvtlegelfeksg 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2434 ------AEEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2498
Cdd:TIGR02169 654 amtggsRAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2499 QARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTE 2578
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2579 LATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMqtvqqEQILQETQALQKSfLSEKDS 2658
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-----EEELEELEAALRD-LESRLG 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2659 LLQRERfiEQEKAKLEQLfQDEVAKAKqlqeeqqRQQQQMEQEKQELVASMEEARRRQREAEEGVRRkqeelQRLEQQRQ 2738
Cdd:TIGR02169 886 DLKKER--DELEAQLREL-ERKIEELE-------AQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-----DEEIPEEE 950
|
890 900 910
....*....|....*....|....*....|....*
gi 1046896947 2739 QQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIA 2773
Cdd:TIGR02169 951 LSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
314-421 |
2.01e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.10 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 314 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 392
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1046896947 393 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 421
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1496-1718 |
2.34e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.47 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1496 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQkr 1573
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1574 siqeelQHLRQSSEAEIQAKAQQveaaersrmrieeeirvvrlqlettERQRGGAEDELQALRARAEEAEAQKRQAQEE- 1652
Cdd:TIGR02794 146 ------EEAAKQAEEEAKAKAAA-------------------------EAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 1653 ---AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERAR 1718
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2415-2750 |
2.52e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.52 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2415 DKDNTQRFLEEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaEAELLQQQKE 2494
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------QAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2495 LAQEQARRLQEDKEQmaqqlveetqgfQRTLEAERQRQLEMSAEAERlklrMAEMSRAQARAEEDAQRFRKQAEEIGE-K 2573
Cdd:pfam17380 342 MAMERERELERIRQE------------ERKRELERIRQEEIAMEISR----MRELERLQMERQQKNERVRQELEAARKvK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2574 LHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAkllQLKSEEMQTVQQEQILQETQALQKSFL 2653
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE---QERQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2654 SEKDSLL--QRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVAsmEEARRRQREAEEGVR------- 2724
Cdd:pfam17380 483 KRDRKRAeeQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA--EEERRKQQEMEERRRiqeqmrk 560
|
330 340
....*....|....*....|....*...
gi 1046896947 2725 --RKQEELQRLEQQRQQQEKLLAEENQR 2750
Cdd:pfam17380 561 atEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1630-2089 |
2.63e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1630 DELQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEAELALrvkAEAEAAREKQRALQALDELKLQAEEAERRL 1709
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL------EELEEELEELEAEL---EELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1710 RQaEAERARQVQVALEtAQRSAEVELQSKRASFAEKTAQLERTLQeehvtvtQLREEAERRAQQQAEAERAREEAERELE 1789
Cdd:COG4717 142 AE-LPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLE-------QLSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1790 RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG--------- 1860
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallfll 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1861 TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstsE 1940
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---E 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1941 KSKQRLEAEAGrfrelAEEAARLRALAEEAKRQRQLAEEdaarqRAEAERVLTEKLAAISEATRLKTEAEIalkekEAEN 2020
Cdd:COG4717 370 QEIAALLAEAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEEL-----EEEL 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 2021 ERLRRLAEDEAFQRRRLEEQaaqhKADIEERLAQLrkASESELERQKGLVEDTLRQRRQVEEEIMALKA 2089
Cdd:COG4717 435 EELEEELEELEEELEELREE----LAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1259-1918 |
2.78e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.57 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1259 EEVLKTHEEHLKE-----AQAVPATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVER 1333
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1334 WRERVTQ-------LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKS-RQEQIQAvPIANSQAAReQL 1405
Cdd:pfam01576 417 LQARLSEserqraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQElLQEETRQ-KLNLSTRLR-QL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1406 RQEKALLEEieRHGEKVEECQKFAKQyinaIKDYELQLITYKAQLEPVASPAK-----KPKVQSGSESVIQEY------- 1473
Cdd:pfam01576 495 EDERNSLQE--QLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLeekaaay 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1474 ------------------VDLRTRYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlaeveaalekqrqlAEA 1535
Cdd:pfam01576 569 dklektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR--------------AEA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1536 HAQAKaqaELEARELQRRMQEEVTRREEAavdaQQQKRSIQEELQHLRQSSEAeiqaKAQQVEAAERSRMRIEEEIRVVR 1615
Cdd:pfam01576 630 EAREK---ETRALSLARALEEALEAKEEL----ERTNKQLRAEMEDLVSSKDD----VGKNVHELERSKRALEQQVEEMK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1616 LQLETTERQRGGAED-------ELQALRA--------RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEA-------- 1672
Cdd:pfam01576 699 TQLEELEDELQATEDaklrlevNMQALKAqferdlqaRDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakkkleld 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1673 --------ELALRVKAEA------------EAAREKQRALQALDELKLQAEEAERRLRQAEAE--RARQVQVALETAQRS 1730
Cdd:pfam01576 779 lkeleaqiDAANKGREEAvkqlkklqaqmkDLQRELEEARASRDEILAQSKESEKKLKNLEAEllQLQEDLAASERARRQ 858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1731 AEVE-----------LQSKRASFAEK------TAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELE---- 1789
Cdd:pfam01576 859 AQQErdeladeiasgASGKSALQDEKrrlearIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQkses 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1790 -RWQL-KANEALRLRLQAEEVA---QQKSLAQA------DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1858
Cdd:pfam01576 939 aRQQLeRQNKELKAKLQEMEGTvksKFKSSIAAleakiaQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHA 1018
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1859 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVR 1918
Cdd:pfam01576 1019 DQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1868-2068 |
2.90e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1868 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1947
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1948 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA 2009
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 2010 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKG 2068
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1569-1750 |
3.40e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.43 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1569 QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVvrlqletterqrggAEDELQalraraEEAEAQKRQ 1648
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERL--------------AAQEQK------KQAEEAAKQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1649 AQEEaerlrrQVQDESQRKRQAEAELAlrvKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAER---ARQVQVALE 1725
Cdd:PRK09510 127 AALK------QKQAEEAAAKAAAAAKA---KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAAA 197
|
170 180
....*....|....*....|....*
gi 1046896947 1726 TAQRSAEVELQSKRASFAEKTAQLE 1750
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2405-2782 |
3.80e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2405 EAENRALILRDKDNTQRFLEEEAEKMKQvaeeaarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmQAVQEATRLKA 2484
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKED--------NRADEATEEAFGKAEEAKKTETGKAEEARKAE-EAKKKAEDARK 1129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2485 EAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKlRMAEMSRAQ-ARAEEDAQRF 2563
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVR-KAEELRKAEdARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2564 rkQAEEIGEKLHRTELAtqEKVTLVQTLEiqrqQSDQDAERLREAIAELEREKEKLKQEAKLLQ-------LKSEEMQTV 2636
Cdd:PTZ00121 1209 --EEERKAEEARKAEDA--KKAEAVKKAE----EAKKDAEEAKKAEEERNNEEIRKFEEARMAHfarrqaaIKAEEARKA 1280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2637 QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQQQQMEQEKQELVASmEEARRRQ 2716
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA-KKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-AEAAADE 1358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 2717 REAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAlahsEEIATSQAAATKA 2782
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA----DELKKAAAAKKKA 1420
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1174-1758 |
4.11e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1174 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLE-------- 1243
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMAlrqqleql 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1244 -----KLKTISLVIRSTQGAEEVLKTH-EEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQpvfntlrdelRGAQEVG 1317
Cdd:PRK04863 592 qariqRLAARAPAWLAAQDALARLREQsGEEFEDSQDVTEYMQQLLERERELTVERDELAARK----------QALDEEI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1318 ERLQQRHGERDveverwrERVTQLLERWQAVLAQTDVRQRELEQLGrqlrYYRESADPLSswlqdaksrqeqiQAVPIAN 1397
Cdd:PRK04863 662 ERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YFSALYGPAR-------------HAIVVPD 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1398 SQAAREQLRQEKALLEEI-------ERHGEKVEECQKFAKQYINAIKDYELQLITYKAqlEPVASPAKKPK----VQSGS 1466
Cdd:PRK04863 718 LSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRAER 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1467 ESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRM-----EEEERLAEQQRaeeRERLAEVEAALEKQRQLAEAHAQAKA 1541
Cdd:PRK04863 796 EELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRR---VELERALADHESQEQQQRSQLEQAKE 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1542 QAELEARELQRRM--------------QEEVTRREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE---- 1601
Cdd:PRK04863 873 GLSALNRLLPRLNlladetladrveeiREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqr 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1602 RSRMRIE--EEIRVVRLQLETTERQR-GGAEDELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKRQAEAELalr 1677
Cdd:PRK04863 953 DAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL--- 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1678 vKAEAEAAREK-QRALQALDELKLQA-EEAERRLRQAEAE------RARQVQVALETAQRSAEVELQS--KRASFAEKTA 1747
Cdd:PRK04863 1026 -KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDY 1104
|
650
....*....|.
gi 1046896947 1748 QLERTLQEEHV 1758
Cdd:PRK04863 1105 HEMREQVVNAK 1115
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1877-2439 |
4.13e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1877 AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAGRFR 1954
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1955 E-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-LTEKLAAIS-EATRLKTEA---EIALKEKEAENERLRRLAE 2028
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeYLDELREIEkRLSRLEEEIngiEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2029 DEAFQRRRLEEQAAQHKA--DIEERLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEIMALKASfekaaagKAELE 2102
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2103 LELGRIRSNAEDTMRSK--------ELAEQEAARqrqlaaeEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 2174
Cdd:PRK03918 419 KEIKELKKAIEELKKAKgkcpvcgrELTEEHRKE-------LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2175 VEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAFvvqqreeelqqtlqqeQNMLERLRSEAEAARRAAEEAEEAR 2254
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEY----------------EKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2255 EQAEREAAQSRKqVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQT 2334
Cdd:PRK03918 553 ELKKKLAELEKK-LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2335 LRQKAQVEQELTTLRLQLEETDHQKSI------------LDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKA 2402
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEeeyeelreeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590
....*....|....*....|....*....|....*..
gi 1046896947 2403 RIEAENRALilrdkdntqRFLEEEAEKMKQVAEEAAR 2439
Cdd:PRK03918 712 ELEKLEKAL---------ERVEELREKVKKYKALLKE 739
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1804-1987 |
4.91e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1804 QAEEVAQQKslaQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1879
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1880 EQGEQQRQLLEEELARLQHEATAatqkRQELEAElAKVRAEMEvllaSKARAEEESRSTSEK-SKQRLEAEAGRFRELAE 1958
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEA----KKKAEAE-AAAKAAAE----AKKKAEAEAKKKAAAeAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*....
gi 1046896947 1959 EAArlRALAEEAKRQRQLAEEDAARQRAE 1987
Cdd:PRK09510 232 AEA--KAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1318-1625 |
5.10e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.37 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1318 ERLQQRHGERDVEVERWRervtQLLERWQAvlaqtdvRQRELEqlgRQLRYYRESAdplsswlQDAKSRQEQIQAVPIAN 1397
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1398 SQAAREQLRQEKALLE-----EIERHGEKVEECQKFAKQYINAIKDYELQ--LITYKAQLEPVASPAKKPKVQSGSESVI 1470
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILeeERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1471 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAELEAREL 1550
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1551 QRRMQEEVTRREEAAvdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQR 1625
Cdd:pfam17380 515 RKLLEKEMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKATeERSRLEAMEREREMMRQIVESEKAR 588
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1901-2055 |
5.22e-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: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1901 TAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEAGRFRELAEEAARLRAlaEEAKRQRQLAEED 1980
Cdd:COG2268 212 TEIAIAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAEREVQRQLEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1981 AARQR------AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 2054
Cdd:COG2268 286 AEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEK 365
|
.
gi 1046896947 2055 L 2055
Cdd:COG2268 366 L 366
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1599-2103 |
5.80e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 59.49 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1599 AAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQ---------VQDESQRKRQ 1669
Cdd:COG3899 731 ALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASarayanlglLLLGDYEEAY 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1670 AEAELALRVKAEAEAAREKQRALQALDEL---KLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKT 1746
Cdd:COG3899 811 EFGELALALAERLGDRRLEARALFNLGFIlhwLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAA 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1747 AQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQqksLAQADAEKQKEEA 1826
Cdd:COG3899 891 AAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAAL---AAALALAAAAAAA 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1827 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1906
Cdd:COG3899 968 AAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLA 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1907 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRA 1986
Cdd:COG3899 1048 ALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAA 1127
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1987 EAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQ 2066
Cdd:COG3899 1128 AARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLA 1207
|
490 500 510
....*....|....*....|....*....|....*..
gi 1046896947 2067 KGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELEL 2103
Cdd:COG3899 1208 ALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1498-2038 |
6.66e-08 |
|
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: 58.98 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1498 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQE 1577
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1578 ELQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALR------ARAEEAEAQKRQAQE 1651
Cdd:pfam05557 133 ELEELQERLD-LLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1652 EAERLRRQVQDESQRKRQAE---AELALRVKAEAEAAR---EKQRALQALDELKLQAEEAERRLRQAEAERARQVQvale 1725
Cdd:pfam05557 212 HNKHLNENIENKLLLKEEVEdlkRKLEREEKYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQ---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1726 taqrsaeveLQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEaerareeaerelERWQLKANEALRLRLQa 1805
Cdd:pfam05557 288 ---------LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED------------LNKKLKRHKALVRRLQ- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1806 eevaQQKSLA--QADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQEL--IRLRAETEQ 1881
Cdd:pfam05557 346 ----RRVLLLtkERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggYKQQAQTLE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1882 GEQQ---RQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK---QRLEAEAGRFRE 1955
Cdd:pfam05557 422 RELQalrQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQ 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1956 LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTeklAAISEATRLKTEAEIAlkekEAENERLRrlaedEAFQRR 2035
Cdd:pfam05557 502 RKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTST---MNFKEVLDLRKELESA----ELKNQRLK-----EVFQAK 569
|
...
gi 1046896947 2036 RLE 2038
Cdd:pfam05557 570 IQE 572
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1710-2628 |
7.21e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.21 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1710 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERElE 1789
Cdd:TIGR00618 56 RRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIH-D 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1790 RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGtaqQRLAAE 1869
Cdd:TIGR00618 135 LLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQL---LTLCTP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1870 QELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAemevllASKARAEEESRSTSEKSKQRLEAE 1949
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL------LKQLRARIEELRAQEAVLEETQER 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1950 AGRFRELAEEAARLRALaEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKtEAEIALKEKEAENERLRRLAED 2029
Cdd:TIGR00618 286 INRARKAAPLAAHIKAV-TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2030 EAFQRRRLEEQAAqhkadIEERLAQLRKASESELERQKGLVEDTLRQRR---QVEEEIMALKASFEKAAAGKAELELELG 2106
Cdd:TIGR00618 364 ATSIREISCQQHT-----LTQHIHTLQQQKTTLTQKLQSLCKELDILQReqaTIDTRTSAFRDLQGQLAHAKKQQELQQR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2107 RI---RSNAEDTMRSKELAEQEAARQRQlaaeeeqrrreaeervqrSLAAEEEAARQRKVALEEVERLKAkvEEARRLRE 2183
Cdd:TIGR00618 439 YAelcAAAITCTAQCEKLEKIHLQESAQ------------------SLKEREQQLQTKEQIHLQETRKKA--VVLARLLE 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2184 RAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQ 2263
Cdd:TIGR00618 499 LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2264 SRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARraqaeqaalKQKQAADAEMEKHKKFAEQTLRQK-AQVE 2342
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK---------LQPEQDLQDVRLHLQQCSQELALKlTALH 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2343 QELTTLrlqLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEElfSVRVQMEELgklkARIEAENRALILRDKDNTQRF 2422
Cdd:TIGR00618 650 ALQLTL---TQERVREHALSIRVLPKELLASRQLALQKMQSEKE--QLTYWKEML----AQCQTLLRELETHIEEYDREF 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2423 LEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2502
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2503 LQEDKEQMAQQLVEETQgfQRTLEAERQRQlemsaEAERLKLRMAEMSRAQAraeedaqRFRKQAEEIGEKLHRTELATQ 2582
Cdd:TIGR00618 801 LKTLEAEIGQEIPSDED--ILNLQCETLVQ-----EEEQFLSRLEEKSATLG-------EITHQLLKYEECSKQLAQLTQ 866
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2583 EKVTLVQTLE----IQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQL 2628
Cdd:TIGR00618 867 EQAKIIQLSDklngINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRF 916
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1804-1990 |
7.45e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.93 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1804 QAEEVAQQKSlAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1883
Cdd:TIGR02794 51 QANRIQQQKK-PAAKKEQERQK---------KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1884 QQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EA 1960
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEA 200
|
170 180 190
....*....|....*....|....*....|
gi 1046896947 1961 ARLRALAEEAKRQRQLAeedAARQRAEAER 1990
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1800-2208 |
7.95e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1800 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRA 1877
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1878 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1957
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1958 EEAARLRALAEEAKRQRQLAEED---------------AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENER 2022
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2023 LRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEIMALKASFEKAAAGKAEl 2101
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2102 elelgRIRSNAEDTMRSKELAEQEAARQRQLaaeeeqrrreaeervqrslaAEEEAARQRKVALEEVERLKAKVEEARRL 2181
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEELEELEEQL--------------------EELLGELEELLEALDEEELEEELEELEEE 440
|
410 420
....*....|....*....|....*..
gi 1046896947 2182 RERAEQESARQLQLAQEAAQKRLQAEE 2208
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEE 467
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4197-4233 |
8.53e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 8.53e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 4197 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4233
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2473-2618 |
9.07e-08 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 58.88 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2473 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLVEEtQGFQRTLEAERQRQLEMSAEAERLKL 2544
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2545 RMAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDQDAERlREAIAELEREKEK 2618
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1516-1985 |
9.34e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 58.88 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1516 RERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQqqkrsiqeelqhLRQSSEAEIQAKAQ 1595
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAA------------LRWALAHGDAELAL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1596 QVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1675
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1676 LRvkAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1755
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1756 EHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGK 1835
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1836 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1915
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1916 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1985
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2323-2775 |
1.14e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2323 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRSQVEEELFSVRVQMEE 2396
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2397 LGKLKARIEAENRALI--LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2474
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2475 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRMAEM 2549
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2550 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKL-KQEAKL 2625
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2626 LQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRER-----FIEQEKAKLEQL--FQDEVAKAKQLQEEQQRQQQQM 2698
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELepFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 2699 EQEKQELVASMEEARRRQREAEEgvrRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATS 2775
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEE---LRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
182-306 |
1.14e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 53.85 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 182 ERDRVQKKTFTKWVNKHLIkhwraeaQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSVRLPREKGRMRfhKLQ 261
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1046896947 262 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 306
Cdd:cd21331 86 NCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1537-2206 |
1.20e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 58.66 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1537 AQAKAQAELearelqrrmQEEVTRRE-EAAVDAQ--QQKRSIQEELQHLR-QSSEAEIQAKAQQVEAAERSRMRIEEEIR 1612
Cdd:PRK10246 164 AKPKERAEL---------LEELTGTEiYGQISAMvfEQHKSARTELEKLQaQASGVALLTPEQVQSLTASLQVLTDEEKQ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1613 -VVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAErlrrqvqdesqrKRQAEAELALRVKAEAEAAREKQRA 1691
Cdd:PRK10246 235 lLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQ------------PQLAALSLAQPARQLRPHWERIQEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1692 LQALDELKLQAEEAERRLRQAEAERARQVQVALETAQrsaevELQSKRASFAEKTAQLER------TLQEEHVTVTQLRE 1765
Cdd:PRK10246 303 SAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLAEHDRfrqwnnELAGWRAQFSQQTS 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1766 EAERRAQQQAEAERAreeaereleRWQLKANEALRLRLQAEEVAQqkslAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1845
Cdd:PRK10246 378 DREQLRQWQQQLTHA---------EQKLNALPAITLTLTADEVAA----ALAQHAEQRPLRQRLVALHGQIVPQQKRLAQ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1846 LAE------QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgEQQRQLLEEELARLQ------------HEATAATQ-- 1905
Cdd:PRK10246 445 LQVaiqnvtQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ-EARIKDLEAQRAQLQagqpcplcgstsHPAVEAYQal 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1906 -------KRQELEAELAK-------VRAEMEVLLASKARAEEESRSTSEKSK------QRLEAEAGRFRELAEEAARLRA 1965
Cdd:PRK10246 524 epgvnqsRLDALEKEVKKlgeegaaLRGQLDALTKQLQRDESEAQSLRQEEQaltqqwQAVCASLNITLQPQDDIQPWLD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1966 LAEEAKRQ-RQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEI---ALKEKEAENERL---RRLAEDEAFQRRRLE 2038
Cdd:PRK10246 604 AQEEHERQlRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALagyALTLPQEDEEASwlaTRQQEAQSWQQRQNE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2039 EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLrqrRQVEEEIMALKASF-----------EKAAAGKAELELELGR 2107
Cdd:PRK10246 684 LTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNW---RQVHEQCLSLHSQLqtlqqqdvleaQRLQKAQAQFDTALQA 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2108 IRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE---VERLKAKVEE-ARRLRE 2183
Cdd:PRK10246 761 SVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLtvtVEQIQQELAQlAQQLRE 840
|
730 740
....*....|....*....|...
gi 1046896947 2184 RAEQESARQLQLAQEAAQKRLQA 2206
Cdd:PRK10246 841 NTTRQGEIRQQLKQDADNRQQQQ 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2364-2632 |
1.44e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2364 EELQRLKAEVTEAARQRSQVE------EELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEA 2437
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2438 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2517
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2518 TQGFQRTLEAERQRQLEMSAEAERLklrmaemSRAQARAEEDAQRFRKQAEEIgeklhRTELAtqekvtlvqtlEIQRQQ 2597
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEAL-------EEALAEAEAALRDLRRELREL-----EAEIA-----------SLERRK 435
|
250 260 270
....*....|....*....|....*....|....*...
gi 1046896947 2598 S--DQDAERLREAIAE-LEREKEKLKQEAKLLQLKSEE 2632
Cdd:COG4913 436 SniPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2431-2647 |
1.49e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.78 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2431 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2510
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2511 AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2590
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 2591 LEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2647
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1223-1671 |
1.67e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1223 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEHLKEAQAVPATLQELEvtkaslkKLRAQAEAQQPV 1302
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-------ALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1303 FNTLRDELRGAQEVGERLQqrhgERDVEVERWRERVTQLLERWQAVLAQTDVR-QRELEQLGRQLRYYRESADPLSSWLQ 1381
Cdd:COG4717 148 LEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1382 DAKSRQEQIQAVpiANSQAAREQLRQEK----------ALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLE 1451
Cdd:COG4717 224 ELEEELEQLENE--LEAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1452 PVASPAKKPKVQSGSESviQEYVDLRTRYSELTTLTSQYIkfisETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ 1531
Cdd:COG4717 302 KEAEELQALPALEELEE--EELEELLAALGLPPDLSPEEL----LELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1532 LAEAHAQAKAQAELEARELQRRmQEEVTRREEAAVDAQQQKRSIQEELQHLRQSS-EAEIQAKAQQVEAAERSRMRIEEE 1610
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREE 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1611 IRVVRLQLETTERqrggaEDELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAE 1671
Cdd:COG4717 455 LAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1653-2109 |
1.73e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 58.11 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1653 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALdelkLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1732
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLAR----LDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1733 VELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1812
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1813 SLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1892
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1893 LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1972
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1973 QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERL 2052
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 2053 AQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIR 2109
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2324-2627 |
1.74e-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: 57.72 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2324 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKAR 2403
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2404 IEAENRAL------ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2475
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2476 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaerqrqlemsaeaeRLKLRMAEMSRAQAR 2555
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE--------------ELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 2556 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQ 2627
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1530-1742 |
2.06e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1530 RQLAEAHAQAKAQAELEARELQRRMQEEVTRR--EEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAER 1602
Cdd:COG3206 147 PELAAAVANALAEAYLEQNLELRREEARKALEflEEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1603 SRMRIEEEIRVVRLQLETTERQRGGAEDE---------LQALRARAEEAEAQKRQAQE-------EAERLRRQVQDESQR 1666
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1667 KRQAEAELALRVKAEAEAAREKQRALQA-LDELKLQAE---EAERRLR--QAEAERARQVQVALETAQRSAEVELQSKRA 1740
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAqLAQLEARLAelpELEAELRrlEREVEVARELYESLLQRLEEARLAEALTVG 386
|
..
gi 1046896947 1741 SF 1742
Cdd:COG3206 387 NV 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1847-2062 |
2.33e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1847 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLA 1926
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1927 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK 1995
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1996 LAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESE 2062
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1802-2237 |
2.38e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.06 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1802 RLQAEEVAQQKSLaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQ 1881
Cdd:pfam05557 59 LLEKREAEAEEAL-REQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSE-LRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1882 GEQQRQLLE----------EELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKAraEEESRSTSEKSKQRLEAEAG 1951
Cdd:pfam05557 137 LQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKS--ELARIPELEKELERLREHNK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1952 RFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLTE----KLAAISEATRLKTEAEIALKEKEAENERLR 2024
Cdd:pfam05557 215 HLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQElqswVKLAQDTGLNLRSPEDLSRRIEQLQQREIV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2025 RLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASESE---LERQKGLVEDTLRQRRQVEEEIMALKA---SFEKAAAGK 2098
Cdd:pfam05557 295 LKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2099 AELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQR-SLAAEEEAARQRKVALEEVERLKAKVEE 2177
Cdd:pfam05557 373 NYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERElQALRQQESLADPSYSKEEVDSLRRKLET 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 2178 ARRLRER-AEQESARQLQLAQEAAQkrlQAEEKAHAFVVQQREEELQQTLQQEQNMLERLR 2237
Cdd:pfam05557 453 LELERQRlREQKNELEMELERRCLQ---GDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQ 510
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1580-1868 |
2.55e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 57.27 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1580 QHLRQSsEAEIQAKAQQVEAAERSRMRIEEeiRVVRLqletterqrggaEDELQALRARAEEAEAQKRQAQEEA-----E 1654
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARL------------EREKAAREARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1655 RLRRQVQDESQRKRQAEAELALRVKAEAEA-AREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEV 1733
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAReARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1734 ELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAeaerareeaerelerwqlkANEALRLRLQAEEVAQQKS 1813
Cdd:PRK05035 574 EVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------------------AVAAAIARAKAKKAEQQAN 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 1814 LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1868
Cdd:PRK05035 635 AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1588-1725 |
2.91e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.82 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1588 AEIQAKAQQVEAAersrmrieeeIRVVRLQLETTERQRGgAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDE--SQ 1665
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGavSQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1666 RKRQaEAELALRV-KAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERArQVQVALE 1725
Cdd:COG1566 148 QELD-EARAALDAaQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALA-QAELNLA 206
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2428-2789 |
3.03e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2428 EKMKQVAEEaarLSVAAQEAARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARRLQED 2506
Cdd:TIGR02169 170 RKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKR-EYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2507 keqmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSraqaraEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2586
Cdd:TIGR02169 246 ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2587 LVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQqEQILQETQALQKSFLSEKDSLLQRERFI 2666
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-EDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2667 EQEKAKLEQLfqdevakaKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAE 2746
Cdd:TIGR02169 395 EKLKREINEL--------KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1046896947 2747 ENQ---RLRERLQRLEEEHRAALAHSEEIATSQAAATKALPNGRDA 2789
Cdd:TIGR02169 467 YEQelyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2336-2675 |
3.12e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2336 RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLK---AEVTEAARQRSQVEeelfsvRVQmEELGKLKARIEAENRALi 2412
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlNLVQTALRQQEKIE------RYQ-ADLEELEERLEEQNEVV- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2413 lrdkdntqrflEEEAEkmkQVAEEAARLSVAAQEAARLR-QLAEE----DLAQQRALA---EKMLKEKMQAVQEATRLKA 2484
Cdd:PRK04863 372 -----------EEADE---QQEENEARAEAAEEEVDELKsQLADYqqalDVQQTRAIQyqqAVQALERAKQLCGLPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2485 E------AELLQQQKELAQEQ---ARRL---QEDKEQMAQ--QLV----------EETQGFQRTL-EAERQRQLEMSAEA 2539
Cdd:PRK04863 438 DnaedwlEEFQAKEQEATEELlslEQKLsvaQAAHSQFEQayQLVrkiagevsrsEAWDVARELLrRLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2540 ERLKLRMAEMS-RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEK 2618
Cdd:PRK04863 518 LRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 2619 LKQEA--------KLLQLKS---EEMQTVQQ-EQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQ 2675
Cdd:PRK04863 598 LAARApawlaaqdALARLREqsgEEFEDSQDvTEYMQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1834-2043 |
3.23e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.50 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1834 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheataATQKRQEL 1910
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1911 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEeakRQRQLAEEDAARQRAEAER 1990
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQE---LQRKKQQEEAERAEAEKQR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 1991 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ 2043
Cdd:pfam15709 454 QKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAAR 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1491-1731 |
3.28e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1491 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQ 1570
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1571 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAE----EAEAQK 1646
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1647 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALET 1726
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*
gi 1046896947 1727 AQRSA 1731
Cdd:COG3883 258 AAGSA 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1311-1736 |
3.30e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1311 RGAQEvgERLQQRHGERDVEVERW--RERVTQLLERWQ-----------AVLAQTDVRQrELEQLGRQLRY-YRESADpl 1376
Cdd:PRK04863 781 RAARE--KRIEQLRAEREELAERYatLSFDVQKLQRLHqafsrfigshlAVAFEADPEA-ELRQLNRRRVElERALAD-- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1377 sswlQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEiERHGEKVEECQ---KFAKQYINAIKDYELQLitykAQLEPV 1453
Cdd:PRK04863 856 ----HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD-ETLADRVEEIReqlDEAEEAKRFVQQHGNAL----AQLEPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1454 AS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAeereRLAEVEAALE 1527
Cdd:PRK04863 927 VSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1528 KQRqlaEAHAQAKAQAElEARELQRRMQEEVTRreeaavdAQQQKRSIQEELQHL--RQSSEAEIQAKAQqveaaersRM 1605
Cdd:PRK04863 1003 RAR---EQLRQAQAQLA-QYNQVLASLKSSYDA-------KRQMLQELKQELQDLgvPADSGAEERARAR--------RD 1063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1606 RIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQAEAELALRV 1678
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnakagwcAVLRLVKDNGVERRLHRRELAYLS 1143
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1679 KAEAEAAREKqrALQALdelklqaeeaerRLRQAEAERARQVQVALETAQRsAEVELQ 1736
Cdd:PRK04863 1144 ADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRLSEDPKR-PERKVQ 1186
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1502-1912 |
3.33e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1502 EEEERLAEQQRaeeRERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRM--------------QEEVTRREEAAVD 1567
Cdd:PRK04863 836 EAELRQLNRRR---VELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlladetladrveeiREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1568 AQQQKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE----RSRMRIE--EEIRVVRLQLETTERQR-GGAEDELQ-ALRA 1637
Cdd:PRK04863 913 VQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqrDAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1638 RAEEAEAQKRQAQEEAerlrRQVQDESQRKRQAEAELalrvKAEAEAAREK-QRALQALDELKLQA-EEAERRLRQAEAE 1715
Cdd:PRK04863 993 RLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDE 1064
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1716 ------RARQVQVALETAQRSAEVELQS--KRASFAEKTAQLERTLQEEHVTVTQ--LREEAERRAQQQAEAERAREEAE 1785
Cdd:PRK04863 1065 lharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDYHEMREQVVNAKAGWCavLRLVKDNGVERRLHRRELAYLSA 1144
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1786 RELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREArrrgkaeeqAVRQ--RELAEQELEKqrqlaegTAQ 1863
Cdd:PRK04863 1145 DELRSMSDKALGALRLAVADNEHLRDVLRLSEDPKRPERKVQFYI---------AVYQhlRERIRQDIIR-------TDD 1208
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1864 QRLAAEQ---ELIRLRAETEQGEQQRQLLEEELA-----RLQHEATAATQKRQELEA 1912
Cdd:PRK04863 1209 PVEAIEQmeiELSRLTEELTSREQKLAISSESVAniirkTIQREQNRIRMLNQGLQN 1265
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1630-2184 |
3.50e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1630 DELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvKAEAEaarekqraLQALDELKLQAEEAERRL 1709
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE---KLEKE--------VKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1710 RQAEAERArqvqvALETAQRsaevELQSKRASFAEKTAQLERTLQEehvtvtqlreeaerraqqqaeaerareeaereLE 1789
Cdd:PRK03918 248 ESLEGSKR-----KLEEKIR----ELEERIEELKKEIEELEEKVKE--------------------------------LK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1790 RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GT 1861
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1862 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR--LQHEATAATQKRQELEAELAKVRAEMEVLLASKARA-------E 1932
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1933 EESR-----------STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAE 1987
Cdd:PRK03918 447 EEHRkelleeytaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1988 AERVLTEKLAAISEATRLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA------ 2058
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneyle 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2059 ---SESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAaagKAELElELGRIRSNAEDTMRSKELAEQEAARQRqlAAE 2135
Cdd:PRK03918 607 lkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYSEEEYEELREEYLELSRELAG--LRA 680
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1046896947 2136 EEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRER 2184
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2321-2674 |
4.16e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.77 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2321 DAEMEKHKKFAEQTLRQKAQVEQELTT--------LRLQLEETDHQKSILDEELQRLKAEV---TEAARQRSQVEEELFS 2389
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2390 VRvqmeeLGKLKARIeaeNRALILRDKDNTQRFLEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRaLAEKM 2468
Cdd:pfam12128 444 SR-----LGELKLRL---NQATATPELLLQLENFDERIERAREEQEAAnAEVERLQSELRQARKRRDQASEALR-QASRR 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2469 LKEKMQAVQEATR------------LKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLE 2534
Cdd:pfam12128 515 LEERQSALDELELqlfpqagtllhfLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2535 MSAEAERLKLRMAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDQDAERLR 2606
Cdd:pfam12128 595 WAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2607 EAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLE 2674
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARR 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1838-2531 |
4.67e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1838 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1917
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1918 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLA 1997
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1998 AISEATRLKTEAEIALKEKEAENERLRRlaedeafQRRRLEeqaaQHKADIEERLAQLRKAseseLERQKGLVEDTLRqr 2077
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEA-------EIASLE----RRKSNIPARLLALRDA----LAEALGLDEAELP-- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2078 rqVEEEIMALKASFEK--AAAgkaelELELGRIRSN----AEDTMRSKELAEQEAARQRqlaaeeeqrrreaeervQRSL 2151
Cdd:COG4913 462 --FVGELIEVRPEEERwrGAI-----ERVLGGFALTllvpPEHYAAALRWVNRLHLRGR-----------------LVYE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2152 AAEEEAARQRKVALEE---VERLKAKVEEARR-LRERAEQ-------ESARQLQLAQEAAQKRLQAEEKAHAFVVQQREE 2220
Cdd:COG4913 518 RVRTGLPDPERPRLDPdslAGKLDFKPHPFRAwLEAELGRrfdyvcvDSPEELRRHPRAITRAGQVKGNGTRHEKDDRRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2221 ELQQTLQQEQNM--LERLRseaeaarraaeeaeeareqaereaaqsrkqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKE 2298
Cdd:COG4913 598 IRSRYVLGFDNRakLAALE-------------------------------AELAELEEELAEAEERLEALEAELDALQER 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2299 AEQEAArraqaeqaaLKQKQAADAEMEkhkkfaeQTLRQKAQVEQELTtlrlQLEETDHQKSILDEELQRLKAEVTEAAR 2378
Cdd:COG4913 647 REALQR---------LAEYSWDEIDVA-------SAEREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2379 QRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEAARLSVAAQEAARLRQLAEEDL 2458
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA---AALGDAVERELRENLEERIDALRARLN 783
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2459 AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLVEETQ----GFQRTLEAERQR 2531
Cdd:COG4913 784 RAEEELERAMRAFNREWPAETADLDADLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIefvaDLLSKLRRAIRE 861
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1938-2381 |
4.74e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1938 TSEKSKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 2016
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2017 EAENERLRRLAEDEAFQRRRLEEQaaqhKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAA 2096
Cdd:COG4717 145 PERLEELEERLEELRELEEELEEL----EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2097 GKAELELELGRIRSNAEDTMRSKELAEQEAArQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK-- 2174
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKas 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2175 -VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEA 2253
Cdd:COG4717 300 lGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2254 REQAEREAAQSRKQVEEAERLKQsaeeqaqaqaQAQAAAEKLRKEAEQEAARRAQAEQAALKQK-QAADAEMEKHKKFAE 2332
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKE----------ELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1046896947 2333 QTLRQKAQVEQELTTLrlqleETDHQKSILDEELQRLKAEVTEAARQRS 2381
Cdd:COG4717 450 ELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWA 493
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1874-2490 |
4.74e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1874 RLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1953
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1954 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE---AENERLRRLA 2027
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2028 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAEL 2101
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2102 ELELGRIRSNAEDtmrskelaeqeaARQRqlaaeeeqrrreaeervQRSLAAEEEAARQRkvaleeverlkakVEEARRL 2181
Cdd:PRK02224 411 EDFLEELREERDE------------LRER-----------------EAELEATLRTARER-------------VEEAEAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2182 RERAEQESARQlqlaqeaaqkrlQAEEKAHAFVVQQREEELQQtlqqeqnmLERLRSEAEAARRAAEEAEEAREQAEREA 2261
Cdd:PRK02224 449 LEAGKCPECGQ------------PVEGSPHVETIEEDRERVEE--------LEAELEDLEEEVEEVEERLERAEDLVEAE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2262 AQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFaEQTLRQKAQV 2341
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL-NSKLAELKER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2342 EQELTTLRLQLEETDHqksiLDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGklkARIEAENRALILRDKDNTQR 2421
Cdd:PRK02224 588 IESLERIRTLLAAIAD----AEDEIERLREKREALAELNDERRERLAEKRERKRELE---AEFDEARIEEAREDKERAEE 660
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2422 FLEEEAEKMKQVAEEAARLSVAA----QEAARLRQLAEEdlaqQRALAEKmlKEKMQAVQEatrlkaEAELLQ 2490
Cdd:PRK02224 661 YLEQVEEKLDELREERDDLQAEIgaveNELEELEELRER----REALENR--VEALEALYD------EAEELE 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2376-2624 |
5.11e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2376 AARQRSQVEEELFSVRVQMEELGKLKARIEAEnRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAE 2455
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2456 EDLAQQRALaekmLKEKMQAVQEATRLKAEAELLQQQKelAQEQARRLQEDKeQMAQQLVEETQGFQRTLEAERQRQLEM 2535
Cdd:COG4942 97 AELEAQKEE----LAELLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2536 SAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLhrtelatqekvtlvQTLEIQRQQSDQDAERLREAIAELERE 2615
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKEL--------------AELAAELAELQQEAEELEALIARLEAE 235
|
....*....
gi 1046896947 2616 KEKLKQEAK 2624
Cdd:COG4942 236 AAAAAERTP 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1524-1694 |
5.34e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1524 AALEKQRQLAEAHAQAKAQAELEARelQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERS 1603
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHR--LKELPAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1604 RMRIEEEIRVVR---------LQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1674
Cdd:COG1579 75 IKKYEEQLGNVRnnkeyealqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180
....*....|....*....|
gi 1046896947 1675 alrvKAEAEAAREKQRALQA 1694
Cdd:COG1579 155 ----EAELEELEAEREELAA 170
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1894-2624 |
5.61e-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: 56.27 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1894 ARLQHEATAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1970
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1971 KRQRQLAEEDAAR---QRAEAERVLTEKLAAISEATRLKTEAEIalkekEAENERLR---RLAEDEAfQRRRLEEQAAQH 2044
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRV-----QAENARLEmhfKLKEDHE-KIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2045 KADIEERLAQLRKASESELERQKGL---VEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKEL 2121
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2122 AEQEaarqrqlAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2201
Cdd:pfam05483 315 LEED-------LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2202 KRLQAEEKAHAFVVQQREEelqqtlqqeqnmLERLRSEAEAARRAAEeaeeareqaereaaqSRKQVEE-AERLKQSAEE 2280
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVE------------LEELKKILAEDEKLLD---------------EKKQFEKiAEELKGKEQE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2281 QAQAQAQAQAAAEKLRkeaeQEAARRAQAEQAALKQKQAADAEMEKHK-KFAEQT------LRQKAQVEQELTTLRLQLE 2353
Cdd:pfam05483 441 LIFLLQAREKEIHDLE----IQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTahcdklLLENKELTQEASDMTLELK 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2354 etDHQKSILDEELQ--RLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkarieaENRALILRDKDNTQRFLEEEAEKMK 2431
Cdd:pfam05483 517 --KHQEDIINCKKQeeRMLKQIENLEEKEMNLRDELESVREEFIQKGD-------EVKCKLDKSEENARSIEYEVLKKEK 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2432 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ---EATRLKAEAELLQQQKELAQEQARRLQEDKE 2508
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2509 QMAQQLVEETQGFQRTLEAERQRQLEMSaeaERLKLRMAEMSraqARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLV 2588
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAEMV---ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAK 741
|
730 740 750
....*....|....*....|....*....|....*.
gi 1046896947 2589 QTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAK 2624
Cdd:pfam05483 742 AALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1504-1881 |
6.09e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.67 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1504 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEevtrREEAAVDAQQQKRSIQEELQHLR 1583
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE----LKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1584 QSSEAEIQAKAQQVEAAERSRMRIEE-EIRVVRLQLETTERqrggaEDELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1662
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLER-----ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1663 ESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEA--ERARQVQVALETAQRSAEvelqSKRA 1740
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAllEELRSLQERLNASERKVE----GLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1741 SFAEKTAQLERTLQEEH---VTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrLRLQAEEVAQQKSLAQA 1817
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHqarLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRI-EKLSAELQRLEERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1818 DAEKQKEEAEREARRRGKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1881
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRREL--QELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1314-1719 |
6.10e-07 |
|
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: 56.21 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1314 QEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSrqeqiqav 1393
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN-------- 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1394 piansqaareQLRQEKALLEEIERHGEKVEECQK---FAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVI 1470
Cdd:TIGR00606 766 ----------DIEEQETLLGTIMPEEESAKVCLTdvtIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1471 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQA---E 1544
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQLVELSTEVQsLIREIKDAKEQDsplE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1545 LEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHL------------------RQSSEAEIQAKAQQVEAAERSRMR 1606
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdienkiqdgkddyLKQKETELNTVNAQLEECEKHQEK 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1607 IEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeAAR 1686
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKR 1068
|
410 420 430
....*....|....*....|....*....|...
gi 1046896947 1687 EKQRALQALDELKLQAEEAERRLRQAEAERARQ 1719
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3619-3655 |
6.17e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 6.17e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 3619 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 3655
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3878-3913 |
6.23e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 6.23e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1046896947 3878 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3913
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
187-303 |
6.35e-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: 50.96 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 187 QKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSVRLPrekgrmrFHKLQNVQIA 266
Cdd:cd21299 5 EERCFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMP-------FKKVENCNQV 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 267 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 303
Cdd:cd21299 71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1925-2726 |
7.14e-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: 56.13 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1925 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATR 2004
Cdd:TIGR00618 50 LYGKLPRRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2005 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ----HKADIEERLAQLRKASESELERQKGLVEDTLRQRRQ- 2079
Cdd:TIGR00618 130 EVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELlmnlFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLc 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2080 VEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAaEEEAAR 2159
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEET-QERINR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2160 QRKVA-----LEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLE 2234
Cdd:TIGR00618 289 ARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2235 RLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2314
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAADAEmEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARqrsqveeELFSVRVQM 2394
Cdd:TIGR00618 449 CTAQCEKLE-KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI-------HPNPARQDI 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2395 EELGKLKARIEA-ENRALILRDK-DNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEk 2472
Cdd:TIGR00618 521 DNPGPLTRRMQRgEQTYAQLETSeEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL- 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2473 MQAVQEATRLKAEA---ELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQlemsaEAERLKLRMAEM 2549
Cdd:TIGR00618 600 TEKLSEAEDMLACEqhaLLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE-----HALSIRVLPKEL 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2550 SRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQdaeRLREAIAELEREKEKLKQEAKLLQlk 2629
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN---ASSSLGSDLAAREDALNQSLKELM-- 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2630 sEEMQTVQQEQILQETQALQKSFLSEKdsLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQmeqEKQELVASM 2709
Cdd:TIGR00618 750 -HQARTVLKARTEAHFNNNEEVTAALQ--TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS---DEDILNLQC 823
|
810
....*....|....*..
gi 1046896947 2710 EEARRRQREAEEGVRRK 2726
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEK 840
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1552-1733 |
7.17e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1552 RRMQEEVTRREEAAVDAQQQKRSIQEElQHLRQSSEAEIQAkaqqveaaersrmriEEEIRVVRLQLETTERQRGGAEDE 1631
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQ---------------EREIETARIAEAEAELAKKKAEER 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1632 LQALRARAEeAEAQKRQAQEEAERLRRQ------------VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELK 1699
Cdd:COG2268 255 REAETARAE-AEAAYEIAEANAEREVQRqleiaerereieLQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR 333
|
170 180 190
....*....|....*....|....*....|....*.
gi 1046896947 1700 LQAE-EAERRLRQAEAERA-RQVQVALETAQRSAEV 1733
Cdd:COG2268 334 AKGLaEAEGKRALAEAWNKlGDAAILLMLIEKLPEI 369
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
189-300 |
7.21e-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: 50.41 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 189 KTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVirsvrlPREKGRMrfhkLQNVQIALD 268
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGC------PRSQSQM----IENVDVCLS 69
|
90 100 110
....*....|....*....|....*....|..
gi 1046896947 269 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 300
Cdd:cd21286 70 FLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2331-2765 |
7.63e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2331 AEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEELfSVRVQMEELGKLKARIEAENRA 2410
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2411 LI-LRDKDNTQRFLEEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2489
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2490 QQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRKQAE 2568
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2569 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvqQEQILQETQAL 2648
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---IAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2649 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQD-----EVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGV 2723
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEEllgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1046896947 2724 RRkQEELQRLEQQRqqqekllaEENQRLRERLQRLEEEHRAA 2765
Cdd:COG4717 463 EQ-LEEDGELAELL--------QELEELKAELRELAEEWAAL 495
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1732-2566 |
8.65e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1732 EVELQSKRASFAEKTAQ-LERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELerwQLKANEALRLRLQAEEVAQ 1810
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEhIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDL---QTKLQEMQMERDAMADIRR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1811 QKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQqrlaaeqELIRLRAETEQGEQQRQLLE 1890
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-------EIRSILVDFEEASGKKIYEH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1891 EELARLQHEA--TAATQKRQELEAELA-------KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEA 1960
Cdd:pfam15921 208 DSMSTMHFRSlgSAISKILRELDTEISylkgrifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1961 ARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 2040
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2041 AAQHKADIEERLAQL-----RKASESELERQK-----------GLVEDTLRqrRQVEEEIMALKasfekaaagkaELELE 2104
Cdd:pfam15921 368 FSQESGNLDDQLQKLladlhKREKELSLEKEQnkrlwdrdtgnSITIDHLR--RELDDRNMEVQ-----------RLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2105 LGRIRSNAEDTMRSKELAEQeaARQRQLAAEEEQRRREAEERVQRSLAAEEEAARqrKVALEEVERLKAKVEEARRLRER 2184
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQ--GKNESLEKVSSLTAQLESTKEMLRKVVEELTAK--KMTLESSERTVSDLTASLQEKER 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2185 AEQESARQLQLAQEAAQKRLQ-----AEEKAHAFVVQQREEELQQTLQQEQNMLERLRseaeaarraaeeaeeareqaer 2259
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQelqhlKNEGDHLRNVQTECEALKLQMAEKDKVIEILR---------------------- 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2260 eaaqsrKQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaeqaalkqkqaadaeMEKHKKFAEQTLRQKA 2339
Cdd:pfam15921 569 ------QQIENMTQL-------------------------------------------------VGQHGRTAGAMQVEKA 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2340 QVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV----EEELFSVRVQMEELGKLKARIE---------A 2406
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrnelnslS 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2407 ENRALILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEK----MLKEKMQAV 2476
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKmqlksaQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRgqidALQSKIQFL 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2477 QEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLvEETQGFQRTLeaeRQRQLEMSAEAERLKLRMAEMSRAQAR 2555
Cdd:pfam15921 754 EEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQERRL---KEKVANMEVALDKASLQFAECQDIIQR 829
|
890
....*....|.
gi 1046896947 2556 AEEDAQRFRKQ 2566
Cdd:pfam15921 830 QEQESVRLKLQ 840
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4300-4328 |
8.80e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 8.80e-07
10 20
....*....|....*....|....*....
gi 1046896947 4300 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4328
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1503-1698 |
8.84e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1503 EEERLAEQQR--AEERERLAEVE----------AALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAvdaqq 1570
Cdd:PRK09510 93 QQKQAAEQERlkQLEKERLAAQEqkkqaeeaakQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1571 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAErsrmrieeeirvvrlqlettERQRGGAEDELQALRARAEEAEAQKRQAQ 1650
Cdd:PRK09510 168 KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE--------------------AKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1046896947 1651 EEAErlrrqvqdesqRKRQAEAELALRVKAEAEAAREKQRAlqALDEL 1698
Cdd:PRK09510 228 AKAA-----------AEAKAAAEKAAAAKAAEKAAAAKAAA--EVDDL 262
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1306-1755 |
1.02e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1306 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKS 1385
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1386 RQEQIQAVpiansQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAkkpkvqsg 1465
Cdd:COG4717 127 LLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1466 SESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEE-ERLAEQQRAEERERLAEVEAAL----------EKQRQ 1531
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEEleeAQEELEELEEELEQLENElEAAALEERLKEARLLLLIAAALlallglggslLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1532 LAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQS-------SEAEIQAKAQQVEAAERSR 1604
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1605 MRIEEEIRVVRLQLETTERQ----RGGAEDElQALRARAEEAEaQKRQAQEEAERLRRQVQDEsqrkrqAEAELALRVKA 1680
Cdd:COG4717 354 REAEELEEELQLEELEQEIAallaEAGVEDE-EELRAALEQAE-EYQELKEELEELEEQLEEL------LGELEELLEAL 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 1681 EAEAAREKqralqaLDELKLQAEEAERRLRQAEAERARqvqVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1755
Cdd:COG4717 426 DEEELEEE------LEELEEELEELEEELEELREELAE---LEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1477-1596 |
1.23e-06 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 53.45 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1477 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELearelqR 1552
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEL------L 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1046896947 1553 RMQEEVTRREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKAQQ 1596
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKE 177
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1529-1657 |
1.28e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 53.90 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1529 QRQLAEAHAQ-AKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKaQQVEAAERSRMRI 1607
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ-QELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1608 EEEIRVVRLQLETTERQRGGAEdELQALRARAEEAEAQKRQAQEEAERLR 1657
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1259-1975 |
1.30e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 54.76 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1259 EEVLKTHEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAqqpvfntLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1337
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1338 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESadplsswlqdaksrqeqiQAVPIANSQAAREQLR-QEKALLEEIE 1416
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAG------------------EAKQLAEAQKEAELLRkQLSKTQEELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1417 RHGEKVEECQKFAKQYInaikdyelqlitykaqLEPVASPAKKPKVQSGSESViQEYVDLRTRYSELTTLTSQYIKFISE 1496
Cdd:pfam07111 215 AQVTLVESLRKYVGEQV----------------PPEVHSQTWELERQELLDTM-QHLQEDRADLQATVELLQVRVQSLTH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1497 TLRRMEEE-ERLAEQQRAEERERLAEVEAALEKQRQLAEA-HAQAKAQaELEARELQRRMQEEVTRREEAAVDAQQQKRS 1574
Cdd:pfam07111 278 MLALQEEElTRKIQPSDSLEPEFPKKCRSLLNRWREKVFAlMVQLKAQ-DLEHRDSVKQLRGQVAELQEQVTSQSQEQAI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1575 IQEELQHLRQSSEAE-IQAKAQQVE--AAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQE 1651
Cdd:pfam07111 357 LQRALQDKAAEVEVErMSAKGLQMElsRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1652 EAERLRR----------------QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAldELKLQA----EEAERRLRQ 1711
Cdd:pfam07111 437 RLSYAVRkvhtikglmarkvalaQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA--ELQLSAhliqQEVGRAREQ 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1712 AEAERARQVQVALETAQrsaevELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerraqqqaeaerareeaerelerw 1791
Cdd:pfam07111 515 GEAERQQLSEVAQQLEQ-----ELQRAQESLASVGQQLEVARQGQ----------------------------------- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1792 QLKANEALRLRlqAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQE 1871
Cdd:pfam07111 555 QESTEEAASLR--QELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEK-ERNQE 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1872 LIRLRAETEQGEQQR-----QLLEEE----LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----S 1937
Cdd:pfam07111 632 LRRLQDEARKEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavP 711
|
730 740 750
....*....|....*....|....*....|....*...
gi 1046896947 1938 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ 1975
Cdd:pfam07111 712 TRESIKGSLTVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1515-2078 |
1.38e-06 |
|
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: 54.65 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1515 ERERLAEVEAALEKQ-----RQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRsiQEELQHLRQ----- 1584
Cdd:pfam05701 35 ERRKLVELELEKVQEeipeyKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQ--DSELAKLRVeemeq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1585 --SSEAEIQAKAQqVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQd 1662
Cdd:pfam05701 113 giADEASVAAKAQ-LEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1663 esqrkrQAEAELALRVKAEAEAAREKQRALQALDELKL-------QAEEAERRLRQaEAERARQVQVALETAqrsaEVEL 1735
Cdd:pfam05701 191 ------ATKESLESAHAAHLEAEEHRIGAALAREQDKLnwekelkQAEEELQRLNQ-QLLSAKDLKSKLETA----SALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1736 QSKRASFAektAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERwqlKANEALRLRLQAEevaqqkSLa 1815
Cdd:pfam05701 260 LDLKAELA---AYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEK---AKDEVNCLRVAAA------SL- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1816 QADAEKQKeeaerearrrgkAEEQAVRQRELA--------EQELEKQRQLAEgTAQQRLAAEQE--------LIRLRAET 1879
Cdd:pfam05701 327 RSELEKEK------------AELASLRQREGMasiavsslEAELNRTKSEIA-LVQAKEKEAREkmvelpkqLQQAAQEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1880 EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK------ARAEEESRSTSEKSKQrlEAEAGRF 1953
Cdd:pfam05701 394 EEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEklalaaIKALQESESSAESTNQ--EDSPRGV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1954 RELAEEAARLRALAEEakrqrqlAEEDAARQRAEAervltekLAAISEAtrlkteaeialkeKEAENERLRRLAEdeafq 2033
Cdd:pfam05701 472 TLSLEEYYELSKRAHE-------AEELANKRVAEA-------VSQIEEA-------------KESELRSLEKLEE----- 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1046896947 2034 rrrLEEQAAQHKADIEERLAQLRKASESELErqkglVEDTLRQRR 2078
Cdd:pfam05701 520 ---VNREMEERKEALKIALEKAEKAKEGKLA-----AEQELRKWR 556
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1578-1745 |
1.47e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1578 ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIrvvrlqlETTERQRGGAEDELQALRARAEEAEAQKRQA--QEEAER 1655
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------EDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1656 LRRQVqdESQRKRQAEAELALRvkaEAEAAREKQRAlqALDELKLQAEEAERRLRQAEAERARQVQvaletAQRSAEVEL 1735
Cdd:COG1579 94 LQKEI--ESLKRRISDLEDEIL---ELMERIEELEE--ELAELEAELAELEAELEEKKAELDEELA-----ELEAELEEL 161
|
170
....*....|
gi 1046896947 1736 QSKRASFAEK 1745
Cdd:COG1579 162 EAEREELAAK 171
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2960-2996 |
1.48e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.48 E-value: 1.48e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 2960 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEM 2996
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1883-2074 |
1.54e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1883 EQQRQLLEEELAR-LQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGRFR----ELA 1957
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAKAAAaakaKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1958 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE-RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrr 2036
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA----- 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 1046896947 2037 LEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTL 2074
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1460-1653 |
1.58e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1460 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1539
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1540 KAQAELEAR--ELQRRMQEEVTRREE---AAVDAQQQKRS----IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEE 1610
Cdd:COG3206 263 PVIQQLRAQlaELEAELAELSARYTPnhpDVIALRAQIAAlraqLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1046896947 1611 IRV---VRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEA 1653
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1835-2208 |
1.59e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1914
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1915 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAERVL 1992
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1993 TEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRRLEEQAAQhkadieerlaqlrkASESELERQKGLVED 2072
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKSQ--------------NGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2073 TLRQRRQVEEEimalkasfEKAAAGKAELELELGRIR-SNAEdtmrsKELAEQEAARQRQLAAEEEQRRREAEERVQRSL 2151
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 2152 AAEEEaaRQRKValEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2208
Cdd:pfam02029 293 LEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1639-1755 |
1.61e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.11 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1639 AEEAEAQKRQAQEEAErLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALdELKLQAEEAErrlrqaeaeraR 1718
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARAEAEA-AYEIAEANAE-----------R 277
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 1719 QVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQE 1755
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEA--EREEAELEADVRK 312
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1617-2023 |
1.65e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.53 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1617 QLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALD 1696
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1697 ELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAE 1776
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1777 AERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1856
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1857 LAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1936
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1937 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 2016
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
....*..
gi 1046896947 2017 EAENERL 2023
Cdd:COG5278 511 AAAEAAL 517
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1537-1751 |
1.80e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.70 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1537 AQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAqqveaAERSRMRIEEEIRvvrl 1616
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1617 qletterqrggaedelQALRARAEEAEAQKRQAQEEAERlrrQVQDESQRKRQAEAelalRVKAEAEAAREKQRALQALD 1696
Cdd:TIGR02794 120 ----------------QAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1697 ELKLQAEEAERRLRQ--AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1751
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2336-2630 |
1.87e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2336 RQKAQVEQELTTLRLQLeeTDHQKSiLDEE-------------LQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkA 2402
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQQA-LDVQqtraiqyqqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--E 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2403 RIEAENRaliLRDKDNTQRFLEEEAEKMKQVAEEaarlsVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKM 2473
Cdd:PRK04863 458 LLSLEQK---LSVAQAAHSQFEQAYQLVRKIAGE-----VSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2474 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEEtqgfqrtLEAERQRQLEMSAEAERLKLRMAE-MSRA 2552
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARA 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2553 QA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT-LVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQ-----EAK 2624
Cdd:PRK04863 603 PAwlAAQDALARLREQSGE--------EFEDSQDVTeYMQQLLERERELTVERDELAARKQALDEEIERLSQpggseDPR 674
|
....*.
gi 1046896947 2625 LLQLKS 2630
Cdd:PRK04863 675 LNALAE 680
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4083-4120 |
2.10e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.10e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1046896947 4083 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 4120
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2316-2501 |
2.66e-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: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2316 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSVRVQME 2395
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2396 ELGKLKARIEaenRAL-ILRDKDNT----QRFLEEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2467
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 1046896947 2468 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2501
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2333-2726 |
2.74e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2333 QTLRQKAQVE------QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRS----QVEEELFSVRVQMEELGKLKA 2402
Cdd:pfam15921 445 QMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdltaSLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2403 RIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedLAQQRALAEKMLKEKMQAVQEAT 2480
Cdd:pfam15921 525 RVDLKLQELQhLKNEGDHLRNVQTECEALKlQMAEKDKVIEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEKEIN 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2481 RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDA 2560
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2561 QRFRKQAEEIgeklhrtELATQEkvtlvqtLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQlkseEMQTVQQEQ 2640
Cdd:pfam15921 681 RNFRNKSEEM-------ETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ----KQITAKRGQ 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2641 IlqetQALQK--SFLSEKDSLLQRER-FIEQEKAKLEQLFQdEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRR-- 2715
Cdd:pfam15921 743 I----DALQSkiQFLEEAMTNANKEKhFLKEEKNKLSQELS-TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKas 817
|
410 420
....*....|....*....|.
gi 1046896947 2716 ----------QREAEEGVRRK 2726
Cdd:pfam15921 818 lqfaecqdiiQRQEQESVRLK 838
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1495-1745 |
3.04e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.33 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1495 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQA-------KAQAELEARELQRRMQEEVTRREEAAVD 1567
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEkesvaerKENNEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1568 AQQQK-RSIQEELQH---LRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLET----------------TERQRGG 1627
Cdd:pfam02029 132 ETEIReKEYQENKWStevRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKkvkyeskvfldqkrghPEVKSQN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1628 AEDELQALRARAEEAEAQKRQAQ----EEAERLRRQVQDESQRKRQAEAElalrvKAEAEAAREKQR-ALQALDELKLQA 1702
Cdd:pfam02029 212 GEEEVTKLKVTTKRRQGGLSQSQereeEAEVFLEAEQKLEELRRRRQEKE-----SEEFEKLRQKQQeAELELEELKKKR 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1703 -------EEAERRLRQAEAERarqvQVALETAQRSAEVELQSKRASFAEK 1745
Cdd:pfam02029 287 eerrkllEEEEQRRKQEEAER----KLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3288-3324 |
3.27e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.27e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 3288 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKET 3324
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
181-304 |
3.42e-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: 49.12 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 181 DERDRVQ--KKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSG--------DSLPRERDvirsvrlpr 250
Cdd:cd21222 9 EAPEKLAevKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGffvplheyHLTPSTDD--------- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 251 ekgrmrfHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 304
Cdd:cd21222 75 -------EKLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2420-2650 |
3.48e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.61 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2420 QRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2499
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2500 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2579
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 2580 ATQEKvtlvqtleIQRQQSDQDAERLREAIAELER-EKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2650
Cdd:pfam13868 191 AQQEK--------AQDEKAERDELRAKLYQEEQERkERQKEREEAEKKARQRQELQQAREEQIELKERRLAE 254
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2367-2651 |
3.71e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.11 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2367 QRLKAEVTEAARQRSQVEEELFSVRVQmeelgKLKARIEAENRALILRDKDNTQRFLEEEAE--KMKQVAEEAARLSVAA 2444
Cdd:pfam05667 220 QEWEEEWNSQGLASRLTPEEYRKRKRT-----KLLKRIAEQLRSAALAGTEATSGASRSAQDlaELLSSFSGSSTTDTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2445 QEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATrlkaeaelLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQ 2522
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQ--------QQREEELEelQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2523 RTLEAERQRQLEMSAEAE--RLKLRMAE--------MSRAQARAEEDAQRFRKQAEEIGEklHRT--------------- 2577
Cdd:pfam05667 367 QVEEELEELKEQNEELEKqyKVKKKTLDllpdaeenIAKLQALVDASAQRLVELAGQWEK--HRVplieeyralkeaksn 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2578 -ELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEA-------KLLQL-KSEEMQTVQQEQILQETQAL 2648
Cdd:pfam05667 445 kEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrsaytrRILEIvKNIKKQKEEITKILSDTKSL 524
|
...
gi 1046896947 2649 QKS 2651
Cdd:pfam05667 525 QKE 527
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
776-868 |
4.10e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.09 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 776 HGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQA 855
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1046896947 856 ALQTQWSWMLQLC 868
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1837-2062 |
4.80e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1837 EEQAVRQRELAEQELEK-QRQLAEgtAQQRL-AAEQELIRLRAETE--QGEQQRQLLEEELARLQHEATAATQKRQELEA 1912
Cdd:COG3206 163 EQNLELRREEARKALEFlEEQLPE--LRKELeEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1913 ELAKVRAEMEVLLASKARAEEeSRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1992
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1993 TEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESE 2062
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1494-1699 |
4.90e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 50.98 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1494 ISETLRRMEEEERLAEQQRAEERERLAEVEAALekqrqlaeahAQAKAQAELEARELqRRMQEEVTRREEAAVDAQQQKR 1573
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQAL----------AQVIANQKRLERQL-EELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1574 siqeelQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKR------ 1647
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKvneals 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 1648 -----QAQEEAERLRRQVQDESQRKrQAEAELALR--VKAEAEAAREKQRALQALDELK 1699
Cdd:COG1842 157 gidsdDATSALERMEEKIEEMEARA-EAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1977-2650 |
5.09e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1977 AEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdEAFQRRRLEEQAAQHKADIEERLAQLR 2056
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2057 KASESELERQKGLVEDT--LRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAA 2134
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2135 eeeqrrreaeervqrslaaEEEAARQRKVALEEVERLkakVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFV 2214
Cdd:PRK03918 346 -------------------KLKELEKRLEELEERHEL---YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2215 VQQREeelqqtlqqeqNMLERLRSEAEAARRAaeeaeeareqaereaaqsRKQVEEAERLKqsaeeqaqaqaqaqaaaek 2294
Cdd:PRK03918 404 EEEIS-----------KITARIGELKKEIKEL------------------KKAIEELKKAK------------------- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2295 lRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEeLQRLKAEVT 2374
Cdd:PRK03918 436 -GKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2375 EAARQRSQVEEELFsvRVQMEELGKLKARIEAENRALilRDKDNTQRFLEEEAEKMKQVAEEAARLsvaaqeaarLRQLA 2454
Cdd:PRK03918 514 KYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKEL--EKLEELKKKLAELEKKLDELEEELAEL---------LKELE 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2455 EEDLAQQRALAEKmLKEKMQAVQEATRLK-AEAELLQQQKELAQEQarrlqedkeqmaqqlveetqgfqRTLEAERQRQL 2533
Cdd:PRK03918 581 ELGFESVEELEER-LKELEPFYNEYLELKdAEKELEREEKELKKLE-----------------------EELDKAFEELA 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2534 EMSAEAERLKLRMAEMSRAQAraEEDAQRFRKQAEEIGEKLHRTElatqekvTLVQTLEIQRQQSDQDAERLREAIAELE 2613
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLR-------AELEELEKRREEIKKTLEKLKEELEERE 707
|
650 660 670
....*....|....*....|....*....|....*..
gi 1046896947 2614 REKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2650
Cdd:PRK03918 708 KAKKELEKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1509-1691 |
5.10e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1509 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRrmqeEVTRREEAAVDAQQQKRSIQEELQHLRqsSEA 1588
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1589 EIQAKAQQVEAAERSRMRIEEEIRVVRLQLETterqrggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1668
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 1046896947 1669 QAEAELALRVKAEAEAAREKQRA 1691
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRK 185
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1559-1702 |
5.33e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.97 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1559 TRREEAAVD-AQQQKRSIQEELQHLRQSS--EAEIQAKAQQVEAAERSRMRIEEEI-RVVRLQletteRQRGGAEDELQA 1634
Cdd:COG1566 78 PTDLQAALAqAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDE 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1635 LRARAEEAEAQKRQAQEEAERLRRQVQDESQrKRQAEAELalrvkAEAEAAREKqrALQALDELKLQA 1702
Cdd:COG1566 153 ARAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQ--AELNLARTTIRA 212
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1878-2208 |
5.54e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1878 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRleaeagrfrela 1957
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKR------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1958 eEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATR-LKTEAEIALKEKEAENERLRRLAEDEAFQRRR 2036
Cdd:pfam02029 72 -EERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKeEKRDSRLGRYKEEETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2037 LEEQAAQHKADIEERLAQLRKASESELErqkgLVEDTLRQRRQVEEE---IMALKASFEKAAAGKAELELELGRIRSNAE 2113
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVPTENFAKEE----VKDEKIKKEKKVKYEskvFLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2114 DTMRSkELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALeEVERLKAKVEEARRLRERAEQ--ESAR 2191
Cdd:pfam02029 227 QGGLS-QSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAEL-ELEELKKKREERRKLLEEEEQrrKQEE 304
|
330
....*....|....*..
gi 1046896947 2192 QLQLAQEAAQKRLQAEE 2208
Cdd:pfam02029 305 AERKLREEEEKRRMKEE 321
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1519-1931 |
5.81e-06 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 52.94 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1519 LAEVEAALEKQRQLAEAHAQAKaqaelEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1587
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAR-----EDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1588 --------AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQ 1659
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1660 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKR 1739
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1740 ASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADA 1819
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1820 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1899
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 1046896947 1900 ATAATQKRQELEAELAKVRAEMEVLLASKARA 1931
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1509-1906 |
6.11e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1509 EQQRAEERERLAEVEAALEKQR----QLAEAHAQAKAQAELEARELQRRM-------QEEVTRREEAAVDAQQQKRSIQE 1577
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRaqeqQLRQQLDQLKEQLQLLNKLLPQANlladetlADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1578 ELQHLR---------QSSEAEIQAKAQQVEAAERSRMRIEEEI--------RVVRLQLETTERQRGGAEDELQALRARAE 1640
Cdd:COG3096 915 HGKALAqleplvavlQSDPEQFEQLQADYLQAKEQQRRLKQQIfalsevvqRRPHFSYEDAVGLLGENSDLNEKLRARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1641 EAEAQKRQAQEEAERLRRQVQDESQR----------KRQAEAEL-----ALRVKAEAEAArekQRALQALDELKLQAEEA 1705
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVlaslkssrdaKQQTLQELeqeleELGVQADAEAE---ERARIRRDELHEELSQN 1071
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1706 ERRLRQAEAERARQvqvaletaqrSAEVELQSKRASFAEKTAQLERTLQEEHVtvtqlreeaerraqqqaeaerareeae 1785
Cdd:COG3096 1072 RSRRSQLEKQLTRC----------EAEMDSLQKRLRKAERDYKQEREQVVQAK--------------------------- 1114
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1786 relERW----QLKANEALRLRLQAEEVAQQkslaqaDAEKQKEEAerearrrgkaeEQAVRQRELAEQELEKQRQLAEGT 1861
Cdd:COG3096 1115 ---AGWcavlRLARDNDVERRLHRRELAYL------SADELRSMS-----------DKALGALRLAVADNEHLRDALRLS 1174
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1862 AQQR---------LAAEQEL-IRLRAETEQGEQQRQLLEE---ELARLQHEATAATQK 1906
Cdd:COG3096 1175 EDPRrperkvqfyIAVYQHLrERIRQDIIRTDDPVEAIEQmeiELARLTEELTSREQK 1232
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1597-1722 |
6.48e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.84 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1597 VEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRAR--------AEEAEAQKRQAQEEAERLRRQVQDEsqrkr 1668
Cdd:COG1193 520 IEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEkeeilekaREEAEEILREARKEAEELIRELREA----- 594
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1669 qaeaelalrvKAEAEAAREKQRALQALDElKLQAEEAERRLRQAEAERARQVQV 1722
Cdd:COG1193 595 ----------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKAKPAKPPEELKV 637
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1519-1613 |
6.52e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 52.65 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1519 LAEVEAALEKQRQLAEAHAQAKAQAELEARelqrRMQEEVTRREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKAQQV 1597
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAE----AQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 1046896947 1598 EAAERSRMRI---EEEIRV 1613
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1569-1715 |
6.59e-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: 50.69 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1569 QQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGA--EDELQALRARAEEAE 1643
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 1644 AQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAE 1715
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2314-2771 |
6.72e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2314 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILdeelqRLKAEVTEAARQRSQVEEELFSVRVQ 2393
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2394 MEELGKLKARIEA--ENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA---RLRQLAEE---DLAQQRALA 2465
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2466 EKMLKEKMQAVQEATRLKAEAELlQQQKELAQEQARRLQEDKEQMAQQLVEETQ-----------GFQRTLEAERQ---- 2530
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihlqeSAQSLKEREQQlqtk 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2531 -----RQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERL 2605
Cdd:TIGR00618 479 eqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2606 REAIAELEREKEKLKQEAKLLQLKSEEMQTVQQeqILQETQALQKSFLSEKDSLLQRERFIEQEKakleqlfQDEVAKAK 2685
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN--ITVRLQDLTEKLSEAEDMLACEQHALLRKL-------QPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2686 QLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAA 2765
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
....*.
gi 1046896947 2766 LAHSEE 2771
Cdd:TIGR00618 710 ETHIEE 715
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2338-2763 |
7.16e-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: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2338 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaEVTEAARQRSQVEEELFSVRVQMEELGKLKAriEAENRALILRDKD 2417
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2418 NTQ-RFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2492
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2493 ----KELAQEQARRLQEDKEQMaQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEmsraqaraEEDAQRFRKQAE 2568
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2569 EIGEKLHRTElatQEKVTLVQT-------LEIQRQQSDQDAERLREAIAEL--EREKEKLKQeaklLQLKSE-EMQTVQQ 2638
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQArekeihdLEIQLTAIKTSEEHYLKEVEDLktELEKEKLKN----IELTAHcDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2639 EQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVakakqlqeeqqRQQQQMEQEKQELVASMEEARRRQRE 2718
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM-----------NLRDELESVREEFIQKGDEVKCKLDK 570
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1046896947 2719 AEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2763
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1508-1936 |
7.22e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.22 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1508 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSE 1587
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1588 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1667
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1668 RQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1747
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1748 QLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAE 1827
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1828 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKR 1907
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 1046896947 1908 QELEAELAKVRAEMEVLLASKARAEEESR 1936
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1426-1757 |
7.22e-06 |
|
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: 52.32 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1426 QKFAKQYINAIKDYelqlitYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1504
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1505 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAR----------ELQRRMQE-EVTRREEAAVDAQQQKR 1573
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1574 SIQEELQHLRQSSEAEiQAKAQQVEAAERSRMRIEEE---IRVVRLQLETTERQRGGAEDELQALRARAEEAE-AQKRQA 1649
Cdd:NF033838 201 RDEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEakrRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEpATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1650 QEEAERLRRQVQDE-------SQRKRQAEAElalRVKAEAEAAREKQR-------ALQALDELKLQAEEAERRLRQAEA- 1714
Cdd:NF033838 280 ENDAKSSDSSVGEEtlpspslKPEKKVAEAE---KKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDVKVKEAELe 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1046896947 1715 ---ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1757
Cdd:NF033838 357 lvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1627-1906 |
7.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1627 GAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAE 1706
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1707 RRLRQAEAERARQVQVALETAQRSA-EVELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerraqqqaeaerareeae 1785
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYLKYLAPA----------------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1786 relerwqlkanealrLRLQAEEVAQQKslaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaqqr 1865
Cdd:COG4942 148 ---------------RREQAEELRADL---AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR------ 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1046896947 1866 laAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1906
Cdd:COG4942 204 --LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
314-421 |
7.66e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 47.88 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 314 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 392
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1046896947 393 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 421
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2320-2561 |
7.89e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2320 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGK 2399
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2400 LkARIEAENRAL-----ILRDKDNTQRFLEEeAEKMKQVAEEAARLsVAAQEAARlrqlaeEDLAQQRALAEKMLKEKMQ 2474
Cdd:COG3883 91 R-ARALYRSGGSvsyldVLLGSESFSDFLDR-LSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2475 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQA 2554
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
....*..
gi 1046896947 2555 RAEEDAQ 2561
Cdd:COG3883 242 AAASAAG 248
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2363-2582 |
8.31e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2363 DEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIlRDKDNTQRFLEEEAEKMKQVAEEAARLSV 2442
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2443 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM---A 2511
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaeL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 2512 QQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQ 2582
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1642-1852 |
8.64e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1642 AEAQKRQAQEEAERLRRQVQDESQRKRQAEaELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQ 1721
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1722 VALETAQRSAEVElqSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEaerelerwqlKANEALRL 1801
Cdd:PRK09510 140 KAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA----------KKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1802 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1852
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1560-1913 |
8.68e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1560 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARA 1639
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1640 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQ 1719
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1720 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1799
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1800 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1879
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 1046896947 1880 EQGEQQRQLLEEELARLQHEATAATQKRQELEAE 1913
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2325-2801 |
9.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2325 EKHKKFAEQTlRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEEL-G 2398
Cdd:COG4913 259 ELAERYAAAR-ERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2399 KLKARIEAENRAL--ILRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA 2475
Cdd:COG4913 338 DRLEQLEREIERLerELEERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2476 VQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM---------------------------AQQLVEETQG 2520
Cdd:COG4913 418 RRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervlggfALTLLVPPEH 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2521 FQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQS-- 2598
Cdd:COG4913 498 YAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA-ELGRRFDYVCVDSPEELRRHPra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2599 -----------------DQDAERL--------REAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKS 2651
Cdd:COG4913 577 itragqvkgngtrhekdDRRRIRSryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2652 FLSEKDsLLQRERFIEQEKAKLEQL--FQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEE 2729
Cdd:COG4913 657 SWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2730 LQRLEQQRQQQEKLLAEE----------NQRLRERLQ-RLEEEHRAALAHSEEIATSQAAATKALPNGRDALDgPSMEAE 2798
Cdd:COG4913 736 LEAAEDLARLELRALLEErfaaalgdavERELRENLEeRIDALRARLNRAEEELERAMRAFNREWPAETADLD-ADLESL 814
|
...
gi 1046896947 2799 PEY 2801
Cdd:COG4913 815 PEY 817
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2485-2771 |
9.77e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2485 EAELLQQQKELAQEQA----RRLQEDKEQMAQQLVEETQGfQRTLEAERQRQLEMS-----AEAERLKLRMAEMSRAQAR 2555
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQERLRQEKE-EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2556 AEEDAQRFRKQAEEI-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDqdaERLREAIAELEREKEKLKQEAKLLQLKSEEM 2633
Cdd:pfam17380 346 RERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2634 QTVQQEQILQETQALQKsFLSEKDSLLQRERFIEQEKA-KLEQLFQDEvakakqlqeeQQRQQQQMEqekqelvasMEEA 2712
Cdd:pfam17380 423 EQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQqQVERLRQQE----------EERKRKKLE---------LEKE 482
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 2713 RRRQREAEEgVRRKQEELQRLEQQRQQQekllaeENQRLRERLQRLEEEHRAALAHSEE 2771
Cdd:pfam17380 483 KRDRKRAEE-QRRKILEKELEERKQAMI------EEERKRKLLEKEMEERQKAIYEEER 534
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1867-1962 |
9.93e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 52.26 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1867 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1946
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 1046896947 1947 EAEAGRFrELAEEAAR 1962
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2321-2777 |
1.01e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2321 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEE-TDHQKSILDE-ELQRLKAEVTEAAR-----QRSQVEEELFSVRVQ 2393
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEElEEERDDLLAEaGLDDADAEAVEARReeledRDEELRDRLEECRVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2394 MEELGK----LKARI-EAENRALILRDKDNTqrfLEEEAEKMK-QVAEEAARLSVAAQEAARLRQL---AEEDLAQQRAL 2464
Cdd:PRK02224 337 AQAHNEeaesLREDAdDLEERAEELREEAAE---LESELEEAReAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2465 AEKMLKEKMQAVQEATRLKAEaelLQQQKELAQEQARRLQEDKEQMAQQLVEETqGFQRTLEAERQRQLEMSAEAERLKL 2544
Cdd:PRK02224 414 LEELREERDELREREAELEAT---LRTARERVEEAEALLEAGKCPECGQPVEGS-PHVETIEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2545 RMAEMSRAQARAEE------DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEK 2618
Cdd:PRK02224 490 EVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2619 LKQEAKLLQLKSEEM-QTVQQEQILQETQALQKSFLSEKDSLL-QRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQrqqq 2696
Cdd:PRK02224 570 AREEVAELNSKLAELkERIESLERIRTLLAAIADAEDEIERLReKREALAELNDERRERLAEKRERKRELEAEFDE---- 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2697 qmeqekqelvASMEEARRRQREAEE------GVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSE 2770
Cdd:PRK02224 646 ----------ARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYD 715
|
....*..
gi 1046896947 2771 EIATSQA 2777
Cdd:PRK02224 716 EAEELES 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1170-1641 |
1.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1170 KDPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAaptlrseleltLGKLEQVRSLSAIYLEKLKTIS 1249
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-----------YQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1250 LVIRSTQGAEEVLKTHEEHLKEAQAVPATLQEL--EVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRhgER 1327
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE--LE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1328 DVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAD--------PLSSWLQDAKSRQEQIQAVPIANSQ 1399
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlglLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1400 AAREQLRQEKaLLEEIERHGEKVEECQKFAKQYINAIKDYElQLITYKAQLEpvaspakkpkvqsgSESVIQEYVDLRTR 1479
Cdd:COG4717 311 PALEELEEEE-LEELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELE--------------EELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1480 YSELTTLTSqyikfiSETLRRMEEeerlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVT 1559
Cdd:COG4717 375 LLAEAGVED------EEELRAALE----QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1560 RREEAavDAQQQKRSIQEELQHLrqSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDE-LQALRAR 1638
Cdd:COG4717 445 EEELE--ELREELAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREErLPPVLER 520
|
...
gi 1046896947 1639 AEE 1641
Cdd:COG4717 521 ASE 523
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4085-4123 |
1.06e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.06e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 4085 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 4123
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1734-2055 |
1.12e-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: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1734 ELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1813
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1814 LAQADAEKQKEEAEREARRRGKAEEQ---AVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLE 1890
Cdd:pfam19220 101 EAEAAKEELRIELRDKTAQAEALERQlaaETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1891 EELARLQheataatqkrqeleaelaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1970
Cdd:pfam19220 174 QENRRLQ------------------ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1971 KRQRQlAEEDAARQRAEAervLTEKLAAiseATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 2050
Cdd:pfam19220 236 VEAHR-AERASLRMKLEA---LTARAAA---TEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER 308
|
....*
gi 1046896947 2051 RLAQL 2055
Cdd:pfam19220 309 RTQQF 313
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1483-1722 |
1.14e-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: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1483 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAELEARELQRrMQEEVTR 1560
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1561 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggAEDELQALRAR-A 1639
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1640 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA---REKQRALQALDELKLQAEEAerrlRQAEAER 1716
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrleREVEVARELYESLLQRLEEA----RLAEALT 384
|
....*.
gi 1046896947 1717 ARQVQV 1722
Cdd:COG3206 385 VGNVRV 390
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1873-2114 |
1.22e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.87 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1873 IRLRA-ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1945
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1946 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAervlteKLAAISEATRLKTEAEIALKEKEAenerlrr 2025
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKA------KKAAQQAANAEAEEEVDPKKAAVA------- 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2026 lAEDEAFQRRRLEEQAAQHKADIEERLAQLRKAS-ESELER---QKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAEL 2101
Cdd:PRK05035 584 -AAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAvAAAIARakaKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQ 662
|
250
....*....|...
gi 1046896947 2102 ELELGRIRSNAED 2114
Cdd:PRK05035 663 QQANAEPEEAEDP 675
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1938-2217 |
1.28e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1938 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA-EIALKEK 2016
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2017 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKAsfeKAAA 2096
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA---EREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2097 GKAELELELGRIRSNAEDTMRSKElaEQEAAR-QRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK- 2174
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKA--ERDELRaKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEe 255
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1046896947 2175 VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQ 2217
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2315-2524 |
1.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRSQVEEELFSVRV 2392
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2393 QMEELGKLKARIEAENRaLILRDKDNTQRFLEEEAE---KMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2469
Cdd:COG3883 110 GSESFSDFLDRLSALSK-IADADADLLEELKADKAEleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2470 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRT 2524
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1792-1988 |
1.31e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.03 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1792 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQE 1871
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1872 lirlrAETEQGEQQRQL-LEEELARLQHEATAATQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAE 1949
Cdd:COG2268 268 -----YEIAEANAEREVqRQLEIAEREREIELQEKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAE 339
|
170 180 190
....*....|....*....|....*....|....*....
gi 1046896947 1950 AGRFRELAEEAARLRALAEEAKRQRQLAEedAARQRAEA 1988
Cdd:COG2268 340 AEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEAAAKP 376
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2314-2616 |
1.37e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.84 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2314 LKQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRSQVEEELFSVRVQ 2393
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2394 MEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2472
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2473 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLVEETQGFQRT---LEAERQRQLEMSAEAERLKLRMAEM 2549
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2550 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDQDAERLREaiaELEREK 2616
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1171-1664 |
1.37e-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: 51.65 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1171 DPARECAQRIAEQQKAQAE-VEGLGKGVARLSAEAEKV-LALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLK-- 1246
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDIkMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNka 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1247 --TISLVIR----STQGAEEVLKTHEEHLKEAQavpatlQELEVTKASLKKLRAQAEAQQPVFNTLRDELrgaqevgERL 1320
Cdd:pfam05483 344 kaAHSFVVTefeaTTCSLEELLRTEQQRLEKNE------DQLKIITMELQKKSSELEEMTKFKNNKEVEL-------EEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1321 QQRHGERDV---EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQL-------RYYRESADPLSSWLQDAKSRQEQI 1390
Cdd:pfam05483 411 KKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseEHYLKEVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1391 QAVPIANSQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK------KPKVQS 1464
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevKCKLDK 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1465 GSESVIQEYVDLRTRYSELTTLTS------QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHA 1537
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKlELELASAKQ 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1538 QAKA-----QAELEAREL-QRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRmriEEEI 1611
Cdd:pfam05483 651 KFEEiidnyQKEIEDKKIsEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 1612 RVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1664
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1585-1756 |
1.38e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1585 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1662
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1663 -ESQRKRQAEAELAL------------RVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAErARQVQVALETAQR 1729
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180
....*....|....*....|....*..
gi 1046896947 1730 SAEVELQSKRASFAEKTAQLERTLQEE 1756
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1936-2102 |
1.40e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1936 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 2014
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2015 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasesELERQKGLVEDTLRQR--RQVEEEIMALKASFE 2092
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARHEAAVLI 175
|
170
....*....|
gi 1046896947 2093 KAAAGKAELE 2102
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1951-2197 |
1.40e-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: 51.05 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1951 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 2030
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2031 AFQRRRLEEQAAQHKADIEE------RLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELE 2104
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2105 LGRIRSN-AEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALeeverLKAKVEEARRLRE 2183
Cdd:pfam07888 194 FQELRNSlAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG-----LGEELSSMAAQRD 268
|
250
....*....|....*
gi 1046896947 2184 RAEQESAR-QLQLAQ 2197
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1550-2183 |
1.48e-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: 51.65 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1550 LQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAe 1629
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLC- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1630 DELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEAAREKQRALQALDELKLQAEEAERRL 1709
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL----RVQAENARLEMHFKLKEDHEKIQHLEEEYKK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1710 RQAEAERarqvQVALETAQrSAEVELQSKRASFaektaqlerTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELE 1789
Cdd:pfam05483 234 EINDKEK----QVSLLLIQ-ITEKENKMKDLTF---------LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1790 RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegTAQQRLaae 1869
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR----TEQQRL--- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1870 qelirlraetEQGEQQRQLLEEELARLQHEATAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1945
Cdd:pfam05483 373 ----------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKGKEQEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1946 LEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLkteaeialkekeaENERLRR 2025
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL-------------ENKELTQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2026 LAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEIMALKASFEKAA 2095
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARSIEYEVLKKE 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2096 AGKAELELELGRIRSNAEDTMRSKELAEQE--------AARQRQLAAEEEQRRREAEERVQRSLAAEE------EAARQR 2161
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQEnkalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEiidnyqKEIEDK 666
|
650 660
....*....|....*....|....*.
gi 1046896947 2162 KVA----LEEVERLKAKVEEARRLRE 2183
Cdd:pfam05483 667 KISeeklLEEVEKAKAIADEAVKLQK 692
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
214-301 |
1.51e-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: 47.44 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 214 LYEDLRDGHNLISLLEvlsgDSLPRERDVIRSVRLPRE-KGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKL 292
Cdd:cd21294 38 LFDECKDGLVLSKLIN----DSVPDTIDERVLNKPPRKnKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHL 113
|
....*....
gi 1046896947 293 TLGLIWTII 301
Cdd:cd21294 114 ILGLIWQII 122
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1629-1987 |
1.56e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1629 EDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA----EAEAAREKQRALQALDELKLQAEE 1704
Cdd:pfam13868 5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERAleeeEEKEEERKEERKRYRQELEEQIEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1705 AERRlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehvtvtqlreeaerraqqqaeaeraREEA 1784
Cdd:pfam13868 85 REQK-RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE-------------------------FNEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1785 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1864
Cdd:pfam13868 139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEI----------EEEKEREIARLRAQQEKAQDEKAERDELRA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1865 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAatQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ 1944
Cdd:pfam13868 209 KLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE--LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM 286
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1046896947 1945 RLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1987
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1808-2051 |
1.63e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.76 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1808 VAQQKSLAQADA--EKQKEEAEREARRRGKAEEQAVRQRelaeQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ 1885
Cdd:NF012221 1535 VATSESSQQADAvsKHAKQDDAAQNALADKERAEADRQR----LEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQ 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1886 RQLLEEELARLQHEATAATQKRQELEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEAGRF----R 1954
Cdd:NF012221 1608 RDAILEESRAVTKELTTLAQGLDALDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQ 1685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1955 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 2034
Cdd:NF012221 1686 KVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQA 1765
|
250
....*....|....*..
gi 1046896947 2035 RRLEEQAAQHKADIEER 2051
Cdd:NF012221 1766 QADAKGAKQDESDKPNR 1782
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3251-3287 |
1.66e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.66e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 3251 KLLSAEKAVTGYRDPYSGQSVSLFQALKKGLIPREQG 3287
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1640-1976 |
1.71e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1640 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQ 1719
Cdd:pfam15709 163 ETPASISHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1720 VQVALETA----QRSAEVELQSKRASFAEKTAQL------------------ERTLQEEHVTVTQLREEAERRAQQQAEA 1777
Cdd:pfam15709 243 LEVAAELSgpdvINSKETEDASERGAFSSDSVVEdpwlsskydaeesqvsidGRSSPTQTFVVTGNMESEEERSEEDPSK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1778 ERAREEAERELERWQLKANEALRLRLQAE----EVAQQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEK 1853
Cdd:pfam15709 323 ALLEKREQEKASRDRLRAERAEMRRLEVErkrrEQEEQRRLQQEQLERAEKM---------REELELEQQRRFEEIRLRK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1854 QRQLAEGTAQQRLAAEQELiRLRAETEQGEQQRQLLEEELARLQHE--------ATAATQKRQELEAELA---KVRAEMe 1922
Cdd:pfam15709 394 QRLEEERQRQEEEERKQRL-QLQAAQERARQQQEEFRRKLQELQRKkqqeeaerAEAEKQRQKELEMQLAeeqKRLMEM- 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1923 vllASKARAEEESRSTSEKSKQRLEAEAGRFRElaEEAARLraLAEEAKRQRQL 1976
Cdd:pfam15709 472 ---AEEERLEYQRQKQEAEEKARLEAEERRQKE--EEAARL--ALEEAMKQAQE 518
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1494-2210 |
1.85e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1494 ISETLRRMEEEERLAEQ-QRAEE-----RERLAEVEAALEKQR-QLAEAHAQAKaQAELEARELQRRMQEEVTRREEaav 1566
Cdd:PRK04863 333 ASDHLNLVQTALRQQEKiERYQAdleelEERLEEQNEVVEEADeQQEENEARAE-AAEEEVDELKSQLADYQQALDV--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1567 daqQQKRSIQ--------EELQHLRQSSE----------AEIQAKAQQVEAAERS---RMRIEEEIR---------VVRL 1616
Cdd:PRK04863 409 ---QQTRAIQyqqavqalERAKQLCGLPDltadnaedwlEEFQAKEQEATEELLSleqKLSVAQAAHsqfeqayqlVRKI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1617 --QLETTERQRGGAEDELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQ 1693
Cdd:PRK04863 486 agEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1694 ALDELKLQAEEA-ERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehvtVTQLREEAERRAQ 1772
Cdd:PRK04863 566 RLESLSESVSEArERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQD----VTEYMQQLLERER 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1773 QQAEAERAREEAERELERW-----QLKANEALRLRLQAEEV---------------------AQQKSLAQA----DAEKQ 1822
Cdd:PRK04863 642 ELTVERDELAARKQALDEEierlsQPGGSEDPRLNALAERFggvllseiyddvsledapyfsALYGPARHAivvpDLSDA 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1823 KEEAEREARRRG-----KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL-RAETEQGEQQRQLLEEELARL 1896
Cdd:PRK04863 722 AEQLAGLEDCPEdlyliEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLFgRAAREKRIEQLRAEREELAER 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1897 QHEATAATQKRQEL--------------------EAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR---LEAEA 1950
Cdd:PRK04863 802 YATLSFDVQKLQRLhqafsrfigshlavafeadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGlsaLNRLL 881
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1951 GRFRELAEE--AARLRALAEEAKRQRQlAEEDAARQRAEAERVltEKLAAI-----SEATRLKTEAEIALKEKEAENERL 2023
Cdd:PRK04863 882 PRLNLLADEtlADRVEEIREQLDEAEE-AKRFVQQHGNALAQL--EPIVSVlqsdpEQFEQLKQDYQQAQQTQRDAKQQA 958
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2024 RRLAedEAFQRRR--LEEQAAQ---HKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGK 2098
Cdd:PRK04863 959 FALT--EVVQRRAhfSYEDAAEmlaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQML 1036
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2099 AELELELGRIrsnaedTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERlkaKVEEA 2178
Cdd:PRK04863 1037 QELKQELQDL------GVPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLER---DYHEM 1107
|
810 820 830
....*....|....*....|....*....|...
gi 1046896947 2179 RRLRERAEQESARQLQLAQE-AAQKRLQAEEKA 2210
Cdd:PRK04863 1108 REQVVNAKAGWCAVLRLVKDnGVERRLHRRELA 1140
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1499-1672 |
1.89e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.72 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1499 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElearELQRRMQEEVTRREEAAVdAQQQKRSIQEE 1578
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE----ERQRQEEEERKQRLQLQA-AQERARQQQEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1579 LQHLRQsseaEIQAKAQQVE---AAERSRMRIEEEIRVVrlqlETTERQRGGAEDELQALRARAEEAEAQKRQAQEEaer 1655
Cdd:pfam15709 428 FRRKLQ----ELQRKKQQEEaerAEAEKQRQKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE--- 496
|
170
....*....|....*..
gi 1046896947 1656 lRRQVQDESQRKRQAEA 1672
Cdd:pfam15709 497 -RRQKEEEAARLALEEA 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2402-2772 |
2.34e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2402 ARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVA------AQEAARLR-QLAEEDLAQQRAL--AEKMLKEK 2472
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAesdleqDYQAASDHlNLVQTALRQQEKIerYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2473 MQAVQEATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLklrMAEMS 2550
Cdd:PRK04863 361 EERLEEQNEVVEEA---DEQQEENEARAEAAEEEVDELKSQLADYQQALdvQQTRAIQYQQAVQALERAKQL---CGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2551 RAQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVQTLeiqRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKS 2630
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEEL----LSLEQKLSVAQAA---HSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2631 EEMQTVQQEQILQETQALQKSFLSEKDSllqrERFIEQEKAKLEQLFQDEvakakqlqeeqqRQQQQMEQEKQELVASME 2710
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDE------------DELEQLQEELEARLESLS 571
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 2711 EARRRQREAEEGVRRKqeelQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEI 2772
Cdd:PRK04863 572 ESVSEARERRMALRQQ----LEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDV 629
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1800-1922 |
2.38e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 50.05 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1800 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQREL--AEQELEKQRQLAE---GTAQQRLAAEQELIR 1874
Cdd:COG1566 80 DLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLdlAQRELERYQALYKkgaVSQQELDEARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1046896947 1875 LRAETEQGEQQRQLLEEELaRLQHEATAATQKRQELEAELAKVRAEME 1922
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGL-REEEELAAAQAQVAQAEAALAQAELNLA 206
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1984-2374 |
2.46e-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: 50.89 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1984 QRAEAERVLTEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasESEL 2063
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2064 ERQKglVEDTLRQRRQVEEEIMALKASFEKaaagkaELE-LELGRIRSNaedtmrSKELAEQEAARQRQLAaeeeqrrre 2142
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2143 aeervqrslaaEEEAARQRKVALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQReee 2221
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK--- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2222 lqqtlqqeqnmleRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAeq 2301
Cdd:pfam17380 474 -------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA-- 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2302 eaarraqaeqaalKQKQAADAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT 2374
Cdd:pfam17380 539 -------------EEERRKQQEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2426-2585 |
2.97e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2426 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2505
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2506 DKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2585
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1600-1719 |
3.15e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.96 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1600 AERSRMRIEEEIRVVRLQLETTERQRggaedELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvK 1679
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQER-----LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQR---K 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1046896947 1680 AEAEAAREKQRALQALDELKLQAEEAERRLRQaEAERARQ 1719
Cdd:pfam05672 81 AEEEAEEREQREQEEQERLQKQKEEAEAKARE-EAERQRQ 119
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1871-2194 |
3.45e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1871 ELIRLRAETEQGEQQ--RQLLEEELARLQHEATAATQKRQeLEAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR 1945
Cdd:pfam05557 3 ELIESKARLSQLQNEkkQMELEHKRARIELEKKASALKRQ-LDRESDRNQElqkRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1946 LEAEAGRFRELAEEAARLRALAE----------EAKRQRQLAEEDAARQRAEAERV---LTEKLAAISEATRLKTEAEIA 2012
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREvisclknelsELRRQIQRAELELQSTNSELEELqerLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2013 LKEKEAENERLRRLAedeafQRRRLEEQAAQHKADIEERLAQLRKAsESELERQKGLVE---DTLRQRRQVEEEIMALKA 2089
Cdd:pfam05557 162 QSSLAEAEQRIKELE-----FEIQSQEQDSEIVKNSKSELARIPEL-EKELERLREHNKhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2090 S---FEKAAAGKAELELELGRIRSNAE-----DTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR 2161
Cdd:pfam05557 236 KlerEEKYREEAATLELEKEKLEQELQswvklAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
330 340 350
....*....|....*....|....*....|...
gi 1046896947 2162 KValEEVERLKAKVEEARRLRERAEqESARQLQ 2194
Cdd:pfam05557 316 LE--QELAQYLKKIEDLNKKLKRHK-ALVRRLQ 345
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1624-1822 |
3.50e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1624 QRGGAEDELQALRARAEEAEAQ-KRQAQEEAerlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALDELKLQA 1702
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVErKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1703 EEAER---RLRQAEAERARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLreeaerraqqqa 1775
Cdd:pfam15709 404 EEEERkqrLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM------------ 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1776 eaerareEAERELERWQLKANEALRLRLQAEEVAQQKS----LAQADAEKQ 1822
Cdd:pfam15709 472 -------AEEERLEYQRQKQEAEEKARLEAEERRQKEEeaarLALEEAMKQ 515
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3507-3545 |
3.51e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.47 E-value: 3.51e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 3507 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3545
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4542-4579 |
3.58e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.58e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1046896947 4542 QRFLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTA 4579
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2408-2772 |
3.63e-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: 50.34 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2408 NRALILRDKDNTQRflEEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2482
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2483 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLkLRMAE 2548
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2549 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQL 2628
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2629 KSEEMQTVQQEQILQEtqalqksfLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAkqlqeeqqrqqqqmeqekQELVAS 2708
Cdd:COG3096 505 RSQQALAQRLQQLRAQ--------LAELEQRLRQQQNAERLLEEFCQRIGQQLDAA------------------EELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2709 MEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQR------LRERLQRLEEEHRAALAHSEEI 2772
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEV 628
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3507-3542 |
3.65e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.65e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1046896947 3507 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3542
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2414-2569 |
3.94e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2414 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2490
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2491 QQKELAQEQARRLQEDKE---QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRaqaRAEEDAQRF---- 2563
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 1046896947 2564 -RKQAEE 2569
Cdd:pfam15709 512 aMKQAQE 518
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1466-1754 |
4.01e-05 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 49.83 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1466 SESVIQEyvDLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-A 1539
Cdd:pfam15450 219 AESSLRE--ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1540 KAQAELE-ARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVE------AAERSRMRIEEEir 1612
Cdd:pfam15450 295 KGQLEESqAGELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1613 VVRLQLETTERQRGGAEDE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRA 1691
Cdd:pfam15450 373 TLGLKLSEAKKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKAREFEVEA 452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 1692 lqaldelklqaeeaerrLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1754
Cdd:pfam15450 453 -----------------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4293-4321 |
4.10e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.10e-05
10 20
....*....|....*....|....*....
gi 1046896947 4293 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4321
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3174-3211 |
4.23e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.23e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1046896947 3174 RQALRGTSVIAGVWLEEAGQKLSIYEALRRDLLQPEVA 3211
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2409-2605 |
4.52e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2409 RALILRDKDNTQRFLEEEAEKMKQVAEEAarLSVAAQEAARLRQLAEEDLAQQRalaekmlkEKMQAVQEatRLKAEAEL 2488
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERR--------NELQKLEK--RLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2489 LQQQKELAQEQARRLQEDKEQMAQQL--VEETQGFQRTLEAERQRQLE----MSAEAERLKLrmaeMSRAQARAEEDAQR 2562
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQqeLEKKEEELEELIEEQLQELErisgLTAEEAKEIL----LEKVEEEARHEAAV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1046896947 2563 FRKQAEEIGEklhrtELATQE-KVTLVQTleIQRQQSDQDAERL 2605
Cdd:PRK12704 174 LIKEIEEEAK-----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2358-2761 |
4.55e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2358 QKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALilRDKDNTQRFLEEEAEKMKQVAEEA 2437
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA--SDHLNLVQTALRQQEKIERYQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2438 ARLSVAAQEAARLRQLAEEDLAQQRALAEkmlkekmQAVQEATRLKA------EAELLQQQKELAQEQA-RRLQEDKE-- 2508
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAE-------AAEEEVDELKSqladyqQALDVQQTRAIQYQQAvQALERAKQlc 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2509 QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlKLRMAEMSRAQAraEEDAQRFRKQAEEIGEklhrtELATQEKVTLV 2588
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQ-KLSVAQAAHSQF--EQAYQLVRKIAGEVSR-----SEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2589 QTLEIQRQQSDQdAERLREAIAELEREKEKLKQEAKLLQ----------LKSEEMQTVQQEQ-ILQETQALQKSFLSEKD 2657
Cdd:PRK04863 503 RRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQRAERLLAefckrlgknlDDEDELEQLQEELeARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2658 SLLQRERfiEQEKAKLEQLFQDEVA--KAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEgvrrkqeelqrleq 2735
Cdd:PRK04863 582 MALRQQL--EQLQARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTV-------------- 645
|
410 420
....*....|....*....|....*.
gi 1046896947 2736 qrqqqekllaeENQRLRERLQRLEEE 2761
Cdd:PRK04863 646 -----------ERDELAARKQALDEE 660
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1174-1723 |
4.59e-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: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1174 RECAQRIAEQQKAQA-EVEGLGKGVARLSAEAEkvlALPEPSPAAPTLRSELELTLGK-LEQVRSLSAIYLEKL-----K 1246
Cdd:pfam07111 86 RETSLQQKMRLEAQAmELDALAVAEKAGQAEAE---GLRAALAGAEMVRKNLEEGSQReLEEIQRLHQEQLSSLtqaheE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1247 TISLVIRSTQGAEEVLKTHE-EHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQPVFNTLRdelrgaQEVGERLQQRHG 1325
Cdd:pfam07111 163 ALSSLTSKAEGLEKSLNSLEtKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLR------KYVGEQVPPEVH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1326 ERDVEVERWR--ERVTQLLE---RWQAVLAQTDVRQREL--------EQLGRQLR--------YYRESADPLSSWLQDAK 1384
Cdd:pfam07111 237 SQTWELERQEllDTMQHLQEdraDLQATVELLQVRVQSLthmlalqeEELTRKIQpsdslepeFPKKCRSLLNRWREKVF 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1385 SRQEQIQAVPIANSQAAReQLRQEKALLEEierhgekveecQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQS 1464
Cdd:pfam07111 317 ALMVQLKAQDLEHRDSVK-QLRGQVAELQE-----------QVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSR 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1465 GSESviqeyvdlRTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAK 1540
Cdd:pfam07111 385 AQEA--------RRRQQQQTASAEEQLKFVvnamSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1541 AQAELEAR-----------ELQRRMQEEVTRREEAAVDAQQQ--KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRI 1607
Cdd:pfam07111 457 ALAQLRQEscpppppappvDADLSLELEQLREERNRLDAELQlsAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRA 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1608 EEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEA-----ERLRRQVQDESQ-----RKRQAEAELALR 1677
Cdd:pfam07111 537 QESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKvaeveTRLREQLSDTKRrlneaRREQAKAVVSLR 616
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1046896947 1678 vKAEAEAAREKQRAlQALDELKLQA--EEAERRLRQA-EAERARQVQVA 1723
Cdd:pfam07111 617 -QIQHRATQEKERN-QELRRLQDEArkEEGQRLARRVqELERDKNLMLA 663
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1123-1702 |
5.00e-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: 49.97 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1123 QQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKDPARECAQRIA-EQQKAQAEVEGLGKGVARLS 1201
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1202 AEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRSTQGAEEVLKTHEEHLKEAQAVpaTLQE 1281
Cdd:TIGR00618 421 DLQGQLAHA----------KKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1282 LEVTKASLKKLRAQAEAQQPVFNTLR---------DELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQT 1352
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1353 DVRQRELEQLGRQLRYYRESADPLSSWLQDAksrQEQIQAVPIANSQAAREQLRQEKALLEEIERHgEKVEECQKFAKQY 1432
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ-DVRLHLQQCSQEL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1433 INAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEERLAEQQR 1512
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM-LAQCQTLLRELETHIEEYDREF 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1513 AEERERLAEVEAALEKQRqlaEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQqkrsIQEELQHLRQSSEAEIQA 1592
Cdd:TIGR00618 721 NEIENASSSLGSDLAARE---DALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ----TGAELSHLAAEIQFFNRL 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1593 KAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAE 1671
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFlSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
570 580 590
....*....|....*....|....*....|.
gi 1046896947 1672 AELALRVKAEAEAAREKQRALQALDELKLQA 1702
Cdd:TIGR00618 874 LSDKLNGINQIKIQFDGDALIKFLHEITLYA 904
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1538-1694 |
5.40e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 48.57 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1538 QAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQ-------EELQHLRQSSEAEIQAKAQQVEAAER--SRMRIE 1608
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELaisrqdyDGATAQLRAAQAAVKAAQAQLAQAQIdlARRRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1609 EEIRVV-RLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALrvkAEAEAAR 1686
Cdd:pfam00529 133 APIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIaEAEAELKL---AKLDLER 209
|
....*...
gi 1046896947 1687 EKQRALQA 1694
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1475-1755 |
5.48e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1475 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAELEARELQRRM 1554
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1555 QEEVTRREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDE 1631
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1632 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEA 1705
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 1706 --ERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQE 1755
Cdd:pfam07888 316 dkDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1838-2159 |
6.47e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1838 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1917
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1918 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLA 1997
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1998 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR 2077
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2078 RQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEA 2157
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
..
gi 1046896947 2158 AR 2159
Cdd:COG4372 368 AD 369
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2441-2719 |
6.52e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2441 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmaQQLVEETQG 2520
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK----QQQLAAISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2521 FQRTLEAERQRQLEMSAEAERlklrmaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDQ 2600
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2601 DAE---RLREAIAE--LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSllqrerfiEQEKAKLEQ 2675
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1046896947 2676 LFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRR-QREA 2719
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1508-1639 |
6.89e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.51 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1508 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ---AKAQAELEARELQRRMQEevtrREEAAVDAQQqkrsiQEELQHLRQ 1584
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQAL----YKKGAVSQQE-----LDEARAALD 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 1585 SSEAEIQAKAQQVEAAeRSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARA 1639
Cdd:COG1566 159 AAQAQLEAAQAQLAQA-QAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1649-1943 |
7.12e-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: 48.61 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1649 AQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELKLQAEEAERRLRQAEAERArqvqvALETAQ 1728
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELA-----ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1729 RSAEVELQSKRASFAEKTAQLERTLQEehvtvtqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQAEEV 1808
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRA----------------------------------LYRLGRQPPLALLLSPEDF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1809 AQQKSLAQAdaekqkeeaereARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL 1888
Cdd:COG4942 132 LDAVRRLQY------------LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 1889 LEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK 1943
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3954-3990 |
7.40e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 7.40e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 3954 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3990
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2323-2773 |
7.99e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2323 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDE---ELQRLKAEVTEAARQRSQVEE---ELFSVRVQMEE 2396
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEErheLYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2397 LGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSvaaQEAARL------------------RQLAEED- 2457
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK---KEIKELkkaieelkkakgkcpvcgRELTEEHr 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2458 ---LAQQRALAEKMLKEKMQAVQEATRLKAEAE----LLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAE 2528
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRelekVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2529 RQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtLEIQRQQSDQDAE-RLRE 2607
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-ERLKELEPFYNEYlELKD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2608 AIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKSFlSEKDSLLQRERFIEQEK------AKLEQL--F 2677
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKrlEELRKELEELEKKY-SEEEYEELREEYLELSRelaglrAELEELekR 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2678 QDEVAKakqlqeeqqrqqqqmeqekqeLVASMEEARRRQREAEEGVRrkqeelqrleqqrqqQEKLLAEENQRLRERLQR 2757
Cdd:PRK03918 689 REEIKK---------------------TLEKLKEELEEREKAKKELE---------------KLEKALERVEELREKVKK 732
|
490
....*....|....*..
gi 1046896947 2758 LE-EEHRAALAHSEEIA 2773
Cdd:PRK03918 733 YKaLLKERALSKVGEIA 749
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2314-2532 |
8.46e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2314 LKQKQAA-DAEMEKHKKFAE-QTLRQ-KAQVEQELTTLRLQLEETDHQksildeelqrlkAEVTEAARQRSQVEEELFSV 2390
Cdd:NF012221 1551 AKQDDAAqNALADKERAEADrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2391 RVQMEELGKlkaRIEA----------------ENRALILRDK-----DNTQRFLEEEAEKMKQ--------VAEEAARLS 2441
Cdd:NF012221 1619 TKELTTLAQ---GLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSE 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2442 VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQlveETQGF 2521
Cdd:NF012221 1696 AGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAKGA 1772
|
250
....*....|.
gi 1046896947 2522 QRTLEAERQRQ 2532
Cdd:NF012221 1773 KQDESDKPNRQ 1783
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2045-2675 |
8.80e-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: 49.07 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2045 KADIEERLAQlRKASESELERQKGLVEDTLRQRrQVEEEIMALKASFEKAAAG-----KAELELELGRIRSNAEDTMRSK 2119
Cdd:pfam12128 199 KSMIVAILED-DGVVPPKSRLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEfntleSAELRLSHLHFGYKSDETLIAS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2120 ELAEQEA--ARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQ 2197
Cdd:pfam12128 277 RQEERQEtsAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2198 EAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEaarraaeeaeeareqaereaaqsrKQVEEAERLKQ- 2276
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLA------------------------KIREARDRQLAv 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2277 -SAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTT---LRLQL 2352
Cdd:pfam12128 413 aEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANaevERLQS 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2353 EET--DHQKSILDEELQRLKAEVTEAARQRSQVEEELFS--------VRVQM----EELGKLKARieaenrALILR---- 2414
Cdd:pfam12128 493 ELRqaRKRRDQASEALRQASRRLEERQSALDELELQLFPqagtllhfLRKEApdweQSIGKVISP------ELLHRtdld 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2415 ---DKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2491
Cdd:pfam12128 567 pevWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFART 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2492 QKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQLEmsAEAERLKLRMAEMSRAQAR--AEEDAQRFRKQAEE 2569
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ERLNSLE--AQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2570 IGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEqILQETQALQ 2649
Cdd:pfam12128 724 EGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE-VLRYFDWYQ 802
|
650 660
....*....|....*....|....*.
gi 1046896947 2650 KSFLSEKDSLLQRERFIEQEKAKLEQ 2675
Cdd:pfam12128 803 ETWLQRRPRLATQLSNIERAISELQQ 828
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1633-1871 |
8.88e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1633 QALRARAEEAEAQKRQAQEEAERLRRQVqDESQRKRQA--EAELALRVKAEAEAAREKQRALQA-LDELKLQAEEAERRL 1709
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1710 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREeaerraqqqaeaerareeaerele 1789
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA------------------------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1790 rwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELA--EQELEKQRQLAEGTAQQRLA 1867
Cdd:COG3206 299 --QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEE 376
|
....
gi 1046896947 1868 AEQE 1871
Cdd:COG3206 377 ARLA 380
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2329-2783 |
8.95e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.75 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2329 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAEN 2408
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2409 RALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2488
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2489 LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2568
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2569 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2648
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2649 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQE 2728
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2729 ELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKAL 2783
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1500-1687 |
9.27e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.46 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1500 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEEL 1579
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1580 QHLRQSSEAEIQAKAqqveaaersrmrieeeirvvrlqlETTERQRGGAEDELqALRARAEEAEAQKRqaQEEAERLRRQ 1659
Cdd:pfam05262 280 KREIEKAQIEIKKND------------------------EEALKAKDHKAFDL-KQESKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 1046896947 1660 VQDESQR-KRQAEAElalrVKAEAEAARE 1687
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1914-2071 |
9.32e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.33 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1914 LAKVRAEmevllASKARAE---EESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALAEEAKrqrqlaeeDAARQRAEAE 1989
Cdd:COG2268 194 IAEIIRD-----ARIAEAEaerETEIAIAQANREAEEAELEQEREIETaRIAEAEAELAKKK--------AEERREAETA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1990 RVLTEKLAAISEAtrlKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHK-ADIEERLAQLRKASESELERQKG 2068
Cdd:COG2268 261 RAEAEAAYEIAEA---NAEREVQRQLEIAEREREIELQEKEA-EREEAELEADVRKpAEAEKQAAEAEAEAEAEAIRAKG 336
|
...
gi 1046896947 2069 LVE 2071
Cdd:COG2268 337 LAE 339
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
182-307 |
1.04e-04 |
|
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: 44.98 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 182 ERDRVQKKTFTKWVNKHLIKHWraeaqrhISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSVRLPREKGRMRfhKLQ 261
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1046896947 262 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 307
Cdd:cd21329 70 NCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1926-2123 |
1.06e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1926 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLTEKLAAISEATRL 2005
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2006 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIM 2085
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1046896947 2086 ALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAE 2123
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2315-2627 |
1.06e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAADAE---MEKHKKFAEQTLRQKAqVEQEL-----------TTLRLQlEETDHQKSILDEELQRLKAE---VTEAA 2377
Cdd:COG3096 297 ARRQLAEEQyrlVEMARELEELSARESD-LEQDYqaasdhlnlvqTALRQQ-EKIERYQEDLEELTERLEEQeevVEEAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2378 RQRSQVEEELFSVRVQMEELGKLKARI-----EAENRAL----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA 2448
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYqqaldVQQTRAIqyqqAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2449 RLR-----QLAEEDLAQQR-----ALAEKMLKE--KMQAVQEATRL-------KAEAELLQQ---------QKELAQEQA 2500
Cdd:COG3096 455 EEVleleqKLSVADAARRQfekayELVCKIAGEveRSQAWQTARELlrryrsqQALAQRLQQlraqlaeleQRLRQQQNA 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2501 RRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE---EIGEKLHRT 2577
Cdd:COG3096 535 ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPawlAAQDALERL 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2578 ELATQEKVTLVQTLEIQRQQSdqdAERLREAIAE---LEREKEKLKQEAKLLQ 2627
Cdd:COG3096 615 REQSGEALADSQEVTAAMQQL---LEREREATVErdeLAARKQALESQIERLS 664
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1606-1751 |
1.07e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.74 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1606 RIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1685
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1686 REKQRAL-----QALDELKLQAEEAERRLRQAEAERaRQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1751
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKK-DTLKARAKAAKAQEKVNEALSGIDSDDATSALER 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2315-2762 |
1.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETdhqKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2394
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2395 EELGKLKARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2469
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSN-----IPARLLALRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2470 ------KEKMQAVQEA---TRLKAEAELLQQQKELAQEQARRLQED-----------------KEQMAQQL----VEETQ 2519
Cdd:COG4913 489 ltllvpPEHYAAALRWvnrLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcVDSPE 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2520 GFQRT--------------------------------LEAERQRQ-LEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2566
Cdd:COG4913 569 ELRRHpraitragqvkgngtrhekddrrrirsryvlgFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERRE 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2567 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---SDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQ 2643
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2644 ETQALQK--SFLSEKDSLLQRERFIEQekakLEQLFQDEVAKAKqlqeeqqrqqqqmeqeKQELVASMEEARRRQREAEE 2721
Cdd:COG4913 728 ELDELQDrlEAAEDLARLELRALLEER----FAAALGDAVEREL----------------RENLEERIDALRARLNRAEE 787
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1046896947 2722 GVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEH 2762
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
341-418 |
1.13e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.22 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 341 DNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 418
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
187-311 |
1.15e-04 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 45.42 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 187 QKKTFTKWVNKHL-----IKHWRAEAQRHISdLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSVRLPrekgrmrFHKLQ 261
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHVVPMNPTDES-LFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTISE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 262 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 311
Cdd:cd21323 96 NLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2318-2478 |
1.17e-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: 46.84 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2318 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQmEEL 2397
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2398 GKLKARIEAENRALILRDKDnTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2477
Cdd:COG1579 92 EALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
.
gi 1046896947 2478 E 2478
Cdd:COG1579 171 K 171
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2434-2885 |
1.19e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 48.43 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2434 AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2513
Cdd:COG4995 23 ALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALALALAAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2514 LVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2593
Cdd:COG4995 103 LAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2594 QRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKL 2673
Cdd:COG4995 183 LLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2674 EQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRE 2753
Cdd:COG4995 263 ALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2754 RLQRLEEEHRAALAHSEEIATSQAAATKALPNGRDALdgpsmeaepeytfEGLRQKVPAQQLQEAGILSMEELQRLTQGH 2833
Cdd:COG4995 343 ALLAAALAAALALAAALALALLAALLLLLAALLALLL-------------EALLLLLLALLAALLLLAAALLALAAAQLL 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 2834 TTVAELTQREDVHRYLKGGSSIAGLLLKP--TNEKLSVYTALQRQLLSPGTALI 2885
Cdd:COG4995 410 RLLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4123-4157 |
1.25e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.25e-04
10 20 30
....*....|....*....|....*....|....*
gi 1046896947 4123 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4157
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1955-2190 |
1.28e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1955 ELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRlaedeafQR 2034
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2035 RRLEEQAAQHKADIEERLAQLRKASESE----LERQKGlVEDTLRQRRQVEEEIMALKASFEKAAAGKAELElelgRIRS 2110
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPplalLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAELA----ALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2111 NAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESA 2190
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1087-1659 |
1.32e-04 |
|
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: 48.58 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1087 ELHYQAFLRDSQDAGGFGPEDRLvaEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLR 1165
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQF--SQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1166 LPLD-------------KDPARECAQRIAEQQKA-QAEVEGLGKgVARLSAEAEKVLAL-----PEPSPAAPTL----RS 1222
Cdd:pfam15921 419 RELDdrnmevqrleallKAMKSECQGQMERQMAAiQGKNESLEK-VSSLTAQLESTKEMlrkvvEELTAKKMTLesseRT 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1223 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEvLKTHEEHLKEAQavpatlqelevtkASLKKLRAQAEAQQPV 1302
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH-LKNEGDHLRNVQ-------------TECEALKLQMAEKDKV 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1303 FNTLRDELRG-AQEVGErlqqrHGerdveverwRERVTQLLERWQavlAQTDVRQRELEqlgrqLRYYRESADPLSSWLQ 1381
Cdd:pfam15921 564 IEILRQQIENmTQLVGQ-----HG---------RTAGAMQVEKAQ---LEKEINDRRLE-----LQEFKILKDKKDAKIR 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1382 DAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIERHGEKVEECQkfaKQYINAIKDYELQLITYKAQLEPVASPAKKPK 1461
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1462 VQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAHAQAKA 1541
Cdd:pfam15921 699 MQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA-------------MKVAMGMQKQITAKRGQIDA 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1542 qaelearelqrrMQEEVTRREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQL 1618
Cdd:pfam15921 746 ------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQelsTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1046896947 1619 ETTERQRGGAEDELQalraraeeaeaqkRQAQEEAeRLRRQ 1659
Cdd:pfam15921 814 DKASLQFAECQDIIQ-------------RQEQESV-RLKLQ 840
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2334-2566 |
1.33e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2334 TLRQKAQVEQELTTLRLQleetdhQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIL 2413
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2414 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2487
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 2488 LLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2566
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1580-2023 |
1.41e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1580 QHLRQSSEAEIQAKAQQVEA----------AERSRMRIEEEIRVVR--LQLETTERQRGGAE-DELQALRAR--AEEAEA 1644
Cdd:PRK10929 30 QELEQAKAAKTPAQAEIVEAlqsalnwleeRKGSLERAKQYQQVIDnfPKLSAELRQQLNNErDEPRSVPPNmsTDALEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1645 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAR---EKQRALQALDELKLQAEEAERRLRQAEAerarqvq 1721
Cdd:PRK10929 110 EILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQLTALQAES------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1722 valetAQRSAEVElqskrasfaektaqlertlqeehvtvtqlreeaerraqqqaeaerareeaerELERWQLKAN---EA 1798
Cdd:PRK10929 183 -----AALKALVD----------------------------------------------------ELELAQLSANnrqEL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1799 LRLRLqaeEVAQQKSlAQADAEKQKEeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAE 1878
Cdd:PRK10929 206 ARLRS---ELAKKRS-QQLDAYLQAL----------RNQLNSQRQRE-AERALESTELLAEQSGDLPKSIVAQFKINREL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1879 TEQGEQQRQLLeEELARLQHEATAATQK-RQELEA------ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEAG 1951
Cdd:PRK10929 271 SQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlreqsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1952 RFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAA---------------ISEATRLK---TEAEI 2011
Cdd:PRK10929 344 QLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLED 418
|
490
....*....|...
gi 1046896947 2012 ALKE-KEAENERL 2023
Cdd:PRK10929 419 ALKEvNEATHRYL 431
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1859-2208 |
1.47e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.98 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1859 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1938
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1939 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEA 2018
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2019 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGK 2098
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2099 AELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEA 2178
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350
....*....|....*....|....*....|
gi 1046896947 2179 RRLRERAEQESARQLQLAQEAAQKRLQAEE 2208
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAE 462
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1173-1865 |
1.47e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.26 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1173 ARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIyleKLKTISLVI 1252
Cdd:PRK10246 256 QQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHT---RQQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1253 RSTQGAEEVLKTHEEHLKEAQAVPATLQELevtkaslkklrAQAEAQQPVFNTLRDELRG-----AQEVGERLQQRhger 1327
Cdd:PRK10246 319 RLQSTMALRARIRHHAAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR---- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1328 dveveRWRERVTQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLSSWLQDAKSRQEQIQAvpiANSQAAR 1402
Cdd:PRK10246 384 -----QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNVTQ 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1403 EQLRQEKALLEEIERHGEKVEE-------CQKFAKqyinaIKDYElqliTYKAQLEPvASPAkkPKVQSGSESVIQEYVD 1475
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLE----AQRAQLQA-GQPC--PLCGSTSHPAVEAYQA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1476 LRtryselttltsqyikfISETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQAE----------L 1545
Cdd:PRK10246 523 LE----------------PGVNQSRLDALEKEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQEEqaltqqwqavC 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1546 EARELQRRMQEEVTRREEAAVDAQQQKRSIQEelQHLRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETterq 1624
Cdd:PRK10246 586 ASLNITLQPQDDIQPWLDAQEEHERQLRLLSQ--RHELQGQIAAHNQQIIQYQQQiEQRQQQLLTALAGYALTLPQ---- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1625 rggAEDELQALRARAEEAeAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEE 1704
Cdd:PRK10246 660 ---EDEEASWLATRQQEA-QSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQT 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1705 AERRLRQaEAERARQVQVALETAqrsaeveLQSKRasFAEKTAQLERTLQEEhvTVTQLREEAERRAQQQAEAERAREEA 1784
Cdd:PRK10246 736 LQQQDVL-EAQRLQKAQAQFDTA-------LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQT 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1785 ERELERWQLKANEALRLRLQAEEVAQQksLAQadaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQ 1864
Cdd:PRK10246 804 AQALAQHQQHRPDGLDLTVTVEQIQQE--LAQ---------------LAQQLRENTTRQGEIRQQ----LKQDADNRQQQ 862
|
.
gi 1046896947 1865 R 1865
Cdd:PRK10246 863 Q 863
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1537-2018 |
1.48e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1537 AQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrl 1616
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1617 qletterqRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlQALD 1696
Cdd:COG3064 78 --------KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAA-EAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1697 ELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAE 1776
Cdd:COG3064 149 AAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1777 AERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1856
Cdd:COG3064 229 SREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1857 LAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1936
Cdd:COG3064 309 GAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1937 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 2016
Cdd:COG3064 389 AGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKA 468
|
..
gi 1046896947 2017 EA 2018
Cdd:COG3064 469 VA 470
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1530-1899 |
1.48e-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: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1530 RQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEE 1609
Cdd:pfam13868 13 SKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1610 EirvvrlqlettERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ 1689
Cdd:pfam13868 93 Y-----------EEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1690 RALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQrsaevelqskrasfAEKTAQLERTLQEEHvtvtqlreeaer 1769
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK--------------AERDELRAKLYQEEQ------------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1770 raqqQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQ 1849
Cdd:pfam13868 216 ----ERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1850 ELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1899
Cdd:pfam13868 292 RRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3841-3877 |
1.49e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.49e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 3841 RYLYGTGSVAGVYLPGSRQTLTIYQALKKGLLSAEVA 3877
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1496-1718 |
1.54e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 47.67 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1496 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAELEARELQRRMQ-----EEVTRREEAA 1565
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQkregtEEVTEEEKAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1566 VDAQQQKRSIQEELQHLRQSSEAEIQAK-----AQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAE 1640
Cdd:PRK07735 93 AKAKAAAAAKAKAAALAKQKREGTEEVTeeekaAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1641 -EAEAQKRQAQEEAERlrRQVQDESQRKRQAEAELALRVKAEAEAAR-EKQRALQ----ALDELKLQAEEAERRLRQAEA 1714
Cdd:PRK07735 173 aKAKAAALAKQKAAEA--GEGTEEVTEEEKAKAKAKAAAAAKAKAAAlAKQKASQgngdSGDEDAKAKAIAAAKAKAAAA 250
|
....
gi 1046896947 1715 ERAR 1718
Cdd:PRK07735 251 ARAK 254
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1810-1956 |
1.64e-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: 46.74 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1810 QQKSLAQA--DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQR 1886
Cdd:pfam17045 101 QRKQLKEAreEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1887 QLLEEELARLQH-----EATAATQKRQELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1956
Cdd:pfam17045 181 QCLEASQSEIQRlrsklERAQDSLCAQELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
187-312 |
1.64e-04 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 45.05 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 187 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSVRLPrekgrmrFHK 259
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FII 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 260 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 312
Cdd:cd21325 94 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4432-4465 |
1.76e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.76e-04
10 20 30
....*....|....*....|....*....|....
gi 1046896947 4432 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4465
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1834-2212 |
1.80e-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: 47.70 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1834 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQHEATAATQK 1906
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1907 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1981
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1982 ARQRAEAERvlteklaaiSEATRL---KTEAEIA---------LKEKEAENERLRRLAEDEAFQRRR---LEEQAAQHKA 2046
Cdd:NF033838 209 AKAKVESKK---------AEATRLekiKTDREKAeeeakrradAKLKEAVEKNVATSEQDKPKRRAKrgvLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2047 DIEErlaqlrKASESELERQKgLVEDTLRQRRQVEEEIMALKASFEKAAAGKAE------------LELELGriRSNAED 2114
Cdd:NF033838 280 ENDA------KSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEIA--ESDVKV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2115 TMRSKELAEQEAARQRqlaaeeeqrrreaeervqrslaaEEEAARQRKvalEEVERLKA---KVEEARRLRERAEQESAR 2191
Cdd:NF033838 351 KEAELELVKEEAKEPR-----------------------NEEKIKQAK---AKVESKKAeatRLEKIKTDRKKAEEEAKR 404
|
410 420
....*....|....*....|.
gi 1046896947 2192 QLQLAQEAAQKRLQAEEKAHA 2212
Cdd:NF033838 405 KAAEEDKVKEKPAEQPQPAPA 425
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1120-1546 |
1.81e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1120 RHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKDPAR--ECAQRIAEQQKAQAEVEG 1192
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1193 LGKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEHLKEA 1272
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1273 QAVPATLQELEVTKAslkklRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVeveRWRERVTQLLERWQAVLAQT 1352
Cdd:COG4717 243 ERLKEARLLLLIAAA-----LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1353 DVRQRELEQLGRQLRYYRE-SADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQE-KALLEEIerHGEKVEECQKFAK 1430
Cdd:COG4717 315 ELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEA--GVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1431 QYiNAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISET---LRRMEEEERL 1507
Cdd:COG4717 393 QA-EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeaeLEQLEEDGEL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1046896947 1508 AE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELE 1546
Cdd:COG4717 472 AEllQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1547-1719 |
1.83e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.15 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1547 ARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqSSEAEIQAKAQQVeaaersrmrieeeirvvrlqlETTERQRG 1626
Cdd:COG3524 175 REDAVRFAEEEVERAEERLRDAREALLAFRNRNGIL--DPEATAEALLQLI---------------------ATLEGQLA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1627 GAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeaarekQRALQALDELKLQAEEAE 1706
Cdd:COG3524 232 ELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSL------------ASLLAEYERLELEREFAE 299
|
170
....*....|....*
gi 1046896947 1707 RRLRQAEA--ERARQ 1719
Cdd:COG3524 300 KAYTSALAalEQARI 314
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1541-1878 |
1.88e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1541 AQAELEARELQRRMQEEVTR--REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQl 1618
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRqkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1619 ETTERQRggaEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA--REKQRALQALD 1696
Cdd:pfam02029 81 EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKwsTEVRQAEEEGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1697 ELKLQAEEAERRLRQAEAERarqvQVALETAQRSAEVELQSKrASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAE 1776
Cdd:pfam02029 158 EEEDKSEEAEEVPTENFAKE----EVKDEKIKKEKKVKYESK-VFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1777 AERAREEAERELERWQlkANEALRLRLQA--EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQElekq 1854
Cdd:pfam02029 233 SQEREEEAEVFLEAEQ--KLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE---- 306
|
330 340
....*....|....*....|....
gi 1046896947 1855 RQLAEGTAQQRLaaEQELIRLRAE 1878
Cdd:pfam02029 307 RKLREEEEKRRM--KEEIERRRAE 328
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2382-2629 |
1.95e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2382 QVEEELFSVRVQMEELGKlkARIEAENRaliLRDKDNTQRFLEEEAEKMKQVAEEAARLsvAAQEAAR--LRQLAEedla 2459
Cdd:COG3096 438 NAEDYLAAFRAKEQQATE--EVLELEQK---LSVADAARRQFEKAYELVCKIAGEVERS--QAWQTARelLRRYRS---- 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2460 qQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQ--EDKEQMAQQLVEETQGFQRTLEAERQRQLEMSA 2537
Cdd:COG3096 507 -QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2538 EAERLKLRMAEMsRAQARAEEDAQ-RFRKQAEEIGEklhrtELATQEKVT--LVQTLEIQRQQSdQDAERLREAIAELER 2614
Cdd:COG3096 586 QLEQLRARIKEL-AARAPAWLAAQdALERLREQSGE-----ALADSQEVTaaMQQLLEREREAT-VERDELAARKQALES 658
|
250 260
....*....|....*....|
gi 1046896947 2615 EKEKLKQ-----EAKLLQLK 2629
Cdd:COG3096 659 QIERLSQpggaeDPRLLALA 678
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2848-2886 |
2.10e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.54 E-value: 2.10e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 2848 YLKGGSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALIL 2886
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2338-2765 |
2.13e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2338 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEaENRALILRDK 2416
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE-DLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2417 DNTQRFLEEEAEKMKQVAEEAARLSVAAQEAArLRQLAEEDLAQQRALAEKMLKEKMQAVQE----ATRLKAEAELLQQQ 2492
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2493 KELAQEQARRLQEDkeqmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2572
Cdd:PRK02224 351 ADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2573 KLH--RTELATQEKVT-----------------------LVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQ 2627
Cdd:PRK02224 427 REAelEATLRTARERVeeaealleagkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2628 LKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERfieQEKAKLEQLFQD--EVAKAKQLQEEQQRQQQQMEQEKQEL 2705
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEKRERAEELR---ERAAELEAEAEEkrEAAAEAEEEAEEAREEVAELNSKLAE 583
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2706 VASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRL---RERLQRLEEEHRAA 2765
Cdd:PRK02224 584 LKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLaekRERKRELEAEFDEA 646
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1275-1687 |
2.22e-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: 46.98 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1275 VPATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGaqevgerlqqrhgerdveverwrervtqLLERWQAVLAQTDV 1354
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAG----------------------------LTRRLSAAEGELEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1355 RQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEierhgekveecqkfAKQYIN 1434
Cdd:pfam19220 88 LVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREE--------------AQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1435 AIKDYELQLITYKAQLEPVAspAKKPKVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQ 1511
Cdd:pfam19220 154 ALQRAEGELATARERLALLE--QENRRLQALSEEQAAELAELTRRLAELETQldaTRARLRALEGQLAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1512 RAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqssEAEIQ 1591
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----EADLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1592 AKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqae 1671
Cdd:pfam19220 308 RRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQRER--- 384
|
410
....*....|....*.
gi 1046896947 1672 AELALrVKAEAEAARE 1687
Cdd:pfam19220 385 AERAL-AQGALEIARE 399
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1556-2040 |
2.22e-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: 47.70 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1556 EEVTRREEAAVDAQQQK--RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAED-EL 1632
Cdd:NF033838 53 NESQKEHAKEVESHLEKilSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQfKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1633 QALRARAEEAEAQK------RQAQEEAERLRRQVQDESQRKRQAE-AELALRVKaEAEAAREKQRALQALDELKLQAEEA 1705
Cdd:NF033838 133 DTLEPGKKVAEATKkveeaeKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1706 ERRLRQAEAERARQVQVALETAQRSAEvelqskrasfaektaqlertlqeehvtvtqlreeaerraqqqaeaerareeae 1785
Cdd:NF033838 212 KVESKKAEATRLEKIKTDREKAEEEAK----------------------------------------------------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1786 relERWQLKANEALRLRLQAEEVAQQKSLAQADAeKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1865
Cdd:NF033838 239 ---RRADAKLKEAVEKNVATSEQDKPKRRAKRGV-LGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAE--AEKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1866 LAAEQElirlRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQR 1945
Cdd:NF033838 313 VEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAK-------EPRNEEKIKQAKAKVESK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1946 LeAEAGRFrelaeeaarlralaEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRR 2025
Cdd:NF033838 382 K-AEATRL--------------EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEK 446
|
490
....*....|....*..
gi 1046896947 2026 LAEDEAFQ--RRRLEEQ 2040
Cdd:NF033838 447 PADQQAEEdyARRSEEE 463
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2318-2571 |
2.26e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2318 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ-----VEEELFSVRV 2392
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvareLLRRLREQRH 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2393 QMEELGKLKARI-EAENRaliLRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2471
Cdd:PRK04863 511 LAEQLQQLRMRLsELEQR---LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2472 KMQAVQEATRLKAEAELLQQqkelAQEQARRLQE---DKEQMAQQLveeTQGFQRTLEAERQRQLEMSAEAERLKLRMAE 2548
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLA----AQDALARLREqsgEEFEDSQDV---TEYMQQLLERERELTVERDELAARKQALDEE 660
|
250 260
....*....|....*....|...
gi 1046896947 2549 MSRAQARAEEDAQRFRKQAEEIG 2571
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAERFG 683
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1949-2058 |
2.28e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.64 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1949 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLTEKLAAISEATRLKTEAEIA-LKEKEAE 2019
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1046896947 2020 NERLRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA 2058
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKA 247
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1835-2050 |
2.33e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1906
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1907 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE-EAKRQRQLAEEDAARQR 1985
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARaKAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1986 AEAERVLTEKL-AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 2050
Cdd:PRK05035 607 VAEVDPKKAAVaAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1223-1757 |
2.36e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1223 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKthEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQPV 1302
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE--EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1303 FNTLRDELRgaQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQ-LGRQLRYYRESADPLSSWLQ 1381
Cdd:pfam02463 472 DLLKETQLV--KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1382 DAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIERHGEKVEecQKFAKQYINAIKDYE-LQLITYKAQLEPVASPAK-- 1458
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL--KSIAVLEIDPILNLAqLDKATLEADEDDKRAKVVeg 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1459 ------------KPKVQSGSESVIQEYVDLRTRYSELTTLTS---QYIKFISETLRRMEEEERLAE-----------QQR 1512
Cdd:pfam02463 628 ilkdteltklkeSAKAKESGLRKGVSLEEGLAEKSEVKASLSeltKELLEIQELQEKAESELAKEEilrrqleikkkEQR 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1513 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQA 1592
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1593 KAQQVEAAERS------RMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQ--AQEEAERLRRQVQDES 1664
Cdd:pfam02463 788 VEEEKEEKLKAqeeelrALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEEEITKEE 867
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1665 QRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAE 1744
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
570
....*....|...
gi 1046896947 1745 KTAQLERTLQEEH 1757
Cdd:pfam02463 948 KEKEENNKEEEEE 960
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2338-2522 |
2.44e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 46.42 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2338 KAQVEQELTTLRLQLEETDHQKsiLDEELQRLKAEVTEAarqrsqVEEELFSV----RVQMEELGKLKARIEAENRALIl 2413
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKR--CQALLQELSAPLEEK------ISQGSYSVpggyQLYLEDREKLVEKYRQVPRKGV- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2414 RDKDNTQRFLEEEA--------------EKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKM 2473
Cdd:cd16269 167 KAEEVLQEFLQSKEaeaeailqadqaltEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKM 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1046896947 2474 QavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLVEETQGFQ 2522
Cdd:cd16269 247 E--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1533-1748 |
2.60e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1533 AEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERsrmRIEEEIR 1612
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1613 VVRLQLETTERQrGGAEDELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDESQRKRQAEA 1672
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1673 ELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1748
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3917-3953 |
2.63e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.63e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 3917 RLLSAERAVTGYRDPYTEQPISLFQAMKKELIPAEEA 3953
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2393-2691 |
2.88e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2393 QMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2472
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2473 MQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMS 2550
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2551 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQlks 2630
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF--- 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 2631 EEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQ 2691
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2463-2685 |
2.91e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2463 ALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLVEETQGFQRTLEAE-RQRQLEMSAEAER 2541
Cdd:COG3883 12 AFADPQIQAKQKELSE---LQAELEAAQAELDALQAELEELNEEYNE-LQAELEALQAEIDKLQAEiAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2542 LKLRMAEMSRAQARAEEDAQRFrkQAEEIGEKLHRteLATQEKVTLVQTLEIQRQQSDQdaERLREAIAELEREKEKLKQ 2621
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLL--GSESFSDFLDR--LSALSKIADADADLLEELKADK--AELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 2622 EAKLLQLKSEEMQTVQQEQilqetQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAK 2685
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQ-----EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2315-2519 |
3.03e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAaDAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR----------S 2381
Cdd:PRK11281 50 KQKLL-EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslrqleS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2382 QVEE-------------------------------ELFSVRVQMEELGKLKARIEAENRALI--LRDKDNT-QRFLEEEA 2427
Cdd:PRK11281 129 RLAQtldqlqnaqndlaeynsqlvslqtqperaqaALYANSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAeQALLNAQN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2428 EKMKQVAEEAARLSVAAQE-----AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAElLQQQKELAQEQARR 2502
Cdd:PRK11281 209 DLQRKSLEGNTQLQDLLQKqrdylTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAAR-IQANPLVAQELEIN 287
|
250
....*....|....*..
gi 1046896947 2503 LqedkeQMAQQLVEETQ 2519
Cdd:PRK11281 288 L-----QLSQRLLKATE 299
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2460-2797 |
3.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2460 QQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLveETQGFQRTLEAERQRQLEMSAEA 2539
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2540 ERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvQTLEIQRQQSDQDAERLREAIAELEREKEKL 2619
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2620 KQEAKLLQLKSEEMQTVQQEQILQETQ----------------------------------ALQKSFLSEKDSLLQRERF 2665
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2666 IEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQrleqqrqqQEKLLA 2745
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--------IAALLA 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 2746 EENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKALPNGRDALDGPSMEA 2797
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE 429
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2595-2721 |
3.17e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2595 RQQSDQDAERLREAIAELEREKEKLKQEAKLLqlkseemqtvqqEQILQETQALQKSFLSEKDSLLQRErfiEQEKAKLE 2674
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAE 572
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1046896947 2675 QLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVAS--MEEARRRQREAEE 2721
Cdd:PRK00409 573 KEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAheLIEARKRLNKANE 621
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3214-3248 |
3.29e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.29e-04
10 20 30
....*....|....*....|....*....|....*
gi 1046896947 3214 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEM 3248
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1842-2102 |
3.48e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1842 RQREL------AEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqheataatqkrQELEAelA 1915
Cdd:COG0497 142 AQRELldafagLEELLEEYREAY----RAWRALKKELEELRADEAERARELDLLRFQL--------------EELEA--A 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1916 KVRAEMEVLLaskaraEEEsrstseksKQRLEAeAGRFRELAEEAarLRALAEEakrqrqlaEEDAARQRAEAERVLtEK 1995
Cdd:COG0497 202 ALQPGEEEEL------EEE--------RRRLSN-AEKLREALQEA--LEALSGG--------EGGALDLLGQALRAL-ER 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1996 LAAISE-----ATRLkTEAEIALKEKEAEnerLRRLAEDEAFQRRRLEEqaaqhkadIEERLAQLRKaseseLERQKGL- 2069
Cdd:COG0497 256 LAEYDPslaelAERL-ESALIELEEAASE---LRRYLDSLEFDPERLEE--------VEERLALLRR-----LARKYGVt 318
|
250 260 270
....*....|....*....|....*....|...
gi 1046896947 2070 VEDTLRQRRQVEEEIMALKASFEKAAAGKAELE 2102
Cdd:COG0497 319 VEELLAYAEELRAELAELENSDERLEELEAELA 351
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2353-2680 |
3.56e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2353 EETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDntqrfLEEEAEKMKQ 2432
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS-----KRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2433 VAEeaarlsvaaqeaaRLRQLAEEdlaqqralaEKMLKEKmqaVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2512
Cdd:PRK03918 264 LEE-------------RIEELKKE---------IEELEEK---VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2513 qLVEETQGFQRTL-EAErqrqlEMSAEAERLKLRMAEMSRAQARAEEDAQRFrkqaEEIGEKLHRTElatqekvtlvqtl 2591
Cdd:PRK03918 319 -LEEEINGIEERIkELE-----EKEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELE------------- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2592 EIQRQQSDQDAERLREAIAELEREKEKLKQE-----AKLLQLKSE-----------------------EMQTVQQEQILQ 2643
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEiskitARIGELKKEikelkkaieelkkakgkcpvcgrELTEEHRKELLE 455
|
330 340 350
....*....|....*....|....*....|....*..
gi 1046896947 2644 ETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDE 2680
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE 492
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1858-2354 |
3.66e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.16 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1858 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV----------RAEMEVLLAS 1927
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1928 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKT 2007
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2008 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAL 2087
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2088 KASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE 2167
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2168 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAA 2247
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2248 EEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKH 2327
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 1046896947 2328 KKFAEQTLRQKAQVEQELTTLRLQLEE 2354
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1891-2114 |
3.71e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1891 EELARLQHEATAATQKRQELEaelaKVRAEMEVLLASKARAEEESRSTSEKskQRLEAEAGRfrELAEEAARLralaeEA 1970
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRK----KKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQK--KQAEEAAKQ-----AA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1971 KRQRQlAEEDAARQRAEAervlteKLAAISEATRLKTEAEIALKEKEA-ENERLRRLAEDEAfQRRRLEEQAAQHKADIE 2049
Cdd:PRK09510 129 LKQKQ-AEEAAAKAAAAA------KAKAEAEAKRAAAAAKKAAAEAKKkAEAEAAKKAAAEA-KKKAEAEAAAKAAAEAK 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2050 ERLAQLRKASESELERQKGLVEdtlrQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAED 2114
Cdd:PRK09510 201 KKAEAEAKKKAAAEAKKKAAAE----AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1852-2125 |
3.83e-04 |
|
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: 46.39 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1852 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK 1928
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1929 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1988
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1989 ErvLTEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLRKASES 2061
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 2062 ELERQKGLVEDTLRQRrqVEEEIMAlkasfekaaagKAELELELGRIRsnaedtmrsKELAEQE 2125
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEETEDA-----------KNKLEWQLKKTL---------QEIAELE 278
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2315-2622 |
3.92e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2394
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2395 EELGKLKArieaenralILRDKdntqrFLEEEAEKmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQ 2474
Cdd:pfam15905 132 LELTRVNE---------LLKAK-----FSEDGTQK---------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2475 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQA 2554
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2555 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQE 2622
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1562-1974 |
3.96e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1562 EEAAvdAQQQKRSIQEELQHLRQSSEAEIQAKaQQVEAAERSrmrIEEEIRVVrlqlettERQRGGAEDELQALRARAEE 1641
Cdd:pfam02029 4 EEEA--ARERRRRAREERRRQKEEEEPSGQVT-ESVEPNEHN---SYEEDSEL-------KPSGQGGLDEEEAFLDRTAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1642 AEAQKRQAQEEAERLRRQVQDESQrkrQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQ 1721
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIA---DEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1722 VALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVtvtqlreeaerraqqqaeaerareeaereleRWQLKANEALRL 1801
Cdd:pfam02029 148 EVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKI-------------------------------KKEKKVKYESKV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1802 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAeeqavrqrelaeqelekQRQLAEGTAQQRLAAEQELIRLRaeteq 1881
Cdd:pfam02029 197 FLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLS-----------------QSQEREEEAEVFLEAEQKLEELR----- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1882 geQQRQLLEEElarlqhEATAATQKRQELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEAGRfRELAEEAA 1961
Cdd:pfam02029 255 --RRRQEKESE------EFEKLRQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAERKLREEEEK-RRMKEEIE 323
|
410
....*....|...
gi 1046896947 1962 RLRALAEEaKRQR 1974
Cdd:pfam02029 324 RRRAEAAE-KRQK 335
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1632-1721 |
4.02e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1632 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEaarekQRALQALDELKLQAEEAERRLRQ 1711
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90
....*....|
gi 1046896947 1712 AEAERARQVQ 1721
Cdd:PRK00409 596 LQKGGYASVK 605
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1908-2093 |
4.05e-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: 45.30 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1908 QELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrleaeagrFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1987
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDE------------------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1988 AERvLTEKLAAISEATrlktEAEIALKEKEAeNERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQK 2067
Cdd:COG1579 75 IKK-YEEQLGNVRNNK----EYEALQKEIES-LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....*.
gi 1046896947 2068 GLVEDTLRQRRQVEEEIMALKASFEK 2093
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1588-1721 |
4.18e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.82 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1588 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1667
Cdd:PRK12678 53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1668 RQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQ 1721
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAE 186
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2336-2767 |
4.21e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.67 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2336 RQKAQVEQELTTLRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALI 2412
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2413 LRDKDNTQRFLEEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2491
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2492 QKELAQEQARRLQEDKEQMAQQLVEE--TQGFQ----RTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRK 2565
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAEVEVERmsAKGLQmelsRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2566 QAEEIG----------EKLHRTELATQEKVTLVQTleiqRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSE-EMQ 2634
Cdd:pfam07111 427 AVARIPslsnrlsyavRKVHTIKGLMARKVALAQL----RQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQlSAH 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2635 TVQQE--------------------QILQETQALQKSFLS---EKDSLLQRERFIEQEKAKLEQ-LFQDEVAKAKQLQEE 2690
Cdd:pfam07111 503 LIQQEvgrareqgeaerqqlsevaqQLEQELQRAQESLASvgqQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2691 QQRQQQQMEQEKQELVASMEEARRRQREAEEGVR----RKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAL 2766
Cdd:pfam07111 583 VAEVETRLREQLSDTKRRLNEARREQAKAVVSLRqiqhRATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLML 662
|
.
gi 1046896947 2767 A 2767
Cdd:pfam07111 663 A 663
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1499-1755 |
4.23e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1499 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAELEarelqrrmqeevtrREEAAVDAQQQKRSIQE 1577
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1578 ELQhLRQSSEAEIQAKAQQVEAAERSR----MRI--------------EEEIRVVRLQLETTERQ---RGGAEDEL-QAL 1635
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARvdleAKIeslkeelaflkknhEEEVRELQAQVSDTQVNvemDAARKLDLtSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1636 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA-LDELKLQAEEAERRLRQAEA 1714
Cdd:pfam00038 173 AEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIeLQSLKKQKASLERQLAETEE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1046896947 1715 ERARQvqvaLETAQRSaeveLQSKRASFAEKTAQLERTLQE 1755
Cdd:pfam00038 253 RYELQ----LADYQEL----ISELEAELQETRQEMARQLRE 285
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1839-2750 |
4.27e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1839 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVR 1918
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1919 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1990
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1991 VLTEKLAAISEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---AQHKADIEERLAQLRKASESELERQK 2067
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2068 GLVEDTLRQRRQVEEEIMALK---ASFEKAAAG-KAELELELGRIRSNAEDTMRSKE-LAEQEAARQRQLAAEEEQRRRE 2142
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKfviKELQQLEGSsDRILELDQELRKAERELSKAEKNsLTETLKKEVKSLQNEKADLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2143 AEervqrSLAAEEEAARQRKVALEEVERL-KAKVEEARRLRERAEQESARQLQLAQEAAQKRlQAEEKAHAF-----VVQ 2216
Cdd:TIGR00606 517 LR-----KLDQEMEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKskeinQTR 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2217 QREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLR 2296
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFIT 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2297 KEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEA 2376
Cdd:TIGR00606 671 QLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK-STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2377 ARQRSQVEEELFSVRVQMEELGKLKARIEAENRA--LILRDKDNTQRFLEEEAEKMKQVAEEAARL-----SVAAQEAAR 2449
Cdd:TIGR00606 750 RNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakVCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQ 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2450 LRQLAEEDL---AQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQedkeQMAQQLVEETQGFQRTLE 2526
Cdd:TIGR00606 830 EKQEKQHELdtvVSKIELNRKLIQDQQEQIQH---LKSKTNELKSEKLQIGTNLQRRQ----QFEEQLVELSTEVQSLIR 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2527 AERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQT-LEIQRQQSDQDAERL 2605
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTV 982
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2606 REAIAELEREKEKLKQEAKLLQLKSEEMQtvQQEQILQETQALQKsfLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAK 2685
Cdd:TIGR00606 983 NAQLEECEKHQEKINEDMRLMRQDIDTQK--IQERWLQDNLTLRK--RENELKEVEEEL-----KQHLKEMGQMQVLQMK 1053
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2686 QLQeeqqrqqqqmeqekQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQR 2750
Cdd:TIGR00606 1054 QEH--------------QKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1835-2215 |
4.40e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 KAEEQAVRQRELAEQElekQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEElarlqheataATQKRQELEAEL 1914
Cdd:COG3064 9 AAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE----------AEQRAAELAAEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1915 AKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTE 1994
Cdd:COG3064 76 AKKLAE-----AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1995 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTL 2074
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2075 RQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAE 2154
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 2155 EEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVV 2215
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3543-3578 |
4.47e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.47e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1046896947 3543 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3578
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2886-2919 |
4.51e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.51e-04
10 20 30
....*....|....*....|....*....|....
gi 1046896947 2886 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2919
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1500-1616 |
4.53e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1500 RMEEEERLAEQQRAEERERLAEVEA---ALEKQ-RQLAEAHAQAKAQAELEARELQRRMQEEV------TRREEAAVDAQ 1569
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKlkeELEEKkEKLQEEEDKLLEEAEKEAQQAIKEAKKEAdeiikeLRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1046896947 1570 QQKRSIQEELQHLRQSSeaEIQAKAQQVEAAERSRMRIEEEIRVVRL 1616
Cdd:PRK00409 604 VKAHELIEARKRLNKAN--EKKEKKKKKQKEKQEELKVGDEVKYLSL 648
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1330-1570 |
4.58e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1330 EVERWRERVTQLLERWQAVLAQTDVRQREL------EQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAARE 1403
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFdptiadEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1404 QLRQ-----EKALLEEIERHGEKVEECQKFAKQyinAIKDYELQLITYKAQLEPVASPAK---------KPKVQSGSESV 1469
Cdd:pfam02029 140 YQENkwsteVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVfldqkrghpEVKSQNGEEEV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1470 IQEYVDLRTRYSELTTL--TSQYIKFISETLRRMEE--------EERLAEQQRAEERERLAEVEAAL---EKQRQLAEAH 1536
Cdd:pfam02029 217 TKLKVTTKRRQGGLSQSqeREEEAEVFLEAEQKLEElrrrrqekESEEFEKLRQKQQEAELELEELKkkrEERRKLLEEE 296
|
250 260 270
....*....|....*....|....*....|....*...
gi 1046896947 1537 AQAKAQAELEAR----ELQRRMQEEVTRREEAAVDAQQ 1570
Cdd:pfam02029 297 EQRRKQEEAERKlreeEEKRRMKEEIERRRAEAAEKRQ 334
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1252-1937 |
4.82e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1252 IRSTQGAEEVLKTHEEHLKEAQAVPATLQE-LEVTKASLKKLRAQAEAQqpvFNTLRDELRGAQEVG-ERLQQRHGERDV 1329
Cdd:pfam12128 250 FNTLESAELRLSHLHFGYKSDETLIASRQEeRQETSAELNQLLRTLDDQ---WKEKRDELNGELSAAdAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1330 EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEK 1409
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1410 AL-LEEIERHGEKVE-ECQKFAKQYINAIKDYELQLITYKAQL-----EPVASPAKKPKVQSGSESVIQEYVDLRTRYSE 1482
Cdd:pfam12128 407 DRqLAVAEDDLQALEsELREQLEAGKLEFNEEEYRLKSRLGELklrlnQATATPELLLQLENFDERIERAREEQEAANAE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1483 LTTLTSqyikfisetlrrmeeEERLAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQA------------------ 1543
Cdd:pfam12128 487 VERLQS---------------ELRQARKRRDQASEALRQASRRLEERQSaLDELELQLFPQAgtllhflrkeapdweqsi 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1544 -ELEARELQRR--MQEEVTrreEAAVDAQQQKRSIQEELQHLR----QSSEAEIQAKAQQVE----AAERSRMRIEEEIR 1612
Cdd:pfam12128 552 gKVISPELLHRtdLDPEVW---DGSVGGELNLYGVKLDLKRIDvpewAASEEELRERLDKAEealqSAREKQAAAEEQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1613 VVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKRQAEAE---LALRVKAEAEAAREK 1688
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAnERLNSLEAQlkqLDKKHQAWLEEQKEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1689 QRALQALDELKLQAEEAER-----RLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEEHVTVTQL 1763
Cdd:pfam12128 709 KREARTEKQAYWQVVEGALdaqlaLLKAAIAARRSGAKAELKALETWYKRDLASLGVD-PDVIAKLKREIRTLERKIERI 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1764 REEAERRAQQQAEAErareeaerelERWQLkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQ 1843
Cdd:pfam12128 788 AVRRQEVLRYFDWYQ----------ETWLQ---RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1844 RELAEQELEKQRQLAEGTAQQRLAAEQElirlRAETEQGEQQRQlLEEELARLQHEATAATQKRQELEAELAKVRAEMEV 1923
Cdd:pfam12128 855 QVRLSENLRGLRCEMSKLATLKEDANSE----QAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLA 929
|
730
....*....|....
gi 1046896947 1924 LLASKARAEEESRS 1937
Cdd:pfam12128 930 ETWESLREEDHYQN 943
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1981-2192 |
4.88e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1981 AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE 2060
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2061 SELERQKGLVEDTLR--QRRQVEEEIMALKASFEKAAAGKA---------ELELELGRIRSNAEDTMRSKELAEQEAARQ 2129
Cdd:COG4942 97 AELEAQKEELAELLRalYRLGRQPPLALLLSPEDFLDAVRRlqylkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2130 RQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQ 2192
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2452-2682 |
5.08e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 46.09 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2452 QLAEEDLAQQRALAEKMLKEKmqavqeatrlkaEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2531
Cdd:COG4487 18 SLYADIVKQRRAEFEKELAER------------LADAAKREAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2532 QLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtLVQTLEIQRQQsdqdaerlreaiaE 2611
Cdd:COG4487 86 ALAVAEEKEK---ELAALQEALAEKDAKLAELQAKELELLKKERELEDAKRE---AELTVEKERDE-------------E 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 2612 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQetqalqksflsekdsllQRERFIEQEKAKLEQLFQDEVA 2682
Cdd:COG4487 147 LDELKEKLKKEEEEKQLAEKSLKVAEYEKQLK-----------------DMQEQIEELKRKKEQGSTQLQG 200
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1835-1978 |
5.15e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLEEELARLQHEATAATQKRQELEAE 1913
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLLELQAESAAVESSGQSRAEALAEAE 726
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 1914 LAKVRAEMEVLLAS-KARAEE-ESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALAE-EAKRQRQLAE 1978
Cdd:PTZ00491 727 ARLIEAEAEVEQAElRAKALRiEAEAELEKLRKRQELELEYEQAQNElEIAKAKELADiEATKFERIVE 795
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2329-2496 |
5.45e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.61 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2329 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRSQVEEELFSVRVQMEEL----------- 2397
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALrsylspnspqv 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2398 GKLKARIEAenralilrdkdntqrfLEeeaekmKQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAV 2476
Cdd:COG3524 252 RQLRRRIAA----------------LE------KQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAAL 309
|
170 180
....*....|....*....|
gi 1046896947 2477 QEAtrlKAEAEllQQQKELA 2496
Cdd:COG3524 310 EQA---RIEAA--RQQRYLA 324
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2043-2461 |
5.69e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2043 QHKADIEERLAQlRKASESELERQKGLVEDTLRQ---RRQVEEEIMALKASFEKAAAGKAELElELGRIRSNAEDTMRSK 2119
Cdd:pfam17380 279 QHQKAVSERQQQ-EKFEKMEQERLRQEKEEKAREverRRKLEEAEKARQAEMDRQAAIYAEQE-RMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2120 ElaeqeaaRQRQLaaeeeqrrreaeervqrslaaeeEAARQRKVALE-----EVERLKAKvEEARRLRERAEQESARQLQ 2194
Cdd:pfam17380 357 E-------RKREL-----------------------ERIRQEEIAMEisrmrELERLQME-RQQKNERVRQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2195 LAQEAAQKRLQAEEKAHAFVvqqreeelqqtlqqeqnmlerlrseaeaarraaeeaeeareqaereaaqsRKQVEEAERl 2274
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQI--------------------------------------------------RAEQEEARQ- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2275 kqsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQaadaEMEKHKKFAEQTLRQKAQVEQElttLRLQLEE 2354
Cdd:pfam17380 435 ------------------REVRRLEEERAREMERVRLEEQERQQ----QVERLRQQEEERKRKKLELEKE---KRDRKRA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2355 TDHQKSILDEELQRLKAEVTEAARQRSQVEEElfsvrvqMEELGKlkaRIEAENRALILRDKDNTQRFLEEE---AEKMK 2431
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRKLLEKE-------MEERQK---AIYEEERRREAEEERRKQQEMEERrriQEQMR 559
|
410 420 430
....*....|....*....|....*....|
gi 1046896947 2432 QVAEEAARLSVAAQEAARLRQLAEEDLAQQ 2461
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2847-2883 |
6.06e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.06e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 2847 RYLKGGSSIAGLLLKPTNEKLSVYTALQRQLLSPGTA 2883
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1838-2033 |
6.08e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1838 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1914
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1915 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAE-AGRFRELAEEAARLRALAEEAKRQRQLAE 1978
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQiAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 1979 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 2033
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1589-1738 |
6.20e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1589 EIQAKAQQVEAAERSrMRIEEEIRvvrlqlETTERQRggAEDELQALRARAEEAEAQ-KRQAQEEAERLRRQVQDESQRK 1667
Cdd:PTZ00491 658 EITTKSQEAAARHQA-ELLEQEAR------GRLERQK--MHDKAKAEEQRTKLLELQaESAAVESSGQSRAEALAEAEAR 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1668 R-QAEAEL--------ALRVKAEAEAAREKQRALQALDELKLQAE---EAERRLRQAEAERARQVQVAL--ET--AQRSA 1731
Cdd:PTZ00491 729 LiEAEAEVeqaelrakALRIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATKFERIVEALgrETliAIARA 808
|
....*..
gi 1046896947 1732 EVELQSK 1738
Cdd:PTZ00491 809 GPELQAK 815
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1471-1611 |
6.49e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1471 QEYVDLRTRYSELTTLtsqyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAREL 1550
Cdd:COG1579 38 DELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1551 QrrMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEI 1611
Cdd:COG1579 114 E--LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1575-1910 |
6.50e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1575 IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAE 1654
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1655 RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVE 1734
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1735 LQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1814
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1815 AQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1894
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|....*.
gi 1046896947 1895 RLQHEATAATQKRQEL 1910
Cdd:COG4372 324 LAKKLELALAILLAEL 339
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1489-1683 |
6.60e-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: 45.29 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1489 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEevtrreeaavda 1568
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKE------------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1569 QQQKRSIQEELQHLRQSSEAEIQAKAQQvEAAERSRMRIEEEiRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQ 1648
Cdd:pfam13868 224 REEAEKKARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 1046896947 1649 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1683
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1792-2087 |
6.66e-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: 45.29 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1792 QLKANEALRLRLQAEEVAQQKslaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQ--ELEKQRQLA-EGTAQQRLAA 1868
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDE---MMEEERERALEEEEEKEEERKEERKRYRQELEEQieEREQKRQEEyEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1869 EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKvRAEMEVLLASKARAEEESRSTSEKSKQRLEA 1948
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEER-EEDERILEYLKEKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1949 EAGRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE 2017
Cdd:pfam13868 183 EREIARLRAQqekaqdekaerDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEE 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 2018 AEN--ERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAL 2087
Cdd:pfam13868 263 FERmlRKQAEDEEIEQEEAEKRRMKRLEHRRElekqIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1493-1709 |
6.78e-04 |
|
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: 44.29 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1493 FISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTR-REEAAVDAQQQ 1571
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKgNEELAREALAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1572 KRSIQeelqhlrqsseaeiqakaQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQE 1651
Cdd:pfam04012 92 KKSLE------------------KQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1652 EAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQaLDELKLQAEEAERRL 1709
Cdd:pfam04012 154 LGSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1864-2019 |
6.97e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1864 QRLAAEQELIRlRAETEQGEQQRQLlEEELARLQHEATAATQKRQELEAELAkvraEMEVLLASKARAEEESRSTSEKSK 1943
Cdd:PRK00409 495 KRLGLPENIIE-EAKKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1944 QRLEAEAgrfrelaeEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 2019
Cdd:PRK00409 569 EEAEKEA--------QQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
187-311 |
7.32e-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: 43.07 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 187 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSVRLPrekgrmrFHK 259
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTI 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 260 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 311
Cdd:cd21324 94 QENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1509-1610 |
7.73e-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: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1509 EQQRAEERERLAEVEAALEKQRQLAEAHAQAkaqaelEARELQRRMQEEVTRREEaaVDAQQQKRSIQEELQHLRQSSEA 1588
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100
....*....|....*....|..
gi 1046896947 1589 EIQAKAQQVEAAERSRMRIEEE 1610
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEA 270
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2364-2572 |
8.28e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2364 EELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKM-----KQVAEEAA 2438
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2439 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLV 2515
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 2516 EETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2572
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1502-1757 |
8.62e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1502 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEA----------------------RELQRRMQEEVT 1559
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELkpsgqggldeeeafldrtakreERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1560 RREEAAVDAQQQKRSIQEELQHlRQSSEAEIQAKAQQVeaaERSRMRIEEEirvvrlqlETTERQRGGAEDELQALRARA 1639
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKEN-NEEEENSSWEKEEKR---DSRLGRYKEE--------ETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1640 EEAEAQKRQAQEEAERLRRQV-QDESQRKRQAEAELALRVKAEAEAAREK-------QRALQALDELKLQAEEAERRLRQ 1711
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRghpevksQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1712 AEAERARQVQVaLETAQRSAEVELQSKRASFAE----KTAQLERTLQEEH 1757
Cdd:pfam02029 233 SQEREEEAEVF-LEAEQKLEELRRRRQEKESEEfeklRQKQQEAELELEE 281
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1555-1703 |
8.75e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.82 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1555 QEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAeiqAKAQQVEaaersrmrIEEEIRVVRLQLETTERQRGGAEDELQ- 1633
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLES---TKSQLQE--------SEQLIAELRSELASLKESNSLAETQLKc 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1634 ------ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE-LALRVKAEAEAAREKQRALQALDELKLQAE 1703
Cdd:pfam05911 749 maesyeDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKcLELQEQLERNEKKESSNCDADQEDKKLQQE 825
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2366-2579 |
8.95e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2366 LQRLKAEVTEAARQRSQVEEElfsvrvQMEELGKLKARIEAENRALilrdkdNTQRFLEEEAEKMkqvAEEAARLSVAAQ 2445
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL------EKERLAAQEQKKQ---AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2446 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLVEETQGFQRT 2524
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2525 LEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2579
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1583-1762 |
8.96e-04 |
|
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: 44.72 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1583 RQSSEAEIQAKAQQVEA-AERSRMRIE-EEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERlRRQV 1660
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1661 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSK-- 1738
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTei 212
|
170 180
....*....|....*....|....
gi 1046896947 1739 RASFAEKTAQLERTLQEEHVTVTQ 1762
Cdd:pfam00529 213 RAPVDGTVAFLSVTVDGGTVSAGL 236
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1482-1721 |
9.13e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 45.75 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1482 ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAELEarELQRRMQE-EVTR 1560
Cdd:pfam13779 517 ELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEM-TQQDLQRMLDRIEELARSGRRAEAQQMLS--QLQQMLENlQAGQ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1561 REEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQAL 1635
Cdd:pfam13779 594 PQQQQQQGQSEMQQAMDELGDLLReqqqlLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEAL 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1636 RARAEEAEAQKRQAQEEAERLRRQVQ-DESQRKRQA-----EAELALRVKAEAEAAREKQRALQALdelklqaEEAERRL 1709
Cdd:pfam13779 674 GDLAERQQALRRRLEELQDELKELGGkEPGQALGDAgramrDAEEALGQGDLAGAVDAQGRALEAL-------RKGAQQL 746
|
250
....*....|..
gi 1046896947 1710 RQAEAERARQVQ 1721
Cdd:pfam13779 747 AEAMQQQQGQGQ 758
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1628-1695 |
9.42e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.42 E-value: 9.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1628 AEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR-----KRQAEAELA-LRVKAEAEAAREKQRALQAL 1695
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKikeeiLAEAKEEAErILEQAKAEIEQEKEKALAEL 115
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2336-2662 |
9.94e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 45.28 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2336 RQKAQVEQELTTLRLQ-LEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVrVQMEE---LGKLKARIEAEN-RA 2410
Cdd:pfam15964 285 QHEAVLAQTHTNVHMQtIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQA-VQMTEeanFEKTKALIQCEQlKS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2411 LILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAEKMLKEKMQAVQEATrlKAEAELL 2489
Cdd:pfam15964 364 ELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE--EAQKQLA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2490 QQQKELAQEQAR-RLQEDKEQMAQqlvEETQGFQRTLEAERQRQLEMS-AEAERLKL-------RMAEMSRAQARAEEDA 2560
Cdd:pfam15964 442 SQEMDVTKVCGEmRYQLNQTKMKK---DEAEKEHREYRTKTGRQLEIKdQEIEKLGLelseskqRLEQAQQDAARAREEC 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2561 QRFrkqAEEIGEKLHRTELATQEKVTLVQTL----EIQRQQSDQDAERLREAIAELEREKE------------------K 2618
Cdd:pfam15964 519 LKL---TELLGESEHQLHLTRLEKESIQQSFsneaKAQALQAQQREQELTQKMQQMEAQHDktvneqyslltsqntfiaK 595
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1046896947 2619 LKQEAKLLQLKSEEMQTVQQEQILQETQalQKSFLSEKDSLLQR 2662
Cdd:pfam15964 596 LKEECCTLAKKLEEITQKSRSEVEQLSQ--EKEYLQDRLEKLQK 637
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1878-2010 |
1.06e-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: 44.99 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1878 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1957
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1958 EEAARLRA-------------LAEEAKRQRQLAEEDAARQRAEAERVlTEKLAAISEATRLKTEAE 2010
Cdd:pfam05262 287 QIEIKKNDeealkakdhkafdLKQESKASEKEAEDKELEAQKKREPV-AEDLQKTKPQVEAQPTSL 351
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1640-1719 |
1.06e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1640 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL----RVKAE--AEAAREKQRALQA-LDELKLQAEEAERRLRQA 1712
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAqqqeLVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 1046896947 1713 EAERARQ 1719
Cdd:PRK11448 218 RKEITDQ 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2450-2624 |
1.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2450 LRQLAEEDLAQQRALAEKMLKEkmqavqeatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAER 2529
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE------------AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2530 QRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAI 2609
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEA 171
|
170
....*....|....*.
gi 1046896947 2610 AELEREKEKL-KQEAK 2624
Cdd:PRK12704 172 AVLIKEIEEEaKEEAD 187
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2343-2624 |
1.14e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2343 QELTTLRLQLEETDHQKSILDEELQRLKaevteaaRQRSQVEEELFSVRVQMEEL-GKLKARIEAENRALILRDKDNtqr 2421
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELK-------EKRDELNEELKELAEKRDELnAQVKELREEAQELREKRDELN--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2422 fleEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEkmLKEKMQAVQ-----EATRLKAEAELLQQQKEL 2495
Cdd:COG1340 71 ---EKVKELKEERDELnEKLNELREELDELRKELAELNKAGGSIDK--LRKEIERLEwrqqtEVLSPEEEKELVEKIKEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2496 AQE-QARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRA--QARAEEDA--QRFRKQAEEI 2570
Cdd:COG1340 146 EKElEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEadELRKEADElhKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 2571 gEKLHRTELATQEKVTLVQTlEIQRQQSDQDAERLREAIAELEREKEKLKQEAK 2624
Cdd:COG1340 226 -DELHEEIIELQKELRELRK-ELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1632-1731 |
1.16e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1632 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEsQRKRQAEAElALRVKAEAEAAREKQRALQALDelklqaEEAERR 1708
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 1046896947 1709 LRQAEAERARQVQVALETAQRSA 1731
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1497-1673 |
1.17e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1497 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ---------LAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVD 1567
Cdd:PRK12678 45 GMRKGELIAAIKEARGGGAAAAAATPAAPAAAARRaaraaaaarQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1568 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEirvvrlqlETTERQRGGAEDELQALRARAEEAEAQKR 1647
Cdd:PRK12678 125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREER 196
|
170 180
....*....|....*....|....*.
gi 1046896947 1648 QAQEEAERLRRQVQDESQRKRQAEAE 1673
Cdd:PRK12678 197 GRDGDDRDRRDRREQGDRREERGRRD 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2155-2639 |
1.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2155 EEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahAFVVQQREEELQQTLQQEQNMLE 2234
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ----LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2235 RLRSEaeaarraaeeaeeareqaereaaqsRKQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2314
Cdd:COG4717 150 ELEER-------------------------LEELRELEE--------------------ELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2315 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA-EVTEAARQRSQVEEELFSVRVQ 2393
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2394 MEELGKLKARIE---AENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQ---LAEEDLAQQRALAEK 2467
Cdd:COG4717 265 GGSLLSLILTIAgvlFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2468 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAqQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2547
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2548 EMSRAQarAEEDAQRFRKQAEEIGEKL--HRTELATQEkvtlvqtLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKL 2625
Cdd:COG4717 424 ALDEEE--LEEELEELEEELEELEEELeeLREELAELE-------AELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
490
....*....|....
gi 1046896947 2626 LQLKSEEMQTVQQE 2639
Cdd:COG4717 495 LKLALELLEEAREE 508
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1796-2018 |
1.19e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 45.23 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1796 NEALRLRLQ-AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--LAEGTAQQRLAAEQEl 1872
Cdd:COG5283 9 DKPFKSALEsAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQalDQAGIDTRQLSAAQR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1873 iRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVRAEME-----VLLASKARAEEESRSTSEKSKQRLE 1947
Cdd:COG5283 88 -RLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQR-LAGAGAAAAaigaaLAASVKPAIDFEDAMADVAATVDLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1948 AEAGRFRELAEEA----ARLRALAEE-AKRQRQLAEEDAARQRAEAervLTEKLAAISEATRLKTE--AEIALKEKEA 2018
Cdd:COG5283 166 KSSEQFKALGKQArelsAQTPQSADDiAAGQAALAQAGVSAEDILA---FTPTAAKLATAFDTDAEeaAEIAAKILNA 240
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1612-1763 |
1.21e-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: 44.36 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1612 RVVRLQLETTERQRGGAEDELQALRA-----RAEEAEAQKrQAQEEAERLRRQVQDesqRKRQAEAELALRVKAEAEAAR 1686
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGqiqqlRTELQELEA-QQQEEAESSREQLQE---LEEQLATERSARREAEAELER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1687 EKQRALQALDELKLQAEEAERRLRQAEAERARQ-VQVALETAQRSAEVELQSK----RASFAEKTAQLERTLQEEHVTVT 1761
Cdd:pfam09787 119 LQEELRYLEEELRRSKATLQSRIKDREAEIEKLrNQLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVL 198
|
..
gi 1046896947 1762 QL 1763
Cdd:pfam09787 199 QL 200
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1886-2198 |
1.22e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1886 RQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1965
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1966 LAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 2045
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2046 ADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQE 2125
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2126 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2198
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
182-307 |
1.23e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.90 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 182 ERDRVQKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSVRLPREKGRMRfhKLQ 261
Cdd:cd21330 9 EGETREERTFRNWMNS-------LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1046896947 262 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 307
Cdd:cd21330 77 NCNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2335-2632 |
1.23e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2335 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIeaenralil 2413
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2414 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2493
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2494 ELAQEQARRLQEDKEQMAQQLVEET--QGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIG 2571
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2572 EKLHR--TELAT--QEKVTLVQTL-EIQRQQS---------------------------DQDAERLREAIAELEREKEKL 2619
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRNMEmlngqsvcpvcgttlgeeksnhiinhyNEKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 1046896947 2620 KQEAKllQLKSEE 2632
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1878-2100 |
1.25e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.97 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1878 ETEQGEQQRQLLEEELARLQ-----------HEATAATQKRQELEAELAKVRAEMEV-----LLASKARAEEESRSTSEK 1941
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHgaeiskleeenREKEKALPKNDDMTIEEAKRRAAAAAkakaaALAKQKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1942 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--AARQRAEAERVLTEKLAAISEATRLKTEAEIAL---KEK 2016
Cdd:PRK07735 91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAkaAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKakaKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2017 EAENERLRRLAEDEAFQRRRLEEQAAQH-KADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEE-IMALKASFEKA 2094
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEeKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKaIAAAKAKAAAA 250
|
....*.
gi 1046896947 2095 AAGKAE 2100
Cdd:PRK07735 251 ARAKTK 256
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1499-1669 |
1.26e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1499 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElEARELQRRMQEEVTRREEAAVDAQQQKRSIQEE 1578
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPE-AAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1579 LQHLRQSSEAEIQAKAQQVEAAERSRMRieeeiRVVRLQLETTERQRGGaEDELQALRARAEEAEAQKRQAQEEAERLRR 1658
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 1046896947 1659 QVQDESQRKRQ 1669
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1617-2080 |
1.28e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1617 QLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR--VKAEAEAAREKQRALQA 1694
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKklAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1695 LDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehVTVTQLREEAERRAQQQ 1774
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA--RAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1775 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1854
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1855 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1934
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1935 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 2014
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 2015 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQV 2080
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2039-2212 |
1.28e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2039 EQAAQHKADIEERLAQLRKASESELERQKGLVED-TLRQRRQVEEEIMALKASfEKAAAgKAELELELGRIRSNAEdtmr 2117
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQANREAEEaELEQEREIETARIAEAEA-ELAKK-KAEERREAETARAEAE---- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2118 sKELAEQEAARQRQLAAEEeqrrreaeervqrslaaeEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQ 2197
Cdd:COG2268 266 -AAYEIAEANAEREVQRQL------------------EIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
170
....*....|....*.
gi 1046896947 2198 -EAAQKRLQAEEKAHA 2212
Cdd:COG2268 327 aEAEAIRAKGLAEAEG 342
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1640-1757 |
1.33e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1640 EEAeaqKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQ 1719
Cdd:PRK00409 505 EEA---KKLIGEDKEKLNELIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046896947 1720 VQVALETAQRSAEVELQSKRASFAEKTAQL-ERTLQEEH 1757
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVkAHELIEAR 613
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2316-2589 |
1.38e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2316 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVR 2391
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2392 VQMEELGKL-----KARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRAL 2464
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2465 AEKMLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDK--EQMAQQLVEETQGFQRTLEAERQRQLEMSAEAER 2541
Cdd:pfam13868 213 EEQERKERQKEREEAeKKARQRQELQQAREEQIELKERRLAEEAerEEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1046896947 2542 LKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2589
Cdd:pfam13868 293 RELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1396-1658 |
1.40e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1396 ANSQAAREQLRQEkalLEEIE-----RHGEKVEECQ-------------KFAKQYINAIKDYELQLITYKAQLEPVASPA 1457
Cdd:PRK10929 19 AATAPDEKQITQE---LEQAKaaktpAQAEIVEALQsalnwleerkgslERAKQYQQVIDNFPKLSAELRQQLNNERDEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1458 KKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEA 1535
Cdd:PRK10929 96 RSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1536 HAQAK---AQAELEARELQ-----------------RRMQEEVTRREEAAVDAQQQkrSIQEELQHLRQsSEAEiqakaq 1595
Cdd:PRK10929 170 LAQAQltaLQAESAALKALvdelelaqlsannrqelARLRSELAKKRSQQLDAYLQ--ALRNQLNSQRQ-REAE------ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1596 qvEAAERSRMRIEEEIRVVRLQLETTERQRggaedEL-QALRARAEEAE---AQKRQAQEEAERLRR 1658
Cdd:PRK10929 241 --RALESTELLAEQSGDLPKSIVAQFKINR-----ELsQALNQQAQRMDliaSQQRQAASQTLQVRQ 300
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2497-2685 |
1.41e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 43.50 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2497 QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigEKLHR 2576
Cdd:pfam15665 13 EAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE--RELKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2577 TELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKL-LQLKSEEMQTVQQEQ---ILQETQALQKSF 2652
Cdd:pfam15665 91 EAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAkHRQEIQELLTTQRAQsasSLAEQEKLEELH 170
|
170 180 190
....*....|....*....|....*....|...
gi 1046896947 2653 LSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAK 2685
Cdd:pfam15665 171 KAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQ 203
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2490-2624 |
1.43e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2490 QQQKELAQEQARRLQEDKEQMAQQLVEETQgfQRTLEAERQRQLEMSAEAERLKLRMAEMSR------AQARAEEDAQRF 2563
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2564 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDQDAERLREAIAelereKEKLKQEAK 2624
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2505-2641 |
1.44e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.28 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2505 EDKEQMAQQLVEETQgfqRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigeklhrtELAT--- 2581
Cdd:COG1842 22 EDPEKMLDQAIRDME---EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGRE--------DLAReal 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2582 QEKVTL---VQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLL--QLKSEEMQTVQQEQI 2641
Cdd:COG1842 91 ERKAELeaqAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEAL 155
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2331-2500 |
1.51e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2331 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAarQRSQVEEELFSVRVQME-ELGKLKARIEAENR 2409
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2410 ALilrdkdntQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAE-- 2487
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEva 363
|
170
....*....|....*....
gi 1046896947 2488 ------LLQQQKELAQEQA 2500
Cdd:COG3206 364 relyesLLQRLEEARLAEA 382
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1777-2206 |
1.53e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.01 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1777 AERAREEAERELERWQLKANEALRLRLQAEevaqqkSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1856
Cdd:COG3903 487 RAAARRRHADYYLALAERAAAELRGPDQLA------WLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1857 LAEGT--AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1934
Cdd:COG3903 561 LREGRrwLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1935 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 2014
Cdd:COG3903 641 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAA 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2015 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKA 2094
Cdd:COG3903 721 AAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAA 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2095 AAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 2174
Cdd:COG3903 801 AAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAA 880
|
410 420 430
....*....|....*....|....*....|..
gi 1046896947 2175 VEEARRLRERAEQESARQLQLAQEAAQKRLQA 2206
Cdd:COG3903 881 AAALLAAAAAAAAAAAAAAAAAAALAAAAAAA 912
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1834-2015 |
1.54e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1834 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEATAATQKRQELEA 1912
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1913 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDaarqrAEAERV 1991
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 1046896947 1992 LTEKLAAISEATRLKTEAEIALKE 2015
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1877-2004 |
1.55e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1877 AETEQGEQQRQLLEEELARLQHEATAATQKR-QELEAELAKVRAEMEVLLAsKARAEEESRSTSEKSKQRLEAEAGRFRE 1955
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1956 LAEEAARLRALAEEAKRQRQLA--EEDAAR-------------QRAEAERVLT-------------EKLAAISEATR 2004
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEvtEEDIAEvvsrwtgipvgklLEGEREKLLNleeelhervigqdEAVEAVADAIR 566
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1835-1975 |
1.56e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 43.82 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA-- 1912
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1913 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1975
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1705-1906 |
1.61e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1705 AERRLRQAEAERARQVQVAlETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerRAQQQAEAERAREEA 1784
Cdd:COG2268 199 RDARIAEAEAERETEIAIA-QANREAEEAELEQEREIETARIAEAEAELAKK-------------KAEERREAETARAEA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1785 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1864
Cdd:COG2268 265 EAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKR 344
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1046896947 1865 RLAAeqelirlrAETEQGEQQRQL-LEEELARLQHEATAATQK 1906
Cdd:COG2268 345 ALAE--------AWNKLGDAAILLmLIEKLPEIAEAAAKPLEK 379
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2331-2579 |
1.73e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2331 AEQTLRQKAQVEQELTTLRLQLEETDHQK----------SILDEELQRLKAEVT-EAARQRSQVEEELFSVRVQMEELGK 2399
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLiRGATEGLCVHSLSKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2400 LKARIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedlaQQRALAEKMlkEKMQAVQ 2477
Cdd:PLN02939 238 LKDDIQFLKAELIeVAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPL------QYDCWWEKV--ENLQDLL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2478 EATRLKAE--AELLQQQKELaqeqarrlqEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2555
Cdd:PLN02939 310 DRATNQVEkaALVLDQNQDL---------RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQL 380
|
250 260
....*....|....*....|....
gi 1046896947 2556 AEEDAQRFRKQAEEIGEKLHRTEL 2579
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESKKRSL 404
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
184-300 |
1.79e-03 |
|
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: 41.49 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 184 DRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVIRSvrlPREKGRMrfhkLQNV 263
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDINGC---PKNRSQM----IENI 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 264 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 300
Cdd:cd21285 75 DACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1838-1981 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1838 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1917
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1918 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1981
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2923-2959 |
1.93e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 1.93e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1046896947 2923 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHG 2959
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2420-2632 |
2.07e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2420 QRFleeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQEATRLKAEAELLQQQKELAQEQ 2499
Cdd:PRK05035 453 ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAARE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2500 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQR-------QLEMSAEAE-----RLKLRMAEMSRAQAR-AEEDAQRFRKQ 2566
Cdd:PRK05035 525 ARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaQQAANAEAEeevdpKKAAVAAAIARAKAKkAAQQAASAEPE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 2567 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEE 2632
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2337-2685 |
2.08e-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: 44.24 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2337 QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENralilrDK 2416
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI------DK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2417 DNTQRFLEEEaekmkqvaeeaaRLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ-K 2493
Cdd:TIGR04523 192 IKNKLLKLEL------------LLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQlN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2494 ELAQEQarrlQEDKEQMAQQLVEETQGFQRTLEAERQRQlEMSAEAERLKlrmaemsraqaraeedaqrfrKQAEEIGEK 2573
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN---------------------NQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2574 LHRTELATQEKVtlVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQlkseemqtvqqEQILQETQALQKsFL 2653
Cdd:TIGR04523 311 ELKSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ-----------RELEEKQNEIEK-LK 376
|
330 340 350
....*....|....*....|....*....|....
gi 1046896947 2654 SEKDSLLQRERFIEQEKAKLEQLF--QDEVAKAK 2685
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIqnQEKLNQQK 410
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1546-1684 |
2.09e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1546 EARELQRRMqEEVTRREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1625
Cdd:COG0542 412 ELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 1626 GGAEDELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEAELALRVKAEAEA 1684
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2464-2780 |
2.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2464 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL---VEETQGFQRTLEAERQRQLEMSAEAE 2540
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELeqaREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2541 RLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAtqekvtlVQTLEIQRQQSDQDAERLREAIAELEREKEKLK 2620
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE-------RQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2621 QEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQQQQMEQ 2700
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL-PRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2701 EKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAAT 2780
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2041-2217 |
2.16e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2041 AAQHKADIEERLAQLRKasesELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKE 2120
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2121 LAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL-----------EEVERLKAKVEEARRLRERAEQES 2189
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaparrEQAEELRADLAELAALRAELEAER 173
|
170 180 190
....*....|....*....|....*....|
gi 1046896947 2190 ARQLQL--AQEAAQKRLQAEEKAHAFVVQQ 2217
Cdd:COG4942 174 AELEALlaELEEERAALEALKAERQKLLAR 203
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1509-1612 |
2.17e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 43.24 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1509 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARElqrrmQEEVTRREEAAVDAQQQKRS-IQEELQHLRQSSE 1587
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAAAA-----AEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046896947 1588 ----------------AEIQAkaqQVEAAERSRMRIEEEIR 1612
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1845-2041 |
2.20e-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: 43.59 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1845 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEV 1923
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1924 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAER----VLTEK 1995
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKlrnqLTSKS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1046896947 1996 LAAISEA---TRLKTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQA 2041
Cdd:pfam09787 160 QSSSSQSeleNRLHQLTE-TLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1600-1930 |
2.22e-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: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1600 AERSRMRIEEEIRVVRLQLETterqrggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQdESQRKRQAEAELALRvk 1679
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMM-------EEERERALEEEEEKEEERKEERKRYRQELEEQIE-EREQKRQEEYEEKLQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1680 aEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvt 1759
Cdd:pfam13868 99 -EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAE--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1760 vtqlreeaERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQ---QKSLAQADAEKQKEEAEREARRRGKA 1836
Cdd:pfam13868 175 --------REEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAEKKARQRQELQQAREEQIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1837 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelaRLQHEATAATQKRQELEAELAK 1916
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE---REEQRAAEREEELEEGERLREE 323
|
330
....*....|....
gi 1046896947 1917 VRAEMEVLLASKAR 1930
Cdd:pfam13868 324 EAERRERIEEERQK 337
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1798-2127 |
2.22e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1798 ALRLRLQAEEVAQQKS-LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLR 1876
Cdd:pfam07888 29 AELLQNRLEECLQERAeLLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1877 AETEQGEQQRQLLEEELAR------LQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStsekSKQRLEAEA 1950
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHearireLEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ----LQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1951 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARqraeaervLTEKLAAiseATRLKTEAEIALKEKEAENERLRRLAEDE 2030
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITT--------LTQKLTT---AHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2031 AFQRRRLEEQAAQ--------HKADIEE-----RLAQLRKASESELERQKGLVEdTLRQRRQVE--------EEIMALKA 2089
Cdd:pfam07888 254 EGLGEELSSMAAQrdrtqaelHQARLQAaqltlQLADASLALREGRARWAQERE-TLQQSAEADkdrieklsAELQRLEE 332
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1046896947 2090 SFEKAAAGKAELELELGRIR--SNAEDTMRSKELAEQEAA 2127
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKdcNRVQLSESRRELQELKAS 372
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1503-2133 |
2.23e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1503 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAELEARELQRRMQ---EEVTRREEAAVDAQQQKRSI 1575
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQadlEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1576 QEELQhlRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQ-----LETTERQRGGAEDELQALRARAEEAEAQKRQAQ 1650
Cdd:PRK04863 378 QEENE--ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEAT 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1651 EEAERLRRQVQDESQRKRQAE--AELALRVKAEAEAAREKQRALQALDELKLQAEEAER----RLRQAEAERARQVQVAL 1724
Cdd:PRK04863 456 EELLSLEQKLSVAQAAHSQFEqaYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1725 ETAQRSAEVELQSK--RASFAEK-TAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWqLKANEALRl 1801
Cdd:PRK04863 536 ERLLAEFCKRLGKNldDEDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAW-LAAQDALA- 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1802 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKaEEQAVRQRELAEQ----------ELEKQRQLAE------------ 1859
Cdd:PRK04863 614 RLREQSGEEFEDSQDVTEYMQQLLERERELTVER-DELAARKQALDEEierlsqpggsEDPRLNALAErfggvllseiyd 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1860 --------------------------GTAQQRLAAEQELIRLRAETEQGEQQ---RQLLEEELAR--LQHEATAATQ--- 1905
Cdd:PRK04863 693 dvsledapyfsalygparhaivvpdlSDAAEQLAGLEDCPEDLYLIEGDPDSfddSVFSVEELEKavVVKIADRQWRysr 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1906 -------KRQELEAELAKVRAEMEVLLASKARAEEESRSTsekskQRLEAEAGRFrelaeeAARLRALAEEAKRQRQLAE 1978
Cdd:PRK04863 773 fpevplfGRAAREKRIEQLRAEREELAERYATLSFDVQKL-----QRLHQAFSRF------IGSHLAVAFEADPEAELRQ 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1979 edAARQRAEAERvlteKLAAISEATRLKTEAEIALKEKEAENERLR---RLAEDEAFQRRRLE-----EQAAQHKADIE- 2049
Cdd:PRK04863 842 --LNRRRVELER----ALADHESQEQQQRSQLEQAKEGLSALNRLLprlNLLADETLADRVEEireqlDEAEEAKRFVQq 915
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2050 --------ERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAElelelgrirsNAEDtMRSKEL 2121
Cdd:PRK04863 916 hgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE----------DAAE-MLAKNS 984
|
730
....*....|..
gi 1046896947 2122 AEQEAARQRQLA 2133
Cdd:PRK04863 985 DLNEKLRQRLEQ 996
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1529-2223 |
2.27e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1529 QRQLAEA---HAQAKAQAELEARELQRRMQEEVTRREeAAVDAQQQKRSIQEELQHLRQSSEAEIQA-KAQQVEAAERSR 1604
Cdd:pfam15921 91 QRRLNESnelHEKQKFYLRQSVIDLQTKLQEMQMERD-AMADIRRRESQSQEDLRNQLQNTVHELEAaKCLKEDMLEDSN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1605 MRIEEeIRVVRLQLEtterqrgGAEDELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEAELALrVKAEA 1682
Cdd:pfam15921 170 TQIEQ-LRKMMLSHE-------GVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDTEISY-LKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1683 EAAREKQRALQA--LDELKLQAEEAERRLRQAEAERARQVQVALETAQ--RSAEVELQSKRASFAEKT----AQLERTLQ 1754
Cdd:pfam15921 241 FPVEDQLEALKSesQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASsaRSQANSIQSQLEIIQEQArnqnSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1755 EEHVTVTQLreeaerraqqqaeaerareeaereleRWQLKanealrlrlQAEEVAQQKSlaqadaekqkeeaerearrrg 1834
Cdd:pfam15921 321 DLESTVSQL--------------------------RSELR---------EAKRMYEDKI--------------------- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 kaeEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1914
Cdd:pfam15921 345 ---EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1915 AKVRAEMEVLLASKARAEEESRSTSEkskQRLEAEAGRFRELaEEAARLRALAEEAKRQ-RQLAEEDAARQRA--EAERV 1991
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQGQME---RQMAAIQGKNESL-EKVSSLTAQLESTKEMlRKVVEELTAKKMTleSSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1992 LTEKLAAISEATRlkteaeiALKEKEAENERLRrlaedeafQRRRLEEQAAQHKADIEERLAQLRKASESeLERQKGLVE 2071
Cdd:pfam15921 498 VSDLTASLQEKER-------AIEATNAEITKLR--------SRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2072 DTLRQRRQVEEEIMALKASFEKAAAG----KAELELELGRIRSNAEDTmrsKELAEQEAARQRQLAaeeeqrrreaeerv 2147
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAmqveKAQLEKEINDRRLELQEF---KILKDKKDAKIRELE-------------- 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2148 qrslaaeeeaARQRKVALEEVERLKAKVEEARRLRERAEQESarqlQLAQEAAQKRLQAEEKAHAFVVQQR-----EEEL 2222
Cdd:pfam15921 625 ----------ARVSDLELEKVKLVNAGSERLRAVKDIKQERD----QLLNEVKTSRNELNSLSEDYEVLKRnfrnkSEEM 690
|
.
gi 1046896947 2223 Q 2223
Cdd:pfam15921 691 E 691
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2423-2561 |
2.28e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.24 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2423 LEEEA------EKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQ 2492
Cdd:PTZ00491 675 LEQEArgrlerQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAE 751
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2493 KELAQEQARRLQEDKEQmaQQLVEetqgfqrtLEAERQRQLeMSAEAERLKLRMAEMSR----AQARAEEDAQ 2561
Cdd:PTZ00491 752 AELEKLRKRQELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3842-3880 |
2.36e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1046896947 3842 YLYGTGSVAGVYLPGSRQTLTIYQALKKGLLSAEVARLL 3880
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1628-1871 |
2.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1628 AEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvKAEAEaarekqralqaLDELKLQAEEAER 1707
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---ALQAE-----------IDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1708 RLRQAEA---ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEA 1784
Cdd:COG3883 80 EIEERREelgERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1785 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1864
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
....*..
gi 1046896947 1865 RLAAEQE 1871
Cdd:COG3883 240 AAAAASA 246
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1835-1992 |
2.56e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEATAATQKRQELEA 1912
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1913 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1988
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....
gi 1046896947 1989 ERVL 1992
Cdd:COG1842 207 EDEL 210
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2413-2586 |
2.60e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2413 LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2492
Cdd:pfam05262 177 ISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2493 KELAQEQAR--------RLQEDKEQMAQQLVEETQgfQRTLEAERQRQlemsAEAERLKLRMAEMSRAQARAEEDAQRFR 2564
Cdd:pfam05262 257 AKNLPKPADtsspkedkQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|..
gi 1046896947 2565 kqaEEIGEKLHRTELATQEKVT 2586
Cdd:pfam05262 331 ---EPVAEDLQKTKPQVEAQPT 349
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2448-2623 |
2.74e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2448 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLVEETQG 2520
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2521 FQRTLEAERQRQLemsaeAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDQ 2600
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREPV 333
|
170 180
....*....|....*....|...
gi 1046896947 2601 dAERLREAIAELEREKEKLKQEA 2623
Cdd:pfam05262 334 -AEDLQKTKPQVEAQPTSLNEDA 355
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1355-1678 |
2.80e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1355 RQRELEQLGRQlryyRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEI----ERHGEKVEECQKFAK 1430
Cdd:pfam02029 12 RRRAREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTakreERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1431 QYINAIKDYElqlitykaqlEPVASPAKKPKVQSGSESVIQEYVDLR-TRYSELTTLTSQyikfiSETLRRMEEEERLAE 1509
Cdd:pfam02029 88 EFDPTIADEK----------ESVAERKENNEEEENSSWEKEEKRDSRlGRYKEEETEIRE-----KEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1510 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAR-ELQRRMQEEVTRREEAAVDAQQQ--KRSIQEELQHLRQSS 1586
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKyESKVFLDQKRGHPEVKSQNGEEEvtKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1587 EAEIQAKAQQVEAAERSRmrieEEIRVVRLQLETTE----RQRGG-AEDELQALRARAEE-----AEAQKRQAQEEAERL 1656
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKL----EELRRRRQEKESEEfeklRQKQQeAELELEELKKKREErrkllEEEEQRRKQEEAERK 308
|
330 340
....*....|....*....|....*...
gi 1046896947 1657 ------RRQVQDESQRKRQAEAELALRV 1678
Cdd:pfam02029 309 lreeeeKRRMKEEIERRRAEAAEKRQKL 336
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1533-1721 |
2.86e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.74 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1533 AEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIR 1612
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1613 vvRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAE-AELALRVKAEAEAAREKQRA 1691
Cdd:PRK12678 147 --EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG--RREERGRDGDdRDRRDRREQGDRREERGRRD 222
|
170 180 190
....*....|....*....|....*....|
gi 1046896947 1692 LQALDELKLQAEEAERRLRQAEAERARQVQ 1721
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1475-1818 |
2.95e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1475 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAELEARELQ-RR 1553
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS-----ELEQLEEELEELNEQlQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1554 MQEEVTRREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQ 1633
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1634 ALRARAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAE 1713
Cdd:COG4372 168 ALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1714 AERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQL 1793
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|....*
gi 1046896947 1794 KANEALRLRLQAEEVAQQKSLAQAD 1818
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGL 350
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1835-2070 |
3.05e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.90 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1835 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQ-RQLLEEELARLqHEATAATQKRQEleae 1913
Cdd:pfam05911 10 KVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKI-HDVVLKKTKEWE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1914 laKVRAEMEVLLAskaraeeesrstsEKSKQRLEAEagrfrelAEEAARLRALAEEAKRQRQLAEEdaaRQRAEAE-RVL 1992
Cdd:pfam05911 85 --KIKAELEAKLV-------------ETEQELLRAA-------AENDALSRSLQERENLLMKLSEE---KSQAEAEiEAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 1993 TEKLAAIS-EATRLKTEAEIALKEKEAENErlrrlaEDEaFQRRRLEEQAAQHKADIeERLAQLrkasESELERQKGLV 2070
Cdd:pfam05911 140 KSRLESCEkEINSLKYELHVLSKELEIRNE------EKN-MSRRSADAAHKQHLESV-KKIAKL----EAECQRLRGLV 206
|
|
| antiphage_ZorA_2 |
NF033915 |
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ... |
1865-2068 |
3.12e-03 |
|
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense.
Pssm-ID: 411476 [Multi-domain] Cd Length: 383 Bit Score: 43.21 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1865 RLAAEQELIRLRAETEQGEQQRQLLEEELA-RLQHEATAATQKRQE-LEAELAKVRAEMEVLLASkaraeeesrSTSEKS 1942
Cdd:NF033915 201 RIPAEQSLVHIAEYSKESKEALQELHERIGdRLQESLNGMSEAMQTaLTDALNNIMAPAIQTLVS---------TTSQQS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1943 KQRLEAEAGRFRElaeeaarlrALAEEAKRQRQLAEEdAARQRAEAERVLTEKLAAISEATRlkteaeialKEKEAENER 2022
Cdd:NF033915 272 TQVLESLVGNFMD---------GMTSAGREQGLQMQQ-AAADVNAAVSGMSERLNQLFNSLS---------EQQGRQMER 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1046896947 2023 LRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKG 2068
Cdd:NF033915 333 AQQQSSTFETQLQRLSGSANERQAQLEQRFEELMSGLTEQLQTQLG 378
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1520-1732 |
3.17e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.87 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1520 AEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEvtRREEAAVDAQQQKRSIQEEL---QHLRQSSEAEIQAKAQQ 1596
Cdd:PRK10811 582 GGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNE--RRDTRDNRTRREGRENREENrrnRRQAQQQTAETRESQQA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1597 VEAA-ERSRMRIEEEIRvvrlqletTERQRGGAEDELQA-LRARAEEAEAQKRQAQEEAERlRRQVQdesQRKRQAEAEL 1674
Cdd:PRK10811 660 EVTEkARTQDEQQQAPR--------RERQRRRNDEKRQAqQEAKALNVEEQSVQETEQEER-VQQVQ---PRRKQRQLNQ 727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1675 ALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1732
Cdd:PRK10811 728 KVRIEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNA 785
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2395-2512 |
3.19e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2395 EELGKLKARIEAENRALILRDKDNTQrfLEEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2474
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2475 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ 2512
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAK 173
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2389-2569 |
3.28e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2389 SVRVQMEE----LGKLKARIEAENRA-LILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEED 2457
Cdd:PRK11637 62 SVRQQQQQraslLAQLKKQEEAISQAsRKLRETQNTLNQLNKQIDELNasiaklEQQQAAQERLLAAQLDAAFRQGEHTG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2458 LAQQRALAEKMLKEKMQA----VQEAtRLKAEAELLQQQKELAQEqaRRLQEDKEQMAQQLVEETQGFQRTLE---AERQ 2530
Cdd:PRK11637 142 LQLILSGEESQRGERILAyfgyLNQA-RQETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEqarNERK 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2531 RQL---------------EMSAEAERLKLRMAEMSR-AQARAEE---DAQRFRKQAEE 2569
Cdd:PRK11637 219 KTLtglesslqkdqqqlsELRANESRLRDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3177-3214 |
3.33e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.08 E-value: 3.33e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1046896947 3177 LRGTSVIAGVWLEEAGQKLSIYEALRRDLLQPEVAVAL 3214
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1492-1751 |
3.34e-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: 43.48 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1492 KFISETLR----RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQR-RMQEEVTRREEAAV 1566
Cdd:pfam05667 250 KRIAEQLRsaalAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAaTSSPPTKVETEEEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1567 DAQQQK--RSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggaedelQALRARA-EEAE 1643
Cdd:pfam05667 330 QQQREEelEELQEQLEDL----ESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ--------YKVKKKTlDLLP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1644 aqkrQAQEEAERLRRQVQDESQRKrqaeAELAlrvkAEAEAAR----EKQRALQalDELKLQAEEAERRLRQAEAERaRQ 1719
Cdd:pfam05667 398 ----DAEENIAKLQALVDASAQRL----VELA----GQWEKHRvpliEEYRALK--EAKSNKEDESQRKLEEIKELR-EK 462
|
250 260 270
....*....|....*....|....*....|..
gi 1046896947 1720 VQVALEtaqrsaevELQSKRASFAEKTAQLER 1751
Cdd:pfam05667 463 IKEVAE--------EAKQKEELYKQLVAEYER 486
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1306-1674 |
3.38e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1306 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLgrqLRYYRESADPLSSWLQDAKS 1385
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1386 RQEQIQAVPIANSQAAREQLRQEKALLEEIERHGEKV-------EECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK 1458
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVleretelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1459 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSqyiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAH 1536
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQ---KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1537 AQAKAQAELEARELQrrMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEiRVVRL 1616
Cdd:pfam07888 266 QRDRTQAELHQARLQ--AAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 1617 QLETT-ERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1674
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2314-2578 |
3.44e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2314 LKQKQAADAEMEKHKK-----FAE-QTLRQK-AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2386
Cdd:COG1340 14 EEKIEELREEIEELKEkrdelNEElKELAEKrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2387 LFSVRVQMEELG-------KLKARIEA-------------ENRALILRDKDntqrfLEEEAEKMKQVAEEAARLSVAAQE 2446
Cdd:COG1340 94 LDELRKELAELNkaggsidKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2447 AARLRQLAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLveetqgfqr 2523
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL--------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2524 tleaerqRQLEMSAEAERLKLRMAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2578
Cdd:COG1340 240 -------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1537-1691 |
3.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1537 AQAKAqaeLEARELQRRMQEEVtrREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEE------- 1609
Cdd:PRK12704 29 AEAKI---KEAEEEAKRILEEA--KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrkle 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1610 EIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQA--------QEEA-ERLRRQVQDEsqrkrqAEAELALRVKA 1680
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKVEEE------ARHEAAVLIKE 177
|
170
....*....|...
gi 1046896947 1681 EAEAARE--KQRA 1691
Cdd:PRK12704 178 IEEEAKEeaDKKA 190
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1527-1658 |
3.56e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1527 EKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKAQQVEAAERSR 1604
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1605 MRIEEEIRVVRLQLETTERQRGGAEDELQalraraeeaEAQKRQAQEEAERLRR 1658
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1789-2084 |
3.57e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.10 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1789 ERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAE-QELEKQRQLAEGTAQ---- 1863
Cdd:pfam15558 42 QKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEdQENQRQEKLERARQEaeqr 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1864 -----QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeMEVLLASKARAEEESRST 1938
Cdd:pfam15558 122 kqcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQA-RKVLVDCQAKAEELLRRL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1939 S-EKSKQRLEAE-----AGRFRELAEEAA-------RLRALAEEAKRQRQLAEEDAARqraEAERVLTEKLAAISEATRL 2005
Cdd:pfam15558 201 SlEQSLQRSQENyeqlvEERHRELREKAQkeeeqfqRAKWRAEEKEEERQEHKEALAE---LADRKIQQARQVAHKTVQD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2006 KTEAEIALK-EKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEI 2084
Cdd:pfam15558 278 KAQRARELNlEREKNHHILKLKVEKEEKCHREGIKEAIKKK---EQRSEQISREKEATLEEARKTARASFHMREKVREET 354
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1598-1715 |
3.71e-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: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1598 EAAERSRMRIE---EEIRVVRLQLETTERQRGGAEDElqalraraeeaeaQKRQAQEEAERLRRQVQDESQRKRQAEAel 1674
Cdd:COG0542 397 EAAARVRMEIDskpEELDELERRLEQLEIEKEALKKE-------------QDEASFERLAELRDELAELEEELEALKA-- 461
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046896947 1675 alRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAE 1715
Cdd:COG0542 462 --RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1876-2013 |
3.75e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 43.32 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1876 RAETEQGEQqrqlleEELARLQHEA-TAATQKrqelEAELAKVRAEMEVLLASKARAEEESRST--------SEKSKQRL 1946
Cdd:PRK12472 191 RAETLAREA------EDAARAADEAkTAAAAA----AREAAPLKASLRKLERAKARADAELKRAdkalaaakTDEAKARA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046896947 1947 EAeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKlaaiSEATRLKTEAEIAL 2013
Cdd:PRK12472 261 EE---RQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKK----AETAKAATDAKLAL 320
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1960-2104 |
3.76e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1960 AARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIAlkEKEAENERLRRLAEDEAFQRRRLEE 2039
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 2040 QAAQ------HKADIEERLAQLRKASESELERQKGLVEDTLRQR--RQVEEEIMALKASFEKAAAGKAELELE 2104
Cdd:PRK12705 103 LENQleerekALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1502-1685 |
4.08e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1502 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQH 1581
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1582 LRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQRggaedELQALRARAEEAEAQKRQAQEEAErlrrqv 1660
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*
gi 1046896947 1661 QDESQRKRQAEAELAlRVKAEAEAA 1685
Cdd:PRK05035 671 EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2334-2758 |
4.08e-03 |
|
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: 43.79 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2334 TLRQKAQVEQELTTLRLQLEETDHQKSILDEELQ----RLkAEVTEAARQRSQVEeelfsvRVQmEELGKLKARIEAENR 2409
Cdd:COG3096 297 ARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdHL-NLVQTALRQQEKIE------RYQ-EDLEELTERLEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2410 ALilrdkdntqrflEEEAEkmkQVAEEAARLSVAAQEAARLR-QLAEE----DLAQQRALAekmlkekmqaVQEATRLKA 2484
Cdd:COG3096 369 VV------------EEAAE---QLAEAEARLEAAEEEVDSLKsQLADYqqalDVQQTRAIQ----------YQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2485 EAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTL--EAERQRQLEMSAEAerLKLRMAEMSRAQA--RAEEDA 2560
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsvADAARRQFEKAYEL--VCKIAGEVERSQAwqTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2561 QRFRKQAEEIGEklhrtelatqekvtlVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQeakllQLKSEEMQTVQQEQ 2640
Cdd:COG3096 502 RRYRSQQALAQR---------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQ-----QLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2641 --ILQETQALQKSFLSEKDSLLQRERfiEQEKAKLEQLFQDEVA--KAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQ 2716
Cdd:COG3096 562 leAQLEELEEQAAEAVEQRSELRQQL--EQLRARIKELAARAPAwlAAQDALERLREQSGEALADSQEVTAAMQQLLERE 639
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1046896947 2717 REAEegvrrkqeelqrleqqrqQQEKLLAEENQRLRERLQRL 2758
Cdd:COG3096 640 REAT------------------VERDELAARKQALESQIERL 663
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1494-1595 |
4.10e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.67 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1494 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAKA-----QAELEARELQRRMQ----EEVT 1559
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEVakiqmQQKIMEKEAEKKISeiedEMHL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1046896947 1560 RREEAAVDAQQQKRSIQEELQHLRQSSE----AEIQAKAQ 1595
Cdd:cd03406 237 AREKARADAEYYRALREAEANKLKLTPEylelKKYQAIAN 276
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1628-1751 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1628 AEDELQALRARAEEAEAQKRQAQEEAERLRRQVQdesqrKRQAEAELALRVKAEA---EAAREKQ--------------R 1690
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLEQQTEQAK-----KLEEKAQAALTKGNEElarEALAEKKslekqaealetqlaQ 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1691 ALQALDELKLQAEEAERRLRQAEAERaRQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1751
Cdd:pfam04012 109 QRSAVEQLRKQLAALETKIQQLKAKK-NLLKARLKAAKAQEAVQTSLGSLSTSSATDSFER 168
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1747-2104 |
4.14e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1747 AQLERTLQEEHVTVtqlreeaERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA 1826
Cdd:pfam07888 34 NRLEECLQERAELL-------QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1827 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1906
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1907 RQELEAELAKVRAemevLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE------ED 1980
Cdd:pfam07888 187 LRSLSKEFQELRN----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEglgeelSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1981 AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEA----ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLR 2056
Cdd:pfam07888 263 MAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1046896947 2057 KAsESELERQKglvEDTLRQRRQVEEEIMALKASFEKAAAGKAELELE 2104
Cdd:pfam07888 343 KL-EVELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAE 386
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1409-1680 |
4.18e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1409 KALLEEIERH------GEK---VEECQKFAKQ---YIN-----AIKDYELQLITYKAqlEPVASPAKKPKVQSGSESVIQ 1471
Cdd:PLN03188 970 KRVQDELEHYrnfydmGERevlLEEIQDLRSQlqyYIDsslpsARKRNSLLKLTYSC--EPSQAPPLNTIPESTDESPEK 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1472 EYVDLRTRYSELTtltSQYIKFISETLRRMEEEERLAEQQRAE--ERERLAEveaALEKQRQLA-EAHAQAKAQ-AELEA 1547
Cdd:PLN03188 1048 KLEQERLRWTEAE---SKWISLAEELRTELDASRALAEKQKHEldTEKRCAE---ELKEAMQMAmEGHARMLEQyADLEE 1121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1548 RELQ-----RRMQEEVTRREEAAVDAqqqkrSIQEELQHLRQSSEAEIQA-KAQQveaaERSRMRIEEEIRVVRLQLETT 1621
Cdd:PLN03188 1122 KHIQllarhRRIQEGIDDVKKAAARA-----GVRGAESKFINALAAEISAlKVER----EKERRYLRDENKSLQAQLRDT 1192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 1622 ER--QRGG--------AEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1680
Cdd:PLN03188 1193 AEavQAAGellvrlkeAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1493-1555 |
4.24e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 43.71 E-value: 4.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1493 FISETLRRmeEEERLAEQQraEERERLAEVEAALEKQRQLAEA-HAQAKAQAELEARELQRRMQ 1555
Cdd:PLN02316 249 FLLEEKRR--ELEKLAKEE--AERERQAEEQRRREEEKAAMEAdRAQAKAEVEKRREKLQNLLK 308
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1364-1576 |
4.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1364 RQLRYYRESADPLSSWLQD-AKSRQEQIQAvpianSQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINA---IKDY 1439
Cdd:COG3206 164 QNLELRREEARKALEFLEEqLPELRKELEE-----AEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1440 ELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------ISETLRRMEEEERLAEQQR 1512
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 1513 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEE-------VTRREEAAVDAQQQKRSIQ 1576
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1526-1732 |
4.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1526 LEKQRQLAEAHAQAKAQAELEARELQRRMQEEvtRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrm 1605
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1606 rieeeirvvrlqLETTERQRGGAEdelQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEAELALRVKAEAEaa 1685
Cdd:PRK12705 100 ------------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1046896947 1686 rekqraLQALDELKLQAEEAerrlrQAEAERARQVQVAlETAQRSAE 1732
Cdd:PRK12705 157 ------EEKAQRVKKIEEEA-----DLEAERKAQNILA-QAMQRIAS 191
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2536-2784 |
4.54e-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: 42.83 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2536 SAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELERE 2615
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2616 KEKLKQE-AKLLQlkseEMQTVQQEQILQetqalqksFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQ 2694
Cdd:COG4942 99 LEAQKEElAELLR----ALYRLGRQPPLA--------LLLSPEDFLDAVRRLQYLKYLAPAR-REQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2695 QQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAE---ENQRLRERLQRLEEEhrAALAHSEE 2771
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAE--AAAAAERT 243
|
250
....*....|...
gi 1046896947 2772 IATSQAAATKALP 2784
Cdd:COG4942 244 PAAGFAALKGKLP 256
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1969-2130 |
4.72e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1969 EAKRQRQLAEEDAARQRAEAERvLTEKlaAISEATRLKTEAEIA-----LKEKEAENERLRRLAEDEAFQRRRLEEQAAQ 2043
Cdd:COG2268 189 LGRRKIAEIIRDARIAEAEAER-ETEI--AIAQANREAEEAELEqereiETARIAEAEAELAKKKAEERREAETARAEAE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2044 HKADIEErlAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELElgrirsnaedtmrskELAE 2123
Cdd:COG2268 266 AAYEIAE--ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE---------------AEAE 328
|
....*..
gi 1046896947 2124 QEAARQR 2130
Cdd:COG2268 329 AEAIRAK 335
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1496-1623 |
4.72e-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: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1496 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAELEAREL-QRRMQEEVTRREEAAVDAQQQKR 1573
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1574 SIQEELQHLRQSSEAeiqAKAQQVEAAErsRMRIEEEIRVVRLQLETTER 1623
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAE--RQRQEREKIMQQEEQERLER 135
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2396-2791 |
4.75e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2396 ELGKLKARIE--AENRALILRDKDNTQRFLEEEAEKMKQ---VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2470
Cdd:PRK02224 214 ELAELDEEIEryEEQREQARETRDEADEVLEEHEERREEletLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2471 EKMQAVQEATRLKAEAELLQQQKElaqeqarRLQEDKEQMaqqlveetqgfQRTLEAERQRQLEMSAEAERLKLRMAEMS 2550
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARRE-------ELEDRDEEL-----------RDRLEECRVAAQAHNEEAESLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2551 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQ--L 2628
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2629 KSEEMQTVQQEQILQE------TQALQKSflSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLqeeqqrqqqqmeqek 2702
Cdd:PRK02224 436 RTARERVEEAEALLEAgkcpecGQPVEGS--PHVETIEEDRERVEELEAELEDL-EEEVEEVEER--------------- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2703 qelVASMEEARRRQREAEEgvrrkqeelqrLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKA 2782
Cdd:PRK02224 498 ---LERAEDLVEAEDRIER-----------LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
....*....
gi 1046896947 2783 LPNGRDALD 2791
Cdd:PRK02224 564 EEEAEEARE 572
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1846-2131 |
4.82e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1846 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL 1925
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1926 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKR-QRQLAEE---DAARQRAEAErvlteklaaise 2001
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQRgERILAYFgylNQARQETIAE------------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2002 atrlkteaeialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLvedtlrqrrqve 2081
Cdd:PRK11637 175 ---------------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTL------------ 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2082 eeiMALKASFEKAAAGKAELELELGRIRSN-AEDTMRSKELAEQEA-------ARQRQ 2131
Cdd:PRK11637 222 ---TGLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1181-1710 |
4.97e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1181 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRSTQGAEE 1260
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1261 VLKTHEEHLKEAQAVPATLQELEVTKASLkklraQAEAQQpVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQ 1340
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1341 LLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLSSWLQDAKSRQEQiqavpIANSQAAREQLRQEKALLEE 1414
Cdd:pfam05557 144 LKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELAR-----IPELEKELERLREHNKHLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1415 IERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKK-PKVQSGSESVIQEYVDLRTRYSEL---------- 1483
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwVKLAQDTGLNLRSPEDLSRRIEQLqqreivlkee 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1484 -TTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQAKA-QAELEARELQRRMQE---E 1557
Cdd:pfam05557 299 nSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVLLLTKERDGyRAILESYDKELTMSNyspQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1558 VTRREEAAVDAQQQKRSIQEELQH--------------LRQSSEAEIQAKAQQVEAAERSRMRieEEIRVVRLQLETTER 1623
Cdd:pfam05557 378 LLERIEEAEDMTQKMQAHNEEMEAqlsvaeeelggykqQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLEL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1624 QRGGAEDELQALRARAE------------------------EAEAQKR----QAQEEAERLRRQVqdesqRKRQAEAELA 1675
Cdd:pfam05557 456 ERQRLREQKNELEMELErrclqgdydpkktkvlhlsmnpaaEAYQQRKnqleKLQAEIERLKRLL-----KKLEDDLEQV 530
|
570 580 590
....*....|....*....|....*....|....*
gi 1046896947 1676 LRVKAEAEAAREKQralqaLDELKLQAEEAERRLR 1710
Cdd:pfam05557 531 LRLPETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3582-3613 |
5.17e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.17e-03
10 20 30
....*....|....*....|....*....|..
gi 1046896947 3582 KLLSAEKAVTGYKDPYSGSTISLFQAMKKGLV 3613
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1568-1704 |
5.32e-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: 42.28 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1568 AQQQKRSIQEELQhlrqsseAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLET-TERQRGGAEDELQALRARAEEAEAQK 1646
Cdd:pfam12037 51 MKKQEQTRQAELQ-------AKIKEYEAAQEQLKIERQRVEYEERRKTLQEETkQKQQRAQYQDELARKRYQDQLEAQRR 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046896947 1647 RQA-----QEEAERLRRQVQDESQRKRQAEAELALR-------VKAEAE--AAREKQRALQALDELKLQAEE 1704
Cdd:pfam12037 124 RNEellrkQEESVAKQEAMRIQAQRRQTEEHEAELRreterakAEAEAEarAKEERENEDLNLEQLREKANE 195
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1937-2212 |
5.63e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.66 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1937 STSEKSKQRLEAEAG-RFRELAEEaarlRALAEEAKRQRQLAEEDAARQRAeaervlTEKLAAISeATRLKTEAEIALKE 2015
Cdd:PRK07735 1 MDPEKDLEDLKKEAArRAKEEARK----RLVAKHGAEISKLEEENREKEKA------LPKNDDMT-IEEAKRRAAAAAKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2016 KEAENERLRRLAEDEAFQRrrlEEQAAQHKAdieerlAQLRKASESELERQKglvEDTLRQRRQVEEEIMALKASFE-KA 2094
Cdd:PRK07735 70 KAAALAKQKREGTEEVTEE---EKAKAKAKA------AAAAKAKAAALAKQK---REGTEEVTEEEKAAAKAKAAAAaKA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2095 AAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 2174
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAA 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1046896947 2175 VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2212
Cdd:PRK07735 218 LAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKT 255
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1592-2029 |
5.75e-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: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1592 AKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAE 1671
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1672 AELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1751
Cdd:COG3064 85 AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1752 TLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREAR 1831
Cdd:COG3064 165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1832 RRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELE 1911
Cdd:COG3064 245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1912 AELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV 1991
Cdd:COG3064 325 GALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLR 404
|
410 420 430
....*....|....*....|....*....|....*...
gi 1046896947 1992 LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED 2029
Cdd:COG3064 405 LDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVA 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2098-2574 |
5.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2098 KAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRsLAAEEEAARQRKVALEEVERLKAKVEE 2177
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2178 ARRLRERAEQESAR------------QLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARR 2245
Cdd:COG4717 134 LEALEAELAELPERleeleerleelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2246 AAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQ------------AQAQAQAAAEKLRKEAEQEAARRAQAEQAA 2313
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2314 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEElfsvrvq 2393
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE------- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2394 meelgklkaRIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQeaaRLRQLAEEDLAQQRALAEKMLKEKM 2473
Cdd:COG4717 367 ---------ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE---QLEELLGELEELLEALDEEELEEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2474 QAVQEatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEmsaEAERLKLRMAEMSRAQ 2553
Cdd:COG4717 435 EELEE-----ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE---EWAALKLALELLEEAR 506
|
490 500
....*....|....*....|..
gi 1046896947 2554 ARAEEDAQ-RFRKQAEEIGEKL 2574
Cdd:COG4717 507 EEYREERLpPVLERASEYFSRL 528
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1604-1721 |
6.01e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.90 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1604 RMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERL---RRQVQDESQR-KRQAEAELALRVK 1679
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLeqkRQEAEEEKERlEESAEMEAEEKEQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1046896947 1680 AEAEaAREKQRALQALDELKLQAEEAERRLrQAEAERARQVQ 1721
Cdd:pfam20492 81 LEAE-LAEAQEEIARLEEEVERKEEEARRL-QEELEEAREEE 120
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1347-1606 |
6.09e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1347 AVLAQTDVR---QRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIERHGEKVE 1423
Cdd:COG4942 14 AAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1424 ECQKFAKQYINAIKDYELQLitYKAQLEPvaspakKPKVQSGSESVIQEYvdlrtRYSELTTLTSQYIKFISETLRRMEE 1503
Cdd:COG4942 94 ELRAELEAQKEELAELLRAL--YRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1504 EERLAEQQRAEERERLAEVEAALEKQRqlaeahaQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLR 1583
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|...
gi 1046896947 1584 QSSEAEIQAKAQQVEAAERSRMR 1606
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKLP 256
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2336-2514 |
6.26e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2336 RQKAQVEQELTTlRLQLEETDHQKSIlDEELQRLKAEVTEAARQRSQVEeelfsVRVQMEELGKLKARIEAENRALILR- 2414
Cdd:COG2268 201 ARIAEAEAERET-EIAIAQANREAEE-AELEQEREIETARIAEAEAELA-----KKKAEERREAETARAEAEAAYEIAEa 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2415 --DKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA-RLRQLAEEDLAQQRALAE-KMLKEKMQAVQEATRLKAEAELLQ 2490
Cdd:COG2268 274 naEREVQRQLEIAEREREIELQEKEAEREEAELEADvRKPAEAEKQAAEAEAEAEaEAIRAKGLAEAEGKRALAEAWNKL 353
|
170 180
....*....|....*....|....
gi 1046896947 2491 QQKELAQEQARRLQEDKEQMAQQL 2514
Cdd:COG2268 354 GDAAILLMLIEKLPEIAEAAAKPL 377
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1335-1719 |
6.39e-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: 42.36 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1335 RERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEE 1414
Cdd:pfam19220 68 RRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1415 ierhgekveecqkfAKQYINAIKDYELQLITYKAQLEPVAspAKKPKVQSGSESVIQEYVDLRTRYSELTTL---TSQYI 1491
Cdd:pfam19220 148 --------------AQAAEKALQRAEGELATARERLALLE--QENRRLQALSEEQAAELAELTRRLAELETQldaTRARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1492 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQ 1571
Cdd:pfam19220 212 RALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1572 KRSIQEELQHLRQSSEAEIQakaqqveaaersrmrieeeirvvrlQLETTERQRGGAEDELQALRARAEEAEAQKRQAQE 1651
Cdd:pfam19220 292 RDTLERRLAGLEADLERRTQ-------------------------QFQEMQRARAELEERAEMLTKALAAKDAALERAEE 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 1652 EAERLRRQVqdesqrkrqaeAELALRVKAEAEAAREKQRALQAldelKLQAEEAERRLRQAEAERARQ 1719
Cdd:pfam19220 347 RIASLSDRI-----------AELTKRFEVERAALEQANRRLKE----ELQRERAERALAQGALEIARE 399
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2314-2535 |
6.51e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2314 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ-VEEELFSVRV 2392
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2393 QMEELGKLKARIEAENRalilrDKDNTQRFLEEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAEKML- 2469
Cdd:pfam13868 199 EKAERDELRAKLYQEEQ-----ERKERQKEREEAEKKARQRQElqQAREEQIELKERRLAEEAEREEEEFERMLRKQAEd 273
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046896947 2470 --KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEM 2535
Cdd:pfam13868 274 eeIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1496-1600 |
6.65e-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: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1496 ETLRRMEEEERLAEQQRAEERERLAEV---EAALEKQRQLAEAHAQAKAQAELE------ARELQRRMQEEVTRREEA-- 1564
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKEkyqEWLQRKARQQTKKREESHKQKAAEsaskslAKPERKVSQEEAKEVLQEwe 148
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046896947 1565 -AVDAQQQKRsiQEELQHLRQSSEAEIQAKAQQVEAA 1600
Cdd:pfam13904 149 rKKLEQQQRK--REEEQREQLKKEEEEQERKQLAEKA 183
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
187-301 |
6.66e-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: 40.34 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 187 QKKTFTKWVNKHLIKHwrAEAQRHI------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRsvrlpreKGRMRFHKL 260
Cdd:cd21292 25 EKVAFVNWINKNLGDD--PDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTID-ERAINK-------KKLTVFTIH 94
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046896947 261 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 301
Cdd:cd21292 95 ENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1510-1881 |
6.80e-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: 42.71 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1510 QQRAEERERLA-EVEAALEKQRQLAEAHA-QAKAQAELEARELQRRMQE--EVTRREEAAVDAQQQKRSIQEELQHLRQS 1585
Cdd:pfam05701 229 KQAEEELQRLNqQLLSAKDLKSKLETASAlLLDLKAELAAYMESKLKEEadGEGNEKKTSTSIQAALASAKKELEEVKAN 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1586 SE-AEIQAKAQQVeAAERSRMRIEEEirvvRLQLETTERQRGGA-------EDELQALRARAEEAEAQKRQAQEEAERLR 1657
Cdd:pfam05701 309 IEkAKDEVNCLRV-AAASLRSELEKE----KAELASLRQREGMAsiavsslEAELNRTKSEIALVQAKEKEAREKMVELP 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1658 RQVQDESQrkrqaEAELAlrvKAEAEAAREkqralqaldELKLQAEEAErrlrQAEAErARQVQVALETAQRSAEVELQS 1737
Cdd:pfam05701 384 KQLQQAAQ-----EAEEA---KSLAQAARE---------ELRKAKEEAE----QAKAA-ASTVESRLEAVLKEIEAAKAS 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1738 KRASFAEKTAQLERTLQEEHVTVTQLREEAErraqqqaeaerareeaerelerwqLKANEALRLRLQAEEVAQQKSLAQA 1817
Cdd:pfam05701 442 EKLALAAIKALQESESSAESTNQEDSPRGVT------------------------LSLEEYYELSKRAHEAEELANKRVA 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1818 DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1881
Cdd:pfam05701 498 EAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQELRKWRAEHEQ 561
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1566-1712 |
6.89e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1566 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrmrieeeirvvrlqletterqrggAEDELQALRARAEEAEAQ 1645
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046896947 1646 KRQAQEEAERLRRQVQdesqrkrQAEAElalrvkaeaEAAREKQRALQALDELKLqaEEAERR------LRQA 1712
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1970-2203 |
7.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1970 AKRQRQLAEEDAARQRAEAERvlteklaaisEATRLKTEAEIALKEkeaENERLRRLAEDEAFQRRR-LEEQaaqhkadi 2048
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKK----------EAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNeLQKL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2049 EERLAQlrkaSESELERQKGLVEDTLRQRRQVEEEIMALKASFEKaaagkaelelelgrirsnaedtmRSKELAEQEAAR 2128
Cdd:PRK12704 88 EKRLLQ----KEENLDRKLELLEKREEELEKKEKELEQKQQELEK-----------------------KEEELEELIEEQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046896947 2129 QRQLaaeeeqrrreaeeRVQRSLAAEEeaARQRkvALEEVERlKAKVEEARRLRErAEQEsarqlqlAQEAAQKR 2203
Cdd:PRK12704 141 LQEL-------------ERISGLTAEE--AKEI--LLEKVEE-EARHEAAVLIKE-IEEE-------AKEEADKK 189
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1838-2098 |
7.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1838 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQheataatQKRQELEAELAKV 1917
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK-------EERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1918 RAEMEVLLASKARAEEESRSTSEKSKqRLEAEAGRF----------RELAEEAARLRALAEEAKRQRQLAEE-DAARQRA 1986
Cdd:COG1340 91 REELDELRKELAELNKAGGSIDKLRK-EIERLEWRQqtevlspeeeKELVEKIKELEKELEKAKKALEKNEKlKELRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1987 EAERV----LTEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASEsE 2062
Cdd:COG1340 170 KELRKeaeeIHKKIKELAEEAQELHEEMIELYKEA---DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRK-E 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 1046896947 2063 LERQKGLVEDTLRQRRQVEEEIMAlKASFEKAAAGK 2098
Cdd:COG1340 246 LKKLRKKQRALKREKEKEELEEKA-EEIFEKLKKGE 280
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1253-1547 |
7.79e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1253 RSTQGAEEVLKTHEEHLKEAQAVPATLQELEVTKAslkkLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE 1332
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAA----IYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1333 RWRE-------------RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYR----ESADPLSSWLQDAKSRQEQIQAVPI 1395
Cdd:pfam17380 376 RMRElerlqmerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRaeqeEARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1396 ANSQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLiTYKAQLEPVASPAKKPKVQSGSESVIQEYVD 1475
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE-RKQAMIEEERKRKLLEKEMEERQKAIYEEER 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1476 LRTRYSElttltsqyikfiSETLRRMEEEERLAEQQR--AEERERLAEVEAALEKQRQLAEAHaqaKAQAELEA 1547
Cdd:pfam17380 535 RREAEEE------------RRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMMRQIVESE---KARAEYEA 593
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1533-1684 |
8.08e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 42.17 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1533 AEAHAQAKAQAELEARElqrrmqeevtrREEAAVDAQQQKRSIQEElqhlrqssEAEIQAKAQQVEAAERSRMRIEEEIR 1612
Cdd:PRK12472 182 AEALAAAPARAETLARE-----------AEDAARAADEAKTAAAAA--------AREAAPLKASLRKLERAKARADAELK 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1613 VV--RLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1684
Cdd:PRK12472 243 RAdkALAAAKTDEAKARAEERQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDA 316
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1338-1615 |
8.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1338 VTQLLERWQAVLAQTDVRQRELEQLGRQLryyrESADplsswlQDAKSRQEQIQAVPIANSQAAREQLrqEKALLEEIER 1417
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQL----AQAP------AKLRQAQAELEALKDDNDEETRETL--STLSLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1418 hgeKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFISET 1497
Cdd:PRK11281 129 ---RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1498 LR-RMEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAELEARELQRRM-QEEVTRREEAAVDAQQQK 1572
Cdd:PRK11281 193 QRvLLQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQEAInSKRLTLSEKTVQEAQSQD 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 1573 RS--------IQEELQHLRQSSEAEIQAKA-------------QQVEAAERSRMRIEEEIRVVR 1615
Cdd:PRK11281 270 EAariqanplVAQELEINLQLSQRLLKATEklntltqqnlrvkNWLDRLTQSERNIKEQISVLK 333
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1685-1739 |
8.10e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046896947 1685 AREKQRALQaldelKLQAEEAERRlRQAEAERARQVQVALETAQRS-AEVELQSKR 1739
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2320-2783 |
8.17e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2320 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSildEELQRLKAEVTEAARQR-SQVEEELFSVRVQMEELg 2398
Cdd:NF041483 209 AEAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAES---DQARRQAAELSRAAEQRmQEAEEALREARAEAEKV- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2399 kLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEeaarlsvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQE 2478
Cdd:NF041483 285 -VAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGE-------ATKEAEALKAEAEQALADARAEAEKLVAEAAEKART 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2479 ATRLKAEAELLQQQKElAQEQARRLQEDKEQMAQQLVEEtqgfqrtleAERQRQlEMSAEAERLKLRMAEMS-RAQARAE 2557
Cdd:NF041483 357 VAAEDTAAQLAKAART-AEEVLTKASEDAKATTRAAAEE---------AERIRR-EAEAEADRLRGEAADQAeQLKGAAK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2558 EDAQRFRKQAEEIGEKLHRTE-LATQEKVTLVQTLEIQRqqsdqdAERLREAIAELE---REKEKLKQEAKLLQLKSEEM 2633
Cdd:NF041483 426 DDTKEYRAKTVELQEEARRLRgEAEQLRAEAVAEGERIR------GEARREAVQQIEeaaRTAEELLTKAKADADELRST 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2634 QTVQQEQILQETQALQKSFLSEKDSLLQRERfIEQEKAKLEQLFQDEVAKAkqlqeeqqrqqqqmeqekqelvASMEEAR 2713
Cdd:NF041483 500 ATAESERVRTEAIERATTLRRQAEETLERTR-AEAERLRAEAEEQAEEVRA----------------------AAERAAR 556
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046896947 2714 RRQREAEEGVRRKQEELqrleqqrqqqekllAEENQRLR----ERLQRLEEEHRAALAHSEEIATSQAAATKAL 2783
Cdd:NF041483 557 ELREETERAIAARQAEA--------------AEELTRLHteaeERLTAAEEALADARAEAERIRREAAEETERL 616
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1844-2301 |
8.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1844 RELAEQELEKQR-QLAEGTAQQRLAAEQELIRLRAETEQGEQQrqllEEELARLQHEATAATQKRQELEAELAKVRAEME 1922
Cdd:COG4717 44 RAMLLERLEKEAdELFKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1923 VLlaSKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEA 2002
Cdd:COG4717 120 KL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2003 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqhKADIEERLAQLR--KASESELERQKGLVEDTLRQRRQV 2080
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARllLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2081 EEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQ 2160
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2161 RKvALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEA 2240
Cdd:COG4717 356 AE-ELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046896947 2241 EAARRAAEEAEeareqaereaaqsrkqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQ 2301
Cdd:COG4717 435 EELEEELEELE-----------------EELEELREELAELEAELEQLEEDGELAELLQEL 478
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2314-2779 |
8.38e-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: 42.50 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2314 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTtlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVE-----EELF 2388
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2389 SVRVQMEELgklKARIEAENRALILRDkDNTQRFLE---EEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2465
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLEmlqSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2466 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLVEETQGFQRTLEaerqrqLEMSAEAERLKlr 2545
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQMLKTNGL------LHTEDREEEIK-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2546 maemsraQARAEEDAQRFRK-QAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAK 2624
Cdd:pfam10174 276 -------QMEVYKSHSKFMKnKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2625 LLQLKSEEMQTV-----QQEQILQETQALQKSFLSE-KDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQM 2698
Cdd:pfam10174 349 ALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQ 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2699 EQEKQE--LVASMEEArrrQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRER---LQRLEEEHRAALAHSEEIA 2773
Cdd:pfam10174 429 TDSSNTdtALTTLEEA---LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKvsaLQPELTEKESSLIDLKEHA 505
|
....*.
gi 1046896947 2774 TSQAAA 2779
Cdd:pfam10174 506 SSLASS 511
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1836-1936 |
8.72e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1836 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1915
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 1046896947 1916 KvRAEMEVLLaskarAEEESR 1936
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2429-2645 |
8.80e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.16 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2429 KMKQvAEEAARLSV--AAQEAARLRQLAEEDLAQQRALAEKmlkeKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2506
Cdd:PRK00106 25 KMKS-AKEAAELTLlnAEQEAVNLRGKAERDAEHIKKTAKR----ESKALKKELLLEAKEEARKYREEIEQEFKSERQEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2507 KeQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLklrmAEMSRAQARAEEDAQRFRKQAEEigeKLHRTELATQEKVT 2586
Cdd:PRK00106 100 K-QIESRLTERATSLDRKDENLSSKEKTLESKEQSL----TDKSKHIDEREEQVEKLEEQKKA---ELERVAALSQAEAR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046896947 2587 LVQTLEIQRQQSDQDAERLREAIAELereKEKLKQEAKllQLKSEEMQTVQQEQILQET 2645
Cdd:PRK00106 172 EIILAETENKLTHEIATRIREAEREV---KDRSDKMAK--DLLAQAMQRLAGEYVTEQT 225
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1506-1673 |
8.85e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 42.33 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1506 RLAEQQRAEERERLAEVEAALEKQRQlaeahaqakAQAELEARELQRRMQEEvtRREeaavdAQQQKRSIQEELQhlrQS 1585
Cdd:PRK10811 644 RQAQQQTAETRESQQAEVTEKARTQD---------EQQQAPRRERQRRRNDE--KRQ-----AQQEAKALNVEEQ---SV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1586 SEAEIQAKAQQVEaAERSRMRIEEEIRVvrLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQ 1665
Cdd:PRK10811 705 QETEQEERVQQVQ-PRRKQRQLNQKVRI--EQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDE 781
|
....*...
gi 1046896947 1666 RKRQAEAE 1673
Cdd:PRK10811 782 ENNAENRD 789
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1834-2275 |
8.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1834 GKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIR--------LRAETEQGEQQRQLLEE------ELARLQHE 1899
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELES--LEGSKRKLEEKIReleerieeLKKEIEELEEKVKELKElkekaeEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1900 ATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEA----KRQ 1973
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkKKLKELEKRLEELEERHELYEEAKAKKEELerlkKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1974 RQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERL-----------RRLAED---EAFQRRRLE- 2038
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgRELTEEhrkELLEEYTAEl 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2039 EQAAQHKADIEERLAQLRKAS---ESELERQKGLV--EDTLRQRRQVEEEIMALKASFEKAAAGKAELELEL-----GRI 2108
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELrelEKVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKliklkGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2109 RSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAA---RQRKVALEEVERLKAKVEEARRLRERA 2185
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEerlKELEPFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2186 EQEsARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSR 2265
Cdd:PRK03918 622 KKL-EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
490
....*....|
gi 1046896947 2266 KQVEEAERLK 2275
Cdd:PRK03918 701 EELEEREKAK 710
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4438-4468 |
8.90e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 8.90e-03
10 20 30
....*....|....*....|....*....|.
gi 1046896947 4438 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4468
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2428-2522 |
8.92e-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: 41.50 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2428 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2501
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 1046896947 2502 RLQEDKEQMAQQLVEETQGFQ 2522
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1499-1580 |
9.18e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.60 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1499 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAELEARELQRRMQEEVTR-----REEAAVDAQ 1569
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKLAAEALAEAQAeaqasKEKARREIE 111
|
90
....*....|.
gi 1046896947 1570 QQKRSIQEELQ 1580
Cdd:PRK07353 112 QQKQAALAQLE 122
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2444-2626 |
9.42e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2444 AQEAARLRQLAEED--LAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLVEETQGF 2521
Cdd:COG1579 3 PEDLRALLDLQELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE-VEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2522 QRTLEAERqrqlemsaEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTElatqekvtlvQTLEIQRQQSDQD 2601
Cdd:COG1579 82 LGNVRNNK--------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE----------AELAELEAELEEK 143
|
170 180
....*....|....*....|....*
gi 1046896947 2602 AERLREAIAELEREKEKLKQEAKLL 2626
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREEL 168
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1843-1936 |
9.46e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 1843 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEME 1922
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 1046896947 1923 VLLASKARAEEESR 1936
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
2501-2679 |
9.55e-03 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 463525 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2501 RRLQEDKE-QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAeedaqrfrkqaeeIGEKLHRTEL 2579
Cdd:pfam12297 209 GRLQEEYErKMAALAAECNLETREKMEAQHQREMAEKEEAEELLKHADEQEALECSS-------------LLDKLHKLEQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046896947 2580 ATQEKVTLVQTLEIQRQQSDQDAERLR--------EAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQALQKS 2651
Cdd:pfam12297 276 EHLQRSLLLRQEEDFAKAQRQLAVFQRvelhkiffTQLKEATRKGELKPEAAKRLLQDYSKIQE-QIEELMDFFQANQRY 354
|
170 180
....*....|....*....|....*...
gi 1046896947 2652 FLSEKdsLLQRErFIEQEKAKLEQLFQD 2679
Cdd:pfam12297 355 HLSER--FAQRE-YLVQSLQSLETRVSG 379
|
|
| |
