|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
199-315 |
2.84e-72 |
|
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: 237.30 E-value: 2.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 199 DRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdlvrnvrlprekGRMRFHKLQNVQIALD 278
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNVQTALD 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220506 279 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 315
Cdd:cd21188 69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
196-326 |
6.44e-70 |
|
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: 231.07 E-value: 6.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 196 DERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlpreKGRMRFHKLQNVQI 275
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 276 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 326
Cdd:cd21235 69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
188-324 |
3.21e-67 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 223.71 E-value: 3.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 188 ERAVIRIADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlpreKGRMRF 267
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRF 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 268 HKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 324
Cdd:cd21236 72 HRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
328-433 |
7.18e-66 |
|
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: 219.12 E-value: 7.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 328 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 407
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1655220506 408 PEDVDVAHPDEKSIITYVSSLYDVMP 433
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
329-433 |
4.71e-64 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 213.79 E-value: 4.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 408
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1655220506 409 EDVDVAHPDEKSIITYVSSLYDVMP 433
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
196-325 |
3.11e-60 |
|
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: 203.34 E-value: 3.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 196 DERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGetlprerdlvrnVRLPREKGRMRFHKLQNVQI 275
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 276 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 325
Cdd:cd21237 69 ALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
329-433 |
2.26e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.82 E-value: 2.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAEReLGVTRLLDP 408
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1655220506 409 EDVDVAHPDEKSIITYVSSLYDVMP 433
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
327-433 |
3.87e-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: 177.16 E-value: 3.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 327 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAEReLGVTRLL 406
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1655220506 407 DPEDVDVAHPDEKSIITYVSSLYDVMP 433
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
188-312 |
5.79e-48 |
|
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: 168.31 E-value: 5.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 188 ERAVIR-IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMR 266
Cdd:cd21246 2 ERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKMR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1655220506 267 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 312
Cdd:cd21246 71 IHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
201-316 |
4.87e-47 |
|
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: 165.25 E-value: 4.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 201 VQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGEtlprerdlvrnvRLPREKGRMRFHKLQNVQIALDF 279
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGK------------KLKPEKGRMRVHHLNNVNRALQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21186 70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
329-429 |
5.78e-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: 162.20 E-value: 5.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 408
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1655220506 409 EDVDVAHPDEKSIITYVSSLY 429
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
329-429 |
5.87e-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: 156.40 E-value: 5.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 408
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655220506 409 EDVDVAHPDEKSIITYVSSLY 429
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
188-312 |
9.96e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 156.30 E-value: 9.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 188 ERAVIR-IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMR 266
Cdd:cd21193 2 EKGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRLR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1655220506 267 FHKLQNVQIALDFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 312
Cdd:cd21193 71 VQKIENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
197-316 |
3.45e-42 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 151.76 E-value: 3.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 197 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGEtlprerdlvrnvRLPREKGRM--RFHKLQN 272
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHFLSN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220506 273 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21241 69 INTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
195-429 |
5.36e-41 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 163.19 E-value: 5.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 195 ADERDRVQKKTFTKWVNKHLMKA-QRHITDLYEDLRDGHNLISLLEVLSGEtlprerDLVRNVRLPRekgrMRFHKLQNV 273
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKD------NAGEYNETPE----TRIHVMENV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 274 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDN 352
Cdd:COG5069 73 SGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 353 FTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQE--NLEQAFSVAERELGVTRLLDPEDV-DVAHPDEKSIITYVSSLY 429
Cdd:COG5069 150 FFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
194-312 |
5.46e-41 |
|
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: 149.41 E-value: 5.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 194 IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMRFHKLQNV 273
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGRMRIHSLENV 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220506 274 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 312
Cdd:cd21318 100 DKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
188-312 |
4.17e-40 |
|
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: 146.35 E-value: 4.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 188 ERAVIR-IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMR 266
Cdd:cd21317 17 ERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMR 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1655220506 267 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 312
Cdd:cd21317 86 IHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1952-2821 |
7.00e-40 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 164.93 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1952 EMDALLQMKIQAEKVSQSNTEKSKQllETEALKMKQLAEEAARLRSV--------AEEAKKQRQLAEDEAARQRAEAEKI 2023
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKAEEArkaedarkAEEARKAEDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2024 ---LKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 2100
Cdd:PTZ00121 1167 eeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2101 IVEETLRQKKVVEEEI-HIIRINFERASKEKSDLEvELKKlkgiADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKV 2179
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMaHFARRQAAIKAEEARKAD-ELKK----AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2180 KKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKqvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKL 2259
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2260 RDEFENAKKLAQAAETAKEKAEKEAALlRQKAEE---AEKLKKAAEdEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAA 2336
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEA-KKKAEEkkkADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2337 LKQKQEADAEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKAlmdEELQRVKAqvndavKQKAQvENELSKVKMQ 2416
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKA---------AEAKKKA---DEAKKAEE------AKKAD-EAKKAEEAKK 1535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2417 MDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKmkslAEEAARLSVEAEETARQrkTAEAELAEQRALAEKMLKEKM 2496
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----AEEDKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKA 1609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2497 QAIQEATKLKAEAEELQKQknqaqEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ 2576
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2577 AKAEEEATRFKKQADEAKvRLQETEKQTTEtvvqklETQRLQSTREADDLKKAIAE-LEKEREKLKRDAQELQNKSKETA 2655
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAK-KAEELKKKEAE------EKKKAEELKKAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2656 SAQQEQMEQQKAmlQQTFLTEKELLLKRERDVEDEKKKLQ--KHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2733
Cdd:PTZ00121 1758 KIAHLKKEEEKK--AEEIRKEKEAVIEEELDEEDEKRRMEvdKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEV 1835
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2734 V-------------------KKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREklESLEVTSKQAASKTKEIE 2794
Cdd:PTZ00121 1836 AdsknmqleeadafekhkfnKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK--DDIEREIPNNNMAGKNND 1913
|
890 900
....*....|....*....|....*..
gi 1655220506 2795 VQTDKVPEEQLVSMTTVETTKKVFNGS 2821
Cdd:PTZ00121 1914 IIDDKLDKDEYIKRDAEETREEIIKIS 1940
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
329-429 |
3.18e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 143.22 E-value: 3.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 408
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1655220506 409 EDVDVAHPDEKSIITYVSSLY 429
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
328-433 |
3.83e-39 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 142.84 E-value: 3.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 328 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 407
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1655220506 408 PEDVDVAHPDEKSIITYVSSLYDVMP 433
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1070-1147 |
7.23e-39 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 140.82 E-value: 7.23e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1070 LSWQYLMRDIHMIKTWNITMFKTLRVEEYRLALRNLEQHYQDFLRDSQDSQMFGAEDRMQVESNYNRANQHYNTMVSS 1147
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
316-429 |
8.53e-39 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 142.12 E-value: 8.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 316 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 395
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 396 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
197-316 |
1.30e-38 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 141.55 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 197 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRERDLVRNvrlprekgrmRFHKLQNVQ 274
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQ----------RAHKLSNIR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220506 275 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21190 71 NALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
199-312 |
2.25e-37 |
|
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: 137.52 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 199 DRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlvrnvrlPREKGRMRFHKLQNVQIALD 278
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANVNKALD 71
|
90 100 110
....*....|....*....|....*....|....
gi 1655220506 279 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 312
Cdd:cd21214 72 FIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
328-429 |
4.67e-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: 136.92 E-value: 4.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 328 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 407
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1655220506 408 PEDVDVAHPDEKSIITYVSSLY 429
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
325-429 |
6.42e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 136.73 E-value: 6.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 325 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTR 404
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1655220506 405 LLDPEDVDVAHPDEKSIITYVSSLY 429
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
332-433 |
1.04e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 135.63 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 332 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 410
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655220506 411 VDVAHPDEKSIITYVSSLYDVMP 433
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
201-314 |
1.33e-36 |
|
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: 135.61 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 201 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdlvrnvrlprEKGRMRFHKLQNVQIALDFL 280
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNKALEFI 73
|
90 100 110
....*....|....*....|....*....|....
gi 1655220506 281 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 314
Cdd:cd21215 74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
197-316 |
1.49e-35 |
|
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: 132.65 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 197 ERDRVQKKTFTKWVNKHLMKAQ--RHITDLYEDLRDGHNLISLLEVLSGEtlprerdlvrnvRLPREKGRMRFHKLQNVQ 274
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRSNIE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220506 275 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21242 69 TALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1964-2767 |
2.68e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.91 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1964 EKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSV---AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 2040
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2041 AEVALKAKEAENERLKRQAED--EAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihi 2118
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA--- 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2119 irinfERASKEKSDLEVELKKLKGIADETQKskakaeeeaeklkklAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQD 2198
Cdd:PTZ00121 1243 -----KKAEEERNNEEIRKFEEARMAHFARR---------------QAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2199 EVERLKQKAAEANKLKDKAEKelekqvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKE 2278
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKK--------AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2279 KAEKEAALLRQKAEE---AEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaakraaaeaaalKQKQEADAEMAKHKKEAE 2355
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAA--------------------KKKADEAKKKAEEKKKAD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2356 QAlKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAqvnDAVKQKAQVenelskvKMQMDELlklKVRIEEENLRLM 2435
Cdd:PTZ00121 1435 EA-KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEE-------AKKADEA---KKKAEEAKKKAD 1500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2436 QKNKDNTQKLLAEEAEKmkslAEEAaRLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQ 2515
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKK----AEEA-KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2516 KNQAQEKAKKL--LEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE----AEKLKLRVKELSSAQAKAEEEATRFKKQ 2589
Cdd:PTZ00121 1576 KNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2590 ADEAKVRLQETEKQTTEtvvqkletqrlqSTREADDLKKAIAELEKEREKLKRDAQElqnKSKETASAQQEQMEQQKAml 2669
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE------------DKKKAEEAKKAEEDEKKAAEALKKEAEE---AKKAEELKKKEAEEKKKA-- 1718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2670 qqtfltekELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQqrqqklmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQK 2749
Cdd:PTZ00121 1719 --------EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--------EEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
810 820
....*....|....*....|
gi 1655220506 2750 E--MEALEKKRLEQEKLLAD 2767
Cdd:PTZ00121 1783 EelDEEDEKRRMEVDKKIKD 1802
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
313-429 |
1.57e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 130.56 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 313 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQA 392
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220506 393 FSVAERELGVTRLLDPEDVDVAHPDEKSIITYVSSLY 429
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
328-426 |
3.24e-34 |
|
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: 128.70 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 328 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 407
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1655220506 408 PEDVDVAHPDEKSIITYVS 426
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
329-429 |
6.20e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 127.91 E-value: 6.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 408
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655220506 409 EDVDVAHPDEKSIITYVSSLY 429
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
188-312 |
4.37e-33 |
|
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: 127.08 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 188 ERAVIR-IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMR 266
Cdd:cd21316 39 ERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMR 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1655220506 267 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 312
Cdd:cd21316 108 IHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
196-316 |
6.14e-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: 125.04 E-value: 6.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 196 DERDRVQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGEtlprerdlvrnvRLPREKGRMRFHKLQNVQ 274
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHALNNVN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220506 275 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21231 69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1685-2728 |
9.20e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 141.82 E-value: 9.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1685 EEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKT 1764
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1765 aatqlqamsfseKTTKLEESLKKEQGtvlqlQEEAEKLRKQeEEANKAREQaeKELETWRlKANEALRLRL-RAEEEAQR 1843
Cdd:PTZ00121 1107 ------------ETGKAEEARKAEEA-----KKKAEDARKA-EEARKAEDA--RKAEEAR-KAEDAKRVEIaRKAEDARK 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1844 KSLAQEEAEKQKTEAERdaKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfEHAEQQRGLldN 1923
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAAR--KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA--------KKAEAVKKA--E 1233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1924 ELQRLKNEVNAAEKQRRQLE-DELAKVRSEMDALLQMKIQAEKvsqsnTEKSKQLLETEALKMKQLAEEAARLRSVAEEA 2002
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEE-----ARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2003 KKQRQLAEDEAARQRAEAEKilkeklaaiNEATRLKTEAEVALKAKEAenerlkRQAEDEAYQRKLledQAAQHKHDIQE 2082
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAK---------KKADAAKKKAEEAKKAAEA------AKAEAEAAADEA---EAAEEKAEAAE 1370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2083 KITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihiirinferasKEKSDlevELKKL---KGIADETQKskakaeeeae 2159
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEED------------KKKAD---ELKKAaaaKKKADEAKK---------- 1425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2160 klkklaaeeerkrreAEEKVKKIAAAEEEAARQRKAaqdevERLKQKAAEANKLKDKAEKELEKQvilAKEAAQKSTAAE 2239
Cdd:PTZ00121 1426 ---------------KAEEKKKADEAKKKAEEAKKA-----DEAKKKAEEAKKAEEAKKKAEEAK---KADEAKKKAEEA 1482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2240 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2319
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE----------AKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2320 KEAEAEAAKRAAAEAAalKQKQEADAEMAKHKKEaeqALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKA-QVND 2398
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEE--AKKAEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeELKK 1627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2399 AVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQ-KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTA 2477
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2478 EAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKnqaqEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLE 2557
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA----EEAKKDEEEKKKIAHLKKEE----EKKAEEIRKEKEA 1779
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2558 ISAEaeklklrvkELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrLQSTREADDLKKAIAELEKER 2637
Cdd:PTZ00121 1780 VIEE---------ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-DSAIKEVADSKNMQLEEADAF 1849
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2638 EKLKRDAQELQNKSKETASaqqeqmeqqkamlqqTFLTEKELLLKRERDVE--DEKKKLQKH-LEDEV-NKAKALKDEQQ 2713
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKEA---------------DFNKEKDLKEDDEEEIEeaDEIEKIDKDdIEREIpNNNMAGKNNDI 1914
|
1050
....*....|....*
gi 1655220506 2714 RQQKLMDEEKKKLQA 2728
Cdd:PTZ00121 1915 IDDKLDKDEYIKRDA 1929
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
332-434 |
9.94e-33 |
|
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: 124.66 E-value: 9.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 332 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-ENLEQAFSVAERELGVTRLLDPE 409
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1655220506 410 DVDVAHPDEKSIITYVSSLYDVMPR 434
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1675-2650 |
1.04e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 141.43 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1675 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEE-EKVRQ 1753
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEaRKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1754 IKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEE--EANKAREQAEKELETWRLKANEAL 1831
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1832 RLRLRAEEEAQRKSlaqEEAEKQKTEAERDAKkkakaeeaalkqkenaEKELEKQRTFAEqiaqqklsaeqeyirlkADF 1911
Cdd:PTZ00121 1219 KAEDAKKAEAVKKA---EEAKKDAEEAKKAEE----------------ERNNEEIRKFEE-----------------ARM 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1912 EHAEQQRGLLDNELQRLKNEVNAAEKQRRQleDELAKvrsemdallqmkiqAEKVSQSNTEKSKQLLETEALKMKQLAEE 1991
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKA--DEAKK--------------AEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1992 AAR----LRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAEN--ERLKRQAEDEAYQ 2065
Cdd:PTZ00121 1327 AKKkadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKK 1406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2066 RKLLEDQAAQHKhdiqekitqlqssSVSELDRQKNIVEETLRQKKVVEEeihiirinferasKEKSDlevELKKLkgiAD 2145
Cdd:PTZ00121 1407 ADELKKAAAAKK-------------KADEAKKKAEEKKKADEAKKKAEE-------------AKKAD---EAKKK---AE 1454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2146 ETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEverlKQKAAEANKLKDKAEKELEKQV 2225
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA----KKKADEAKKAEEAKKADEAKKA 1530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2226 ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRdeFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEA 2305
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2306 AKQAKaqKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKelglvklQLDETDKQKAlm 2385
Cdd:PTZ00121 1609 AEEAK--KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-------KKAEEDKKKA-- 1677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2386 dEELQRVKAQVNDAVKQKAQVENELSKVKmqmdellKLKVRIEEENLRLMQKNKDNTQKLLaeEAEKMKSLAEEAARLSV 2465
Cdd:PTZ00121 1678 -EEAKKAEEDEKKAAEALKKEAEEAKKAE-------ELKKKEAEEKKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAE 1747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2466 EAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKlkaeaEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQ 2545
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-----EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN 1822
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2546 KSLEAE----------RKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETeKQTTETVVQKLETQ 2615
Cdd:PTZ00121 1823 DSKEMEdsaikevadsKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA-DEIEKIDKDDIERE 1901
|
970 980 990
....*....|....*....|....*....|....*
gi 1655220506 2616 RLQSTREADDLKKAIAELEKErEKLKRDAQELQNK 2650
Cdd:PTZ00121 1902 IPNNNMAGKNNDIIDDKLDKD-EYIKRDAEETREE 1935
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
328-426 |
1.72e-32 |
|
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: 123.79 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 328 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 407
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1655220506 408 PEDVDVAHPDEKSIITYVS 426
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
316-429 |
7.74e-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: 122.25 E-value: 7.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 316 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 395
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 396 AERELGVTRLLDPEDV-DVAHPDEKSIITYVSSLY 429
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1593-2141 |
9.09e-32 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 137.38 E-value: 9.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1593 SQRQGLAVDAEKQK--QNIQLELTQLknlseqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLR 1670
Cdd:COG1196 200 RQLEPLERQAEKAEryRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1671 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1750
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1751 VRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWR--LKAN 1828
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEeaLAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1829 EALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK 1908
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1909 ADFEHAEQQRGLLDNELQ---------------RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQM-KIQAEKVSQSNTE 1972
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGveaayeaaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLdKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1973 KSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRA----EAEKILKEKLAAINEATRLKTEAEVALKAK 2048
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2049 EAENERLKRQAEDEAYQ------RKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRIN 2122
Cdd:COG1196 674 LLEAEAELEELAERLAEeeleleEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
570 580
....*....|....*....|
gi 1655220506 2123 FERASKEK-SDLEVELKKLK 2141
Cdd:COG1196 754 EELPEPPDlEELERELERLE 773
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1542-2755 |
1.13e-31 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 137.65 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1542 SEKLKEDEKKRMAEIQAQleTQKQLAEgHAKSVAK--AELEAqelklkmkEDASQRQGLAVDAEKQKQNIQLELT----- 1614
Cdd:NF041483 85 ADQLRADAERELRDARAQ--TQRILQE-HAEHQARlqAELHT--------EAVQRRQQLDQELAERRQTVESHVNenvaw 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1615 --QLKNLSEQEIRsknQQLEEaqvSRRKLEEEIHLIRIQ---LQTTIKQKSTADDELQKlrdqaAEAEKVRKAAQEEAER 1689
Cdd:NF041483 154 aeQLRARTESQAR---RLLDE---SRAEAEQALAAARAEaerLAEEARQRLGSEAESAR-----AEAEAILRRARKDAER 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1690 LRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQ-AE--------EAERRLKQAEEEKVRQIKVVEEV 1760
Cdd:NF041483 223 LLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQeAEealrearaEAEKVVAEAKEAAAKQLASAESA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1761 -AQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQ-LQEEAEKLRKqeEEANKAREQAEKELETWRLK-ANEALRLRLRA 1837
Cdd:NF041483 303 nEQRTRTAKEEIARLVGEATKEAEALKAEAEQALAdARAEAEKLVA--EAAEKARTVAAEDTAAQLAKaARTAEEVLTKA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1838 EEEAQRKS-LAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQ---RTFAEQIAQQKLSAEQEYIRLKADFEh 1913
Cdd:NF041483 381 SEDAKATTrAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEyraKTVELQEEARRLRGEAEQLRAEAVAE- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1914 AEQQRGlldnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQ-MKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEA 1992
Cdd:NF041483 460 GERIRG------EARREAVQQIEEAARTAEELLTKAKADADELRStATAESERVRTEAIERATTLRRQAEETLERTRAEA 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1993 ARLRSVAEE-AKKQRQLAEDEAARQRAEAEKILKEKLA-AINEATRLKTEAEVALKAKE-------AENERLKRQAEDEA 2063
Cdd:NF041483 534 ERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERLTAAEealadarAEAERIRREAAEET 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2064 YQrklLEDQAAqhkhdiqEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIhiirinferASKEKSDLEVELKKLKGI 2143
Cdd:NF041483 614 ER---LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENV---------AVRLRSEAAAEAERLKSE 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2144 ADETqKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKA----AEANKLKDKAEK 2219
Cdd:NF041483 675 AQES-ADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSeellASARKRVEEAQA 753
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2220 ELEKqviLAKEAAQKST----AAEQKAQDVlsknkedllsqeklRDEFENAKKLAQAAETAkekaekeaalLRQKAEE-A 2294
Cdd:NF041483 754 EAQR---LVEEADRRATelvsAAEQTAQQV--------------RDSVAGLQEQAEEEIAG----------LRSAAEHaA 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2295 EKLKKAAEDEA--------AKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKqkqEADAEMAKHKKEAEQaLKQKSQVEK 2366
Cdd:NF041483 807 ERTRTEAQEEAdrvrsdayAERERASEDANRLRREAQEETEAAKALAERTVS---EAIAEAERLRSDASE-YAQRVRTEA 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2367 ELGLVKLQLDETdKQKALMDEELQRVK----AQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLR--------- 2433
Cdd:NF041483 883 SDTLASAEQDAA-RTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRadaaaqaeq 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2434 LMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEET-ARQRKTAEAELAEQRALAEKMLKEkmqAIQEATKLKAE-AEE 2511
Cdd:NF041483 962 LIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVkAEAAAEAERLRTEAREEADRTLDE---ARKDANKRRSEaAEQ 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2512 LQKQKNQAQEKAKKLLEDKQEIQQR--LDKETQGfQKSLEAERKRQLEISAEA--------EKLKLRVKELSSAqakAEE 2581
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQEEALRttTEAEAQA-DTMVGAARKEAERIVAEAtvegnslvEKARTDADELLVG---ARR 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2582 EATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAElekEREKLKRDAQELQNKSKETASAqqeq 2661
Cdd:NF041483 1115 DATAIRERAEELRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEE---QLAEAEAKAKELVSDANSEASK---- 1187
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2662 meqqkamLQQTFLTEKELLLKrerdvEDEKKKlqkhlEDEVNKAKALKDEQQRQQKLMDEEKKKLqaiMDEAVKKQKEAE 2741
Cdd:NF041483 1188 -------VRIAAVKKAEGLLK-----EAEQKK-----AELVREAEKIKAEAEAEAKRTVEEGKRE---LDVLVRRREDIN 1247
|
1290
....*....|....
gi 1655220506 2742 AEMKNKQKEMEALE 2755
Cdd:NF041483 1248 AEISRVQDVLEALE 1261
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1618-2452 |
3.18e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 136.42 E-value: 3.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1618 NLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKvRKAAQEEAERLRKQvnEE 1697
Cdd:PTZ00121 1056 HEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARK-AEEAKKKAEDARKA--EE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1698 TQKKKNAedelkRKSEAEKEAARQKQKALDELQKHKMQAEEAER--RLKQAEE-EKVRQIKVVEEVAQKTAATQLQAMSF 1774
Cdd:PTZ00121 1133 ARKAEDA-----RKAEEARKAEDAKRVEIARKAEDARKAEEARKaeDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1775 SEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQE-EAEK 1853
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1854 QKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVN 1933
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1934 AAEKQRRQLE---DELAKVRSEMDALLQMKIQAEKVSQSNTE-KSKQLLETEALKMKQLAEE---AARLRSVAEEAKKQR 2006
Cdd:PTZ00121 1368 AAEKKKEEAKkkaDAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEkkkADEAKKKAEEAKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2007 QLAEDEAARQRAEAekiLKEKLAAINEATRLKTEAEVALKAKEAEN--ERLKRQAED----EAYQRKLLEDQAAQHKHDI 2080
Cdd:PTZ00121 1448 EAKKKAEEAKKAEE---AKKKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEakkaAEAKKKADEAKKAEEAKKA 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2081 QEKITQLQSSSVSELDRQKNIVE-ETLRQKKVVEEEIHIIRInfERASKEKSDLEVELKKlkgiADETQKSKAKAEEEAE 2159
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKaDELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRK----AEEAKKAEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2160 KLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKaaqdEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2239
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK----KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2240 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALlrQKAEE-----AEKLKKAAEDEAAKQAKAQKD 2314
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL--KKAEEenkikAEEAKKEAEEDKKKAEEAKKD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2315 AErlrkeaeaeaakrAAAEAAALKQKQEADAEMAKHKKEA--EQALKQKSqvEKELGLVKLQLDETDKQKALMDEELQRV 2392
Cdd:PTZ00121 1753 EE-------------EKKKIAHLKKEEEKKAEEIRKEKEAviEEELDEED--EKRRMEVDKKIKDIFDNFANIIEGGKEG 1817
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2393 KAQVNDA----VKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKD-NTQKLLAEEAEK 2452
Cdd:PTZ00121 1818 NLVINDSkemeDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADfNKEKDLKEDDEE 1882
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1505-2116 |
3.47e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.45 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1505 QEYVTLRTRYSELS-TLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQE 1583
Cdd:COG1196 213 ERYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1584 LKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTAD 1663
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1664 DELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRL 1743
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1744 KQAEEEKVRQIKVVEEVAQKTAATQLQamsfsekttkleeslkkeqgtVLQLQEEAEKLRKQEEEANKAREQAEKELETW 1823
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAA---------------------LAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1824 RLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTF----------AEQI 1893
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkiraraALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1894 AQQKLSAEQEYIRLKADFEHAEQQRGLLDNEL---QRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmkiqaekvSQSN 1970
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA--------GGSL 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1971 TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 2050
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2051 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQS---SSVSELDRQKNIVEETLRQKKVVEEEI 2116
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlLAIEEYEELEERYDFLSEQREDLEEAR 811
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
200-317 |
4.25e-31 |
|
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: 120.25 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlpREKGRMRFHKLQNVQIALDF 279
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKF----------NKRPTFRSQKLENVSVALKF 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220506 280 LKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 317
Cdd:cd21311 84 LEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1731-2318 |
9.88e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.91 E-value: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1731 KHKMQAEEAERRLKQAEE----------EKVRQIKVVEEvaQKTAATQLQAMSFSEKTTKLEESLKKEQgtvlQLQEEAE 1800
Cdd:COG1196 169 KYKERKEEAERKLEATEEnlerledilgELERQLEPLER--QAEKAERYRELKEELKELEAELLLLKLR----ELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1801 KLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAE 1880
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1881 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMK 1960
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1961 IQAEKVSQSNTEKSKQLLETEAlkmkQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 2040
Cdd:COG1196 403 EELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2041 AEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQ-----------------------LQSSSVSELDR 2097
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavavligveaayeaaleaalaaaLQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2098 QKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEE 2177
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2178 KVKKIAAAEEEAARQRKAAQD-EVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQ 2256
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGgSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2257 EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEaAKQAKAQKDAERL 2318
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE-RELERLEREIEAL 779
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
201-316 |
2.98e-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: 117.39 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 201 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRerdLVRNVRlprekgrMRFHKLQNVQIALDFL 280
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIKKPL-------NQHQKLENVTLALKAM 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655220506 281 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21227 74 AEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1666-2268 |
5.11e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.60 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1666 LQKLRDQAAEAEKVRKAAQEEAERlrkQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ 1745
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKEL---EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1746 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1825
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1826 KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYI 1905
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1906 RLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkiQAEKVSQSNTEKSKQLLETEALKM 1985
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-----AARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1986 KQLAEEAARLRSVAEEAkkQRQLAEDEAARQRAEAekilkekLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ 2065
Cdd:COG1196 514 LLLAGLRGLAGAVAVLI--GVEAAYEAALEAALAA-------ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2066 RKLLEDQAAQHKhdIQEKITQLQSSSVSELDRQKNIVEETLrqkkvveeEIHIIRINFERASKEKSDLEVELKKLKGIAD 2145
Cdd:COG1196 585 RAALAAALARGA--IGAAVDLVASDLREADARYYVLGDTLL--------GRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2146 EtqkSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQV 2225
Cdd:COG1196 655 G---GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1655220506 2226 ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKK 2268
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1529-2124 |
5.26e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 132.57 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1529 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQN 1608
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1609 IQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihliRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1688
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1689 RLRKQVNEETQK---KKNAEdELKRKSEAEKEAARQKQKAlDELQKHKMQAEEAERRLKQAEE-EKVRQIKVVEEVAQKT 1764
Cdd:PTZ00121 1382 AAKKKAEEKKKAdeaKKKAE-EDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKA 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1765 AATQLQAmsfsEKTTKLEESLKK--EQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrLKANEALRL-RLRAEEEA 1841
Cdd:PTZ00121 1460 EEAKKKA----EEAKKADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA--KKAEEAKKAdEAKKAEEA 1533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1842 QRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLL 1921
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1922 DNELQRLKNE-VNAAEKQRRQLEDELAKVRSEMDALLQMKiQAEKVSQSNTEKSKQLLETEalkmKQLAEEAARlrsvAE 2000
Cdd:PTZ00121 1614 KAEEAKIKAEeLKKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEED----KKKAEEAKK----AE 1684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2001 EAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEValkaKEAENERLKRQAEDEAYQRKLLEDQAAQhKHDI 2080
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKI 1759
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1655220506 2081 QEKITQLQSSSVSELDRQKNIVEETLRQK-----KVVEEEIHIIRINFE 2124
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEdekrrMEVDKKIKDIFDNFA 1808
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
332-433 |
7.14e-30 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 116.21 E-value: 7.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 332 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 410
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655220506 411 VDVAHPDEKSIITYVSSLYDVMP 433
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
334-429 |
1.00e-29 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 115.91 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 334 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED-VD 412
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1655220506 413 VAHPDEKSIITYVSSLY 429
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
332-431 |
2.81e-29 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 114.30 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 332 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED- 410
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1655220506 411 VDVAHPDEKSIITYVSSLYDV 431
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
197-318 |
2.89e-29 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 114.60 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 197 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRERDLVRNvrlprekgrmRFHKLQNVQ 274
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSH----------RIFRLNNIA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220506 275 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 318
Cdd:cd21191 71 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
201-316 |
7.19e-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: 113.57 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 201 VQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPRERdlvrnvrlprekGRMRFHKLQNVQIALDF 279
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNRVLQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21232 70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
200-314 |
8.08e-29 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 113.34 E-value: 8.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDlvrnvrlprEKGRMRFHKLQNVQIALDF 279
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVSTALKF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 314
Cdd:cd21183 74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1629-2504 |
1.73e-28 |
|
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: 127.09 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1629 QQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADdELQKLRDQAAEAEK-----VRKAAQEEAERLRKQVNEETQKKKN 1703
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAE-RYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1704 AEDELK-----------RKSEAEKEAARQkQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAm 1772
Cdd:TIGR02168 258 LTAELQeleekleelrlEVSELEEEIEEL-QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1773 sfSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR--LRLRAEEEAQRKSLAQEE 1850
Cdd:TIGR02168 336 --AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1851 AEKQKTEAERdakkKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKN 1930
Cdd:TIGR02168 414 DRRERLQQEI----EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1931 EVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALkmkqLAEEAARLRSVAEEAKKQRQ--L 2008
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA----LGGRLQAVVVENLNAAKKAIafL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2009 AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAEnerlkrQAEDEAyqRKLLE------------DQAA-- 2074
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKL--RKALSyllggvlvvddlDNALel 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2075 QHKHDIQEKITQLQSSSV---------------SELDRQKNIvEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKK 2139
Cdd:TIGR02168 638 AKKLRPGYRIVTLDGDLVrpggvitggsaktnsSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2140 LKGIADETQKskakaeeeaeklkklaaeeerKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEK 2219
Cdd:TIGR02168 717 LRKELEELSR---------------------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2220 ELekqvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKK 2299
Cdd:TIGR02168 776 EL-------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2300 AAEDEAAKQAKAQKDAErlrkeaeaeaakraaaeaaalkqkqeadAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETD 2379
Cdd:TIGR02168 849 ELSEDIESLAAEIEELE----------------------------ELIEELESELEALLNERASLEEALALLRSELEELS 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2380 KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKlkvRIEEE---NLRLMQKNKDNTQKLLAEEAEKMKSL 2456
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE---RLSEEyslTLEEAEALENKIEDDEEEARRRLKRL 977
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2457 AEEAARL---SVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATK 2504
Cdd:TIGR02168 978 ENKIKELgpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1529-2252 |
2.38e-28 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 127.18 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1529 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAEleaqelKLKMKEDASQrqglaVDAEKQKQN 1608
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE------ELRKAEDARK-----AEAARKAEE 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1609 IQleltQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQ-EEA 1687
Cdd:PTZ00121 1211 ER----KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1688 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAT 1767
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1768 QLQAMSFSEKTTKLEESLKK--EQGTVLQLQEEAEKLRKQEEEANKArEQAEKELETWRLKANE---ALRLRLRAEEEAQ 1842
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKaeEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEEkkkADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1843 RKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK--ELEKQRTFAEQIAQQKLSAEQEyiRLKAD----FEHAEQ 1916
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEA--KKKADeakkAEEAKK 1523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1917 QRGLLDNELQRLKNEVNAAEKQRRQleDELAKVRSEMDAllQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR 1996
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1997 SVAEEAK-KQRQLAEDEAARQRAE----AEKILKEKLAAINEATRLKTEAEVALKAKEAEN---ERLKRQAEDEayQRKL 2068
Cdd:PTZ00121 1600 LYEEEKKmKAEEAKKAEEAKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEED--KKKA 1677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2069 LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKgiADETQ 2148
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEE 1755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2149 KSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA----NKLKDKAEKELEKQ 2224
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGnlviNDSKEMEDSAIKEV 1835
|
730 740
....*....|....*....|....*...
gi 1655220506 2225 VILAKEAAQKSTAAEQKAQDVLSKNKED 2252
Cdd:PTZ00121 1836 ADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1788-2651 |
4.29e-28 |
|
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: 125.55 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1788 EQGTVLQLQE-EAEKLRKQEEEA------NKAREQAEKELEtwrlKANEAL-RLR-LRAEEEAQRKSLaqeeaEKQKTEA 1858
Cdd:TIGR02168 142 EQGKISEIIEaKPEERRAIFEEAagiskyKERRKETERKLE----RTRENLdRLEdILNELERQLKSL-----ERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1859 ERdakkkakaeeaaLKQKENAEKELEKqrtfaEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQ 1938
Cdd:TIGR02168 213 ER------------YKELKAELRELEL-----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1939 RRQLEDELAKVRSEMDAL------LQMKIQAEKVSQSNTEKSKQLLETEALKMKQ----LAEEAARLRSVAEEAKKQRQL 2008
Cdd:TIGR02168 276 VSELEEEIEELQKELYALaneisrLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELKEELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2009 AE---DEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKIT 2085
Cdd:TIGR02168 356 LEaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2086 QLQSSSVSELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLA 2165
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELER---LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2166 AEEERKRREAEEKVKKIAAAEEEAA---------------RQRKAAQDEVERLKQKAA------EANKLKDKAEKELEKQ 2224
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGYEAaieaalggrlqavvvENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDRE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2225 VILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALL----------------- 2287
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssi 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2288 ---RQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQV 2364
Cdd:TIGR02168 673 lerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2365 EKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDElLKLKVRIEEENLRLMQKNKDNTQK 2444
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRERLESLER 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2445 LLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAK 2524
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2525 KLLEDKQEIQQRLDKETQGFQKsLEAERKRQLEISAEAEKLKLR-VKELSSAQAKAEEEATRFKKQADEAKVRL------ 2597
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIKELgpvnla 990
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2598 QETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKS 2651
Cdd:TIGR02168 991 AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNEN 1044
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1876-2764 |
7.47e-28 |
|
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: 125.08 E-value: 7.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1876 KENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK----ADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1951
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1952 EMDAlLQMKIQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAI 2031
Cdd:pfam02463 259 EIEK-EEEKLAQVLKENKEEEKEKKLQEEEL---KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2032 NEATRLKTEAEVALKAKEAENErlkrqAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRqkkv 2111
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEE-----EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK---- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2112 veeeihIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAeekvkkiaaaeeeaar 2191
Cdd:pfam02463 406 ------EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD---------------- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2192 qrkaaQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQ 2271
Cdd:pfam02463 464 -----ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2272 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAE-RLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2350
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLiPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2351 KKEAEQALKQKSQVE--KELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIE 2428
Cdd:pfam02463 619 DKRAKVVEGILKDTEltKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2429 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSveAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2508
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI--NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2509 AEELQKQKNQAQEKAKKLLEDKQEiqqrldketqgfqkslEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2588
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQE----------------EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2589 QADEAKVRLQETEKQTTEtvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM 2668
Cdd:pfam02463 841 ELKEEQKLEKLAEEELER--LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2669 LQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQR-QQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNK 2747
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRlLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890
....*....|....*..
gi 1655220506 2748 QKEMEALEKKRLEQEKL 2764
Cdd:pfam02463 999 RLEEEKKKLIRAIIEET 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1286-2040 |
2.46e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.71 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1286 IRNTKDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEaEADQATFDRLQDELKAATSV--SDKMTRLHSERDA 1363
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELrkAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1364 ElehyrqlagsllerwqavfaqiDLRQRElsllgrhmnsykqsyewliqwlrEARLRQEKIEAAPVwdskalkeQLTQEK 1443
Cdd:PTZ00121 1209 E----------------------EERKAE-----------------------EARKAEDAKKAEAV--------KKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1444 KLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIQeyvtlrtryselstltSQ 1523
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK----------------AE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1524 YIKFILETQRRLEDDEKASE--KLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKA--ELEAQELKLKMKEDASQRQGLA 1599
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEakKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1600 VDAEKQKQNIQLELTQLKNLSEqEIRSKNQQLEEAQVSRRKLEEeihliriqLQTTIKQKSTAdDELQKLRDQAAEAEKV 1679
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAE-EDKKKADELKKAAAAKKKADE--------AKKKAEEKKKA-DEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1680 RKAAQE--EAERLRKQVNEetqkkKNAEDELKRKSEAEKEAARQKQKAlDELQKHKMQAEEAERRLKQAEE-EKVRQIKV 1756
Cdd:PTZ00121 1450 KKKAEEakKAEEAKKKAEE-----AKKADEAKKKAEEAKKADEAKKKA-EEAKKKADEAKKAAEAKKKADEaKKAEEAKK 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1757 VEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlr 1836
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL--- 1600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1837 AEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEkELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQ 1916
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1917 QRGllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR 1996
Cdd:PTZ00121 1680 AKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1655220506 1997 SVAEEAKKQRQLAEDeaarQRAEAEKILKEKLAAINEATRLKTE 2040
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1976-2800 |
5.24e-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: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1976 QLLETEALKMKQLAEEAA---RLRSVAEEAkkQRQLAEDEAARQRAEAekILKEKLAAINeatRLKTEAEVALKAKEAEN 2052
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKET--ERKLERTRENLDRLED--ILNELERQLK---SLERQAEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2053 ErlKRQAEDEAYQRKLleDQAAQHKHDIQEKITQLQSSsVSELDRQKNIVEETLRQKKV----VEEEIHIIRINFERASK 2128
Cdd:TIGR02168 221 E--LRELELALLVLRL--EELREELEELQEELKEAEEE-LEELTAELQELEEKLEELRLevseLEEEIEELQKELYALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2129 EKSDLEVELKKLKGIADETQKSKakaeeeaeklkklaaeeerkrreaeekvKKIAAAEEEAARQRKAAQDEVERLKQKAA 2208
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQL----------------------------EELEAQLEELESKLDELAEELAELEEKLE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2209 EANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLR 2288
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2289 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQK----SQV 2364
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2365 EKELGLVKLQLD----------ETDKQ-----KALMDEELQRVKAQVNDAVKQ--KAQVENELSKVKMQmdELLKLKVRI 2427
Cdd:TIGR02168 508 VKALLKNQSGLSgilgvlseliSVDEGyeaaiEAALGGRLQAVVVENLNAAKKaiAFLKQNELGRVTFL--PLDSIKGTE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2428 EEENLRLMQKNKDNTQKLLAEEAEKMKSLA----------------EEAARLSVEAEETAR------QRKTAEAELAEQR 2485
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRivtldgDLVRPGGVITGGS 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2486 ALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2565
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2566 KLRVKELSSAQAKAEEEATRFKKQADEAkvrlqETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQ 2645
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEA-----EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2646 ELQNKsKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKK 2725
Cdd:TIGR02168 821 NLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 2726 LQAIMDEAVKKQKEAEAEMKNKQKEMEALEkKRLEQEKLLADENK-KLREKLE-SLEVTSKQAASKTKEIEVQTDKV 2800
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLE-LRLEGLEVRIDNLQeRLSEEYSlTLEEAEALENKIEDDEEEARRRL 974
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2000-2828 |
2.31e-26 |
|
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: 120.08 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2000 EEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQhKHD 2079
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD-EQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2080 IQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAE 2159
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2160 KLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2239
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2240 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2319
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2320 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQ--VN 2397
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVraLT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2398 DAVKQKAQVENELSKVKMQMDELLKLKV-------RIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARL------- 2463
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIdpilnlaQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKesglrkg 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2464 -SVEAEETARQRKTAEAELAEQRALAEKMLKEKM--------QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQ 2534
Cdd:pfam02463 652 vSLEEGLAEKSEVKASLSELTKELLEIQELQEKAeselakeeILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2535 QRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLET 2614
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2615 QRLQSTREADDLKKaiAELEKEREKLKRDAQELQNKSKETASAQQEQmEQQKAMLQQTFLTEKELLLKRERDVEDEKKKL 2694
Cdd:pfam02463 812 EEAELLEEEQLLIE--QEEKIKEEELEELALELKEEQKLEKLAEEEL-ERLEEEITKEELLQELLLKEEELEEQKLKDEL 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2695 QKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK-----------EAEAEMKNKQKEMEALEKKRLEQEK 2763
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyeeepeellleEADEKEKEENNKEEEEERNKRLLLA 968
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2764 LLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNGSVEAVKKD 2828
Cdd:pfam02463 969 KEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGW 1033
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
200-314 |
2.97e-26 |
|
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: 106.03 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDlvrnvrlprEKGRMRFHKLQNVQIALDF 279
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVSVALEF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 314
Cdd:cd21228 74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
314-429 |
3.27e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 106.32 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 314 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAF 393
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220506 394 SVAERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1813-2542 |
1.35e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 117.35 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1813 REQAEKELEtwRLKANEAlRLRLRAEE-EAQRKSLaQEEAEK-------QKTEAERDAKKKAKAEEAALKQKENAEKELE 1884
Cdd:COG1196 174 KEEAERKLE--ATEENLE-RLEDILGElERQLEPL-ERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1885 KqrtfaeqiaqqklsAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE 1964
Cdd:COG1196 250 E--------------LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1965 KVSQSNTEKSKQLLETEALKMKQLAEEAARLRSvAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVA 2044
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2045 LKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihiirinfE 2124
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL--------A 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2125 RASKEKSDLEVELKKLKGIADEtqkskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaARQRKAAQDEVERLK 2204
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAE-------------------------------------------AAARLLLLLEAEADY 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2205 QKAAEANKLKDKAEKELEKQVILAkEAAQKSTAAEQKAQDVLSknkedLLSQEKLRDEFENAKKLAQaaetakekAEKEA 2284
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVA-VLIGVEAAYEAALEAALA-----AALQNIVVEDDEVAAAAIE--------YLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2285 ALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQV 2364
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2365 EKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKvRIEEENLRLMQKNKDNTQK 2444
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL-AEAEEERLEEELEEEALEE 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2445 LLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEK----MQAIQEATKLKAEAEELQKQKNQAq 2520
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnLLAIEEYEELEERYDFLSEQREDL- 807
|
730 740
....*....|....*....|..
gi 1655220506 2521 EKAKKLLEdkqEIQQRLDKETQ 2542
Cdd:COG1196 808 EEARETLE---EAIEEIDRETR 826
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
200-317 |
2.13e-25 |
|
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: 104.34 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDlvrnvrlPREKgrMRFHKLQNVQIALDF 279
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVSVALEF 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 317
Cdd:cd21310 86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1881-2732 |
2.41e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 116.69 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1881 KELEKQrtfAEQIAQQKLSAEQeYIRLKADFEHAeqQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlQMK 1960
Cdd:TIGR02168 196 NELERQ---LKSLERQAEKAER-YKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL-EEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1961 IQAEKVSQSNTEKSKQLLETEalkMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 2040
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKE---LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2041 AEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHK------HDIQEKITQLQSSsVSELDRQKNIVEETLRQKKVVEE 2114
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2115 EIhiiriNFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRK 2194
Cdd:TIGR02168 425 EL-----LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2195 AAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKED-------LLSQEKLRDEF---- 2263
Cdd:TIGR02168 500 NLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAakkaiafLKQNELGRVTFlpld 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2264 -ENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAE------------DEAAKQAKAQKDAERLRKEAEAEAAKRA 2330
Cdd:TIGR02168 580 sIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2331 AAEAAALKQKQ---EADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVE 2407
Cdd:TIGR02168 660 VITGGSAKTNSsilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2408 NELSKVKMQMDELlklkvrieeenlrlmqknkdntQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAeqral 2487
Cdd:TIGR02168 740 AEVEQLEERIAQL----------------------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----- 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2488 aekmlkekmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEKLKL 2567
Cdd:TIGR02168 793 ---------QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT----ERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2568 RVKELSSAQAKAEEEATRFKKQADEAKVRLQ--ETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQ 2645
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALAllRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2646 ELQnkskETASAQQEqmeqqkaMLQQTFLTEKELLLKRERDVEDEKKKLQKHLED--EVNKA--KALKDEQQRQQKL--- 2718
Cdd:TIGR02168 940 NLQ----ERLSEEYS-------LTLEEAEALENKIEDDEEEARRRLKRLENKIKElgPVNLAaiEEYEELKERYDFLtaq 1008
|
890
....*....|....*..
gi 1655220506 2719 ---MDEEKKKLQAIMDE 2732
Cdd:TIGR02168 1009 kedLTEAKETLEEAIEE 1025
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
334-429 |
2.55e-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: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 334 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED-VD 412
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1655220506 413 VAHPDEKSIITYVSSLY 429
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1622-2544 |
2.92e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 116.61 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1622 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKK 1701
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1702 KNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamsfSEKTTKL 1781
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD---------EEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1782 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERD 1861
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE-------ELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1862 AKkkakaeeaalkqkENAEKELEKQRTFAEQIaqqklsaeqeyirlkadfEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ 1941
Cdd:pfam02463 393 KE-------------EELELKSEEEKEAQLLL------------------ELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1942 LEDELAKVRSEMDALLQMKIQAEKVSqsntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAE 2021
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELEL----KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2022 KILKEKL-AAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 2100
Cdd:pfam02463 518 DGVGGRIiSAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2101 IVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKL----KGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAE 2176
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLkesaKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2177 EKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEanKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQ 2256
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKE--ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2257 EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaaKRAAAEAAA 2336
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL---------EEEQLLIEQ 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2337 LKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELskvkmQ 2416
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK-----E 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2417 MDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEaelAEQRALAEKMLKEKM 2496
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK---RLLLAKEELGKVNLM 978
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2497 QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGF 2544
Cdd:pfam02463 979 AIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
193-316 |
3.15e-25 |
|
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: 103.68 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 193 RIADERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMRFHKL 270
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRVHFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655220506 271 QNVQIALDFLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21247 81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
316-429 |
5.14e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 102.86 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 316 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 395
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 396 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
329-429 |
6.28e-25 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 102.12 E-value: 6.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 408
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1655220506 409 ED-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21198 80 ADmVLLSVPDKLSVMTYLHQIR 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
329-433 |
7.06e-25 |
|
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: 101.79 E-value: 7.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 408
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1655220506 409 EDVDVAHPDEKSIITYVSSLYDVMP 433
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
330-429 |
7.67e-25 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 101.87 E-value: 7.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 330 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPE 409
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1655220506 410 D-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
328-434 |
2.08e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.82 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 328 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ--ENLEQAFSVAERELGVTR 404
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDklENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1655220506 405 -LLDPEdvDVAHPDEKSIITYVSSLYDVMPR 434
Cdd:pfam00307 81 vLIEPE--DLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2206-2780 |
2.28e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2206 KAAEAN--KLKDKAEkELEKQV-ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEK 2282
Cdd:COG1196 182 EATEENleRLEDILG-ELERQLePLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2283 EaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraaaeaaaLKQKQEADAEMAKHKKEAEQALKQKS 2362
Cdd:COG1196 261 E---LAELEAELEELRLELEELELELEEAQAEEYEL------------------LAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2363 QVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKnKDNT 2442
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2443 QKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK 2522
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2523 AKKLLEDKQEIQQRLD------KETQGFQKSLEAERK---------------------RQLEISAEAEKLKLRVKELSSA 2575
Cdd:COG1196 479 LAELLEELAEAAARLLllleaeADYEGFLEGVKAALLlaglrglagavavligveaayEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2576 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAE-----------LEKEREKLKRDA 2644
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYyvlgdtllgrtLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2645 QELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKK 2724
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2725 KLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADEN------KKLREKLESLE 2780
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEelerelERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2447-2806 |
2.59e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2447 AEEAEKMKSLAEEAARLsvEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2526
Cdd:COG1196 209 AEKAERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2527 LEDKQEIQQRLDKETQgfQKSLEAERKRQLEisAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQtte 2606
Cdd:COG1196 287 QAEEYELLAELARLEQ--DIARLEERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2607 tvvqkletqRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtfltEKELLLKRERD 2686
Cdd:COG1196 360 ---------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA--------LLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2687 VEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLmDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLA 2766
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655220506 2767 DENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLV 2806
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
332-432 |
1.76e-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: 97.92 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 332 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPEDV 411
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1655220506 412 DVAHPDEKSIITYVSSLYDVM 432
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
204-313 |
2.84e-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: 97.00 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 204 KTFTKWVNKHLMKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlVRNVRlpreKGRMRFHKLQNVQIALDFLKH 282
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVD-----KKKVA----ASLSRFKKIENINLALSFAEK 71
|
90 100 110
....*....|....*....|....*....|.
gi 1655220506 283 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 313
Cdd:smart00033 72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1528-2451 |
4.93e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 109.29 E-value: 4.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1528 ILETQRRLEDDEKASEKLKEDEKKrmAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1607
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKK--ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1608 NIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1687
Cdd:pfam02463 263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-----KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1688 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQktaat 1767
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE----- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1768 qlqamsfsekttkleeslkkeqgtvlqlqeeaekLRKQEEEANKAREQAEKEletwrlKANEALRLRLRAEEEAQRKSLA 1847
Cdd:pfam02463 413 ----------------------------------LARQLEDLLKEEKKEELE------ILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1848 QEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQR 1927
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1928 LKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQ 2007
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2008 LAEDEAARQRAEAEKILKEKlaainEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQL 2087
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDT-----ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2088 QSSSVSELDRQKNIVEETLRQKKVVE---EEIHIIRINFERASKEKSDLEVELKKLKgIADETQKSKAKAEEEAEKLKKL 2164
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKklkLEAEELLADRVQEAQDKINEELKLLKQK-IDEEEEEEEKSRLKKEEKEEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2165 AAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERlkqkaAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQD 2244
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR-----ALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2245 VLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEA 2324
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2325 EAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKqksQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKA 2404
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE---EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1655220506 2405 QVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAE 2451
Cdd:pfam02463 999 RLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGS 1045
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
969-1035 |
5.58e-23 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 95.02 E-value: 5.58e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 969 QLKPRNpaTPIKSKLPIQAVCDFKQMEITVHRGDECALLNNSQPYKWRVLNDKGSEASVPSICFLVP 1035
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
316-429 |
6.22e-23 |
|
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: 97.10 E-value: 6.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 316 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 395
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 396 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1290-2096 |
2.65e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 107.15 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1290 KDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELkaatsvsdkmtRLHSERDAELEHYR 1369
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI-----------RKFEEARMAHFARR 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1370 QLAGSLLERWQAVfaqiDLRQRELSllgRHMNSYKQSYEwlIQWLREARLRQEKIEAApvwdsKALKEQLTQEKKLLEEI 1449
Cdd:PTZ00121 1269 QAAIKAEEARKAD----ELKKAEEK---KKADEAKKAEE--KKKADEAKKKAEEAKKA-----DEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1450 EKNKDQIENCQKDAKAYIDSLKDYefqilAYRALQDPIASPLKKPKMESASDNIIQEyvtlrtryselstltSQYIKFIL 1529
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADE-----AEAAEEKAEAAEKKKEEAKKKADAAKKK---------------AEEKKKAD 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLK--EDEKKRMAEIQAQLETQKQLAEghAKSVAKAELEAQELKlKMKEDASQRQGLAVDAEKQKQ 1607
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1608 NIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihliriqlqttiKQKStadDELQKlRDQAAEAEKVRKAAQ-EE 1686
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA------------KKKA---DEAKK-AEEAKKADEAKKAEEaKK 1535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1687 AERLRKQvnEETQKKknaeDELKRKSEAEK-EAARQKQKALDELQKHKMQAEEAErRLKQAEEEKVRQIKVVEEVAQKTA 1765
Cdd:PTZ00121 1536 ADEAKKA--EEKKKA----DELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMK 1608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1766 ATQL----QAMSFSEKTTKLEESLKKEQGTVLQLQEE---AEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlRAE 1838
Cdd:PTZ00121 1609 AEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-----KKA 1683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1839 EEAQRKSlaqEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIaqqKLSAEQEyirlKADFEHAEQQR 1918
Cdd:PTZ00121 1684 EEDEKKA---AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA---KKEAEED----KKKAEEAKKDE 1753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1919 GLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQ---------AEKVSQSNTEKSKQLLETEALKMKQLA 1989
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikdifdnFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1990 EEAARLRSVAEEAK--------KQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAED 2061
Cdd:PTZ00121 1834 EVADSKNMQLEEADafekhkfnKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNND 1913
|
810 820 830
....*....|....*....|....*....|....*
gi 1655220506 2062 EAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELD 2096
Cdd:PTZ00121 1914 IIDDKLDKDEYIKRDAEETREEIIKISKKDMCIND 1948
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1377-1956 |
3.85e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1377 ERWQAVfaQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIEknkDQI 1456
Cdd:COG1196 213 ERYREL--KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELE---LEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1457 ENCQKDAKAYIDSLKDYEFQILAYRALQdpiasplkkpkmESASDNIIQEYVTLRTRYSELSTLTSQyIKFILETQRRLE 1536
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERR------------RELEERLEELEEELAELEEELEELEEE-LEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1537 DDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQL 1616
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1617 KNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRI--QLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1694
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELlaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1695 NEETQKKKNAE-----------DELKRKSEAEKEAARQKQKALDELQkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQK 1763
Cdd:COG1196 511 KAALLLAGLRGlagavavligvEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1764 TAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQR 1843
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1844 KSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN 1923
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
570 580 590
....*....|....*....|....*....|...
gi 1655220506 1924 ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1956
Cdd:COG1196 747 LLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
201-316 |
4.71e-22 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 93.89 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 201 VQKKTFTKWVNKHLMKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLPrerdlvrnvrlPREKGRMRFHKLQNVQIALD 278
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINLALD 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220506 279 FLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:pfam00307 71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1530-2422 |
6.69e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLkEDEKKRMAEIQAQLETQKQLAEG-HAKSVAKAELEAQELKLKMKEdasqrqglAVDAEKQKQN 1608
Cdd:TIGR02168 176 ETERKLERTRENLDRL-EDILNELERQLKSLERQAEKAERyKELKAELRELELALLVLRLEE--------LREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1609 IQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1688
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1689 RLRkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEkvrqikvVEEVAQKTAATQ 1768
Cdd:TIGR02168 327 ELE-------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1769 LQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQ 1848
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1849 EEAEKQKTEAErdakkkakaEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQ---------EYIRLKADFEHAeqqrg 1919
Cdd:TIGR02168 473 AEQALDAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAA----- 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1920 lLDNELQ-RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR-- 1996
Cdd:TIGR02168 539 -IEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1997 ------------SVAEEAKKQRQLAEDEA---------------ARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKE 2049
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2050 AENERLK---RQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNI---VEETLRQKKVVEEEIHIIRINF 2123
Cdd:TIGR02168 698 KALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskeLTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2124 ERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERL 2203
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2204 KQKAAEANKLKDKAEKELekqvilakEAAQKSTAAEQKAQDVLSKNKEDLlsQEKLRDEFENAKKlaqaaetakekaeke 2283
Cdd:TIGR02168 858 AAEIEELEELIEELESEL--------EALLNERASLEEALALLRSELEEL--SEELRELESKRSE--------------- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2284 aalLRQKAEEA-EKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAeqalkqks 2362
Cdd:TIGR02168 913 ---LRRELEELrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI-------- 981
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2363 qveKELGLVKLQ-LDETDKQKalmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLK 2422
Cdd:TIGR02168 982 ---KELGPVNLAaIEEYEELK----ERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2191-2732 |
1.01e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLA 2270
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2271 QAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2350
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2351 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE 2430
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2431 NLRLMQ--------KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEA 2502
Cdd:COG1196 500 EADYEGflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2503 TKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQ--KSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAE 2580
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2581 EEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE 2660
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2661 QMEQQKAMLQQTFLTEKELLLKRErDVEDEKKKLQKHLE----------DEVNKAKALKDEQQRQQKLMDEEKKKLQAIM 2730
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLE-ELERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAI 818
|
..
gi 1655220506 2731 DE 2732
Cdd:COG1196 819 EE 820
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
316-429 |
2.02e-21 |
|
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: 92.83 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 316 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 395
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 396 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
200-317 |
3.73e-21 |
|
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: 92.07 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDlvrnvrlprEKGRMRFHKLQNVQIALDF 279
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVSVALEF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 317
Cdd:cd21308 90 LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
200-317 |
3.89e-21 |
|
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: 92.07 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdlvrnvrlpREKGRMRFHKLQNVQIALDF 279
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVSVALEF 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 317
Cdd:cd21309 87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
329-429 |
5.13e-21 |
|
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: 90.87 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 408
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1655220506 409 EDVDV--AHPDEKSIITYVSSLY 429
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1529-2607 |
5.92e-21 |
|
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: 102.18 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1529 LETQRRLEDDEKASEKLKEdEKKRMAE-IQAQLETQKQLAEGHAKSVA-KAELEA--QELKLKMKEDASQRQGLAVDAEK 1604
Cdd:pfam01576 22 QKAESELKELEKKHQQLCE-EKNALQEqLQAETELCAEAEEMRARLAArKQELEEilHELESRLEEEEERSQQLQNEKKK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1605 QKQNIQLELTQLKnlsEQEIRSKNQQLEE--AQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEkvrka 1682
Cdd:pfam01576 101 MQQHIQDLEEQLD---EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEE----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1683 aqEEAERLRKQVNEETQKKKNAEDELKR--KSEAEKEAARQKQKA-LDELQKH----KMQAEEAERRLKQAEEE-KVRQI 1754
Cdd:pfam01576 173 --EKAKSLSKLKNKHEAMISDLEERLKKeeKGRQELEKAKRKLEGeSTDLQEQiaelQAQIAELRAQLAKKEEElQAALA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1755 KVVEEVAQKTAATQlqamsfsekttkleeSLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrLKANEALRLR 1834
Cdd:pfam01576 251 RLEEETAQKNNALK---------------KIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEA--LKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1835 LRAEEEAQRKSLAQEEAEKQKT---EAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADF 1911
Cdd:pfam01576 314 TTAAQQELRSKREQEVTELKKAleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1912 E-------HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE----KVSQSNTEKSKQLLET 1980
Cdd:pfam01576 394 RtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniKLSKDVSSLESQLQDT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1981 EAL---KMKQLAEEAARLRSVAEEAKK-QRQLAEDEAARQRAEAEkilkeklaaineatrlkteaevaLKAKEAENERLK 2056
Cdd:pfam01576 474 QELlqeETRQKLNLSTRLRQLEDERNSlQEQLEEEEEAKRNVERQ-----------------------LSTLQAQLSDMK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2057 RQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQ--SSSVSELDRQKNiveetlrqkkvveeeihiirinfeRASKEKSDLE 2134
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEekAAAYDKLEKTKN------------------------RLQQELDDLL 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2135 VELKKLKGIADETQKskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERlKQKAAEANKLK 2214
Cdd:pfam01576 587 VDLDHQRQLVSNLEK-----------------------------------------KQKKFDQMLAEE-KAISARYAEER 624
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2215 DKAEKELE----KQVILAKEAAQKSTAAEQ--KAQDVLSKNKEDLLSQE----KLRDEFENAKKLAQAAETAkekaekea 2284
Cdd:pfam01576 625 DRAEAEAReketRALSLARALEEALEAKEEleRTNKQLRAEMEDLVSSKddvgKNVHELERSKRALEQQVEE-------- 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2285 alLRQKAEEAEKLKKAAED-----EAAKQA-KAQKDAErlrkeAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQAL 2358
Cdd:pfam01576 697 --MKTQLEELEDELQATEDaklrlEVNMQAlKAQFERD-----LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAV 769
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2359 KQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKqkaqvenELSKVKMQMDELL--------KLKvRIEEE 2430
Cdd:pfam01576 770 AAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQR-------ELEEARASRDEILaqskesekKLK-NLEAE 841
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2431 NLRL-------------MQKNKDNTQKLLAEEAEKMKSLAEEAARLSV-------EAEETA--------RQRKTAE---- 2478
Cdd:pfam01576 842 LLQLqedlaaserarrqAQQERDELADEIASGASGKSALQDEKRRLEAriaqleeELEEEQsntellndRLRKSTLqveq 921
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2479 --AELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK-QEIQQRLDKETQGFQKS-------- 2547
Cdd:pfam01576 922 ltTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKiAQLEEQLEQESRERQAAnklvrrte 1001
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2548 ---------LEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRfkkqADEAKVRLQETEKQTTET 2607
Cdd:pfam01576 1002 kklkevllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR----ANAARRKLQRELDDATES 1066
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1436-2142 |
6.37e-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: 102.06 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1436 KEQLTQEKKLLEEIEKNKDQIENCQKDAKAYID------------SLKDYEFQILAYRALQDPIASP------------- 1490
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERQAEKAERYKElkaelrelelalLVLRLEELREELEELQEELKEAeeeleeltaelqe 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1491 ---------LKKPKMESASDNIIQEYVTLrtrYSELSTLTSQyIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLE 1561
Cdd:TIGR02168 265 leekleelrLEVSELEEEIEELQKELYAL---ANEISRLEQQ-KQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1562 TQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQeIRSKNQQLEEAQVSRRKL 1641
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE-IERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1642 EEEIHLIRIQLQTtiKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRkseaekeaARQ 1721
Cdd:TIGR02168 420 QQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ--------LQA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1722 KQKALDELQKHKMQAEEAERRLKQAEEEK-------VRQIKVVEE---------------VAQKTAATQLQAMSF----- 1774
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlSELISVDEGyeaaieaalggrlqaVVVENLNAAKKAIAFlkqne 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1775 SEKTTKLEESLKKE---QGTVLQLQEEAEKLRKQEEEANKAREQAEKELETW--------------RLKANEALRLRL-- 1835
Cdd:TIGR02168 570 LGRVTFLPLDSIKGteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddldnalELAKKLRPGYRIvt 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1836 ---------------RAEEEAQRKSLAQE--EAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKL 1898
Cdd:TIGR02168 650 ldgdlvrpggvitggSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1899 SAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL----LQMKIQAEKVSQSNTEKS 1974
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqiEQLKEELKALREALDELR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1975 KQLLETE------ALKMKQLAEEAARLRSVAEEAKKQ-RQLAED--EAARQRAEAEKILKEKLAAINEATRLKTEAEVAL 2045
Cdd:TIGR02168 810 AELTLLNeeaanlRERLESLERRIAATERRLEDLEEQiEELSEDieSLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2046 KAKEAENERLKRQAEDEAYQRKLLEDQ---AAQHKHDIQEKITQLQsssvSELDRQKniveETLRQKKVVEEEIHIIRIN 2122
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRREleeLREKLAQLELRLEGLE----VRIDNLQ----ERLSEEYSLTLEEAEALEN 961
|
810 820
....*....|....*....|
gi 1655220506 2123 FERASKEKsdLEVELKKLKG 2142
Cdd:TIGR02168 962 KIEDDEEE--ARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1291-1956 |
1.34e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 101.29 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1291 DAEDTVKSYESRLRDVSKvpaEEKEVEAHRSQLKAMRAEAEAD-----------QATFDRLQDELKAATSVSDKMTRLHS 1359
Cdd:TIGR02168 299 RLEQQKQILRERLANLER---QLEELEAQLEELESKLDELAEElaeleekleelKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1360 ERDAELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQ--------EKIEAAPVWD 1431
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleelEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1432 SKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqiLAYRALQDPIASPLKKPKMESASDNIIQEYVTLR 1511
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ---ENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1512 TRYS-ELSTLTSQYIKFILetQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKE 1590
Cdd:TIGR02168 533 EGYEaAIEAALGGRLQAVV--VENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1591 DASQRQGLA--------VDAEKQKQNIQLELTQLKNL--------------------SEQEIRSKNQQLEEAQVSRRKLE 1642
Cdd:TIGR02168 611 DPKLRKALSyllggvlvVDDLDNALELAKKLRPGYRIvtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEELE 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1643 EEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQK 1722
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1723 QKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKL 1802
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1803 RKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKkakaeeaalkqkenAEKE 1882
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE--------------LRRE 916
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 1883 LEKQRTFAEQIAQQKLSAEQEYIRLKadfehaEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1956
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
333-431 |
1.44e-20 |
|
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: 89.72 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 333 KLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD-PEDV 411
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1655220506 412 DVAHPDEKSIITYVSSLYDV 431
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1314-2071 |
2.48e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 100.13 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1314 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL 1393
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1394 sllgRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDY 1473
Cdd:TIGR02168 312 ----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1474 EFQILAYRALQDPIASPLKKPKMESAS--DNIIQEYVTLRTRYS-----ELSTLTSQYIKFILETQRRLEDDEKASEKLK 1546
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDrrERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1547 E----------DEKKRMAEIQAQ---LETQKQLAEGHAKSVAKAELEAQEL---------KLKMKE-------------- 1590
Cdd:TIGR02168 468 EeleeaeqaldAAERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLsgilgvlseLISVDEgyeaaieaalggrl 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1591 -----DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKN----QQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST 1661
Cdd:TIGR02168 548 qavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDreilKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1662 ADDELQKLRDQAAEAEKVRkAAQEEAERLRK---------QVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKH 1732
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYR-IVTLDGDLVRPggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1733 KMQAEEAERRLKQAEEEKVRQIkvveevaqktAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA 1812
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQI----------SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1813 REQAEKELETwrlkaNEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAkaeeaalkqKENAEKELEKQRTFAEQ 1892
Cdd:TIGR02168 777 LAEAEAEIEE-----LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER---------LESLERRIAATERRLED 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1893 IAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTE 1972
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1973 KSKQL-LETEALKMkQLAEEAARLRS----VAEEAKKQRQLAEDEAARQRAEAEKiLKEKLAA---INEAtrlkteaevA 2044
Cdd:TIGR02168 923 KLAQLeLRLEGLEV-RIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LENKIKElgpVNLA---------A 991
|
810 820 830
....*....|....*....|....*....|
gi 1655220506 2045 LKAKEAENER---LKRQAEDEAYQRKLLED 2071
Cdd:TIGR02168 992 IEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
329-428 |
3.91e-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: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 408
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|..
gi 1655220506 409 EDVdVAH--PDEKSIITYVSSL 428
Cdd:cd21255 80 ADM-VLLpiPDKLIVMTYLCQL 100
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
325-432 |
1.02e-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: 87.31 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 325 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTR 404
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1655220506 405 LLDPEDV-DVAHPDEKSIITYVSSLYDVM 432
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
329-428 |
6.59e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 84.90 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 408
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1655220506 409 ED-VDVAHPDEKSIITYVSSL 428
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1292-1980 |
7.61e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.39 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1292 AEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAAtsvsdkmtrlHSERDAELEHYRQL 1371
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------LEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1372 AGSLLERWQAVFAQIDLRQRELSLLGRhmnsykqsyewliqwlREARLRQEKIEAApvWDSKALKEQLTQEKKLLEEIEK 1451
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEE----------------RLEELEEELAELE--EELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1452 NKDQIENCQKDAKAyidslkdyefqilayralqdpiasplKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILET 1531
Cdd:COG1196 352 ELEEAEAELAEAEE--------------------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1532 QRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEgHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQL 1611
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1612 ELTQLKNLSE-QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQkLRDQAAEAEKVRKAAQEEAERL 1690
Cdd:COG1196 485 ELAEAAARLLlLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-AALAAALQNIVVEDDEVAAAAI 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1691 rkqvneETQKKKNAEdelkRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQ 1770
Cdd:COG1196 564 ------EYLKAAKAG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1771 AMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEE 1850
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1851 AEKQKTEAERDakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLkN 1930
Cdd:COG1196 714 EERLEEELEEE------------ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-G 780
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1931 EVN-------AAEKQRRQ-LEDELAKVRSEMDALLQMkiqaekVSQSNTEKSKQLLET 1980
Cdd:COG1196 781 PVNllaieeyEELEERYDfLSEQREDLEEARETLEEA------IEEIDRETRERFLET 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2510-2807 |
1.26e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2510 EELQKQKNQAqEKAKKLLEDKQEIQQRLD-KETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2588
Cdd:COG1196 203 EPLERQAEKA-ERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2589 QADEAKVRLQETEKQttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKsKETASAQQEQMEQQKAM 2668
Cdd:COG1196 282 ELEEAQAEEYELLAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2669 LQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAImdEAVKKQKEAEAEmKNKQ 2748
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEE-ALAE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2749 KEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVS 2807
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1710-2816 |
1.47e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 94.47 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1710 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLkkeq 1789
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEIL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1790 gtvlqlqEEAEKLRKQEEEANKAREQAEKELETWRLKANEALrlrlrAEEEAQRKSLaqeEAEKQKTEAERDAKKKAKAE 1869
Cdd:pfam01576 78 -------HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL-----DEEEAARQKL---QLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1870 EAALKQKENAEKELEKQRtfaeqIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNA---AEKQRRQLEDEL 1946
Cdd:pfam01576 143 LEDQNSKLSKERKLLEER-----ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1947 AKVRSEMdalLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE----AKKQRQLAEDEAARQRAEAEK 2022
Cdd:pfam01576 218 TDLQEQI---AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELeaqiSELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2023 I-LKEKLAAineatrLKTEAEVALKAKEAENE-RLKRQAEDEAYQrKLLEDQAAQHKHDIQEkITQLQSSSVSELDRQkn 2100
Cdd:pfam01576 295 RdLGEELEA------LKTELEDTLDTTAAQQElRSKREQEVTELK-KALEEETRSHEAQLQE-MRQKHTQALEELTEQ-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2101 iVEETLRQKKVVEEEIHIIrinferaSKEKSDLEVELKKLKGIADETQKskakaeeeaeklkklaaeeerKRREAEEKVK 2180
Cdd:pfam01576 365 -LEQAKRNKANLEKAKQAL-------ESENAELQAELRTLQQAKQDSEH---------------------KRKKLEGQLQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2181 KIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKqviLAKEAAQkstaAEQKAQDVLSknkedlLSQEKLR 2260
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKDVSS----LESQLQDTQE------LLQEETR 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2261 DEFENAKKlaqaaetakekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraAAEAAALKQK 2340
Cdd:pfam01576 483 QKLNLSTR------------------LRQLEDERNSLQEQLEEEEEAKRNVERQLSTL------------QAQLSDMKKK 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2341 QEADAEMakhkkeAEQALKQKSQVEKELGLVKLQLDEtdkqKALMDEELQrvkaqvndavKQKAQVENELSKVKMQMDEL 2420
Cdd:pfam01576 533 LEEDAGT------LEALEEGKKRLQRELEALTQQLEE----KAAAYDKLE----------KTKNRLQQELDDLLVDLDHQ 592
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2421 LKLKvrieeENLRLMQKNKDntqKLLAEEAEKMKSLAEEAARlsveAEETARQRKTAEAELAeqRALAEkmLKEKMQAIQ 2500
Cdd:pfam01576 593 RQLV-----SNLEKKQKKFD---QMLAEEKAISARYAEERDR----AEAEAREKETRALSLA--RALEE--ALEAKEELE 656
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2501 EATK-LKAEAEELQKQKNQAQ------EKAKKLLEDK-QEIQQRLDKETQGFQKSLEAerKRQLEISAEAEKLKLRvKEL 2572
Cdd:pfam01576 657 RTNKqLRAEMEDLVSSKDDVGknvhelERSKRALEQQvEEMKTQLEELEDELQATEDA--KLRLEVNMQALKAQFE-RDL 733
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2573 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVV--QKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNK 2650
Cdd:pfam01576 734 QARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRE 813
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2651 SKETASAQQEQMEQQKAMLQQTFLTEKELLLKRE---------RDVEDEKKKLQKHLEDEVNKAKALKDEQQR---QQKL 2718
Cdd:pfam01576 814 LEEARASRDEILAQSKESEKKLKNLEAELLQLQEdlaaserarRQAQQERDELADEIASGASGKSALQDEKRRleaRIAQ 893
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2719 MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEA---LEKKRLEQEKLLADENKKLREKLESLE--VTSKQAAS----- 2788
Cdd:pfam01576 894 LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAersTSQKSESARQQLERQNKELKAKLQEMEgtVKSKFKSSiaale 973
|
1130 1140
....*....|....*....|....*....
gi 1655220506 2789 -KTKEIEVQTDKVPEEQLVSMTTVETTKK 2816
Cdd:pfam01576 974 aKIAQLEEQLEQESRERQAANKLVRRTEK 1002
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1539-2539 |
1.55e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 94.36 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1539 EKASEKLKEDEKkRMAEIQAQLETQKQLAEGHAKSVAKAElEAQELKLKMKE-DASQRQGLAVDAEKQKQNIqleltqlk 1617
Cdd:TIGR02169 173 EKALEELEEVEE-NIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyEGYELLKEKEALERQKEAI-------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1618 nlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLqttikqkstaddelqklrdqAAEAEKVRKAAQEEAERLRKQVNEE 1697
Cdd:TIGR02169 243 ---ERQLASLEEELEKLTEEISELEKRLEEIEQLL--------------------EELNKKIKDLGEEEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1698 TQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLkqaEEEKVRQIKVVEEVAqktaatqlqamsfsEK 1777
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI---EEERKRRDKLTEEYA--------------EL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1778 TTKLEESLKkeqgtvlQLQEEAEKLRKQEEEANKAREqaekELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTE 1857
Cdd:TIGR02169 363 KEELEDLRA-------ELEEVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1858 AERDAKKKAKAeeaalkqKENAEKELEKQrtfaeqiaqqklsaEQEYIRLKADFEHAEQqrglldnELQRLKNEVNAAEK 1937
Cdd:TIGR02169 432 IEAKINELEEE-------KEDKALEIKKQ--------------EWKLEQLAADLSKYEQ-------ELYDLKEEYDRVEK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1938 QRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEAlKMKQLAEEAARLRSVAEEAKKQRQLAEDEAArqR 2017
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA-QLGSVGERYATAIEVAAGNRLNNVVVEDDAV--A 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2018 AEAEKILKEKlaAINEATRLKteaevalkakeaenerLKRQAEDEAYQRKLLEDQAAQHKHDiqekitqlqsssVSELDR 2097
Cdd:TIGR02169 561 KEAIELLKRR--KAGRATFLP----------------LNKMRDERRDLSILSEDGVIGFAVD------------LVEFDP 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2098 Q-KNIVEETLRQKKVVE--EEIHIIRINFERASkeksdLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE 2174
Cdd:TIGR02169 611 KyEPAFKYVFGDTLVVEdiEAARRLMGKYRMVT-----LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2175 AEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAA-------QKSTAAEQKAQDVLS 2247
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEedlssleQEIENVKSELKELEA 765
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2248 KNKEDLLSQEKLRDEFENAKklaqaaetakekaekeAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaa 2327
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLE----------------ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ---------- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2328 kraaAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDEtdkqkalMDEELQRVKAQVNDAVKQKAQVE 2407
Cdd:TIGR02169 820 ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLK 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2408 NELSKVKMQMDEllkLKVRIEEENLRLMQKNK-DNTQKLLAEEA-EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQR 2485
Cdd:TIGR02169 889 KERDELEAQLRE---LERKIEELEAQIEKKRKrLSELKAKLEALeEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2486 ALaEKMLKEKMQAIQeatklkaEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDK 2539
Cdd:TIGR02169 966 EI-RALEPVNMLAIQ-------EYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
329-427 |
1.90e-18 |
|
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: 83.44 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGKLFNAIIHKHRPALLDMS-QVYRQSNQENLEQAFSVAERELGVTRLLD 407
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNeSLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1655220506 408 PEDVDVAHPDEKSIITYVSS 427
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2346-2794 |
2.31e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 93.59 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2346 EMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVE---NELSKVKMQMDELLK 2422
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2423 lKVRIEEENLRLMQKNKDNTQKLLAE------EAEKMKSLAEEAARLSVEAEETARQRKTAEAELA---EQRALAEKMLK 2493
Cdd:PRK03918 253 -SKRKLEEKIRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSrleEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2494 EKMQAIQEATKLKAEAEELQKQKN------QAQEKAKKLLEDKQEIQQRL-DKETQGFQKSLEAERKRQLEISAEAEKLK 2566
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEeleerhELYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2567 LRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLetqrlqsTREADDLKKAIAELEKEREKLKRDAQE 2646
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEY-------TAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2647 LQN--KSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKL------QKHLEDEVNKAKALKDEQQRQQKL 2718
Cdd:PRK03918 485 LEKvlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2719 MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLE----------QEKLLADENKKLREKLESLEVTSKQAAS 2788
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdaekelerEEKELKKLEEELDKAFEELAETEKRLEE 644
|
....*.
gi 1655220506 2789 KTKEIE 2794
Cdd:PRK03918 645 LRKELE 650
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
332-428 |
3.01e-18 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 82.75 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 332 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ----ENLEQAFSVAERELGVTRLLD 407
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1655220506 408 PEDVDVAHPDEKSIITYVSSL 428
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
331-429 |
3.22e-18 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 83.12 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 331 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 410
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1655220506 411 -VDVAHPDEKSIITYVSSLY 429
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1797-2651 |
6.84e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.05 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1797 EEAEKLRKQEEEANKAREQAEKELETWRLKANEALR---LRLRAEE-EAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAA 1872
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1873 LKQKENAEKELEKQRTFAEQIAQQ-KLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1951
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1952 EMDALlQMKIQAEKVSQ-SNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED----------------EAA 2014
Cdd:TIGR02169 337 EIEEL-EREIEEERKRRdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkreldrlqEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2015 RQRAEAEKILKEKLAAINEA-TRLKTEAEVALKAKEAENERLKRQAED-EAYQRKLLEDQAAQHKhdIQEKITQLQSSsV 2092
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEWKLEQLAADlSKYEQELYDLKEEYDR--VEKELSKLQRE-L 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2093 SELDRQKNIVEETLRQKKVVEEEI------------HIIRInferasKEKSDLEVEL---KKLKGIADETQ--------- 2148
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaQLGSV------GERYATAIEVaagNRLNNVVVEDDavakeaiel 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2149 -KSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVER---LKQKAAEANKLKDKAekeleKQ 2224
Cdd:TIGR02169 567 lKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAARRLMGKY-----RM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2225 VILAKEAAQKS---TAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAA 2301
Cdd:TIGR02169 642 VTLEGELFEKSgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2302 EDEAAK-QAKAQKDAERLRKEAEAEAAkraaaeaaaLKQKQEA-DAEMAKHKKEAEqalkqksqvEKELGLVKLQLDETD 2379
Cdd:TIGR02169 722 EKEIEQlEQEEEKLKERLEELEEDLSS---------LEQEIENvKSELKELEARIE---------ELEEDLHKLEEALND 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2380 KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnlrlmqknKDNTQKLLAEEAEKMKSLAEE 2459
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE--------IQELQEQRIDLKEQIKSIEKE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2460 AARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdk 2539
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-- 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2540 etqgfqKSLEAERKRQLEISAE---AEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQEtekqttetvvqkLETQR 2616
Cdd:TIGR02169 934 ------SEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDE------------LKEKR 995
|
890 900 910
....*....|....*....|....*....|....*
gi 1655220506 2617 LQSTREADDLKKAIAELEKEREKLKRDAQELQNKS 2651
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKREVFMEAFEAINEN 1030
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
202-314 |
1.11e-17 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 81.47 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 202 QKKTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPRerdlvrnvrlPREKGRMRFHKLQNVQIALDF 279
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQACLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 314
Cdd:cd21212 71 LAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1782-2660 |
1.13e-17 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 91.43 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1782 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlraeeeaqRKSLAQEEAEKQKTEAERD 1861
Cdd:NF041483 7 QESHRADDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEA------------RRSLASRPAYDGADIGYQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1862 AKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQqklsaeqeyirlkadfEHAEQQrglldnelQRLKNEVNAAEKQRRQ 1941
Cdd:NF041483 75 EQLLRNAQIQADQLRADAERELRDARAQTQRILQ----------------EHAEHQ--------ARLQAELHTEAVQRRQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1942 -LEDELAKVRSEMDALLQMKIQ-AEKVSQSNTEKSKQLL-ETEALKMKQLAEEAARLRSVAEEAkKQRQLAEDEAArqRA 2018
Cdd:NF041483 131 qLDQELAERRQTVESHVNENVAwAEQLRARTESQARRLLdESRAEAEQALAAARAEAERLAEEA-RQRLGSEAESA--RA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2019 EAEKILKeklaaineatRLKTEAEVALKAKEAENERLKRQAEdeayqrklledqaaqhkhdiqekitQLQSSSVSELDRQ 2098
Cdd:NF041483 208 EAEAILR----------RARKDAERLLNAASTQAQEATDHAE-------------------------QLRSSTAAESDQA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2099 KNIVEETLRQkkvveeeihiirinferASKEKSDLEVELKKLKGIADETqkskakaeeeaeklkklaaeeerKRREAEEK 2178
Cdd:NF041483 253 RRQAAELSRA-----------------AEQRMQEAEEALREARAEAEKV-----------------------VAEAKEAA 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2179 VKKIAAAEEEAARQRKAAQDEVERLKQKA--------AEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQ------- 2243
Cdd:NF041483 293 AKQLASAESANEQRTRTAKEEIARLVGEAtkeaealkAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQlakaart 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2244 --DVLSKNKEDllSQEKLRDEFENAKKLAQaaetakEKAEKEAALLRQKAEEAEKLKKAAEDEA----AKQAKAQKDAER 2317
Cdd:NF041483 373 aeEVLTKASED--AKATTRAAAEEAERIRR------EAEAEADRLRGEAADQAEQLKGAAKDDTkeyrAKTVELQEEARR 444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2318 LrkeaeaeaakraAAEAAALKQKQEADAEM--AKHKKEAEQALKQKSQVEKELgLVKLQLDETD-KQKALMDEELQRVKA 2394
Cdd:NF041483 445 L------------RGEAEQLRAEAVAEGERirGEARREAVQQIEEAARTAEEL-LTKAKADADElRSTATAESERVRTEA 511
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2395 qVNDAVKQKAQVENELSKVKMQMDELlklkvRIE-EENLRLMQKNKDNTQKLLAEEAE-----KMKSLAEEAARLSVEAE 2468
Cdd:NF041483 512 -IERATTLRRQAEETLERTRAEAERL-----RAEaEEQAEEVRAAAERAARELREETEraiaaRQAEAAEELTRLHTEAE 585
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2469 EtarQRKTAEAELAEQRALAEKMLKEkmqAIQEATKLKAE-AEELQKQKNQAQEKAKKLledkqeiqqRLDKETQGFQKS 2547
Cdd:NF041483 586 E---RLTAAEEALADARAEAERIRRE---AAEETERLRTEaAERIRTLQAQAEQEAERL---------RTEAAADASAAR 650
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2548 LEAE----RKRQlEISAEAEKLKlrvkelssaqAKAEEEATRFKKQADEAKVRLqETEKQTTETVVQKLETQRlqsTREA 2623
Cdd:NF041483 651 AEGEnvavRLRS-EAAAEAERLK----------SEAQESADRVRAEAAAAAERV-GTEAAEALAAAQEEAARR---RREA 715
|
890 900 910
....*....|....*....|....*....|....*....
gi 1655220506 2624 DD-LKKAIAELEKEREKLKRDAQE-LQNKSKETASAQQE 2660
Cdd:NF041483 716 EEtLGSARAEADQERERAREQSEElLASARKRVEEAQAE 754
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
331-434 |
1.22e-17 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 81.63 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 331 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 410
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1655220506 411 VDV--AHPDEKSIITYVSSLYDVMPR 434
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
331-430 |
1.98e-17 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 80.78 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 331 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 410
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1655220506 411 VDVA--HPDEKSIITYVSSLYD 430
Cdd:cd21261 83 MMVMgrKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
331-429 |
4.48e-17 |
|
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: 80.13 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 331 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 410
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1655220506 411 -VDVAHPDEKSIITYVSSLY 429
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
333-431 |
1.04e-16 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 78.77 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 333 KLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPEDVD 412
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMA 87
|
90 100
....*....|....*....|
gi 1655220506 413 VAH-PDEKSIITYVSSLYDV 431
Cdd:cd21250 88 SAEePDKLSMVMYLSKFYEL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2200-2809 |
1.11e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.19 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2200 VERLKQKAAEANKLKDK--AEKELEKQVILA--------KEAAQKSTAAEQKAQDVLSKNKEDLLSQ-EKLRDEFENAKK 2268
Cdd:TIGR02168 202 LKSLERQAEKAERYKELkaELRELELALLVLrleelreeLEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2269 LAQAAETAkekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAakraaaeaaalKQKQEADAEMA 2348
Cdd:TIGR02168 282 EIEELQKE----------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-----------SKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2349 KHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSkvkmqmdELLKLKVRIE 2428
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-------RLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2429 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2508
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2509 AEELQKQKNQAQEKAKKLLEDKQEIQQRLD------KETQGFQKSLEA---------------ERKRQLEISAEAEKLKL 2567
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAalggrlqavvvenlnAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2568 RVKELSSAQAKAEEEATRFKKQADEAKVRLQeTEKQTTETVVQKLETQRLQSTREADDL--------------------- 2626
Cdd:TIGR02168 574 TFLPLDSIKGTEIQGNDREILKNIEGFLGVA-KDLVKFDPKLRKALSYLLGGVLVVDDLdnalelakklrpgyrivtldg 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2627 -----------------------KKAIAELEKEREKLKRDAQELQNKSKEtASAQQEQMEQQKAMLQQTFLTEKELLLKR 2683
Cdd:TIGR02168 653 dlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2684 ERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2763
Cdd:TIGR02168 732 RKDLARLEAEVEQ-LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2764 LLADENKKLREKLESLEVTSKQAASKTKEIEV--QTDKVPEEQLVSMT 2809
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDleEQIEELSEDIESLA 858
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1875-2760 |
1.22e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.20 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1875 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLL----DNELQRLKNEVNAAEKQRRQLEDELAKVR 1950
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1951 SEMDallQMKIQAEKVSQSNTEKsKQLLETEALKMKQLAEEaarlrsvaEEAKKQRQLAEDEAarQRAEAEKILKEKLAA 2030
Cdd:TIGR02169 251 EELE---KLTEEISELEKRLEEI-EQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2031 INEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVS------ELDRQKNIVEE 2104
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrdELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2105 TLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQkskakaeeeaeklkklaaeeeRKRREAEEKVKKIAA 2184
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE---------------------EEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2185 AEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEkQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQeklrdefe 2264
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGT-------- 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2265 nakkLAQaaetakekaekeaaLLRQKAEEAEKLKKAA----------EDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEA 2334
Cdd:TIGR02169 527 ----VAQ--------------LGSVGERYATAIEVAAgnrlnnvvveDDAVAKEAIELLKRRKAGRATFLPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2335 AALKQKQEADAEMA----KHKKEAEQALKQksqVEKELGLVklqlDETDKQKALMD---------EELQRVKAQVNDAVK 2401
Cdd:TIGR02169 589 DLSILSEDGVIGFAvdlvEFDPKYEPAFKY---VFGDTLVV----EDIEAARRLMGkyrmvtlegELFEKSGAMTGGSRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2402 QKAQVENELSkvkmQMDELLKLKVRIEEenlrlMQKNKDNtqklLAEEAEKMKSLAEEA-ARLSVEAEETARQRKTAEAE 2480
Cdd:TIGR02169 662 PRGGILFSRS----EPAELQRLRERLEG-----LKRELSS----LQSELRRIENRLDELsQELSDASRKIGEIEKEIEQL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2481 LAEQRALAEKM--LKEKMQAIQEA-TKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD----KETQGFQKSLEAERK 2553
Cdd:TIGR02169 729 EQEEEKLKERLeeLEEDLSSLEQEiENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVS 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2554 RQLEISAEAEKlklRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRlqstrEADDLKKAIAEL 2633
Cdd:TIGR02169 809 RIEARLREIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAALRDL 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2634 EKEREKLKRDAQELQNKSKETASAQQEQMEQ--QKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDE 2711
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQieKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2712 QQRQQKLMD---------EEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLE 2760
Cdd:TIGR02169 961 QRVEEEIRAlepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2432-2797 |
2.54e-16 |
|
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: 86.72 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2432 LRLMQKNKDNTQKLLAEEAEKMkslaeEAARLSVEAEETARQ----RKTAEAELAEQRALaekmlkEKMQAIQeatklkA 2507
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKM-----EQERLRQEKEEKAREverrRKLEEAEKARQAEM------DRQAAIY------A 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2508 EAEELqkqknqAQEKAKKLLEDKQEIQQRldketqgfqkslEAERKRQLEISAEAEklklRVKELSSAQAKAEEEATRFK 2587
Cdd:pfam17380 338 EQERM------AMERERELERIRQEERKR------------ELERIRQEEIAMEIS----RMRELERLQMERQQKNERVR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2588 KQADEA-KVRLQETEKQtTETVVQKLETQRLQSTREaDDLKKAIAELEKEREK-LKRDAQELQNKSKETASAQQEQMEQQ 2665
Cdd:pfam17380 396 QELEAArKVKILEEERQ-RKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERK 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2666 KAMLQQtfltEKElllKRERDVEDEKKKlqKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQ-AIMDEavKKQKEAEAEm 2744
Cdd:pfam17380 474 RKKLEL----EKE---KRDRKRAEEQRR--KILEKELEERKQAMIEEERKRKLLEKEMEERQkAIYEE--ERRREAEEE- 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2745 KNKQKEMEalEKKRLEQEKLLADENkklREKLESLEVTS------KQAASKTKEIEVQT 2797
Cdd:pfam17380 542 RRKQQEME--ERRRIQEQMRKATEE---RSRLEAMERERemmrqiVESEKARAEYEATT 595
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2355-2772 |
2.83e-16 |
|
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: 86.70 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2355 EQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDEL---LKLKVRIEEEN 2431
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVvteFEATTCSLEEL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2432 LRLMQKNKDNTQkllaeeaEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRalaeKMLKEKMQAIQEATKLKAEAEE 2511
Cdd:pfam05483 365 LRTEQQRLEKNE-------DQLKIITMELQKKSSELEEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2512 LQKQKN------QAQEKAKKLLEDKQEI----QQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSA------ 2575
Cdd:pfam05483 434 LKGKEQelifllQAREKEIHDLEIQLTAiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtl 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2576 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEK-----EREKLKRDAQ----- 2645
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEnarsiEYEVLKKEKQmkile 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2646 --------ELQNKSKETASAQQEQME-QQKAMLQQTFLTEKELLL-KRERDVEDEKKKLQKHLEdevNKAKALKDEQQRQ 2715
Cdd:pfam05483 594 nkcnnlkkQIENKNKNIEELHQENKAlKKKGSAENKQLNAYEIKVnKLELELASAKQKFEEIID---NYQKEIEDKKISE 670
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2716 QKLMdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEAL-EKKRLEQEKLLADENKKL 2772
Cdd:pfam05483 671 EKLL-EEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALmEKHKHQYDKIIEERDSEL 727
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1414-1956 |
3.23e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1414 LREARLRQEKIEAApVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqilayRALQDPIASPLKK 1493
Cdd:PRK03918 216 LPELREELEKLEKE-VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI------EELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1494 PKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmAEIQAQLETQKQLAEGHAKS 1573
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-KELEKRLEELEERHELYEEA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1574 VAKAElEAQELKLKMKEDASQR-QGLAVDAEKQKQNIQLE---LTQLKNLSEQEIRSKNQQLEEAQVSRRKLeeeihlir 1649
Cdd:PRK03918 368 KAKKE-ELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEiskITARIGELKKEIKELKKAIEELKKAKGKC-------- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1650 iqlqTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEetqkKKNAEDELKRKSE--AEKEAARQKQKALD 1727
Cdd:PRK03918 439 ----PVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE----LRELEKVLKKESEliKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1728 ELQKHkmQAEEAERRLKQAEEEKVRQIKVVEEVaqktaatqlqamsfsektTKLEESLKKEQGTVLQLQEEAEKLRKQEE 1807
Cdd:PRK03918 511 KLKKY--NLEELEKKAEEYEKLKEKLIKLKGEI------------------KSLKKELEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1808 EankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEK-- 1885
Cdd:PRK03918 571 E----LAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEElr 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1886 ------QRTFAEQ----IAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDeLAKVRSEMDA 1955
Cdd:PRK03918 647 keleelEKKYSEEeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
.
gi 1655220506 1956 L 1956
Cdd:PRK03918 726 L 726
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
203-312 |
3.61e-16 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 76.99 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 203 KKTFTKWVNKHL-MKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlpREKGRMRFHKLQNVQIALDFLK 281
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFLNACK 70
|
90 100 110
....*....|....*....|....*....|...
gi 1655220506 282 HRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 312
Cdd:cd00014 71 KLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1922-2774 |
5.97e-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: 85.89 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1922 DNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkiqaekvsqsNTEKSKQLLETEALKMKQLAEEAARLRSVaEE 2001
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERL-------------RREREKAERYQALLKEKREYEGYELLKEK-EA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2002 AKKQRQLAEDEAARQRAEAEKIlKEKLAAINEatrlktEAEVALKAKEAENERLKRQAEDE--AYQRKLledqaaqhkHD 2079
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKL-TEEISELEK------RLEEIEQLLEELNKKIKDLGEEEqlRVKEKI---------GE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2080 IQEKITQLQSSsVSELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAE 2159
Cdd:TIGR02169 299 LEAEIASLERS-IAEKERELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2160 KLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA-NKLKDKAEKELEKQVILaKEAAQKSTAA 2238
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnAAIAGIEAKINELEEEK-EDKALEIKKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2239 EQKaqdvLSKNKEDLlsqEKLRDEFENAKKLAQAAETAKEKaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAE-- 2316
Cdd:TIGR02169 454 EWK----LEQLAADL---SKYEQELYDLKEEYDRVEKELSK-------LQRELAEAEAQARASEERVRGGRAVEEVLKas 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2317 ---------RLRKEAEAEAAKRAAAEAAALKQKQEADAEMAkhkKEAEQALKQ-KSQVEKELGLVKLQLDETDKQKALMD 2386
Cdd:TIGR02169 520 iqgvhgtvaQLGSVGERYATAIEVAAGNRLNNVVVEDDAVA---KEAIELLKRrKAGRATFLPLNKMRDERRDLSILSED 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2387 E------ELQRVKAQVNDAVKQKAQ---VENELSKVKMQMDEL-------------------------LKLKVRIEEENL 2432
Cdd:TIGR02169 597 GvigfavDLVEFDPKYEPAFKYVFGdtlVVEDIEAARRLMGKYrmvtlegelfeksgamtggsraprgGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2433 RLMQKNKDNTQKLLA---EEAEKMKSLAEEA-ARLSVEAEETARQRKTAEAELAEQRALAEKM--LKEKMQAIQEA-TKL 2505
Cdd:TIGR02169 677 QRLRERLEGLKRELSslqSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEEKLKERLeeLEEDLSSLEQEiENV 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2506 KAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD----KETQGFQKSLEAERKRQLEISAEAEKlklRVKELSSAQAKAEE 2581
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQ---KLNRLTLEKEYLEK 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2582 EATRFKKQADEAKVRLQETEKQTTETVVQKLETQrlqstREADDLKKAIAELEKEREKLKRDAQELQNKSKEtasaQQEQ 2661
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-----EELEELEAALRDLESRLGDLKKERDELEAQLRE----LERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2662 MEQQKAMLQQTFLTEKELLLKRErDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKL--MDEEKKKLQAIMDEAVKKQKE 2739
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELqrVEEEIRALEPVNMLAIQEYEE 983
|
890 900 910
....*....|....*....|....*....|....*
gi 1655220506 2740 AEAEMKNKQKEMEALEKKRLEQEKLLADENKKLRE 2774
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
199-310 |
6.17e-16 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 76.42 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 199 DRVQKKTFTKWVNKHLMKAQ-RHITDLYEDLRDGHNLISLLEVLSGETLPRERDLvrnvrlpreKGRMRFHKLQNVQIAL 277
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDL---------EPKNRIQMIQNLHLAM 72
|
90 100 110
....*....|....*....|....*....|....
gi 1655220506 278 DFL-KHRQVKLVNIRNDDIADGNPKLTLGLIWTI 310
Cdd:cd21225 73 LFIeEDLKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
334-429 |
6.67e-16 |
|
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: 76.63 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 334 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDPED-VD 412
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1655220506 413 VAHPDEKSIITYVSSLY 429
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2342-2712 |
7.01e-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: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2342 EADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLD--ETDKQKALMDEELQRVK---------AQVNDAVKQKAQVENEL 2410
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKreyegyellKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2411 SKVKmqmDELLKLKVRIEEENLRLMQKNKDntqkllaeeaekmksLAEEAARLSVEAEETARQRKTAEAELAEQRALAEK 2490
Cdd:TIGR02169 247 ASLE---EELEKLTEEISELEKRLEEIEQL---------------LEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2491 MLKEKMQaiqeatklkaEAEELQKQKNQAQEKAKKLLEDKQEiqqrldketqgFQKSLEAERKRQLEISAEAEKLKlrvK 2570
Cdd:TIGR02169 309 SIAEKER----------ELEDAEERLAKLEAEIDKLLAEIEE-----------LEREIEEERKRRDKLTEEYAELK---E 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2571 ELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTR-----EADDLKKAIAELEKEREKLKRDAQ 2645
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELqrlseELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2646 ELQNKSKEtasaQQEQMEQQKAMLQQtflTEKELLLKRE--RDVEDEKKKLQKHLEDEVNKAKALKDEQ 2712
Cdd:TIGR02169 445 DKALEIKK----QEWKLEQLAADLSK---YEQELYDLKEeyDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1614-2146 |
8.14e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.09 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1614 TQLKNLSEqEIRSKNQQLEEAQVSRRKLEE--EIHLIRIQLQTTIKQkstaddELQKLRDQAAEAEKVRKAAQEEAERLR 1691
Cdd:PRK02224 213 SELAELDE-EIERYEEQREQARETRDEADEvlEEHEERREELETLEA------EIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1692 KQVNEETQKKKNAEDELKRkSEAEKEAARQKQKALDElqkhkmQAEEAERRLkqaeeekvrqikvvEEVAQKTAATQLQA 1771
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGL-DDADAEAVEARREELED------RDEELRDRL--------------EECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1772 MSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEaqRKSLAQEEA 1851
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF--LEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1852 EKQKTEAERDAKKkakaeeaalkqkENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNE 1931
Cdd:PRK02224 423 ELREREAELEATL------------RTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1932 VNAAEKQRRQLEDeLAKVRSEMDALLQmkiQAEKVSQSNTEKsKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED 2011
Cdd:PRK02224 491 VEEVEERLERAED-LVEAEDRIERLEE---RREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2012 EAARQRAEAeKILKEKLAAINEA-TRLKTEAEVALKAKEAE------NERLKRQAEdeayqrklLEDQAAQHKHDIQEKI 2084
Cdd:PRK02224 566 EAEEAREEV-AELNSKLAELKERiESLERIRTLLAAIADAEdeierlREKREALAE--------LNDERRERLAEKRERK 636
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2085 TQLQS----SSVSELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 2146
Cdd:PRK02224 637 RELEAefdeARIEEAREDKERAEEYLEQ---VEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2351-2793 |
9.64e-16 |
|
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: 84.69 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2351 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKV----R 2426
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2427 IEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLK 2506
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2507 AEAEELQKQknqaqekakklLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELssaqakaEEEATRF 2586
Cdd:TIGR04523 391 SQINDLESK-----------IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL-------TNQDSVK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2587 KKQADEAKVRLQETEKQTTETvvqKLETQRLQSTREadDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQK 2666
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVL---SRSINKIKQNLE--QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2667 AMlqQTFLTEKELLLKrerDVEDEKKKLqkhleDEVNKAKALKDEQQRQQKLMDE---EKKKLQAIMDEAVKKQKEAEAE 2743
Cdd:TIGR04523 528 KL--ESEKKEKESKIS---DLEDELNKD-----DFELKKENLEKEIDEKNKEIEElkqTQKSLKKKQEEKQELIDQKEKE 597
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2744 MKNKQKEMEALEKKRLEQEKLLADENKKlREKLESLEVTSKQAASKTKEI 2793
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQE 646
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1314-2149 |
9.83e-16 |
|
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: 85.02 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1314 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEhyrqlagSLLERWQAVFAQIDLRQREL 1393
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK-------LQEEELKLLAKEEEELKSEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1394 SLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQiencqkdakayidslkdy 1473
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------------ 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1474 efQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRyselstlTSQYIKFILETQRRLEDDEKaseklkeDEKKRM 1553
Cdd:pfam02463 365 --QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-------EEKEAQLLLELARQLEDLLK-------EEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1554 AEIQAQLETQKQLAEGHAKSVaKAELEAQELKLKMKEdasqrqglavDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEE 1633
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEE-KEELEKQELKLLKDE----------LELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1634 AQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE 1713
Cdd:pfam02463 498 RSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGA 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1714 AEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGtvl 1793
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL--- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1794 qLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAAL 1873
Cdd:pfam02463 655 -EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1874 KQKENAEKELEKQRTFAEQ--IAQQKLSAEQEYIRLKADFEHAEQQRglldNELQRLKNEVNAAEKQRRQLEDELAKVRS 1951
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEekSRLKKEEKEEEKSELSLKEKELAEER----EKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1952 EMDALLQMKIQAEKVSQSN---TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKL 2028
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEkikEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2029 AAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSsvseldrQKNIVEETLRQ 2108
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE-------ENNKEEEEERN 962
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1655220506 2109 KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQK 2149
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1517-2417 |
1.31e-15 |
|
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: 84.84 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1517 LSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKK----------RMAEIQAQLETQK-QLA---------------EGH 1570
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAELRaQLAkkeeelqaalarleeETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1571 AKSVA-KAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSE---------QEIRSKNQQleEAQVSRRK 1640
Cdd:pfam01576 258 QKNNAlKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttaaqQELRSKREQ--EVTELKKA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1641 LEEEIHLIRIQLQTTIKQKSTADDELQKLRDQA----AEAEKVRKAAQEEAERLRKQVN-------EETQKKKNAEDELK 1709
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAkrnkANLEKAKQALESENAELQAELRtlqqakqDSEHKRKKLEGQLQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1710 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsEKTTKLEESLKkeq 1789
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKLNLSTR--- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1790 gtVLQLQEEAEKLRKQEEEANKAREQAEKELETWR----------------LKANEALRLRLRAEEEAQRKSLAQEEAEK 1853
Cdd:pfam01576 491 --LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaqlsdmkkkleedagtLEALEEGKKRLQRELEALTQQLEEKAAAY 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1854 QKTEA--ERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQ---EYIRLKADFEHAEQQRGLLDNELQRL 1928
Cdd:pfam01576 569 DKLEKtkNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARyaeERDRAEAEAREKETRALSLARALEEA 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1929 KNEVNAAEKQRRQLedelakvRSEMDALLQMKIQAEKvSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKkqrql 2008
Cdd:pfam01576 649 LEAKEELERTNKQL-------RAEMEDLVSSKDDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK----- 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2009 aedeaarqraeaekilkeklaaineaTRLkteaEVALKAKEAENERlKRQAEDEayqrklledQAAQHKHDIQEKITQLQ 2088
Cdd:pfam01576 716 --------------------------LRL----EVNMQALKAQFER-DLQARDE---------QGEEKRRQLVKQVRELE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2089 SssvsELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEE 2168
Cdd:pfam01576 756 A----ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2169 ERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKlkDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSK 2248
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGAS--GKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2249 NKEDLLSQ--EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE--AAKQAKAQKDAERLRKEAEA 2324
Cdd:pfam01576 910 DRLRKSTLqvEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSsiAALEAKIAQLEEQLEQESRE 989
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2325 EAAKRAAAEAAALKQKqEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKA 2404
Cdd:pfam01576 990 RQAANKLVRRTEKKLK-EVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNE 1068
|
970
....*....|...
gi 1655220506 2405 QVENELSKVKMQM 2417
Cdd:pfam01576 1069 SMNREVSTLKSKL 1081
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1510-2438 |
1.62e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 84.33 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1510 LRTRYSELSTLTsQYIKfILETQRRLEDDEK-------ASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQ 1582
Cdd:TIGR00606 171 LKQKFDEIFSAT-RYIK-ALETLRQVRQTQGqkvqehqMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1583 ELKLKMKEDASQRQGLavdaekqkQNIQLELTQLKNlSEQEIRSKNQQLEEAQVS-RRKLEEEIHLIRIQLQTTIKQKSt 1661
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKI--------MKLDNEIKALKS-RKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKE- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1662 addelQKLRDQAAEAEKVRKAA----QEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1737
Cdd:TIGR00606 319 -----RELVDCQRELEKLNKERrllnQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1738 EAERRLKQAEEEKVRQI-KVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1816
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1817 EKELETWRlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAeeaalkqKENAEKELEKQ-RTFAEQIAQ 1895
Cdd:TIGR00606 474 LELDQELR----KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD-------QEMEQLNHHTTtRTQMEMLTK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1896 QKLSAEQEYIRLKAdfEHAEQQRGLLDN--ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEK 1973
Cdd:TIGR00606 543 DKMDKDEQIRKIKS--RHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1974 SKQLLET--EALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATR-LKTEAEVALKAKEA 2050
Cdd:TIGR00606 621 LSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2051 ENERL----KRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSEL-DRQKNIVEETLRQKKVVEE-EIHIIRINFE 2124
Cdd:TIGR00606 701 QSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELrNKLQKVNRDIQRLKNDIEEqETLLGTIMPE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2125 RASKEksDLEVELKKLKGIADETQKSKAKAEEEAEKL-----KKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDE 2199
Cdd:TIGR00606 781 EESAK--VCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2200 VERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEK 2279
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2280 AEKEAALLRQKAEEAEKLKKAAEDeaakqaKAQKDAERlrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALK 2359
Cdd:TIGR00606 939 AQDKVNDIKEKVKNIHGYMKDIEN------KIQDGKDD---------------------YLKQKETELNTVNAQLEECEK 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2360 QKSQVEKELGLVKLQLDETDKQKALMDEELQRVKaqVNDAVKqkaQVENELSKVKMQMDELLKLKVRIE----EENLRLM 2435
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK--RENELK---EVEEELKQHLKEMGQMQVLQMKQEhqklEENIDLI 1066
|
...
gi 1655220506 2436 QKN 2438
Cdd:TIGR00606 1067 KRN 1069
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1812-2613 |
2.16e-15 |
|
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: 84.01 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1812 AREQAEKELETWRLKANEaLRLRLRAEEEAQ-------RKSLAQEEAEKQKTEAERDA-----KKKAKAEEAALKQKENA 1879
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKD-LQRRLNESNELHekqkfylRQSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1880 EKELEKQRTFAE-----------QIAQQKLSAE---QEYIRLKADFEHAEQQRGLLDNELQRL--KNEVNAAEKQRRQLE 1943
Cdd:pfam15921 151 VHELEAAKCLKEdmledsntqieQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1944 DELAKVRSEM----DALLQMKIQA----EKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAAR 2015
Cdd:pfam15921 231 TEISYLKGRIfpveDQLEALKSESqnkiELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2016 QRAEAEKILKEKLAAINEatrLKTEAEVALKAKEAENERLKRQ---AEDEAYQRKLLEDQAAQHKHDIQEkitQLQSSSV 2092
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDD---QLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2093 SELDRQKNIVEETLRQKKVVEEEIHiIRINFERASKEKSDLEVELKKLKGIAdETQKSkakaeeeaeklkklaaeeerkr 2172
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRLWDRDTG-NSITIDHLRRELDDRNMEVQRLEALL-KAMKS---------------------- 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2173 reaeekvkkiaAAEEEAARQRKAAQDEVERLKQKAAEANKLkdKAEKELEKQVIlAKEAAQKST--AAEQKAQDVLSKNK 2250
Cdd:pfam15921 441 -----------ECQGQMERQMAAIQGKNESLEKVSSLTAQL--ESTKEMLRKVV-EELTAKKMTleSSERTVSDLTASLQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2251 EDLLSQEKLRDEFENAKKLAQAaetakekaekeaallrqKAEEAEKLKKaaEDEAAKQAKAQKDAERLrkeaeaeAAKRA 2330
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDL-----------------KLQELQHLKN--EGDHLRNVQTECEALKL-------QMAEK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2331 AAEAAALKQKQEADAEM-AKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAvkqkaqvenE 2409
Cdd:pfam15921 561 DKVIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL---------E 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2410 LSKVKM--QMDELLKLKVRIEEENLRLMQKNKDNTQKL--LAEEAEKMK-SLAEEAARLSVEAEETARQRKTAEAELAEQ 2484
Cdd:pfam15921 632 LEKVKLvnAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2485 RALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLledkQEIQQRLDKETQgFQKSLEAERKRQLE-ISAEAE 2563
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL----EEAMTNANKEKH-FLKEEKNKLSQELStVATEKN 786
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2564 KLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQE----TEKQTTETVVQKLE 2613
Cdd:pfam15921 787 KMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEcqdiIQRQEQESVRLKLQ 840
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1962-2698 |
2.77e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 83.48 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1962 QAEKVSQSNTEKSKQLLEtEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEA 2041
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLM-NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2042 EVALKAKEAENERLKRQAEdEAYQRKLLEDQAAQHKHDIQEKITQLQ--SSSVSELDRQKNIVEETLRQKKVVEEEIHII 2119
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKRE-AQEEQLKKQQLLKQLRARIEELRAQEAvlEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2120 RINFERASKEKSdLEVELKKLKGIAdeTQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDE 2199
Cdd:TIGR00618 311 RIHTELQSKMRS-RAKLLMKRAAHV--KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2200 VERLKQKAAEANKLKDKAEKELEKQvilakEAAQKSTAAEQkaQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEK 2279
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATI-----DTRTSAFRDLQ--GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2280 AEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAaeaaaLKQKQEADAEMAKHKKEAEQALK 2359
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-----PNPARQDIDNPGPLTRRMQRGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2360 QKSQVEKELGLVKLQLDETDKQKALMDEELQRVK------AQVNDAVKQKAQ-VENELSKVKMQMDELLKLKVRIEEENL 2432
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQqsfsilTQCDNRSKEDIPnLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2433 RLMQK--NKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQR--------KTAEAELAEQRALAEKMLKEKMQAI--- 2499
Cdd:TIGR00618 616 ALLRKlqPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehalsiRVLPKELLASRQLALQKMQSEKEQLtyw 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2500 -----QEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQgFQKSLEAERKRQLEISAEAEK---LKLRVKE 2571
Cdd:TIGR00618 696 kemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFnnnEEVTAAL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2572 LSSAQ-AKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnK 2650
Cdd:TIGR00618 775 QTGAElSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL-K 853
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2651 SKETASAQQEQMEQQKAMLQQtfltEKELLLKRERDVEDEKKKLQKHL 2698
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQL----SDKLNGINQIKIQFDGDALIKFL 897
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2339-2794 |
3.21e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.17 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2339 QKQEADAEMAKHkkeaEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQV-------NDAVKQKAQVENELS 2411
Cdd:PRK02224 235 TRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeeleeerDDLLAEAGLDDADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2412 KVKMQMDELLKLKVRIEE--ENLRLMQKNKDNTQKLLAEEAEKMKSLA----EEAARLSVEAEETARQRKTAEAELAEQR 2485
Cdd:PRK02224 311 AVEARREELEDRDEELRDrlEECRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESELEEAREAVEDRREEIEELE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2486 ALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2565
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETI 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2566 ---KLRVKELSSAQAKAEEEATRFKKQADEAKvRLQETEKQttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKR 2642
Cdd:PRK02224 471 eedRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDR-----IERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2643 DAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELL-LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDE 2721
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAeLKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2722 EKKKLQAimdeavKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2794
Cdd:PRK02224 625 RRERLAE------KRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4227-4265 |
3.65e-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: 3.65e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 4227 LLEAQIATGGIIDPQESHRLPVETAYERGLFDEEMNQIL 4265
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1994-2780 |
3.76e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.19 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1994 RLRSVAE-EAKKQRQLAEDEAARQR-AEAEKILKEKlaaINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLED 2071
Cdd:TIGR02169 161 EIAGVAEfDRKKEKALEELEEVEENiERLDLIIDEK---RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2072 QAAQHKHDIQEKITQLQSSSVSELDRQKNIV-------EETLRQKKVVEEEIHIIRinferasKEKSDLEVELKKLKGIA 2144
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEeieqlleELNKKIKDLGEEEQLRVK-------EKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2145 DETQkskakaeeeaeklkklaaeeerkrreaeEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELekq 2224
Cdd:TIGR02169 311 AEKE----------------------------RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY--- 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2225 vilaKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE 2304
Cdd:TIGR02169 360 ----AELKEELEDLRAELEEVDKEFAE---TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2305 AAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQE---ADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQ 2381
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2382 KALMDEELQRVKAQVNDAVKQKAQ-----------------VENELskVKMQMDELLKL------------KVRIEEENL 2432
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGSVGERyataievaagnrlnnvvVEDDA--VAKEAIELLKRrkagratflplnKMRDERRDL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2433 RLMQKNK---------DNTQK------------LLAEEAEKMKSLAEEAARLSVEAE------------ETARQR----K 2475
Cdd:TIGR02169 591 SILSEDGvigfavdlvEFDPKyepafkyvfgdtLVVEDIEAARRLMGKYRMVTLEGElfeksgamtggsRAPRGGilfsR 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2476 TAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQkqknQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQ 2555
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS----QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2556 LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEK 2635
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2636 EREKLKRDAQELQNKSKETASaqQEQMEQQKAMLQQTFLTEKELLLKR----ERDVEDEKKKLQKHLEDEVNKAKALKDE 2711
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKE--QIKSIEKEIENLNGKKEELEEELEEleaaLRDLESRLGDLKKERDELEAQLRELERK 904
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2712 QQrQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAdENKKLREKLESLE 2780
Cdd:TIGR02169 905 IE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIRALE 971
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1601-2012 |
4.28e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.51 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1601 DAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIR--IQLQTTIKQKSTADDELQKLRDQAAEAEK 1678
Cdd:COG4717 75 ELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1679 VRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ------AEEEKVR 1752
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEeleeleEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1753 QIKVVEEVAQKTAATQLQAMSFS---------------------------EKTTKLEESLKKEQGTVLQLQEEAEKLRKQ 1805
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlflvlGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1806 EEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEK 1885
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1886 QRTFAEqiAQQKLSAEQEYIRLKADFEHAEQQRGLLDN---ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLqmkiq 1962
Cdd:COG4717 394 AEEYQE--LKEELEELEEQLEELLGELEELLEALDEEEleeELEELEEELEELEEELEELREELAELEAELEQLE----- 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1963 aekvSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDE 2012
Cdd:COG4717 467 ----EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
329-429 |
5.36e-15 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 74.34 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 408
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1655220506 409 ED-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1602-1932 |
7.17e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 81.71 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1602 AEKQKQNiqleltQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliriqlqttikQKSTADDELQKLRDQAAEAEKVRK 1681
Cdd:pfam17380 285 SERQQQE------KFEKMEQERLRQEKEEKAREVERRRKLEE--------------AEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1682 AAQEEAERLRkqvneetQKKKNAEDELKRKSEAEKEAARQKQkaLDELQKHKMQAE-------EAERRLKQAEEEKVRQI 1754
Cdd:pfam17380 345 ERERELERIR-------QEERKRELERIRQEEIAMEISRMRE--LERLQMERQQKNervrqelEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1755 KVVEEVAQKTAATQLQAMsfSEKTTKLEESLKKEQGTV----LQLQEEAEKLRKQEEEANKAREQAEKELETwRLKANEA 1830
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEAR--QREVRRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1831 LRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkKAKAEEAALKQKENAEKELEKQRTFAE--QIAQQKLSAEQEYIRLK 1908
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEERKRKLLEKEME---ERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRLE 569
|
330 340
....*....|....*....|....
gi 1655220506 1909 ADFEHAEQQRGLLDNELQRLKNEV 1932
Cdd:pfam17380 570 AMEREREMMRQIVESEKARAEYEA 593
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2180-2787 |
1.21e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.26 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2180 KKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKL 2259
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2260 RDEFENAKKLAQAAETAKEKAEKEAALlRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEaeaeaakraaaeaaaLKQ 2339
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE---------------ING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2340 KQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDE-----------ELQRVKAQVNDAVKQKAQVEN 2408
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkrltglTPEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2409 ELSKVKmqmDELLKLKVRIEEENLRLMQKNK--------------DNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQR 2474
Cdd:PRK03918 406 EISKIT---ARIGELKKEIKELKKAIEELKKakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2475 KTAEAELAEQRAL-AEKMLKEKMQAIQEATKlKAEAEELQKQKNQAQEKAKKLLEDKQEIqqrldketqgfqKSLEAERK 2553
Cdd:PRK03918 483 RELEKVLKKESELiKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEI------------KSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2554 RQLEISAEAEKLKLRVKELSSAQAKAEEEATRFK-KQADEAKVRLQETEKqttetvvqkletqrlqSTREADDLKKAIAE 2632
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEP----------------FYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2633 LEKEREKLKRDAQELQNKSKETASAQQEqMEQQKAMLQQtfltekellLKRERDVEDEKKKLQKHLEDEvNKAKALKDEQ 2712
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKR-LEELRKELEE---------LEKKYSEEEYEELREEYLELS-RELAGLRAEL 682
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2713 QRQQKLMDEEKKKLqaimdeavKKQKEAEAEMKNKQKEMEALEKKRleqekllaDENKKLREKLESLEVTSKQAA 2787
Cdd:PRK03918 683 EELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKAL--------ERVEELREKVKKYKALLKERA 741
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
204-317 |
1.35e-14 |
|
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: 73.04 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 204 KTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSgetlPRERDLVRNVRLPREKGRMrFHKLQNVQIALDFLKHR 283
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIK----PGVVDWSRVNKPFKKLGAN-MKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 1655220506 284 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 317
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1529-1809 |
1.36e-14 |
|
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: 80.94 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1529 LETQR-RLEDDEKASE-----KLKEDEKKRmaeiQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQR---QGLA 1599
Cdd:pfam17380 296 MEQERlRQEKEEKAREverrrKLEEAEKAR----QAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERirqEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1600 VDAEKQKQ--NIQLELTQLKNLSEQEIRS-KNQQLEEAQVSRRKLEEEIHLIRIQLQttikQKSTADDELQKLRDQAA-E 1675
Cdd:pfam17380 372 MEISRMREleRLQMERQQKNERVRQELEAaRKVKILEEERQRKIQQQKVEMEQIRAE----QEEARQREVRRLEEERArE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1676 AEKVRKAAQE-----------EAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLK 1744
Cdd:pfam17380 448 MERVRLEEQErqqqverlrqqEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQK 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 1745 QAEEEKVRQIKVVEEVAQKTAA----TQLQAMSFSEKTTKLeESLKKEQGTVLQLQeEAEKLRKQEEEA 1809
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQEMEerrrIQEQMRKATEERSRL-EAMEREREMMRQIV-ESEKARAEYEAT 594
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3244-3282 |
1.86e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.86e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 3244 LLEAQAATGFVIDPVKNEKVSVDDAVKSGLVGPELHEQL 3282
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
329-429 |
2.32e-14 |
|
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: 71.98 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 408
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1655220506 409 ED-VDVAHPDEKSIITYVSSLY 429
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
202-314 |
2.38e-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: 71.95 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 202 QKKTFTKWVNKHLMK--AQRHITDLYEDLRDGHNLISLLEVLSGETLPrerDLVRNvrlPREKGRMRfhklQNVQIALDF 279
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKVLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220506 280 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 314
Cdd:cd21213 71 MASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2476-2812 |
3.57e-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: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2476 TAEAELAEQRALAE-KMLKEKMQAIQEATK-LKAEAEELQKQKNQAqEKAKKLLEDKQEIQQR-LDKETQGFQKSLEAER 2552
Cdd:TIGR02169 165 VAEFDRKKEKALEElEEVEENIERLDLIIDeKRQQLERLRREREKA-ERYQALLKEKREYEGYeLLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2553 KRQLEISAEAEKLKL----RVKELSSAQAKAEEEATRFKKQADEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKK 2628
Cdd:TIGR02169 244 RQLASLEEELEKLTEeiseLEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE-KIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2629 AIAELEKEREKLKRDAQELqnksketaSAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ------KHLEDEV 2702
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEEL--------EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2703 NKAKALKDEQQRQQKLMDEEKKKL---QAIMDEAVK----KQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKK---L 2772
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLseeLADLNAAIAgieaKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655220506 2773 REKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMTTVE 2812
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2377-2794 |
3.75e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2377 ETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvrieEENLRLMQKNKDNTQKLLAEEAEK---M 2453
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERreeL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2454 KSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQaqekakkLLEDKQEI 2533
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREE-------LEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2534 QQRLDKE---TQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQ 2610
Cdd:PRK02224 327 RDRLEECrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2611 --KLETQRLQSTREADDLKKAIAELEKEREKLK---RDAQELQNKSK--------------ETASAQQEQMEQQKAMLQQ 2671
Cdd:PRK02224 407 lgNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2672 TFLTEKELLLKRER-----DVEDEKKKLQ---KHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAE 2743
Cdd:PRK02224 487 LEEEVEEVEERLERaedlvEAEDRIERLEerrEDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2744 MKNKQKEMEALEKKRleqekllaDENKKLREKLESLEVTSKQAASKTKEIE 2794
Cdd:PRK02224 567 AEEAREEVAELNSKL--------AELKERIESLERIRTLLAAIADAEDEIE 609
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1675-2369 |
4.10e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 79.63 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1675 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEA-ARQKQKALDELQKHKMQAEEAERrlKQAEEEKVRQ 1753
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAeLLTLRSQLLTLCTPCMPDTYHER--KQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1754 IKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRL 1833
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1834 RLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENA-EKELEKQRTFAEQIAQQKlSAEQEYIRLKADFE 1912
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHiRDAHEVATSIREISCQQH-TLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1913 HAEQQRGLLDNELQRLKNEVNAAEKQ---RRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQ---LLETEALKMK 1986
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRtsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLekiHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1987 QLAEEAARLRSVAEEAKKQRQLAEDEAARQrAEAEKILKEKLAAINEA----------TRLKTEAEVALKAKEAENERLK 2056
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNPArqdidnpgplTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2057 RQAEDEAYQRKLLEDQAAQHKHDIQeKITQLQSSSVSELDRQKNIVEETLrqkKVVEEEIHIIRINFERASKEKSDLEVE 2136
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQ---DLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2137 LKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAE-EEAARQRKAAQDEVERLKQKAAEANKLKD 2215
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2216 KAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKK-------------------------LA 2270
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKarteahfnnneevtaalqtgaelshLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2271 QAAETAKEKAEKEAALLRQKaeEAEKLKKAAEDEAAKQAKAQKDAERLrkEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2350
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTL--EAEIGQEIPSDEDILNLQCETLVQEE--EQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
730
....*....|....*....
gi 1655220506 2351 KKEAEQALKQKSQVEKELG 2369
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKLN 879
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
329-426 |
5.51e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.87 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLD 407
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1655220506 408 PEDVDVAHPDEKSIITYVS 426
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1530-2087 |
5.67e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLK--EDEKKRMAEIQAQLETQKQLAEGHAksVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1607
Cdd:COG4913 239 RAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1608 NIQLELTQLKNLSEQEIRSKNQQLEEaqvsrrkLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1687
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRLEQ-------LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1688 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKM----QAEEAERRLKQA---EEEKVR------QI 1754
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEAlglDEAELPfvgeliEV 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1755 KVVEEVAQK-------TAATQL--------QAMSFSEKTT--------KLEESLKKEQGTVLQLQEEAEKLrkqEEEANK 1811
Cdd:COG4913 470 RPEEERWRGaiervlgGFALTLlvppehyaAALRWVNRLHlrgrlvyeRVRTGLPDPERPRLDPDSLAGKL---DFKPHP 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1812 AREQAEKEL--------------------------------------------ETWRL-KANEALRLRLRAEEEAQRKSL 1846
Cdd:COG4913 547 FRAWLEAELgrrfdyvcvdspeelrrhpraitragqvkgngtrhekddrrrirSRYVLgFDNRAKLAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1847 AQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaEQIAQqklsAEQEYIRLKA---DFEHAEQQrglldn 1923
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---REIAE----LEAELERLDAssdDLAALEEQ------ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1924 eLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAK 2003
Cdd:COG4913 694 -LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2004 KQRQLAEDEAARQRAEAEKILKE--------------KLAAINE-ATRLKTEAEVALKAKEAENERLKRQAEDEayQRKL 2068
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIE--FVAD 850
|
650
....*....|....*....
gi 1655220506 2069 LEDQAAQHKHDIQEKITQL 2087
Cdd:COG4913 851 LLSKLRRAIREIKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1421-2002 |
9.27e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.54 E-value: 9.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1421 QEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAkayidslkdyefqilayralqdpiasplkkpkmesas 1500
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA------------------------------------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1501 DNIIQEYvtlRTRYSELSTLTsqyikfilETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELE 1580
Cdd:PRK02224 240 DEVLEEH---EERREELETLE--------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1581 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKS 1660
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1661 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELK--RKSEAEKEAARQKQKA------------L 1726
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRtaRERVEEAEALLEAGKCpecgqpvegsphV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1727 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQE 1806
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1807 EEankareqAEKELETWRLKANEAlrlRLRAEEEAQRksLAQEEAEKQKTEAERDAKKKAKAEEAALkqkENAEKELEKQ 1886
Cdd:PRK02224 547 AE-------LEAEAEEKREAAAEA---EEEAEEAREE--VAELNSKLAELKERIESLERIRTLLAAI---ADAEDEIERL 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1887 RTFAEQIAQQKlsaEQEYIRLKADFEHAEQQRGLLDNE-LQRLKNEVNAAEKQRRQLEDELAKVRSEMDAlLQMKIQAek 1965
Cdd:PRK02224 612 REKREALAELN---DERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDD-LQAEIGA-- 685
|
570 580 590
....*....|....*....|....*....|....*..
gi 1655220506 1966 vsqsnTEKSKQLLETEALKMKQLAEEAARLRSVAEEA 2002
Cdd:PRK02224 686 -----VENELEELEELRERREALENRVEALEALYDEA 717
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1530-2039 |
9.84e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.54 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLKED----EKKRMA---EIQAQLETQKQLAEGHAKSVAKAELEAQElklkmKEDASQRQGlavDA 1602
Cdd:PRK02224 248 ERREELETLEAEIEDLRETiaetEREREElaeEVRDLRERLEELEEERDDLLAEAGLDDAD-----AEAVEARRE---EL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1603 EKQKQNIQLELTQlknlSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRiqlqttiKQKSTADDELQKLRDQAAEAEKVRKA 1682
Cdd:PRK02224 320 EDRDEELRDRLEE----CRVAAQAHNEEAESLREDADDLEERAEELR-------EEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1683 AQEEAERLRKQVNEETQKKKNAEDELKRKSEaEKEAARQKQKALD-ELQKHKMQAEEAERRLKQAE----EEKVRQIKVV 1757
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELRE-ERDELREREAELEaTLRTARERVEEAEALLEAGKcpecGQPVEGSPHV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1758 EEVAQKtaatqlqamsfSEKTTKLE---ESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR 1834
Cdd:PRK02224 468 ETIEED-----------RERVEELEaelEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1835 LRAEEEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQ-EYIR-LKADFE 1912
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAA--------------EAEEEAEEAREEVAELNSKLAELKERIESlERIRtLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1913 HAEQQRGLLDNELQRLkNEVNaaeKQRRQLEDELAKVRSEMDAllqmKIQAEKVS--QSNTEKSKQLLETEALKMKQLAE 1990
Cdd:PRK02224 603 DAEDEIERLREKREAL-AELN---DERRERLAEKRERKRELEA----EFDEARIEeaREDKERAEEYLEQVEEKLDELRE 674
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1991 EAARLRSVAEEAKkqRQLAEDEAARQRAEAEKILKEKLAAI-NEATRLKT 2039
Cdd:PRK02224 675 ERDDLQAEIGAVE--NELEELEELRERREALENRVEALEALyDEAEELES 722
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
331-429 |
2.68e-13 |
|
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: 68.92 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 331 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 410
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1655220506 411 VdVAHPDEKSIITYVSSLY 429
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3908-3946 |
2.81e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.58 E-value: 2.81e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 3908 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPELHDKL 3946
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
195-313 |
2.94e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 68.85 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 195 ADERDrvqKKTFTKWVNKHLMKAQrhITDLYEDLRDGhnlISLLEVLsgETLprERDLVRNVRLPREKGRMRFHKLQNVQ 274
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKKVENCN 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220506 275 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 313
Cdd:cd21219 69 YAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2199-2846 |
3.14e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.70 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2199 EVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDEFENAkklaqaAETAKE 2278
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQ---SQEDLRNQLQNT------VHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2279 KAEKEAALLRQKAEEAEKLKKA--AEDEAAKQAKA------QKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2350
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMmlSHEGVLQEIRSilvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2351 K------KEAEQALKQKSQVEKELGLVKLQldetDKQKALMDEElqrvKAQVNDAVKQKAQVENELSKVKMQMdELLKLK 2424
Cdd:pfam15921 237 KgrifpvEDQLEALKSESQNKIELLLQQHQ----DRIEQLISEH----EVEITGLTEKASSARSQANSIQSQL-EIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2425 VRieEENLRLMQKNKDntqklLAEEAEKMKSLAEEAARLSVEA-EETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAT 2503
Cdd:pfam15921 308 AR--NQNSMYMRQLSD-----LESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2504 KLKAEAEELQKQKNQAQEKAKKL-----------------LEDKQEIQQRLDKETQGFQKSLEAERKRQLE-ISAEAEKL 2565
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQMAaIQGKNESL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2566 KlrvkELSSAQAKAEEEATRFKKQADE---AKVRLQETEKQTTETVVQKLETQR-LQSTR-EADDLKKAIAELEKEREKL 2640
Cdd:pfam15921 461 E----KVSSLTAQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQEKERaIEATNaEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2641 KRDAQELQNKSKETASAQQEQMEQQKAM--LQQTFLTEKELLLKRERD---VEDEKKKLQKHLED---EVNKAKALKDEQ 2712
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIeiLRQQIENMTQLVGQHGRTagaMQVEKAQLEKEINDrrlELQEFKILKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2713 qrqqklmDEEKKKLQA-IMDEAVKKQKEAEAemknKQKEMEALEKKRLEQEKLLaDENKKLREKLESL----EVTSKQAA 2787
Cdd:pfam15921 617 -------DAKIRELEArVSDLELEKVKLVNA----GSERLRAVKDIKQERDQLL-NEVKTSRNELNSLsedyEVLKRNFR 684
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2788 SKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNgSVEAvkKDGASPLAFEGIRESVPAER 2846
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTLK-SMEG--SDGHAMKVAMGMQKQITAKR 740
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1818-2804 |
5.71e-13 |
|
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: 76.24 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1818 KELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK------ELEKQRTFAE 1891
Cdd:TIGR00606 158 QEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEirdqitSKEAQLESSR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1892 QIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEvnaaEKQRRQLEDELAKVRsemdallqmkiqaEKVSQSNT 1971
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR----KKQMEKDNSELELKM-------------EKVFQGTD 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1972 EKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLA-------EDEAARQRAEAEKILKEKLAAINEATRLKTEAEVA 2044
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqektelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2045 LKAKEAENERLKRQAEDEAYQRKLLEDQ-AAQHKHDIQEKITqLQSSSVSELDRQKNIVEETLRQKKVVeeeihiirinf 2123
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQEDEAKtAAQLCADLQSKER-LKQEQADEIRDEKKGLGRTIELKKEI----------- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2124 eraskeksdLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAaqdEVERL 2203
Cdd:TIGR00606 449 ---------LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA---DLDRK 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2204 KQKAAEANKLKDKAEKELEKQVILAKeaaqKSTAAEQKAQDVLSKNKEDLLSQEKlrdEFENAKKLAQAAETAKEKaeke 2283
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQMEMLTK----DKMDKDEQIRKIKSRHSDELTSLLG---YFPNKKQLEDWLHSKSKE---- 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2284 aalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAalkqkQEADAEMAKHKKEAEQALKQKSQ 2363
Cdd:TIGR00606 586 ---INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-----QDEESDLERLKEEIEKSSKQRAM 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2364 VEKELGLVKLQLDETD--------------KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLkvriee 2429
Cdd:TIGR00606 658 LAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL------ 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2430 enLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAEL-AEQRALAEKMLKEKMQAIQEATKLKAE 2508
Cdd:TIGR00606 732 --APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEeSAKVCLTDVTIMERFQMELKDVERKIA 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2509 AEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQgfqkSLEAERKRQLEISAEAEKLKLRVKELSSAqakaeeeatrfKK 2588
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS----KIELNRKLIQDQQEQIQHLKSKTNELKSE-----------KL 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2589 QADEAKVRLQETEKQTTEtvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM 2668
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVE-----LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEK 949
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2669 LQQTFLTEKELllkrERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQ----------- 2737
Cdd:TIGR00606 950 VKNIHGYMKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqdnltlrk 1025
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2738 -----KEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQ 2804
Cdd:TIGR00606 1026 renelKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFR 1097
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1446-2148 |
7.23e-13 |
|
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: 75.87 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1446 LEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPI------ASPLKKPKMESASDNIIQEYVTLRTRYSELST 1519
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKreyegyELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1520 LTSQYIKFILETQRRLEDDEKASEKLKEDE----KKRMAEIQAQLETQKqlaeghaKSVAKAELEAQELKLKMKEDASQR 1595
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvKEKIGELEAEIASLE-------RSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1596 QGLAVDAEKQKQNI---QLELTQLKNL---SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL 1669
Cdd:TIGR02169 332 DKLLAEIEELEREIeeeRKRRDKLTEEyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1670 RDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1749
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1750 kvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA---EKELETWR-- 1824
Cdd:TIGR02169 492 -------LAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvEDDAVAKEai 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1825 --LKANEALRL------RLRAEEEAQRKSLAQ-------------EEAEK------------QKTEAERDAKKKAKA--- 1868
Cdd:TIGR02169 565 elLKRRKAGRAtflplnKMRDERRDLSILSEDgvigfavdlvefdPKYEPafkyvfgdtlvvEDIEAARRLMGKYRMvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1869 --------------EEAALKQKENAEKELEKQRTFAEQIaqQKLSAEQEyiRLKADFEHAEQQRGLLDNELQRLKNEVNA 1934
Cdd:TIGR02169 645 egelfeksgamtggSRAPRGGILFSRSEPAELQRLRERL--EGLKRELS--SLQSELRRIENRLDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1935 AEKQRRQLEDELAKVRSEMDAlLQMKIQAEKVSQSNTEKSKQLLETEalkMKQLAEEAARLRsvAEEAKKQRQLAEDEAA 2014
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQEIENVKSELKELEAR---IEELEEDLHKLE--EALNDLEARLSHSRIP 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2015 RQRAEAEKIlKEKLAAINEATRlktEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSvSE 2094
Cdd:TIGR02169 795 EIQAELSKL-EEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-EE 869
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2095 LDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQ 2148
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2993-3031 |
7.24e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 7.24e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 2993 FLDVQLATGGIIDPVNSHRLPLQTAYKQGQFDPDMNKKL 3031
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
793-983 |
7.50e-13 |
|
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: 70.94 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 793 QLHTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGVQTTGDKLLRDGHPGRKTIEAF 872
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 873 TAALQTQWSWILQLCCCIETHLKENTAHFQFFSDVKEAEERIKKMQDTMKRKYTCDrsiTVTRLEDLVQDAADEREQLNE 952
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1655220506 953 IKTHLEGLKRRAKTIVQLKPRNPATPIKSKL 983
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2338-2568 |
7.70e-13 |
|
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: 73.64 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2338 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKvkmQM 2417
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE---LL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2418 DELLKLKvRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALaekmLKEKMQ 2497
Cdd:COG4942 111 RALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL----LAELEE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2498 AIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLR 2568
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1680-2089 |
7.96e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.19 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1680 RKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE--KVRQIKVV 1757
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1758 EEVAQKTAATQLQAMSFSEKTTKLEESLKkeqgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRlRLRA 1837
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLE-------ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1838 EEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIA----------------------- 1894
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1895 ---QQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAK--VRSEMDALLQMKIQAEKVSQS 1969
Cdd:COG4717 280 flvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeeLLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1970 NTEKSKQLLETE--ALKMKQLAEEAARLRSVAEEAKKQRQLAE--DEAARQRAEAEKILKEKLAAINEATRLKTEAEVAL 2045
Cdd:COG4717 360 EEELQLEELEQEiaALLAEAGVEDEEELRAALEQAEEYQELKEelEELEEQLEELLGELEELLEALDEEELEEELEELEE 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2046 KAKEAENER---LKRQAEDEAYQRKLLEDQAAQH-KHDIQEKITQLQS 2089
Cdd:COG4717 440 ELEELEEELeelREELAELEAELEQLEEDGELAElLQELEELKAELRE 487
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3320-3358 |
1.11e-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: 1.11e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 3320 LLEAQLSTGGIIDPVKSYRVPQEVACKRGYFNEEMAKTL 3358
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4497-4535 |
1.20e-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: 1.20e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 4497 LLEAQACTGGIIDPNTGEKFSVADAMNKGLVDKIMVDRI 4535
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2572-2791 |
1.56e-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: 72.87 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2572 LSSAQAKAEEEATRFKKQADEAKVRLQETEK--QTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQN 2649
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2650 KSKETAS---AQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ------KHLEDEVNKAKALKDEQQRQQKLMD 2720
Cdd:COG4942 91 EIAELRAeleAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2721 EEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD---ENKKLREKLESLEVTSKQAASKTK 2791
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2575-2794 |
1.71e-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: 72.49 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2575 AQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKEt 2654
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2655 asaQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHledevnkaKALKDEQQRQQKLMDEEKKKLQAIMDEAV 2734
Cdd:COG4942 102 ---QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2735 KKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2794
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
331-426 |
1.99e-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: 66.26 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 331 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLDPE 409
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1655220506 410 DVDVAHPDEKSIITYVS 426
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1530-2088 |
2.51e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.09 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEkaSEKLKEDEKKRMAEIQAQLETQKQ-------------LAEGHAKSV---AKAELEAQELKLKMKEDAS 1593
Cdd:NF041483 603 ERIRREAAEE--TERLRTEAAERIRTLQAQAEQEAErlrteaaadasaaRAEGENVAVrlrSEAAAEAERLKSEAQESAD 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1594 QRQGLAV-------------------DAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQT 1654
Cdd:NF041483 681 RVRAEAAaaaervgteaaealaaaqeEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVE 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1655 TIKQKST-----ADDELQKLRD-----------------QAAE--AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKR 1710
Cdd:NF041483 761 EADRRATelvsaAEQTAQQVRDsvaglqeqaeeeiaglrSAAEhaAERTRTEAQEEADRVRSDAYAERERASEDANRLRR 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1711 KSEAEKEAA-----RQKQKALDELQKHKMQAEEAERRLK--------QAEEEKVRQIKVVEEVAQK------TAATQLQA 1771
Cdd:NF041483 841 EAQEETEAAkalaeRTVSEAIAEAERLRSDASEYAQRVRteasdtlaSAEQDAARTRADAREDANRirsdaaAQADRLIG 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1772 MSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQeeeankAREQAEKELETwrlKANEALRLRlraEEEAQRKSLAQEEA 1851
Cdd:NF041483 921 EATSEAERLTAEARAEAERLRDEARAEAERVRAD------AAAQAEQLIAE---ATGEAERLR---AEAAETVGSAQQHA 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1852 EKQKTEAERDAKKKAKAEEAALKQK--------ENAEKELEKQRT-FAEQIAQQKLSAEQEYIRLKADfEHAEQQRGLLD 1922
Cdd:NF041483 989 ERIRTEAERVKAEAAAEAERLRTEAreeadrtlDEARKDANKRRSeAAEQADTLITEAAAEADQLTAK-AQEEALRTTTE 1067
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1923 NELQRlKNEVNAAEKQRRQLEDE--------LAKVRSEMDALLqmkIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAAR 1994
Cdd:NF041483 1068 AEAQA-DTMVGAARKEAERIVAEatvegnslVEKARTDADELL---VGARRDATAIRERAEELRDRITGEIEELHERARR 1143
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1995 -----LRSVAEEAKKQRQLAEDEAARQRAEAEKILKE--------KLAAINEATRLKTEAEVALKAKEAENERLKRQAED 2061
Cdd:NF041483 1144 esaeqMKSAGERCDALVKAAEEQLAEAEAKAKELVSDanseaskvRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEA 1223
|
650 660 670
....*....|....*....|....*....|...
gi 1655220506 2062 EAY------QRKLleDQAAQHKHDIQEKITQLQ 2088
Cdd:NF041483 1224 EAKrtveegKREL--DVLVRRREDINAEISRVQ 1254
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1656-2068 |
2.57e-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: 73.62 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1656 IKQKSTADDELQKLRDQAAEAEKV--RKAAQEEAERLRKQVNEETQKKkNAEDELKRKSEAEKEAARQKQKALDELQKHK 1733
Cdd:pfam17380 213 IQMSTVAPKEVQGMPHTLAPYEKMerRKESFNLAEDVTTMTPEYTVRY-NGQTMTENEFLNQLLHIVQHQKAVSERQQQE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1734 MQAEEAERRLKQAEEEKVRQIkvveevaqktaatqlqamsfsEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEAnkar 1813
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREV---------------------ERRRKLEEAEKARQA---EMDRQAAIYAEQERMA---- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1814 EQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQeeaEKQKTEAERDAKKKAKAEEAALKQKENAEKElEKQRTFAEQI 1893
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQELEAARKVKILEE-ERQRKIQQQK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1894 AQ-QKLSAEQEYIRlKADFEHAEQQRgllDNELQRLKNEVNAAEKQ---RRQLEDELAKVRSEMDALLQMKIQAEkvsqs 1969
Cdd:pfam17380 420 VEmEQIRAEQEEAR-QREVRRLEEER---AREMERVRLEEQERQQQverLRQQEEERKRKKLELEKEKRDRKRAE----- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1970 ntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLA-EDEAARQRAEAEK---ILKEKLAAINEATRLKTEAEVAL 2045
Cdd:pfam17380 491 --EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEERRRIQEQMRKATEERSRL 568
|
410 420
....*....|....*....|...
gi 1655220506 2046 KAKEAENERLKRQAEDEAYQRKL 2068
Cdd:pfam17380 569 EAMEREREMMRQIVESEKARAEY 591
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
197-308 |
2.87e-12 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 66.29 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 197 ERDRvQKKTFTKWVNKhlMKAQRHITDLYEDLRDGhnLIsLLEVLSGeTLPRERDLVRNVRLPREKGRMRFHKLQNVQIA 276
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDG--LI-LLQAYDK-VIPGSVNWKKVNKAPASAEISRFKAVENTNYA 76
|
90 100 110
....*....|....*....|....*....|..
gi 1655220506 277 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIW 308
Cdd:cd21300 77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2090-2794 |
2.88e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2090 SSVSELDRQKnivEETLRQKKVVEEEIHIIRI-------NFERASKEKSDLEvELKKLKGIADETQKSKAKAEEEAEKLK 2162
Cdd:TIGR02169 163 AGVAEFDRKK---EKALEELEEVEENIERLDLiidekrqQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2163 KLAAEEErkrreaeekVKKIAAAEEEAARQRKAAQDEVERLKQKAAEAN-KLKDKAEKE-----------------LEKQ 2224
Cdd:TIGR02169 239 KEAIERQ---------LASLEEELEKLTEEISELEKRLEEIEQLLEELNkKIKDLGEEEqlrvkekigeleaeiasLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2225 VILAKEAAQKSTAAEQKAQDVLSKNKEDLlsqEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE 2304
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEI---EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2305 aakqakaQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKAL 2384
Cdd:TIGR02169 387 -------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2385 MDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE------NLRLMQKNKDNTQKLLAE--EAEKMKSL 2456
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrggraVEEVLKASIQGVHGTVAQlgSVGERYAT 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2457 AEEAA---RLS---VEAEETA-------RQRKTAEA------ELAEQRALAEKMLKEK---------------------- 2495
Cdd:TIGR02169 540 AIEVAagnRLNnvvVEDDAVAkeaiellKRRKAGRAtflplnKMRDERRDLSILSEDGvigfavdlvefdpkyepafkyv 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2496 ------MQAIQEATKLKA-------EAEELQK--------------QKNQAQEKAKklLEDKQEIQQRLDKETQGFQKSL 2548
Cdd:TIGR02169 620 fgdtlvVEDIEAARRLMGkyrmvtlEGELFEKsgamtggsraprggILFSRSEPAE--LQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2549 EAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvQKLETQRLQStrEADDLKK 2628
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN---VKSELKELEA--RIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2629 AIAELEKEREKLKRD-AQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERdVEDEKkklqKHLEDEVNKAKA 2707
Cdd:TIGR02169 773 DLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEI----QELQEQRIDLKE 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2708 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADEN---KKLREKLESLEVTSK 2784
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLE 927
|
810
....*....|
gi 1655220506 2785 QAASKTKEIE 2794
Cdd:TIGR02169 928 ALEEELSEIE 937
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2099-2662 |
3.41e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2099 KNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKlkklaaeeerkrreaeek 2178
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS------------------ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2179 VKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEkqvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEK 2258
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-----LSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2259 LRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLK-KAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAAL 2337
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKaKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2338 KQKQEAdAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKAL---------MDEELQRVKAQVNDAVKQKAQVEN 2408
Cdd:PRK03918 409 KITARI-GELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLeeytaelkrIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2409 ------ELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKL-------------LAEEAEKMKSLAEEAARLSVEAEE 2469
Cdd:PRK03918 488 vlkkesELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLkekliklkgeiksLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2470 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATK----LKAEAEELQKQKNQaQEKAKKLLEDKQEIQQRLDKETQGFQ 2545
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNeyleLKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2546 KSLEAERKRQLEisAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvqkletqRLQSTREADD 2625
Cdd:PRK03918 647 KELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE---------REKAKKELEK 715
|
570 580 590
....*....|....*....|....*....|....*..
gi 1655220506 2626 LKKAIAELEKEREKLKRdaqeLQNKSKETASAQQEQM 2662
Cdd:PRK03918 716 LEKALERVEELREKVKK----YKALLKERALSKVGEI 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1613-2036 |
3.97e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.88 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1613 LTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRK 1692
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1693 QVN--EETQKKKNAEDELKRKSEaEKEAARQKQKALDELQKhkmQAEEAERRLKQAEEEkvrqikVVEEVAQKTAATQLQ 1770
Cdd:COG4717 124 LLQllPLYQELEALEAELAELPE-RLEELEERLEELRELEE---ELEELEAELAELQEE------LEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1771 AMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEE--EANKAREQAEKELETWRL----------------------- 1825
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARLllliaaallallglggsllslil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1826 ----------------------KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKEL 1883
Cdd:COG4717 274 tiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1884 EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQ--QRGLLDNELQRLKNEVNAAEkqrRQLEDELAKVRSEMDALLQMKI 1961
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELE---EQLEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 1962 QAEKvsqsntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATR 2036
Cdd:COG4717 431 EEEL------EELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1472-2141 |
4.04e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.83 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1472 DYEFQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKaseKLKEDEKK 1551
Cdd:pfam05483 38 DPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKEN---KLQENRKI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1552 rmaeIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQR-------QGLAVDAEK------QKQNIQLELTQLKN 1618
Cdd:pfam05483 115 ----IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnllkETCARSAEKtkkyeyEREETRQVYMDLNN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1619 LSEQEIRSKNQQLEEAQVSRR----KLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1694
Cdd:pfam05483 191 NIEKMILAFEELRVQAENARLemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1695 NEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLK-------QAEEEKVRQIkvvEEVAQKTAAT 1767
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQM---EELNKAKAAH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1768 QLQAMSFSEKTTKLEESLKKEQGTVLQ-------LQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlrAEEE 1840
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKnedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKL---LDEK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1841 AQRKSLAQE-------------EAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ--KLSAEQEYI 1905
Cdd:pfam05483 425 KQFEKIAEElkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdKLLLENKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1906 RLKAD---FEHAEQQRGLLDNELQ--RLKNEVNAAEKQRRQLEDELAKVRSEM-DALLQMKIQAEKvSQSNTEKSKQLLE 1979
Cdd:pfam05483 505 TQEASdmtLELKKHQEDIINCKKQeeRMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDK-SEENARSIEYEVL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1980 TEALKMKQLAEEAARLRSVAEEAKK--QRQLAEDEAARQRAEAE-------KILKEKLAAINEATRLKTEAEVALKAKEA 2050
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEI 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2051 ENERLKRQA-EDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKkvvEEEIHIIRINFERASKE 2129
Cdd:pfam05483 664 EDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSA 740
|
730
....*....|..
gi 1655220506 2130 KSDLEVELKKLK 2141
Cdd:pfam05483 741 KAALEIELSNIK 752
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
220-311 |
4.06e-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: 65.69 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 220 HITDLYEDLRDGHNLISLLEVLSGEtlpreRDLVRNVRLPrEKGRMRfhKLQNVQIALDFLKHRQV----KLVNIRNDDI 295
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGD-----WSLLSKLRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGITAKDI 96
|
90
....*....|....*.
gi 1655220506 296 ADGNPKLTLGLIWTII 311
Cdd:cd21223 97 VDGHREKTLALLWRII 112
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2337-2640 |
7.28e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.68 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2337 LKQKQEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLdeTDKQKALmdEELQRVKAQVNDAVK--QKAQVENELSKVk 2414
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEA---RAEAAEEEVDELKSQL--ADYQQAL--DVQQTRAIQYQQAVQalERAKQLCGLPDL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2415 mqmdELLKLKVRIEEenlrLMQKNKDNTQKLLAEE-----AEKMKSLAEEAARL------SVEAEETARQRKTAEAELAE 2483
Cdd:PRK04863 436 ----TADNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLRE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2484 QRALAEKM--LKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE 2561
Cdd:PRK04863 508 QRHLAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2562 AEKLKLRVKELSS-AQA--KAEEEATRFKKQADEAkvrlQETEKQTTETVVQKLETQRlQSTREADDLKKAIAELEKERE 2638
Cdd:PRK04863 588 LEQLQARIQRLAArAPAwlAAQDALARLREQSGEE----FEDSQDVTEYMQQLLERER-ELTVERDELAARKQALDEEIE 662
|
..
gi 1655220506 2639 KL 2640
Cdd:PRK04863 663 RL 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1178-1859 |
7.79e-12 |
|
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: 72.46 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1178 TKIKDLRLKLDGCESrtvTRLRQPVDKEPLKACAQKTAEQMKVQSEL-EGLKKDLNSITEKTEEILASPQ---QSSSAPM 1253
Cdd:pfam15921 117 TKLQEMQMERDAMAD---IRRRESQSQEDLRNQLQNTVHELEAAKCLkEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSIL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1254 LRSElDVTLKKMDHVYGLSSVYLDKLKT-IDIVIRNTkdaeDTVKSY-ESRLrdvskVPAEEkeveahrsQLKAMRAEAE 1331
Cdd:pfam15921 194 VDFE-EASGKKIYEHDSMSTMHFRSLGSaISKILREL----DTEISYlKGRI-----FPVED--------QLEALKSESQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1332 ADQATFdrLQDElkaatsvSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL----SLLGRHMNSYKQSY 1407
Cdd:pfam15921 256 NKIELL--LQQH-------QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQArnqnSMYMRQLSDLESTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1408 EWLIQWLREA-RLRQEKIEA---------APVWDSKALKEQLTQE--------KKLLEEIEKNKDQIENCQKDAKAYID- 1468
Cdd:pfam15921 327 SQLRSELREAkRMYEDKIEElekqlvlanSELTEARTERDQFSQEsgnlddqlQKLLADLHKREKELSLEKEQNKRLWDr 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1469 -------------SLKDYEFQILAYRALQDPIASPLKKpKMESASDNIIQEYVTLRtrysELSTLTSQyIKFILETQRRL 1535
Cdd:pfam15921 407 dtgnsitidhlrrELDDRNMEVQRLEALLKAMKSECQG-QMERQMAAIQGKNESLE----KVSSLTAQ-LESTKEMLRKV 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1536 EDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAK----AELEAQELK-LKMKEDASQR-----QGLAVDAEKQ 1605
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrVDLKLQELQhLKNEGDHLRNvqtecEALKLQMAEK 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1606 KQNIQLELTQLKNLSeQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQ--TTIKQKSTA----------DDELQKLRDQA 1673
Cdd:pfam15921 561 DKVIEILRQQIENMT-QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefKILKDKKDAkirelearvsDLELEKVKLVN 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1674 AEAEKVRkaAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALD-ELQKHKMQAEEAERRLKQA------ 1746
Cdd:pfam15921 640 AGSERLR--AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSAQSELEQTrntlks 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1747 -EEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1825
Cdd:pfam15921 718 mEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
730 740 750
....*....|....*....|....*....|....
gi 1655220506 1826 KANealrlrlRAEEEAQRKSLAQEEAEKQKTEAE 1859
Cdd:pfam15921 798 QER-------RLKEKVANMEVALDKASLQFAECQ 824
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2443-2764 |
8.05e-12 |
|
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: 69.95 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2443 QKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK 2522
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2523 AKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEklkLRVKELSSAQAKAEEEATRFKKQADEAKvrlqetEK 2602
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED---ERILEYLKEKAEREEEREAEREEIEEEK------ER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2603 QTTETVVQKLETQRLQSTREADDLKKAIAELE-KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQtfltekelll 2681
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQErKERQKEREEAEKKARQRQELQQAREEQIELKERRLAE---------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2682 KRERDVEDEKKKLQKHLEDEvnkaKALKDEQQRQQKLMDEEKKKLQAIMDE---AVKKQKEAEAEMKNKQKEMEALEKKR 2758
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDE----EIEQEEAEKRRMKRLEHRRELEKQIEEreeQRAAEREEELEEGERLREEEAERRER 330
|
....*.
gi 1655220506 2759 LEQEKL 2764
Cdd:pfam13868 331 IEEERQ 336
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
331-430 |
9.58e-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: 64.28 E-value: 9.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 331 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSN---QENLEQAFSVAERE-LGVTRLL 406
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
|
90 100
....*....|....*....|....
gi 1655220506 407 DPEDVdVAHPDEKSIITYVSSLYD 430
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
698-887 |
1.19e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 67.47 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 698 LRYIQDLLGWVEENQRRVDDGEWGSDLPAVESQLGSHRGLHQSVEEFRSKIERAKADESQI---SPASKAAYRDYLAKLE 774
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 775 LQYDKLLHDSKAR---LRYLVQLHTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGV 851
Cdd:cd00176 86 QRWEELRELAEERrqrLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220506 852 QTTGDKLLRDGHP-GRKTIEAFTAALQTQWSWILQLC 887
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2478-2803 |
1.34e-11 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 71.20 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2478 EAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK---AKKLLEDKQEiQQRLDKETQGFqKSLEaerkr 2554
Cdd:NF033838 103 ELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKveeAEKKAKDQKE-EDRRNYPTNTY-KTLE----- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2555 qLEIsAEAEkLKLRVKELSSAQAKAEEEATRFKKQADEAKVRlqetEKQTTETVVQKLETQRLQSTREADdlKKAIAELE 2634
Cdd:NF033838 176 -LEI-AESD-VEVKKAELELVKEEAKEPRDEEKIKQAKAKVE----SKKAEATRLEKIKTDREKAEEEAK--RRADAKLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2635 KEREKLKRDAQELQNKSKETASAQQEQM----EQQKAMLQQTFLTEKEL---LLKRERDVEDEKKKLqkhlEDEVNKAKA 2707
Cdd:NF033838 247 EAVEKNVATSEQDKPKRRAKRGVLGEPAtpdkKENDAKSSDSSVGEETLpspSLKPEKKVAEAEKKV----EEAKKKAKD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2708 LKDEQQRQQKlmDEEKKKLQAIMDEAVKKQKEAEAEM-KNKQKEMEALEKKRLEQEKLladENKKLR-EKLESLEVTSKQ 2785
Cdd:NF033838 323 QKEEDRRNYP--TNTYKTLELEIAESDVKVKEAELELvKEEAKEPRNEEKIKQAKAKV---ESKKAEaTRLEKIKTDRKK 397
|
330
....*....|....*...
gi 1655220506 2786 AASKTKEIEVQTDKVPEE 2803
Cdd:NF033838 398 AEEEAKRKAAEEDKVKEK 415
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2378-2790 |
1.40e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2378 TDKQKALMDEELQRVKAQVNDAVKQK---AQVENELSKVKMQMDELLKLKVRIEEE--NLRLMQKNKDNTQKLLAEEAEk 2452
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAE- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2453 MKSLAEEAARLSVEAE---ETARQRKTAEAELAE-QRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLE 2528
Cdd:COG4717 141 LAELPERLEELEERLEelrELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2529 DKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE------------ATRFKKQADEAKVR 2596
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2597 LQETEKQTTETVVQKLETQRLQSTREADDLKKAI--AELEKEREKLKRDAQELQNKSKETASAQQEQ-MEQQKAMLQQTF 2673
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQLEElEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2674 LTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKL----MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQK 2749
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeLEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1655220506 2750 EMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKT 2790
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1671-1911 |
1.40e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.79 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1671 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1750
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1751 VRQIKVVEEV---AQKTA-ATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlk 1826
Cdd:COG4942 100 EAQKEELAELlraLYRLGrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1827 anealrlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR 1906
Cdd:COG4942 178 -------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1655220506 1907 LKADF 1911
Cdd:COG4942 251 LKGKL 255
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2917-2954 |
1.63e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.63e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1655220506 2917 LLEAQAASGYIVDPVKNKLLTVDEAVKEELIGPELHTR 2954
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3651-3685 |
2.04e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.04e-11
10 20 30
....*....|....*....|....*....|....*
gi 1655220506 3651 LLEAQFATGGIIDPVSSHRVPNDVAIQRGYLSKQM 3685
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1601-2141 |
2.14e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1601 DAEKQKQNIQLELTQLKNlSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR 1680
Cdd:PRK03918 190 NIEELIKEKEKELEEVLR-EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1681 KAAQEEAERLRKQVNEETQKKKNAEdELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRqikvVEEV 1760
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1761 AQKTAATQlqamsfsEKTTKLEESLKKEQgTVLQLQEEAEKLRKQE-----EEANKAREQAEKELETWRLKANEALRLRL 1835
Cdd:PRK03918 344 KKKLKELE-------KRLEELEERHELYE-EAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1836 RAEEEAQRKSLAQEEAEKQK----------TEAERDAKKKAKAEEAALKQKE--NAEKELEKQRTFAEQIaQQKLSAEQE 1903
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKgkcpvcgrelTEEHRKELLEEYTAELKRIEKElkEIEEKERKLRKELREL-EKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1904 YIRLKadfEHAEQQRGlLDNELQRL-KNEVNAAEKQRRQLEDELAKVRSEMdallqmkiqaekvsqsntekskQLLETEA 1982
Cdd:PRK03918 495 LIKLK---ELAEQLKE-LEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEI----------------------KSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1983 LKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDE 2062
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2063 AYQRKLLEDQAAQHKhDIQEKITQLQSSSVSEldRQKNIVEETLRqkkvVEEEIHIIRINFERASKEKSDLEVELKKLK 2141
Cdd:PRK03918 629 DKAFEELAETEKRLE-ELRKELEELEKKYSEE--EYEELREEYLE----LSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2545-2771 |
2.35e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2545 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvVQKLETQRLQSTREAD 2624
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-----LAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2625 DLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQ--QTFLTEKELLLKRERDVEDEKKKLQKHLEDEV 2702
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2703 NKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKK 2771
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2512-2809 |
2.42e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.54 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2512 LQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEisaEAEKLKlrvkelssaQAKAEEEATRFKKQAD 2591
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLE---EAEKAR---------QAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2592 EAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKERE-KLKRDAQELqnkskETASAQQEQMEQQKAMLQ 2670
Cdd:pfam17380 342 MAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQqKNERVRQEL-----EAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2671 QTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKalKDEQQRQQKL-----MDEEKKKLQAIMDEAVKKQKEAEAE-M 2744
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR--LEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQrR 494
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2745 KNKQKEMEALEKKRLEQE---KLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMT 2809
Cdd:pfam17380 495 KILEKELEERKQAMIEEErkrKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1572-2419 |
2.61e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.52 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1572 KSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRS--KNQQLEEAQVSRR------KLEE 1643
Cdd:pfam05483 9 KSFNKCTEDDFEFPFAKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGDCHYQEglKDSDFENSEGLSRlysklyKEAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1644 EIHLIRIQLQTTIKQKSTaddelqKLRDQAAEAEKVRKAAQE---EAERLRKQVNEETQKKKNAEDELKRKSEAEKEAAR 1720
Cdd:pfam05483 89 KIKKWKVSIEAELKQKEN------KLQENRKIIEAQRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1721 QKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQaMSFS-----EKTTKLEESLKKEQGT---- 1791
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLE-MHFKlkedhEKIQHLEEEYKKEINDkekq 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1792 ----VLQLQEEAEKLRKQ----EEEANKAREQAEK-ELETWRLKANEALRLRLRAEEEAQRKSLaQEEAEKQKTeAERDA 1862
Cdd:pfam05483 242 vsllLIQITEKENKMKDLtfllEESRDKANQLEEKtKLQDENLKELIEKKDHLTKELEDIKMSL-QRSMSTQKA-LEEDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1863 KKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQklsaeqeyirLKADFEHAEQqrgLLDNELQRLKNEvnaaEKQRRQL 1942
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE----------FEATTCSLEE---LLRTEQQRLEKN----EDQLKII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1943 EDELAKVRSEMDALLQMKiqaekvsqSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAK-KQRQLAEDEAARQRAEAE 2021
Cdd:pfam05483 383 TMELQKKSSELEEMTKFK--------NNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFLLQAREKEIHD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2022 KILKEKLAAINEATRLKteaEVALKAKEAENERLKRQAEDEAYQRKLLEDQaaqhkhdiqeKITQLQSSSVSELDRQKni 2101
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLK---EVEDLKTELEKEKLKNIELTAHCDKLLLENK----------ELTQEASDMTLELKKHQ-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2102 vEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKK 2181
Cdd:pfam05483 520 -EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2182 IAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKedlLSQEKLRD 2261
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK---ISEEKLLE 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2262 EFENAKKLaqaaetakekaekeaallrqkAEEAEKLKKAAEDEAAKQAKaqkdaerlrkeaeaeaakraaaeaaalkqkq 2341
Cdd:pfam05483 676 EVEKAKAI---------------------ADEAVKLQKEIDKRCQHKIA------------------------------- 703
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2342 EADAEMAKHKKEAEQALKQKsqvEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDE 2419
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1289-2001 |
2.79e-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: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1289 TKDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRL---HSERDAEL 1365
Cdd:TIGR00618 207 TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQeavLEETQERI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1366 EHYRQLAGSLLE---------RWQAVFAQIDLRQREL-SLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKAL 1435
Cdd:TIGR00618 287 NRARKAAPLAAHikavtqieqQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1436 -KEQLTQEKKLLEEIEKNKDQIENCQKDAKAyIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRY 1514
Cdd:TIGR00618 367 iREISCQQHTLTQHIHTLQQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1515 SELSTLTSQYIKFIL--ETQRRLeDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELE-AQELKLKMKED 1591
Cdd:TIGR00618 446 AITCTAQCEKLEKIHlqESAQSL-KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1592 ASQRQGLAVDAEKQKQniqleltqlknlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIriqlqttikqkstaDDELQKLRD 1671
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQL-------------ETSEEDVYHQLTSERKQRASLKEQMQEI--------------QQSFSILTQ 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1672 QAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE-------AERRLK 1744
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalhalQLTLTQ 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1745 QAEEEKVRQIKVVEEVAQKTAATQLQAM-SFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETW 1823
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1824 RLKANEALRlrlRAEEEAQRKSLAQEEAEKQKTEAErdakkkaKAEEAALKQKENAEKELE-KQRTFAEQIAQQKLSAEQ 1902
Cdd:TIGR00618 738 EDALNQSLK---ELMHQARTVLKARTEAHFNNNEEV-------TAALQTGAELSHLAAEIQfFNRLREEDTHLLKTLEAE 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1903 EYIRLKADFEHAEQQRGLLDNELQRLKNevnaaekQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA 1982
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLS-------RLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
730
....*....|....*....
gi 1655220506 1983 LKMKQLAEEAARLRSVAEE 2001
Cdd:TIGR00618 881 INQIKIQFDGDALIKFLHE 899
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1631-2150 |
3.03e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1631 LEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVnEETQKKKNAEDELKR 1710
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1711 K---SEAEKEAARQKQKALDE-LQKHKMQAEEAERRLKQAeEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLK 1786
Cdd:PRK03918 239 EieeLEKELESLEGSKRKLEEkIRELEERIEELKKEIEEL-EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1787 KEQGTVLQLQEEAEKLRKQEEEANKAREQAEK------ELETWRLKANEALRLRLRAEE-EAQRKSLAQEEAEKQKTEAE 1859
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1860 RdakkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKA------------DFEHAEQQRGLLDNELQR 1927
Cdd:PRK03918 398 K--------------AKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1928 LKNEVNAAEKQRRQLEDELAKVRSEMDA---LLQMKIQAEKVSQSNTEKSKQLLEtealKMKQLAEEAARLRSVAEEAKK 2004
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLKELEEKLKKYNLE----ELEKKAEEYEKLKEKLIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2005 QRQLAEDEAARqraeaEKILKEKLAAINEATRlKTEAEVALKAKEAENERLKRQAEDE--------AYQRKLLEDQAAQH 2076
Cdd:PRK03918 540 EIKSLKKELEK-----LEELKKKLAELEKKLD-ELEEELAELLKELEELGFESVEELEerlkelepFYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2077 KHDIQEKITQLQSS---SVSELDRQKNIVEETLRQ-----KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQ 2148
Cdd:PRK03918 614 LEREEKELKKLEEEldkAFEELAETEKRLEELRKEleeleKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
..
gi 1655220506 2149 KS 2150
Cdd:PRK03918 694 KT 695
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1433-2083 |
3.10e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.14 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1433 KALKE-QLTQEK---KLLEEIEKNKDQIEncQKDAKAYIDSLkdyefqilayraLQDPIA-SPLKKPKMESASDNIIQEY 1507
Cdd:pfam05483 120 KAIQElQFENEKvslKLEEEIQENKDLIK--ENNATRHLCNL------------LKETCArSAEKTKKYEYEREETRQVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1508 VTLRTRYSELST----LTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQ---LETQKQLAEGHAKSVAKAELE 1580
Cdd:pfam05483 186 MDLNNNIEKMILafeeLRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1581 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKS 1660
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1661 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQ---VNEETQKKKNAEDE---LKRKSEAEKEAAR----QKQKALDELQ 1730
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkiITMELQKKSSELEEmtkFKNNKEVELEELKkilaEDEKLLDEKK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1731 KHKMQAEEAERR------LKQAEEEKVRQIKVveEVAQKTAATQLQAMSFSEKTTKLE-ESLKKEQGTV---------LQ 1794
Cdd:pfam05483 426 QFEKIAEELKGKeqelifLLQAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEkEKLKNIELTAhcdklllenKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1795 LQEEAE----KLRKQEEEANKAREQAEKELEtwRLKANEALRLRLRAEEEAQRKSLAQ---------EEAEKQKTEAERD 1861
Cdd:pfam05483 504 LTQEASdmtlELKKHQEDIINCKKQEERMLK--QIENLEEKEMNLRDELESVREEFIQkgdevkcklDKSEENARSIEYE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1862 AKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqeyirlkadfeHAEQQRGLLDNElqrlknEVNAAEKQRRQ 1941
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN---------------KALKKKGSAENK------QLNAYEIKVNK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1942 LEDELAKVRS---EMDALLQMKIQAEKVSQSNtekskqlLETEALKMKQLAEEAARLRSVAEEaKKQRQLAEDEA--ARQ 2016
Cdd:pfam05483 641 LELELASAKQkfeEIIDNYQKEIEDKKISEEK-------LLEEVEKAKAIADEAVKLQKEIDK-RCQHKIAEMVAlmEKH 712
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2017 RAEAEKILKEKLAAI-------NEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEK 2083
Cdd:pfam05483 713 KHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1697-2756 |
3.36e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 70.46 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1697 ETQKKKNAEDELKRKSEAEKEAARQKQKALDelQKHKMQAEEAERRLKQAEEEKVRQI--KVVEEVAQKTAATQLqAMSF 1774
Cdd:TIGR00606 167 EGKALKQKFDEIFSATRYIKALETLRQVRQT--QGQKVQEHQMELKYLKQYKEKACEIrdQITSKEAQLESSREI-VKSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1775 SEKTTKLEESLKK---EQGTVLQLQEEAEKLRKQEEEankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLaqEEA 1851
Cdd:TIGR00606 244 ENELDPLKNRLKEiehNLSKIMKLDNEIKALKSRKKQ----MEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTV--REK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1852 EKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRG-LLDNELQrlkn 1930
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpFSERQIK---- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1931 evNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKK----QR 2006
Cdd:TIGR00606 394 --NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2007 QLAEDEAARQRAEAEKILKEKlaaiNEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ-------RKLLEdQAAQHKHD 2079
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEK----NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhtttRTQME-MLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2080 IQEKITQLQSSSVSELDRQKNiveeTLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLkgiadETQKSkakaeeeae 2159
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLG----YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL-----EQNKN--------- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2160 klkklaaeeerkrreaeekvkKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLkDKAEKELEKQvilAKEAAQKSTAAE 2239
Cdd:TIGR00606 609 ---------------------HINNELESKEEQLSSYEDKLFDVCGSQDEESDL-ERLKEEIEKS---SKQRAMLAGATA 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2240 QKAQDVlsknkedllsqEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2319
Cdd:TIGR00606 664 VYSQFI-----------TQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2320 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKqkalmdeeLQRVKAQVNDA 2399
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI--------MERFQMELKDV 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2400 VKQKAQVENELSKVKMqmdellklkvrieeeNLRLMQKNKDNTQKllAEEAEKMKSLAEEAARLSVEAEETARQRKTAEA 2479
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDL---------------DRTVQQVNQEKQEK--QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2480 ELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldkETQGFQKSLEAERKRQLEIS 2559
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE---KEELISSKETSNKKAQDKVN 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2560 AEAEKLKLRVKELSSAQAKAEEEATRFKKQAD----EAKVRLQETEKQTTE------TVVQKLETQRLQSTREADDLKka 2629
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGKDDYLKQKEtelnTVNAQLEECEKHQEKinedmrLMRQDIDTQKIQERWLQDNLT-- 1022
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2630 iaeLEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLT---EKELLLKRERDVEDEKKKLQKHLedevnKAK 2706
Cdd:TIGR00606 1023 ---LRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLikrNHVLALGRQKGYEKEIKHFKKEL-----REP 1094
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2707 ALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEK 2756
Cdd:TIGR00606 1095 QFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINK 1144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1683-2223 |
3.38e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1683 AQEEAERLRKQVNEetqKKKNAEDELKRKSEAE---KEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKvrqiKVVEE 1759
Cdd:PRK03918 163 AYKNLGEVIKEIKR---RIERLEKFIKRTENIEeliKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1760 VAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEK--ELETWRLKANEALRlrlRA 1837
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELR---EI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1838 EEEAQRKSLAQEEAEKQKTEAERDakkkAKAEEAALKQKENAEKELEKQRTFAEqiaqqklsaeqEYIRLKADFEHAEQQ 1917
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHE-----------LYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1918 RGLL-DNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQS---------------NTEKSKQLLETE 1981
Cdd:PRK03918 378 KKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1982 ALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQR--------AEAEKILKEKLAAINeATRLKTEAEVALKAKEAEN- 2052
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelAEQLKELEEKLKKYN-LEELEKKAEEYEKLKEKLIk 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2053 ---------ERLKRQAEDEAYQRKLLE--DQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQkkvveeeihiiri 2121
Cdd:PRK03918 537 lkgeikslkKELEKLEELKKKLAELEKklDELEEELAELLKELEELGFESVEELEERLKELEPFYNE------------- 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2122 nFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE-AEEKVKKIAAAEEEAARQRKAAQDEV 2200
Cdd:PRK03918 604 -YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAEL 682
|
570 580
....*....|....*....|...
gi 1655220506 2201 ERLKQKAAEANKLKDKAEKELEK 2223
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEE 705
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2289-2640 |
4.06e-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: 69.77 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2289 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKqeadaemakhKKEAEQALKQK--SQVEK 2366
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER----------KRELERIRQEEiaMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2367 ELGLVKLQLDETDKQkalmdeelQRVKAQVNDAVKQKAQVENELSKVKMQMDELlkLKVRIEEENLRlmqknkdntqkll 2446
Cdd:pfam17380 377 MRELERLQMERQQKN--------ERVRQELEAARKVKILEEERQRKIQQQKVEM--EQIRAEQEEAR------------- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2447 aeeAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQAQEKAKKL 2526
Cdd:pfam17380 434 ---QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE--------------ERKRKKLELEKEKRDRKRAEEQRRKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2527 LEdkQEIQQRLdketqgfQKSLEAERKRQLeISAEAEKlklRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE 2606
Cdd:pfam17380 497 LE--KELEERK-------QAMIEEERKRKL-LEKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
330 340 350
....*....|....*....|....*....|....
gi 1655220506 2607 tvvqklETQRLQSTREADDLKKAIAELEKEREKL 2640
Cdd:pfam17380 564 ------ERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1592-2000 |
8.20e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.21 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1592 ASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKnQQLEEAQVSRRKLEEEI-----HLIRiqLQTTIKQKSTAD--- 1663
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMA-RELEELSARESDLEQDYqaasdHLNL--VQTALRQQEKIEryq 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1664 DELQKLRDQAAEAEKVRKAAQEEAERLRKQvneetqkKKNAEDELKrkseaekEAARQ---KQKALDELQKHKMQAEEAE 1740
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEAR-------LEAAEEEVD-------SLKSQladYQQALDVQQTRAIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1741 RRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK--QEEEANKAREQAEK 1818
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiaGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1819 ELETWRLKANEALRLR-LRAE-EEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELE----KQRTFAEQ 1892
Cdd:COG3096 500 LLRRYRSQQALAQRLQqLRAQlAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEeleeQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1893 IAQ-----QKLSAEQEYIRLKADFEHAEQQRglldneLQRLKNEVNAAekqrrqLEDelakvRSEMDALLQMKIQAE--- 1964
Cdd:COG3096 580 RSElrqqlEQLRARIKELAARAPAWLAAQDA------LERLREQSGEA------LAD-----SQEVTAAMQQLLERErea 642
|
410 420 430
....*....|....*....|....*....|....*..
gi 1655220506 1965 KVSQSNTEKSKQLLETEALKMKQLA-EEAARLRSVAE 2000
Cdd:COG3096 643 TVERDELAARKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4151-4189 |
9.94e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.26 E-value: 9.94e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 4151 LLEAQAATGYVIDPIKNLKLNVTEAVKMGVVGPEFKDKL 4189
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4573-4611 |
1.13e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.26 E-value: 1.13e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 4573 FLEVQYLTGGLIEPDTTGRVSIDEAVKKGSLDARTAQKL 4611
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1841-2095 |
1.33e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1841 AQRKSLAQEEAEKQKTEAerdakkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGL 1920
Cdd:COG4942 17 AQADAAAEAEAELEQLQQ----------------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1921 LDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAE 2000
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2001 EAKKQRQlaedEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDI 2080
Cdd:COG4942 161 ELAALRA----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*
gi 1655220506 2081 QEKITQLQSSSVSEL 2095
Cdd:COG4942 237 AAAAERTPAAGFAAL 251
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2194-2780 |
1.76e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 67.69 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2194 KAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAqdVLSKNKEDLLSQEKLRDEFENAKKLAQAA 2273
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA--VLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2274 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKE 2353
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2354 AEQALKQKSQV-----EKELGLVKLQLDETDKQKALMDEELQ---RVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKV 2425
Cdd:TIGR00618 387 QKTTLTQKLQSlckelDILQREQATIDTRTSAFRDLQGQLAHakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2426 RIEEENLRLMQKnkdntQKLLAEEAEKMKSLAEEAARLSVEAEETARQrkTAEAELAEQRALAEKMLKEKMQA-IQEATK 2504
Cdd:TIGR00618 467 SLKEREQQLQTK-----EQIHLQETRKKAVVLARLLELQEEPCPLCGS--CIHPNPARQDIDNPGPLTRRMQRgEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2505 LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLE-AERKRQLEISAEAEKLKLRVKELSSAQAKAEEEA 2583
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2584 trfKKQADEAKVRLQETEKQTTETVVQKLETQrlqsTREADDLKKaiaelEKEREKLKR-DAQELQNKSKETASAQQEQM 2662
Cdd:TIGR00618 620 ---KLQPEQDLQDVRLHLQQCSQELALKLTAL----HALQLTLTQ-----ERVREHALSiRVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2663 EQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKA-----LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQ 2737
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSdlaarEDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1655220506 2738 KEAEAEMKNKQKEMEaLEKKRLEQEKLLADENKKLREKLESLE 2780
Cdd:TIGR00618 768 EEVTAALQTGAELSH-LAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1523-2146 |
1.81e-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: 67.84 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1523 QYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtQKQLAEGHAKSVAKAELEAQElklkmkedasqrqglavDA 1602
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1603 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQ---VSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL--RDQAAEAE 1677
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRkmmLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1678 KVRKAAQEEAERLRKQVNEetqkkknAEDELkrksEAEKEAARQKQKALdeLQKHKmqaEEAERRLKQAEEEkvrqikvV 1757
Cdd:pfam15921 224 KILRELDTEISYLKGRIFP-------VEDQL----EALKSESQNKIELL--LQQHQ---DRIEQLISEHEVE-------I 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1758 EEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVL----QLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALrl 1833
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMrqlsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL-- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1834 rlrAEEEAQRKSLAQEEA----EKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKA 1909
Cdd:pfam15921 359 ---TEARTERDQFSQESGnlddQLQKLLAD--------------LHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1910 DFEHAEQQRglLDNELQRLKNEVNAaekqrrQLEDELAKVRSEMDALlqmkiqaEKVSQ--SNTEKSKQLLE--TEALKM 1985
Cdd:pfam15921 422 DDRNMEVQR--LEALLKAMKSECQG------QMERQMAAIQGKNESL-------EKVSSltAQLESTKEMLRkvVEELTA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1986 KQLAEEAARlRSVAEEAKkqrQLAEDEAARQRAEAE--KILKEKLAAINEATRLKTEAEvALKAKEAENERLKRQAEDEA 2063
Cdd:pfam15921 487 KKMTLESSE-RTVSDLTA---SLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQMAEKD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2064 YQRKLLEDQAaqhkhdiqEKITQL---QSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKE----KSDLEVE 2136
Cdd:pfam15921 562 KVIEILRQQI--------ENMTQLvgqHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRElearVSDLELE 633
|
650
....*....|
gi 1655220506 2137 LKKLKGIADE 2146
Cdd:pfam15921 634 KVKLVNAGSE 643
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2352-2593 |
1.81e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2352 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvrieEEN 2431
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--------EKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2432 LRLMQKNKDNTQKLLAE---EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmQAIQEATKLKAE 2508
Cdd:COG4942 92 IAELRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR----------EQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2509 AEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2588
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 1655220506 2589 QADEA 2593
Cdd:COG4942 242 RTPAA 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1291-1843 |
2.43e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1291 DAEDTVKSYESRLRDV-SKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYR 1369
Cdd:COG1196 278 ELELELEEAQAEEYELlAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1370 QLAGSLLERWQAVFAQIDLRQRElsllgrhmnsykqsyewliqwlrEARLRQEKIEAApvwdsKALKEQLTQEKKLLEEI 1449
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEE-----------------------LEELAEELLEAL-----RAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1450 EKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDpiasplkkpKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFIL 1529
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALE---------EAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAE-------------GHAKSVAKAELEAQELKLKMKEDASQRQ 1596
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligvEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1597 GLAVDAEKQKQNIQ--LELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAA 1674
Cdd:COG1196 561 AAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1675 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQI 1754
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1755 KVVEEVAQKTAATQLQamsfsekttkLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwRLKA-Nealrl 1833
Cdd:COG1196 721 LEEEALEEQLEAEREE----------LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE--ALGPvN----- 783
|
570
....*....|
gi 1655220506 1834 rLRAEEEAQR 1843
Cdd:COG1196 784 -LLAIEEYEE 792
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1622-1952 |
2.74e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 66.43 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1622 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR-KAAQEEAERLRKQVNEETQK 1700
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRqKRLQEALERQKEFDPTIADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1701 KKNAEDELKRKSEAEKEAARQKQKALDELQKHKMqaEEAERRLKQAEEEKVRQ-IKVVEEVAQKTAATQLQAMSFSEKTT 1779
Cdd:pfam02029 97 KESVAERKENNEEEENSSWEKEEKRDSRLGRYKE--EETEIREKEYQENKWSTeVRQAEEEGEEEEDKSEEAEEVPTENF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1780 KLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAE 1859
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1860 RdakkkakaeeaalkqkENAEKELEKqrtfAEQIAQQKLSAEQEYIRLKadfEHAEQQRGLLDNELQRLKNEVN----AA 1935
Cdd:pfam02029 255 R----------------RRQEKESEE----FEKLRQKQQEAELELEELK---KKREERRKLLEEEEQRRKQEEAerklRE 311
|
330
....*....|....*..
gi 1655220506 1936 EKQRRQLEDELAKVRSE 1952
Cdd:pfam02029 312 EEEKRRMKEEIERRRAE 328
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4495-4532 |
2.74e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 57.88 E-value: 2.74e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1655220506 4495 QRLLEAQACTGGIIDPNTGEKFSVADAMNKGLVDKIMV 4532
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1995-2716 |
2.75e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 67.16 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1995 LRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaaINEATRLKTE--AEVALKAKEAENERLKRQAEDEAYQRKLLEdQ 2072
Cdd:NF041483 78 LRNAQIQADQLRADAERELRDARAQTQRILQEH---AEHQARLQAElhTEAVQRRQQLDQELAERRQTVESHVNENVA-W 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2073 AAQHKHDIQEKITQLQSSSVSELDrqKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKlkgiadETQKSKA 2152
Cdd:NF041483 154 AEQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARK------DAERLLN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2153 KAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRkaAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAA 2232
Cdd:NF041483 226 AASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQR--MQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAN 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2233 QK--STAAEQKAQDVLSKNKEdllsQEKLRDEFENAKKLAQAAETakekaekeaallRQKAEEAEKLK-KAAEDEAAKQA 2309
Cdd:NF041483 304 EQrtRTAKEEIARLVGEATKE----AEALKAEAEQALADARAEAE------------KLVAEAAEKARtVAAEDTAAQLA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2310 KAQKDAER-LRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKE------LGLVKLQLD------ 2376
Cdd:NF041483 368 KAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDdtkeyrAKTVELQEEarrlrg 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2377 ETDKQKALMDEELQRVKAQV-NDAVKQ----KAQVENELSKVKMQMDElLKLKVRIEEENLRLMQKNKDNTQKLLAEEAe 2451
Cdd:NF041483 448 EAEQLRAEAVAEGERIRGEArREAVQQieeaARTAEELLTKAKADADE-LRSTATAESERVRTEAIERATTLRRQAEET- 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2452 kMKSLAEEAARLSVEAEETAR-QRKTAEAELAEQRALAEK-MLKEKMQAIQEATKLKAEAEE----LQKQKNQAQEKAKK 2525
Cdd:NF041483 526 -LERTRAEAERLRAEAEEQAEeVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEErltaAEEALADARAEAER 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2526 LLEDKQEIQQRLDKETqgfqksleAERKRQLEISAEAEKLKLR---VKELSSAQAKAEEEATRFKKQADEAKVRLQETEK 2602
Cdd:NF041483 605 IRREAAEETERLRTEA--------AERIRTLQAQAEQEAERLRteaAADASAARAEGENVAVRLRSEAAAEAERLKSEAQ 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2603 QTTETVVQKLETqrlQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQkamlqqtfltEKELLLK 2682
Cdd:NF041483 677 ESADRVRAEAAA---AAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQ----------SEELLAS 743
|
730 740 750
....*....|....*....|....*....|....*.
gi 1655220506 2683 RERDVEDEKKKLQKHLEDEVNKAKAL--KDEQQRQQ 2716
Cdd:NF041483 744 ARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQ 779
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1418-1767 |
3.23e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.69 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1418 RLRQEKIEaapvwdsKALKEQLTQEKK-LLEEIEKNKdQIENCQKDAKAYIDSlkdyefqilayralQDPIASPLKKPKM 1496
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDR--------------QAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1497 ESASDniiQEYVTLRTRYSELSTLTSQYIKFILETQRRLE--------DDEKASEKLKEDEKKRMAEIQAQLETQKQLAE 1568
Cdd:pfam17380 345 ERERE---LERIRQEERKRELERIRQEEIAMEISRMRELErlqmerqqKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1569 ghAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlsEQEIRSKNQQLEEAQVSRRKLEEEihli 1648
Cdd:pfam17380 422 --MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQ---- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1649 riqlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEEtQKKKNAEDElkRKSEAEKEAARQkqkalde 1728
Cdd:pfam17380 493 ---------RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEE--RRKQQEMEERRR------- 553
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1655220506 1729 LQKHKMQAEEAERRLKQAEEEK--VRQIKVVEEVAQKTAAT 1767
Cdd:pfam17380 554 IQEQMRKATEERSRLEAMERERemMRQIVESEKARAEYEAT 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1592-1828 |
3.25e-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: 65.56 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1592 ASQRQGLAVDAEKQKQNIQLELTQLknlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRD 1671
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1672 QAAEAEKVRKAAQEE-AERLRK-QVNEETQKKK---NAED--ELKRKSEAEKEAARQKQKALDELQKhkmQAEEAERRLK 1744
Cdd:COG4942 91 EIAELRAELEAQKEElAELLRAlYRLGRQPPLAlllSPEDflDAVRRLQYLKYLAPARREQAEELRA---DLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1745 QAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWR 1824
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....
gi 1655220506 1825 LKAN 1828
Cdd:COG4942 248 FAAL 251
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1599-2000 |
3.25e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1599 AVDAEKQKQNIQLELtqlkNLSEQEIRSKNQQLEEAQVSRRKLEEEI-----HLIRIQ----LQTTIKQkstADDELQKL 1669
Cdd:PRK04863 288 ALELRRELYTSRRQL----AAEQYRLVEMARELAELNEAESDLEQDYqaasdHLNLVQtalrQQEKIER---YQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1670 RDQAAEAEKVRKAAQEEAERLRkqvneetqkkknaedelKRKSEAEKEAARQK------QKALDELQKHKMQAEEAERRL 1743
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENE-----------------ARAEAAEEEVDELKsqladyQQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1744 KQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK------QEEEANKAREqAE 1817
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevsRSEAWDVARE-LL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1818 KELETWRLKAN--EALRLRLRaeeEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQ 1895
Cdd:PRK04863 503 RRLREQRHLAEqlQQLRMRLS---ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1896 QKLSAEQEYIRLKADFEHAEQQRglldnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSN--TEK 1973
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARA-------PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERdeLAA 652
|
410 420
....*....|....*....|....*...
gi 1655220506 1974 SKQLLETEALKMKQL-AEEAARLRSVAE 2000
Cdd:PRK04863 653 RKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2573-2837 |
3.68e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 65.24 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2573 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSK 2652
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2653 ETASAQQEQMEQQKAMLQ-------QTFLTEKELLlkrerdvedekKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKK 2725
Cdd:COG3883 90 ERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL-----------SKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2726 LQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2805
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270
....*....|....*....|....*....|..
gi 1655220506 2806 VSMTTVETTKKVFNGSVEAVKKDGASPLAFEG 2837
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3984-4022 |
3.76e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.72 E-value: 3.76e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 3984 LLEAQNATGGLMDPEYCFHLPTDVAMQRGYINKETLDRI 4022
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 ... |
1297-2106 |
4.06e-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: 66.74 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1297 KSYESRLRDVSKVPAEEKEVEAHRSQLKamraeaEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLL 1376
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLK------NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1377 ERWQAVFAQIDLRQREL-SLLGRHMNSYKQSYEwLIQWLREARLR----QEKIEAAPVWDSKALKeqltQEKKLLEEIEK 1451
Cdd:pfam01576 229 AQIAELRAQLAKKEEELqAALARLEEETAQKNN-ALKKIRELEAQiselQEDLESERAARNKAEK----QRRDLGEELEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1452 NKDQIENCQkDAKAYIDSLkdyefqilayRALQDPIASPLKKpKMESASDNIIQEYVTLRTRYSE-LSTLTSQyikfiLE 1530
Cdd:pfam01576 304 LKTELEDTL-DTTAAQQEL----------RSKREQEVTELKK-ALEEETRSHEAQLQEMRQKHTQaLEELTEQ-----LE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1531 TQRRledDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEdasqrqglavdAEKQKQNIQ 1610
Cdd:pfam01576 367 QAKR---NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE-----------SERQRAELA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1611 LELTQLKNlseqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTikQKSTADDELQKLrdqaAEAEKVRkAAQEEAERL 1690
Cdd:pfam01576 433 EKLSKLQS----ELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT--QELLQEETRQKL----NLSTRLR-QLEDERNSL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1691 RKQVNEETQKKKNAEdelkrkseaekeaaRQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKtaatqlq 1770
Cdd:pfam01576 502 QEQLEEEEEAKRNVE--------------RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ------- 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1771 amsFSEKTT---KLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRK--- 1844
Cdd:pfam01576 561 ---LEEKAAaydKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKetr 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1845 ----SLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK---ELEKQRTFAEQIAQQ------------------KLS 1899
Cdd:pfam01576 638 alslARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKnvhELERSKRALEQQVEEmktqleeledelqatedaKLR 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1900 AEQEYIRLKADF--------EHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDelAKVRSEMDaLLQMKIQAEKVSQSNT 1971
Cdd:pfam01576 718 LEVNMQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA--AKKKLELD-LKELEAQIDAANKGRE 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1972 EKSKQLLETEAlKMKQLAEEAARLRSVAEEAKKQRQlaEDEAARQRAEAEKI-LKEKLAAINEATRlKTEAEVALKAKEA 2050
Cdd:pfam01576 795 EAVKQLKKLQA-QMKDLQRELEEARASRDEILAQSK--ESEKKLKNLEAELLqLQEDLAASERARR-QAQQERDELADEI 870
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2051 ENERLKRQAEDEAYQRklLEDQAAQHKHDIQEKitQLQSSSVSELDRQKNIVEETL 2106
Cdd:pfam01576 871 ASGASGKSALQDEKRR--LEARIAQLEEELEEE--QSNTELLNDRLRKSTLQVEQL 922
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2429-2658 |
6.05e-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: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2429 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRalaekmlkekmqaiQEATKLKAE 2508
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--------------AELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2509 AEELQKQKNQAQEKAKKLLED--KQEIQQRLD-----KETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE 2581
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2582 EATRFKKQADEAKVRLQ--ETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQ 2658
Cdd:COG4942 172 ERAELEALLAELEEERAalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1438-2146 |
6.27e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1438 QLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQIlayralqdpIASPLKKPKMESASDNIIQEyvtLRTRYSEL 1517
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKI---------NNSNNKIKILEQQIKDLNDK---LKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1518 STLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmaeiqaqLETQKQLAEgHAKSVAKAELEAQELKLKMKedasqrqg 1597
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQK-------KENKKNIDK-FLTEIKKKEKELEKLNNKYN-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1598 lavDAEKQKQNIQLELTQLKNlseqEIRSKNQQLEEAQVSRRKLEeeihliriQLQTTIKQKSTADDELQKlrdQAAEAE 1677
Cdd:TIGR04523 163 ---DLKKQKEELENELNLLEK----EKLNIQKNIDKIKNKLLKLE--------LLLSNLKKKIQKNKSLES---QISELK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1678 KVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVV 1757
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1758 EEVAQKTAATQLQamSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrlKANEALRLrlra 1837
Cdd:TIGR04523 305 EQDWNKELKSELK--NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE---KQNEIEKL---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1838 EEEAQRKSLAQEEAEKQKTEAERdakkkakaeeaALKQKENAEKELEKQrtfAEQIAQQKLSAEQEYIRLKADFEHAEQQ 1917
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQ---IKKLQQEKELLEKEIERLKETIIKNNSE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1918 RGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmKIQAEKVSQSNTEKSKQLLETEALKmKQLAEEAARLRS 1997
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI---KQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1998 VAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQA-EDEAYQRKLLEDQAAQH 2076
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSlKKKQEEKQELIDQKEKE 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2077 KHDIQEKITqLQSSSVSELDRQKNIVEETLRQ-----------KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIAD 2145
Cdd:TIGR04523 598 KKDLIKEIE-EKEKKISSLEKELEKAKKENEKlssiiknikskKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
.
gi 1655220506 2146 E 2146
Cdd:TIGR04523 677 D 677
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1649-1861 |
6.66e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1649 RIQLQttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE---ETQKKKNAEDELKRKSEAEKEAARQKQKA 1725
Cdd:PRK09510 66 RQQQQ----QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKErlaAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1726 ldeLQKHKMQAEEAERRL----KQAEEEKVRQikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEK 1801
Cdd:PRK09510 142 ---AAAAKAKAEAEAKRAaaaaKKAAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1802 LRKQEEEANKAREQAEKELEtwrlkanealrlrlrAEEEAQRKSLAQEEAEKQKTEAERD 1861
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAEAK---------------AAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2231-2788 |
6.77e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.02 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2231 AAQKSTAAEQKAQDVLSKNKEDLLSQekLRDEfenakklaqaaetakekaekeaalLRQKAEEAEKLKKAAeDEAAKQAK 2310
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRT--LDDQ------------------------WKEKRDELNGELSAA-DAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2311 AQKDAerlrkeaeaeaakraaaEAAALKQKQEADAEmaKHKKEAEQALKQKSQVEKELGLVKLQLD-------ETDKQKA 2383
Cdd:pfam12128 322 SELEA-----------------LEDQHGAFLDADIE--TAAADQEQLPSWQSELENLEERLKALTGkhqdvtaKYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2384 LMDEELQRVKAQVND--------AVKQKAQVENELSKVKMQM------------DELLKLKVRIEEENLRLMQknkdntq 2443
Cdd:pfam12128 383 KIKEQNNRDIAGIKDklakireaRDRQLAVAEDDLQALESELreqleagklefnEEEYRLKSRLGELKLRLNQ------- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2444 kLLAEEAEKMKslaeeaarLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKA 2523
Cdd:pfam12128 456 -ATATPELLLQ--------LENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2524 KKLLEDKQEIQQRLDKETQGFQKSLEAERKRQL--------EISAEAEK-------LKLRVKELSSAQAKAEEEATRfkk 2588
Cdd:pfam12128 527 LQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELlhrtdldpEVWDGSVGgelnlygVKLDLKRIDVPEWAASEEELR--- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2589 qadeAKVRLQETEKQTTETVVQKLETQrlqstreaddLKKAIAELEKEREKLKRDAQELQNkSKETASAQQEQMEQQKAM 2668
Cdd:pfam12128 604 ----ERLDKAEEALQSAREKQAAAEEQ----------LVQANGELEKASREETFARTALKN-ARLDLRRLFDEKQSEKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2669 LQQTFLTEKELLLKRERDVEDEKKKLQKHLED--EVNKAKALKDEQQRQQK---LMDEEKKKLQAIMDEAVKKQKEAEAE 2743
Cdd:pfam12128 669 KNKALAERKDSANERLNSLEAQLKQLDKKHQAwlEEQKEQKREARTEKQAYwqvVEGALDAQLALLKAAIAARRSGAKAE 748
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2744 MKNKQKEME-ALEKKRLEQEKL--LADENKKLREKLESLEVTSKQAAS 2788
Cdd:pfam12128 749 LKALETWYKrDLASLGVDPDVIakLKREIRTLERKIERIAVRRQEVLR 796
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1529-1903 |
8.94e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.38 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1529 LETQRRLEDDEKASEKLKEDEKKrmAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQN 1608
Cdd:pfam02463 669 SELTKELLEIQELQEKAESELAK--EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1609 I---QLELTQLKNLSEQEIRSKNQQLEEAQVSRR-------KLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEK 1678
Cdd:pfam02463 747 EeeeEEEKSRLKKEEKEEEKSELSLKEKELAEERekteklkVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1679 VRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAL----DELQKHKMQAEEAERRLKQAEEEKVRQI 1754
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLkeeeLEEQKLKDELESKEEKEKEEKKELEEES 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1755 KVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRLR 1834
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG----KVNLMAIEE 982
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 1835 LRAEEEAQRKslaqEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQE 1903
Cdd:pfam02463 983 FEEKEERYNK----DELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAE 1047
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1664-2146 |
9.80e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1664 DELQKLRDQAAEAEKVRKAAQEEAERLRkQVNEETQKKKNAEDELkRKSEAEKEAAR--QKQKALDELQKhkmQAEEAER 1741
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERL-AELEYLRAALRlwFAQRRLELLEA---ELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1742 RLKQAEEEKVRQikvveEVAQKTAATQLQAmsfsekttkLEESLKKEQGTVL-QLQEEAEKLRKQEEEANKAREQAEKEL 1820
Cdd:COG4913 303 ELARLEAELERL-----EARLDALREELDE---------LEAQIRGNGGDRLeQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1821 ET--WRLKANEA--LRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkkakaeeaaLKQKENAEKELEKQRtfaEQIAQQ 1896
Cdd:COG4913 369 AAlgLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAA-----------LRDLRRELRELEAEI---ASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1897 KLSAEQEYIRLKADFEHAeqqRGLLDNELQ--------RLKNEV--NAAEK----QRRQL---EDELAKVRSEMDAL-LQ 1958
Cdd:COG4913 435 KSNIPARLLALRDALAEA---LGLDEAELPfvgelievRPEEERwrGAIERvlggFALTLlvpPEHYAAALRWVNRLhLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1959 MKIQAEKVSQSNTEKSKQLLETEALKMK--------------QLAEEAARLR--SVAE---------------------E 2001
Cdd:COG4913 512 GRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrawleaELGRRFDYVCvdSPEElrrhpraitragqvkgngtrhE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2002 AKKQRQLAED-----EAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLleDQAAQH 2076
Cdd:COG4913 592 KDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAERE 669
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2077 KHDIQEKITQLQSSS--VSELDRQkniVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 2146
Cdd:COG4913 670 IAELEAELERLDASSddLAALEEQ---LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1681-1941 |
1.15e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.71 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1681 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELqKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1760
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL-EQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1761 AQKTAATQLQamsfsekttkleeslKKEQGTVLQLQEEAEKlrKQEEEAN-KAREQAEKELETWRLKANEAlrlrLRAEE 1839
Cdd:TIGR02794 125 KAKQAAEAKA---------------KAEAEAERKAKEEAAK--QAEEEAKaKAAAEAKKKAEEAKKKAEAE----AKAKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1840 EAQRKslAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRG 1919
Cdd:TIGR02794 184 EAEAK--AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSN----------AEKQGG 251
|
250 260
....*....|....*....|..
gi 1655220506 1920 LLDNELQRLKNEVNAAEKQRRQ 1941
Cdd:TIGR02794 252 ARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
203-311 |
1.17e-09 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 58.74 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 203 KKTFTKWVNKHLMKaQRHIT----------DLYEDLRDGHNLISLLEVLSGETLPrERDLVRnvrlprEKGRMRFHKLQN 272
Cdd:cd21217 3 KEAFVEHINSLLAD-DPDLKhllpidpdgdDLFEALRDGVLLCKLINKIVPGTID-ERKLNK------KKPKNIFEATEN 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220506 273 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 311
Cdd:cd21217 75 LNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1891-2646 |
1.30e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.74 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1891 EQIAQQKLSAEQEYIRlKADFEHAEQQRGL---LDNELQRLKNEVNAAEKQRRQLEDELAKVRSemdaLLQMKIQAEKVS 1967
Cdd:pfam05483 51 EQVANSGDCHYQEGLK-DSDFENSEGLSRLyskLYKEAEKIKKWKVSIEAELKQKENKLQENRK----IIEAQRKAIQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1968 QSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEvALKA 2047
Cdd:pfam05483 126 QFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2048 kEAENERLKRQAedeayqrKLLEDQaaqhkhdiqEKITQLQSSSVSELDRQKNIVEETLRQkkvveeeihiirinferaS 2127
Cdd:pfam05483 205 -QAENARLEMHF-------KLKEDH---------EKIQHLEEEYKKEINDKEKQVSLLLIQ------------------I 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2128 KEKsdlEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKA 2207
Cdd:pfam05483 250 TEK---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2208 AEANKLKDKAEKELEKqvilaKEAAQKSTAAEQKAQDVlskNKEDLL--SQEKLRDEFENAKKLAQAAETAKEKAEKEAA 2285
Cdd:pfam05483 327 CQLTEEKEAQMEELNK-----AKAAHSFVVTEFEATTC---SLEELLrtEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2286 LLRQKAEEAEKLKKA-AEDEaaKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQV 2364
Cdd:pfam05483 399 FKNNKEVELEELKKIlAEDE--KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2365 EKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQK 2444
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2445 LLAEEAE---KMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQE 2521
Cdd:pfam05483 557 FIQKGDEvkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2522 KAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ---------------AKAEEEATRF 2586
Cdd:pfam05483 637 KVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQY 716
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2587 KKQADE--AKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQE 2646
Cdd:pfam05483 717 DKIIEErdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1211-1749 |
1.37e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1211 AQKTAEQMKVQSELEGLKKDLNSITEKTEEILASPQQsssapmLRSELDVTLKKMDHvyglssvylDKLKTIDIVIRNTK 1290
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYE------LLAELARLEQDIAR---------LEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1291 DAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQ 1370
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1371 LAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIE 1450
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1451 KNKDQIENCQKDAKAYIDSLKDyefQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILE 1530
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLE---AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1531 tqRRLEDDEKASEKLKEDEKKR--------MAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDA 1602
Cdd:COG1196 554 --EDDEVAAAAIEYLKAAKAGRatflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1603 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1682
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 1683 AQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELqkhKMQAEEAERRLKQAEEE 1749
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE---PPDLEELERELERLERE 775
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2239-2819 |
1.45e-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: 64.99 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2239 EQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERL 2318
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2319 RKEAEAEaakraaaeaaaLKQKQEADAEMAKHKkEAEQALKQKSQVEKELGLVKlQLDETDKQKALMDEELQ-------R 2391
Cdd:TIGR00618 259 QQLLKQL-----------RARIEELRAQEAVLE-ETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQskmrsraK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2392 VKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNT-QKLLAEEAEKMKSLAEEAARLSVEAEET 2470
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTlTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2471 ARQRKTAEAELAEQRALAEKMLKEKMQaiQEATKLKAEAEELQKQKNQAQEKAKKLLEdkQEIQQRLDKETQGFQkSLEA 2550
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQ--QELQQRYAELCAAAITCTAQCEKLEKIHL--QESAQSLKEREQQLQ-TKEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2551 ERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVrlqetekqtTETVVQKLETQRLQSTREADDLKKAI 2630
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP---------LTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2631 AELEKEREKLKRDAQELQnksketasaqqeQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHledevnkAKALKD 2710
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQ------------QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-------EDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2711 EQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMkNKQKEMEALEKKRLEQEKLLADENKKL----REKLESLEVTSKQA 2786
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT-ALHALQLTLTQERVREHALSIRVLPKEllasRQLALQKMQSEKEQ 691
|
570 580 590
....*....|....*....|....*....|...
gi 1655220506 2787 ASKTKEIEVQTDKVPEEQLvsmTTVETTKKVFN 2819
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELE---THIEEYDREFN 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2289-2794 |
1.46e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2289 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEA-DAEMAKHKKEAEQALKQKSQVEKE 2367
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEElRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2368 LGLVKLQLDETDkqkalmDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlKLKVRIEEENLrlmQKNKDNTQKLLA 2447
Cdd:COG4913 325 LDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAAL-GLPLPASAEEF---AALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2448 EEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRA----LAEKMLkEKMQAIQEATKLKAE-----AEELQ-KQKN 2517
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnIPARLL-ALRDALAEALGLDEAelpfvGELIEvRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2518 QAQEKA-------------------KKLLE--DKQEIQQRLDkeTQGFQKSLEAERKRQLEISAEAEKLKLRVkelSSAQ 2576
Cdd:COG4913 474 ERWRGAiervlggfaltllvppehyAAALRwvNRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDFKP---HPFR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2577 AKAEEEATRfkkQADEAKVR----LQETEKQTTET---------------------------VVQKLETQRlqstREADD 2625
Cdd:COG4913 549 AWLEAELGR---RFDYVCVDspeeLRRHPRAITRAgqvkgngtrhekddrrrirsryvlgfdNRAKLAALE----AELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2626 LKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKA 2705
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2706 KALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQ 2785
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
....*....
gi 1655220506 2786 AASKTKEIE 2794
Cdd:COG4913 782 LNRAEEELE 790
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
197-316 |
1.50e-09 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 59.24 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 197 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDLVRNVRLPREKGRMRfhKLQNVQIA 276
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655220506 277 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 316
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2498-2728 |
1.64e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2498 AIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQA 2577
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2578 KAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrLQSTREADDLKKAIAELEKEREKLKRDAQELQNKsKETASA 2657
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2658 QQEQMEQQKAMLQQtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQA 2728
Cdd:COG4942 172 ERAELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1626-1855 |
1.87e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1626 SKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE 1705
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1706 DELKRKSE--AEKEAARQKQKALDELQ--KHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKL 1781
Cdd:COG4942 97 AELEAQKEelAELLRALYRLGRQPPLAllLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 1782 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRL--RLRAEEEAQRKSLAQEEAEKQK 1855
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
195-314 |
2.37e-09 |
|
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: 57.98 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 195 ADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdLVRNVRLPREKGrmrfHKLQNVQ 274
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVP----LHEYHLTPSTDD----EKLHNVK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1655220506 275 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 314
Cdd:cd21222 82 LALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1631-2088 |
2.48e-09 |
|
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: 63.88 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1631 LEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEdelKR 1710
Cdd:NF033838 71 LSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEAT---KK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1711 KSEAEKEAARQKQK-----ALDELQKHKMQAEEAERRLKQAEEEKVRQikvveevaqktaatqlqamsfSEKTTKLEESL 1785
Cdd:NF033838 148 VEEAEKKAKDQKEEdrrnyPTNTYKTLELEIAESDVEVKKAELELVKE---------------------EAKEPRDEEKI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1786 KKEQGTVLQLQEEAEKLRKQEEEANKAREqaekeletwrlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkk 1865
Cdd:NF033838 207 KQAKAKVESKKAEATRLEKIKTDREKAEE--------------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG---- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1866 AKAEEAALKQKENAEKELEKQrTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRlknevNAAEKQRRQLEDE 1945
Cdd:NF033838 269 VLGEPATPDKKENDAKSSDSS-VGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR-----NYPTNTYKTLELE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1946 LAKVRSEM-DALLQMkIQAEKVSQSNTEKSKQLLEtealKMKQLAEEAARLrsvaEEAKKQRQLAEDEAARQRAEAEKIl 2024
Cdd:NF033838 343 IAESDVKVkEAELEL-VKEEAKEPRNEEKIKQAKA----KVESKKAEATRL----EKIKTDRKKAEEEAKRKAAEEDKV- 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2025 KEKLAainEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKllEDQAAQHKHDIQEKITQLQ 2088
Cdd:NF033838 413 KEKPA---EQPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQA--EEDYARRSEEEYNRLTQQQ 471
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2446-2828 |
4.11e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.20 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2446 LAEEAEKMKSLaeeaaRLSVEAEetarqRKTAEAELAEQRALAEKMLK--EKMQAIQEATKLKAEaEELQKQKNQAQEK- 2522
Cdd:pfam05483 83 LYKEAEKIKKW-----KVSIEAE-----LKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLE-EEIQENKDLIKENn 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2523 -AKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSsAQAKAEEEATRFKKQADEAKVR-LQET 2600
Cdd:pfam05483 152 aTRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELR-VQAENARLEMHFKLKEDHEKIQhLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2601 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKR--DAQELQNKSKETASAQQE----QMEQQKAMLQQTFL 2674
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQleEKTKLQDENLKELIEKKDhltkELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2675 TEKELllkrERDVEDEKKKLQKHLED------EVNKAKA-------------------LKDEQQRQQKLMDEekkkLQAI 2729
Cdd:pfam05483 311 TQKAL----EEDLQIATKTICQLTEEkeaqmeELNKAKAahsfvvtefeattcsleelLRTEQQRLEKNEDQ----LKII 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2730 MDEAVKKQKEAEAEMKNKQ-KEMEALE-KKRLEQEKLLADENKKLREKLESLEVTSKQAAS--KTKEIEVQtdkvpeEQL 2805
Cdd:pfam05483 383 TMELQKKSSELEEMTKFKNnKEVELEElKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFllQAREKEIH------DLE 456
|
410 420
....*....|....*....|...
gi 1655220506 2806 VSMTTVETTKKVFNGSVEAVKKD 2828
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTE 479
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2490-2763 |
4.23e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2490 KMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGfqksLEAERKRQLEISAEAEKLKLRV 2569
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK----LEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2570 KELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE-TVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQ 2648
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2649 NKSKEtasaqqeqmeqqkamlqqtfLTEKElllKRERDVEDEKKKLQKHLED------EVNKAKALKDEQQR-QQKLMDE 2721
Cdd:PRK03918 328 ERIKE--------------------LEEKE---ERLEELKKKLKELEKRLEEleerheLYEEAKAKKEELERlKKRLTGL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1655220506 2722 EKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2763
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2191-2799 |
4.41e-09 |
|
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: 63.21 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAK-EAAQKSTAAEQKAQ------DVLSKNKEDLLSQEK-LRDE 2262
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANsELTEARTERDQFSQesgnldDQLQKLLADLHKREKeLSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2263 FENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLK---KAAEDEAAKQAKAQKDAerlrkeaeaeaakraaaeaaaLKQ 2339
Cdd:pfam15921 397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEallKAMKSECQGQMERQMAA---------------------IQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2340 KQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNdavKQKAQVENELSKVKMQMDE 2419
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIE---ATNAEITKLRSRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2420 LLKLK--------VRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARlsveaeetarqrkTAEAelaeqralaekM 2491
Cdd:pfam15921 533 LQHLKnegdhlrnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR-------------TAGA-----------M 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2492 LKEKMQAIQEATKLKAEAEELqkqknqaqekakKLLEDKQEIQQRldketqgfqkSLEAeRKRQLEIsaeaEKLKLrvke 2571
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEF------------KILKDKKDAKIR----------ELEA-RVSDLEL----EKVKL---- 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2572 lssaqAKAEEEATRfkkqadeakvrlqetekqttetVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDaqeLQNKS 2651
Cdd:pfam15921 638 -----VNAGSERLR----------------------AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2652 KE---TASAQQEQMEQQKAMLQQTFLTekellLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEkkklqa 2728
Cdd:pfam15921 688 EEmetTTNKLKMQLKSAQSELEQTRNT-----LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEA------ 756
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2729 iMDEAvkkqkeaeaemkNKQKEMEALEKKRLEQE-KLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDK 2799
Cdd:pfam15921 757 -MTNA------------NKEKHFLKEEKNKLSQElSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1629-2137 |
4.47e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1629 QQLEEAQVSRRKLEEEI-HLIRIQlqttikqksTADDELQKLRDQAAEAEKVRKA-----AQEEAERLRKQVNEETQKKK 1702
Cdd:COG4913 235 DDLERAHEALEDAREQIeLLEPIR---------ELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1703 NAEDELKRKSEAEKEAARQKQKALDELQKHKMQA-EEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS----FSEK 1777
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1778 TTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwRLKANealRLRLRAEEEAQRKSLAQE----EAEK 1853
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--SLERR---KSNIPARLLALRDALAEAlgldEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1854 Q--------KTEAERdakkkakaeeaalkqKENA-EKELEKQRT-----------FAEQIAQQKLSAEQEYIRLKADFEH 1913
Cdd:COG4913 461 PfvgelievRPEEER---------------WRGAiERVLGGFALtllvppehyaaALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1914 AEQQRGLLDNELQRLKNEVNAAekqRRQLEDELA------KVRSEMD------------------ALLQMKIQAEKVSQ- 1968
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPF---RAWLEAELGrrfdyvCVDSPEElrrhpraitragqvkgngTRHEKDDRRRIRSRy 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1969 ----SNTEKsKQLLETEAlkmKQLAEEAARLRSVAEEAKKQRQLAED--EAARQRAE-----------AEKI--LKEKLA 2029
Cdd:COG4913 603 vlgfDNRAK-LAALEAEL---AELEEELAEAEERLEALEAELDALQErrEALQRLAEyswdeidvasaEREIaeLEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2030 AINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQ- 2108
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAa 758
|
570 580 590
....*....|....*....|....*....|.
gi 1655220506 2109 --KKVVEEEIHIIRINFERASKEKSDLEVEL 2137
Cdd:COG4913 759 lgDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1356-2107 |
4.60e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1356 RLHSERDAELEhyRQLAGSLLERWQAVFAQIDLRqRELSLLGRHMNSYKQSYEWLIQWL---REARLRQEKIEAAPVwDS 1432
Cdd:PRK04863 282 RVHLEEALELR--RELYTSRRQLAAEQYRLVEMA-RELAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIERYQA-DL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1433 KALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLK----DYE--FQILAYRALQDPIA-SPLKKPK-----MESAS 1500
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqlaDYQqaLDVQQTRAIQYQQAvQALERAKqlcglPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1501 DNI---IQEYVT-----------LRTRYSELSTLTSQYIKfILETQRRLEDD-------EKASEKLKEDEKKRMAEIQAQ 1559
Cdd:PRK04863 438 DNAedwLEEFQAkeqeateellsLEQKLSVAQAAHSQFEQ-AYQLVRKIAGEvsrseawDVARELLRRLREQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1560 lETQKQLAEghaksvAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELtqlknlsEQEIRSKNQQLEEAQVSRR 1639
Cdd:PRK04863 517 -QLRMRLSE------LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL-------EARLESLSESVSEARERRM 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1640 KLEEEIHLIRIQLQTTIKQKS---TADDELQKLRDQAAEA----EKVRKAAQEEAERLRK--QVNEETQKKKNA-EDELK 1709
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARAPawlAAQDALARLREQSGEEfedsQDVTEYMQQLLEREREltVERDELAARKQAlDEEIE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1710 RKSEAE-KEAARQKQKA----------------LDElqkhkmqAEEAERRLKQAeeekvRQIKVVEEVaqKTAATQLQAM 1772
Cdd:PRK04863 663 RLSQPGgSEDPRLNALAerfggvllseiyddvsLED-------APYFSALYGPA-----RHAIVVPDL--SDAAEQLAGL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1773 ---------------SFSEKTTKLEEslkKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrlkanealrLRLRA 1837
Cdd:PRK04863 729 edcpedlyliegdpdSFDDSVFSVEE---LEKAVVVKIADRQWRYSRFPEVPLFGRAAREKRIEQ----------LRAER 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1838 EEEAQRksLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKqrtfaeqiAQQKLSaEQEyiRLKADFEHAEQQ 1917
Cdd:PRK04863 796 EELAER--YATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQ--------LNRRRV-ELE--RALADHESQEQQ 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1918 rglLDNELQRLKNEVNAAEK--------QRRQLEDELAKVRSEMDALLqmkiQAEKVSQSNtEKSKQLLETEALKMKQLA 1989
Cdd:PRK04863 863 ---QRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAE----EAKRFVQQH-GNALAQLEPIVSVLQSDP 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1990 EEAARLRSVAEEAKKQRQlaedeAARQRAEAEKILKEKLAAineatrLKTEAEVALKAKEAE-NERLKRQAEDEAYQRKL 2068
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQR-----DAKQQAFALTEVVQRRAH------FSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTR 1003
|
810 820 830
....*....|....*....|....*....|....*....
gi 1655220506 2069 LEDQAAQHKHDIQEKiTQLQSSSVSELDRQKNIVEETLR 2107
Cdd:PRK04863 1004 AREQLRQAQAQLAQY-NQVLASLKSSYDAKRQMLQELKQ 1041
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2473-2669 |
6.68e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.36 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2473 QRKTAEAELAEQRalaekmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldKETQGFQKSLEAER 2552
Cdd:PRK09510 68 QQQQKSAKRAEEQ-------RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA--KQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2553 KRQLEisAEAEKLKLRVKELSSAQAKAEEEATRF------KKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDL 2626
Cdd:PRK09510 139 AKAAA--AAKAKAEAEAKRAAAAAKKAAAEAKKKaeaeaaKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655220506 2627 KKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAML 2669
Cdd:PRK09510 217 KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2343-2584 |
6.70e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.38 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2343 ADAEMAKHKKEAEQALKQKSQVEKelglvklQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELL- 2421
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2422 KLKVRIeeenlRLMQKNKDNTQKLLA-EEAEKMKSLAEEAARLSVEAEETAR---QRKTAEAELAEQRALAEKMLKEKMQ 2497
Cdd:COG3883 87 ELGERA-----RALYRSGGSVSYLDVlLGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2498 AIQEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQA 2577
Cdd:COG3883 162 LKAE---LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
....*..
gi 1655220506 2578 KAEEEAT 2584
Cdd:COG3883 239 AAAAAAS 245
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1538-1861 |
6.72e-09 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 62.05 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1538 DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKsvakaeleAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQ-- 1615
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAK--------FKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1616 --LKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKqkstaDDELQ---KLRDQAAEAEKVRKAAQEEAERL 1690
Cdd:pfam03528 75 aeMENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVR-----EYEVQfhrRLEQERAQWNQYRESAEREIADL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1691 RKQVNEeTQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvAQKTAATQLQ 1770
Cdd:pfam03528 150 RRRLSE-GQEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLE-AEKSCRTDLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1771 amsfsekttkLEESLKKEQGTVLQlqEEAEKLRKQEEEANKAREQAEKE---------------LETWRLKANEALRL-- 1833
Cdd:pfam03528 228 ----------MYVAVLNTQKSVLQ--EDAEKLRKELHEVCHLLEQERQQhnqlkhtwqkandqfLESQRLLMRDMQRMes 295
|
330 340 350
....*....|....*....|....*....|...
gi 1655220506 1834 -----RLRAEEEAQRKSlaQEEAEKQKTEAERD 1861
Cdd:pfam03528 296 vltseQLRQVEEIKKKD--QEEHKRARTHKEKE 326
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2287-2647 |
7.17e-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: 61.83 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2287 LRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKE--------AEQAL 2358
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELsasseelsEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2359 KQKSQVEKELGLVKLQLD-ETDKQKALMDE-ELQRVKAQVNDAVKQKAQVENElskvkmqmDELLKLKVRIEEENLRLMQ 2436
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2437 KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKmqaiQEATKLKAEAEELQKQK 2516
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE----RKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2517 NQAQ-EKAKKLLEDKQ-------------EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE 2582
Cdd:pfam07888 268 DRTQaELHQARLQAAQltlqladaslalrEGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2583 ATRFKkqaDEAKVRLQETEkqttetvvqkletqrlqstREADDLKKAIAELEKEREKLKRDAQEL 2647
Cdd:pfam07888 348 LGREK---DCNRVQLSESR-------------------RELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1660-2110 |
7.68e-09 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 62.38 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1660 STADDELQkLRDQAAEAEKVRKAAQEEaerlrkqVNEETQKKKNAEDElkRKSEAEKeaARQKQKALDELQKhkMQAEEa 1739
Cdd:PRK10929 20 ATAPDEKQ-ITQELEQAKAAKTPAQAE-------IVEALQSALNWLEE--RKGSLER--AKQYQQVIDNFPK--LSAEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1740 eRRLKQAEEEKVRQIkvveEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKE 1819
Cdd:PRK10929 85 -RQQLNNERDEPRSV----PPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1820 LEtwrlkaneALRLRLRAEEEAQRKSLaQEEAEKQKTEAErdakkkakaeeaalkqkenaekELEkqrtfaeqIAQqkLS 1899
Cdd:PRK10929 160 LQ--------TLGTPNTPLAQAQLTAL-QAESAALKALVD----------------------ELE--------LAQ--LS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1900 A--EQEYIRLKADFEHAEQQRglLDNELQRLKNEVNAaekqRRQLEDELAKVRSEMdallqmkiQAEKVSQSNTEKSKQL 1977
Cdd:PRK10929 199 AnnRQELARLRSELAKKRSQQ--LDAYLQALRNQLNS----QRQREAERALESTEL--------LAEQSGDLPKSIVAQF 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1978 LETEALKMkQLAEEAARLRSVAEeakKQRQLAEDeaARQRAEAEKILKEKL------AAINEATRlkteAEVALKAKEAE 2051
Cdd:PRK10929 265 KINRELSQ-ALNQQAQRMDLIAS---QQRQAASQ--TLQVRQALNTLREQSqwlgvsNALGEALR----AQVARLPEMPK 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2052 NERLKRQAEDEAYQRKLLEDQAAQhkhdiQEKITQLQSSSVSEL-DRQKNIVEETLRQKK 2110
Cdd:PRK10929 335 PQQLDTEMAQLRVQRLRYEDLLNK-----QPQLRQIRQADGQPLtAEQNRILDAQLRTQR 389
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
329-428 |
9.14e-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: 56.23 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYrQSNQ--ENLEQAFSVAERELGVTRLL 406
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCPDWESW-DPNQpvQNAREAMQQADDWLGVPQVI 86
|
90 100
....*....|....*....|..
gi 1655220506 407 DPEDVDVAHPDEKSIITYVSSL 428
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQF 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1709-2142 |
9.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1709 KRKSEAEKEAARQKQKALDELqkhkmqaEEAERRLKQAEEEKVRQIKVVEEVAQKTAatQLQAMSFSEKTTKLEESLKKE 1788
Cdd:COG4717 53 KEADELFKPQGRKPELNLKEL-------KELEEELKEAEEKEEEYAELQEELEELEE--ELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1789 QGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkanealrlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKkkaka 1868
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELR---------ELEEELEELEAELAELQEELEELLEQLSLA----- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1869 eeaalkqkenAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQR--------- 1939
Cdd:COG4717 190 ----------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaall 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1940 --RQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQR 2017
Cdd:COG4717 260 alLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2018 AEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEA--YQRKLLEDQAAQHKHDIQEKITQLQSSSVSEL 2095
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2096 DRQKNIVEETLRQK-KVVEEEIHIIRINFERASKEKSDLEVELKKLKG 2142
Cdd:COG4717 420 ELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1530-1860 |
1.05e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 61.42 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksvakaelEAQELKLKMKEdasqrqglavdaekQKQNI 1609
Cdd:pfam02029 53 SGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDP-----------TIADEKESVAE--------------RKENN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1610 QLEltqlknlseqeirSKNQQLEEAQVSRRKLEEEIHliriqlQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAER 1689
Cdd:pfam02029 108 EEE-------------ENSSWEKEEKRDSRLGRYKEE------ETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1690 LRKQV-NEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAtq 1768
Cdd:pfam02029 169 VPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ----NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1769 lqamsFSEKTTKLEESLKKEQGTVlqlQEEAEKLRKQEEEANKAREQAEKELEtWRLKANEALRLRlRAEEEAQRKSLAQ 1848
Cdd:pfam02029 243 -----FLEAEQKLEELRRRRQEKE---SEEFEKLRQKQQEAELELEELKKKRE-ERRKLLEEEEQR-RKQEEAERKLREE 312
|
330
....*....|..
gi 1655220506 1849 EEAEKQKTEAER 1860
Cdd:pfam02029 313 EEKRRMKEEIER 324
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1322-1751 |
1.05e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1322 QLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQL--AGSLLERWQAVFAQIDLRQRELSLLGRH 1399
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1400 MNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKdyefQILA 1479
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE----EELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1480 YRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFI-----------LETQRRLEDDEKASEKLKED 1548
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1549 EKKRM---AEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlSEQEIR 1625
Cdd:COG4717 311 PALEEleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE--DEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1626 SKNQQLEEaqvsRRKLEEEIHLIRIQLQTTIKQKSTADDELQK--LRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKN 1703
Cdd:COG4717 389 AALEQAEE----YQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1704 AE--DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKV 1751
Cdd:COG4717 465 LEedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1927-2608 |
1.10e-08 |
|
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: 61.57 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1927 RLKNEVNAAEKQRRQLEDELAKVRSEM--------DALLQMKIQAEKVSQSNTE------KSKQL---LETEALKMKQLA 1989
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELknkekelkNLDKNLNKDEEKINNSNNKikileqQIKDLndkLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1990 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEaevaLKAKEAENERLKRQAEDEAYQRKLL 2069
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2070 EDQaaqhKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFErASKEKSDLEVELKKLKGIADETQK 2149
Cdd:TIGR04523 179 EKE----KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ-LKDNIEKKQQEINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2150 skakaeeeaeklkklaaeeerkrreaeeKVKKIAAAEEEAARQRKAAQDEVERLKQKAaeanklkdkaeKELEKQviLAK 2229
Cdd:TIGR04523 254 ----------------------------QLNQLKDEQNKIKKQLSEKQKELEQNNKKI-----------KELEKQ--LNQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2230 EAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENA---------------KKLAQAAETAKEKAEKEAALLRQKAEEA 2294
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnnkiisqlneqiSQLKKELTNSESENSEKQRELEEKQNEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2295 EKLKKAAED--EAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQ-KQEADAEMAKHKKEAEQALKQKSQVEKELGLV 2371
Cdd:TIGR04523 373 EKLKKENQSykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQeKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2372 KLQLDETDKQKALMDEELQRVKAQVNdavKQKAQVENELSKVKMQMDELLKLKvrieEENLRLMQKNKDNTQkllaeeae 2451
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQKQKELKSKEKELKKLN----EEKKELEEKVKDLTK-------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2452 KMKSLAEEAARLSVEAEETARQRKTAEAELAE--QRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLED 2529
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2530 KQEIQQRLDKETQgfqksLEAERKRQLE-ISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETV 2608
Cdd:TIGR04523 598 KKDLIKEIEEKEK-----KISSLEKELEkAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1661-1900 |
1.17e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1661 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAE 1740
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1741 RRLKQAEeekvRQIKVVEEVAQ----KTAATQLQAMS-FSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQ 1815
Cdd:COG3883 93 RALYRSG----GSVSYLDVLLGsesfSDFLDRLSALSkIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1816 AEKELETwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQ 1895
Cdd:COG3883 169 AKAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
....*
gi 1655220506 1896 QKLSA 1900
Cdd:COG3883 248 GAGAA 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2410-2807 |
1.32e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2410 LSKVKMQMDELLKLKVRIEEENLRLMQKNkdntQKLLAEEAEKMKSLAEEAARLsveaEETARQRKTAEAELAEQRALae 2489
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREE-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2490 kmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRV 2569
Cdd:COG4717 118 ---LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2570 KELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIA------------------ 2631
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllslilt 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2632 -----------------ELEKEREKLKRDAQELQNKSKETASAQQEQMEQ----------QKAMLQQTFLTEKELLLKRE 2684
Cdd:COG4717 275 iagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELlaalglppdlSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2685 RDVEDEKKKLQKHLEDEVN---KAKALKDEQQRQQKLMDEEKKKlqaimdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQ 2761
Cdd:COG4717 355 EAEELEEELQLEELEQEIAallAEAGVEDEEELRAALEQAEEYQ------ELKEELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1655220506 2762 EklLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVS 2807
Cdd:COG4717 429 E--LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA 472
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2337-2671 |
1.57e-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: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2337 LKQKQEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLdeTDKQKALmdEELQRVKAQVNDAVKQKAQVENELskvkmQ 2416
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEA---RLEAAEEEVDSLKSQL--ADYQQAL--DVQQTRAIQYQQAVQALEKARALC-----G 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2417 MDELlklkvriEEENLrlmqknKDNTQKLLAEEAEKMKSLAEEAARLSVeAEETARQRktaEAELAEQRALAEKMlkEKM 2496
Cdd:COG3096 431 LPDL-------TPENA------EDYLAAFRAKEQQATEEVLELEQKLSV-ADAARRQF---EKAYELVCKIAGEV--ERS 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2497 QAIQEATKLKAEAEELQKQKNQAQEKAKKL--LEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSS 2574
Cdd:COG3096 492 QAWQTARELLRRYRSQQALAQRLQQLRAQLaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2575 AQAKAEEEATRFKKQADEAKVRLQETEKQ-----TTETVVQKLETQRLQSTREADDLKKAIAE-LEKEREkLKRDAQELQ 2648
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALERLREQSGEALADSQEVTAAMQQlLERERE-ATVERDELA 650
|
330 340
....*....|....*....|...
gi 1655220506 2649 nksketasAQQEQMEQQKAMLQQ 2671
Cdd:COG3096 651 --------ARKQALESQIERLSQ 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1338-1784 |
1.60e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1338 DRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREA 1417
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1418 RLRQEKieaapvwdsKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQIlaYRALQDPiasplkKPKME 1497
Cdd:COG4717 129 PLYQEL---------EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL--EELLEQL------SLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1498 SASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKA 1577
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1578 ELEAQEL------------------KLKMKEDASQRQGLAVDAEKQKQNIQLELTQL---KNLSEQEIRSKNQQLEEAQV 1636
Cdd:COG4717 272 ILTIAGVlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1637 SRRKLEEEIHLIRIQ-LQTTIKQ-----KSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE-----ETQKKKNAE 1705
Cdd:COG4717 352 LLREAEELEEELQLEeLEQEIAAllaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEleellEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1706 DELKRKSEAEKEAARQKQKALDELQ--KHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEE 1783
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAelEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
.
gi 1655220506 1784 S 1784
Cdd:COG4717 512 E 512
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
204-310 |
1.71e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 55.04 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 204 KTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPRERDLvrnvrlPREKGRMrfhkLQNVQIALDFLK 281
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGC------PRSQSQM----IENVDVCLSFLA 72
|
90 100
....*....|....*....|....*....
gi 1655220506 282 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 310
Cdd:cd21286 73 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
333-428 |
1.81e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.16 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 333 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-----------------------EN 388
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 389 LEQAFSVAER-----------ELG-VTRLLDPEDVDVAHPDEKSIITYVSSL 428
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2435-2700 |
2.70e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.88 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2435 MQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEaTKLKAEAEELQK 2514
Cdd:pfam02029 68 TAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETE-IREKEYQENKWS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2515 QKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAK 2594
Cdd:pfam02029 147 TEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2595 VRLQETEKQTTETVVQKLET-QRLQSTREADDlKKAIAELEKEREKLKRDAQELQ---NKSKETASAQQEQMEQQKAMLQ 2670
Cdd:pfam02029 227 QGGLSQSQEREEEAEVFLEAeQKLEELRRRRQ-EKESEEFEKLRQKQQEAELELEelkKKREERRKLLEEEEQRRKQEEA 305
|
250 260 270
....*....|....*....|....*....|....
gi 1655220506 2671 QTFLTEKELLLKRERDVEDEK----KKLQKHLED 2700
Cdd:pfam02029 306 ERKLREEEEKRRMKEEIERRRaeaaEKRQKLPED 339
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1779-2140 |
2.70e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.91 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1779 TKLEESLKkEQGTVLQLQEEAEKLRKQEeeankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEA 1858
Cdd:pfam07888 34 NRLEECLQ-ERAELLQAQEAANRQREKE------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1859 ERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQ 1938
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1939 RRQLEDELAKVRSEMD----ALLQMKIQAEKVSQSNTEKSKQLLETEALK--MKQLAEEAARLRSVAEEAKkqRQLAEDE 2012
Cdd:pfam07888 187 LRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2013 AARQRAEAEkILKEKLAAINEATRLkTEAEVALKAKEA----ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQ 2088
Cdd:pfam07888 265 AQRDRTQAE-LHQARLQAAQLTLQL-ADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2089 SSSVsELDRQKNIveeTLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKL 2140
Cdd:pfam07888 343 KLEV-ELGREKDC---NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2191-2541 |
2.97e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.91 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRKAAQDEVERLKqkaAEANKLKDKAEKELEKQvilakEAAQKSTAAEQKAQDVLSKNKEDllSQEKLRDEFENAKKLA 2270
Cdd:pfam07888 73 RQRRELESRVAELK---EELRQSREKHEELEEKY-----KELSASSEELSEEKDALLAQRAA--HEARIRELEEDIKTLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2271 QAAETAKEKAEKeaalLRQKAEEAEKLKKAAEDE-AAKQAKAQKDAERLRKEAE--AEAAKRAAAEAAALKQKQEADAEM 2347
Cdd:pfam07888 143 QRVLERETELER----MKERAKKAGAQRKEEEAErKQLQAKLQQTEEELRSLSKefQELRNSLAQRDTQVLQLQDTITTL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2348 AKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQ-------RVKAQVNDAVKQKAQVENELSKVKMQMDEL 2420
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQAELHQARLQAAQLTLQLADASLALREG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2421 lKLKVRIEEENLRL-MQKNKDNTQKLLAEEAEKMKSLAEEAArlsveaeetarQRKTAEAELAEQRALAEKMLKEKMQAI 2499
Cdd:pfam07888 299 -RARWAQERETLQQsAEADKDRIEKLSAELQRLEERLQEERM-----------EREKLEVELGREKDCNRVQLSESRREL 366
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1655220506 2500 QEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKET 2541
Cdd:pfam07888 367 QE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2349-2643 |
3.30e-08 |
|
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: 59.05 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2349 KHKKEAEQALKQKSQvEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQK-------AQVENELSKVKmQMDELL 2421
Cdd:pfam15905 64 KSQKNLKESKDQKEL-EKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKtslsasvASLEKQLLELT-RVNELL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2422 KLKVrieeenlrlmqkNKDNTQKllaeeaeKMKSLAEEAARLsveaeetarqRKTAEAELAEQRALAEKMLKeKMQAIQe 2501
Cdd:pfam15905 142 KAKF------------SEDGTQK-------KMSSLSMELMKL----------RNKLEAKMKEVMAKQEGMEG-KLQVTQ- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2502 aTKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAErKRQLEISAEAEKLKLRVKELSSAQAKAEE 2581
Cdd:pfam15905 191 -KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVE-KYKLDIAQLEELLKEKNDEIESLKQSLEE 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2582 EATRFKKQADEAKVRLQETEKQtTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRD 2643
Cdd:pfam15905 269 KEQELSKQIKDLNEKCKLLESE-KEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1222-1747 |
3.51e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.30 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1222 SELEGLKKDLNSITEKTEEIlaspqqSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKTIDIVIRNTKDAEDTVKSYES 1301
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENI------KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1302 RLR--DVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKmTRLHSERDAELEHYRQlAGSLLERW 1379
Cdd:PRK01156 257 EIKtaESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK-KQILSNIDAEINKYHA-IIKKLSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1380 QAVFAQIDLRQRE--------LSLLGRHMN--SYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEI 1449
Cdd:PRK01156 335 QKDYNDYIKKKSRyddlnnqiLELEGYEMDynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1450 EKNKDQIENCQKDAKAYIDSLKDYEFQILAYRA-LQDPIASPLKKPKM-ESASDNIIQEYVTLRTRyselstltsqyikf 1527
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENLDELSRNMEmLNGQSVCPVCGTTLgEEKSNHIINHYNEKKSR-------------- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1528 ILETQRRLEDDEKASEKLKEDEKKRMAEIQAQlETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDaekqkq 1607
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESE-EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKN------ 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1608 niqleltQLKNLSEQEIRSKNQQLEEAQVSRRKLeeEIHLIRIQLQTTIKQKSTADDELQKLR----DQAAEAEKVRKAA 1683
Cdd:PRK01156 554 -------RYKSLKLEDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESRLQEIEigfpDDKSYIDKSIREI 624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 1684 QEEAERLRKQVNeETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAE 1747
Cdd:PRK01156 625 ENEANNLNNKYN-EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1506-1996 |
3.65e-08 |
|
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: 59.84 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1506 EYVTLRTRyseLSTLTSQYikfiletqrrlEDDEKASEKLKED---EKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQ 1582
Cdd:pfam10174 304 ELLALQTK---LETLTNQN-----------SDCKQHIEVLKESltaKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1583 ELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQeIRSKNQQLEEAQVSRRKLEEEihliriqlqttikqKSTA 1662
Cdd:pfam10174 370 DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQ-LRDKDKQLAGLKERVKSLQTD--------------SSNT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1663 DDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKmqAEEAERR 1742
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA--SSLASSG 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1743 LKQAEEEKVRQIkvveEVAQKTaatqlqamsfsEKTTKLEESLKKEQGTVLQLQ---EEAEKLRKQEEEANKAREQAEK- 1818
Cdd:pfam10174 513 LKKDSKLKSLEI----AVEQKK-----------EECSKLENQLKKAHNAEEAVRtnpEINDRIRLLEQEVARYKEESGKa 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1819 ELETWRLKanEALRlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEkELEKQRTfaEQIAQQKL 1898
Cdd:pfam10174 578 QAEVERLL--GILR-EVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQ-LLEEARR--REDNLADN 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1899 SAEQEYIRLKADFEHAEQQrglLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLL 1978
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQE---LDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAISEKDANIALL 728
|
490
....*....|....*...
gi 1655220506 1979 ETEALKMKQLAEEAARLR 1996
Cdd:pfam10174 729 ELSSSKKKKTQEEVMALK 746
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2482-2707 |
3.70e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2482 AEQRALAEKMLKEKMQAIQEATK----LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLE 2557
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2558 ISAEAEKLKLRVKE-LSSAQAKAEEEATRFKKQADEAK--VRLQETEKQTTETVVQKLETQRlqstREADDLKKAIAELE 2634
Cdd:COG4942 95 LRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLdaVRRLQYLKYLAPARREQAEELR----ADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2635 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKEL--LLKRERDVEDEKKKLQKHLEDEVNKAKA 2707
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELaeLQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2192-2673 |
4.32e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2192 QRKAAQDEVERLKQKAAEANKLKDKAEkELEKQvilaKEAAQkstAAEQKAQDVLSKNKEDLLSQEKLRDEFEnakKLAQ 2271
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIE-RYEEQ----REQAR---ETRDEADEVLEEHEERREELETLEAEIE---DLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2272 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADA------ 2345
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAhneeae 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2346 ----EMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELl 2421
Cdd:PRK02224 346 slreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2422 KLKVRIEEENLRLMQKNKDNTQKLLA-----------EEAEKMKSLAE--------EAARLSVEAEETARQRKTAEAE-- 2480
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEagkcpecgqpvEGSPHVETIEEdrerveelEAELEDLEEEVEEVEERLERAEdl 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2481 ---------LAEQRALAEKMLKEKMQAIQE-----------ATKLKAEAEELQKQKNQAQEKAKKLLE-------DKQEI 2533
Cdd:PRK02224 505 veaedrierLEERREDLEELIAERRETIEEkreraeelrerAAELEAEAEEKREAAAEAEEEAEEAREevaelnsKLAEL 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2534 QQRLDketqgfqkSLEAERKRQLEIsAEAEKLKLRVKELSSAQAKAEEE------ATRFKKQADEAKV---RLQE--TEK 2602
Cdd:PRK02224 585 KERIE--------SLERIRTLLAAI-ADAEDEIERLREKREALAELNDErrerlaEKRERKRELEAEFdeaRIEEarEDK 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2603 QTTETVVQKLETQRLQSTREADDLKKAI-------AELEKEREKLKR-------------DAQELQNKSKET-ASAQQEQ 2661
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIgavenelEELEELRERREAlenrvealealydEAEELESMYGDLrAELRQRN 735
|
570
....*....|..
gi 1655220506 2662 MEQQKAMLQQTF 2673
Cdd:PRK02224 736 VETLERMLNETF 747
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1433-1980 |
4.50e-08 |
|
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: 59.65 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1433 KALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIqeYVTLRT 1512
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL--LSNLKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1513 RYSELSTLTSQYIKFIlETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEda 1592
Cdd:TIGR04523 209 KIQKNKSLESQISELK-KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE-- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1593 sqrqglavdAEKQKQNIQLELTQLKNLSEQ--------EIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD 1664
Cdd:TIGR04523 286 ---------LEKQLNQLKSEISDLNNQKEQdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1665 ELQKLRDQAAEA----EKVRKAAQ---EEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1737
Cdd:TIGR04523 357 ENSEKQRELEEKqneiEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1738 EAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAE 1817
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1818 KELETwrlkanealrlrLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaEQIAQQK 1897
Cdd:TIGR04523 510 EKVKD------------LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN---KEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1898 lsaeQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQL 1977
Cdd:TIGR04523 575 ----QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
...
gi 1655220506 1978 LET 1980
Cdd:TIGR04523 651 KET 653
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1725-2318 |
4.61e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1725 ALDELQKHKMQAEEAERRLKQAEEeKVRQIKVVEEVAQKTAATQLQAmsfsektTKLEESlkKEQGTVLQLQEEAEKLRK 1804
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE-QIELLEPIRELAERYAAARERL-------AELEYL--RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1805 QEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQ-EEAEKQKTEAERdakkkakaeeaalkQKENAEKEL 1883
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLER--------------ELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1884 EKQRTFAEQIAQQKLSAEQEYIRLKAdfeHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmkiqa 1963
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER----- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1964 ekvSQSN-TEKSKQLLEteALKmKQLAEEAARLRSVAEEAkkqrQLAEDEAARQRAeAEKIL--------------KEKL 2028
Cdd:COG4913 434 ---RKSNiPARLLALRD--ALA-EALGLDEAELPFVGELI----EVRPEEERWRGA-IERVLggfaltllvppehyAAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2029 AAINeATRLKTEAeVALKAKEAENERLKRQAEDEAYQRKL----------LEDQAAQHKHDIQ-EKITQL---------- 2087
Cdd:COG4913 503 RWVN-RLHLRGRL-VYERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawLEAELGRRFDYVCvDSPEELrrhpraitra 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2088 ----QSSSVSELDRQKNIVEE------TLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEE 2157
Cdd:COG4913 581 gqvkGNGTRHEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2158 AEKLKKLaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERLKqkaaEANKLKDKAEKELEKQVILAKEAAQKSTA 2237
Cdd:COG4913 661 IDVASAE--------------------------REIAELEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2238 AEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEE-AEKLKKAAEDEAAKQAKAQKDAE 2316
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElRENLEERIDALRARLNRAEEELE 790
|
..
gi 1655220506 2317 RL 2318
Cdd:COG4913 791 RA 792
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1881-2317 |
4.75e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1881 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAE--KQRRQLEDELAKVRSEMDALLQ 1958
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1959 mkiqaekvsqsntekskqlletealKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLK 2038
Cdd:COG4717 154 -------------------------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2039 TEAEVALKAKEAENERLKRQAEDEayqRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHI 2118
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2119 IRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQD 2198
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2199 EvERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdLLSQEKLRDEFENAKKLAQAAETAKE 2278
Cdd:COG4717 366 E-ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE-LEELLEALDEEELEEELEELEEELEE 443
|
410 420 430
....*....|....*....|....*....|....*....
gi 1655220506 2279 KAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAER 2317
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1681-1867 |
4.84e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1681 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKaldelqkhkmQAEEAERRLKQAEEEKVRQIKVVEEV 1760
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----------QAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1761 AQKTAATQlqAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEA-NKAREQAEKELETwRLKANEALRLRLRAEE 1839
Cdd:PRK09510 145 AKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAaAKAAAEAKKKAEA-EAKKKAAAEAKKKAAA 221
|
170 180
....*....|....*....|....*...
gi 1655220506 1840 EAQRKSLAQEEAEKQKTEAERDAKKKAK 1867
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2214-2655 |
4.87e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2214 KDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKlaqaaetakekaekEAALLRQKAEE 2293
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--------------ELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2294 AEKLKKAAEDEAAKQAKAQKDAErlRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKS-QVEKELGLVK 2372
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAE--LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2373 LQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQmDELLKLKVRIEEENLRL----MQKNKDNTQKLLAE 2448
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLallgLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2449 EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA--------IQEATKLKAEAEELQKQKNQAQ 2520
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlsPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2521 EKAKKLleDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVrlqET 2600
Cdd:COG4717 358 ELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---EE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 2601 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKERE--KLKRDAQELQNKSKETA 2655
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELA 489
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1572-2149 |
4.91e-08 |
|
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: 59.77 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1572 KSVAKAELEAQELKLKMKED--ASQRQGLAvdaekqKQNIQLELTQLKNLSEQ-EIRSKnqQLEEAqvsrRKLEEEIHLI 1648
Cdd:pfam07111 18 QDVLERRLDTQRPTVTMWEQdvSGDGQGPG------RRGRSLELEGSQALSQQaELISR--QLQEL----RRLEEEVRLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1649 RiqlQTTIKQKstaddelQKLRDQAAEAEKV---RKAAQEEAERLR-----------------------------KQVNE 1696
Cdd:pfam07111 86 R---ETSLQQK-------MRLEAQAMELDALavaEKAGQAEAEGLRaalagaemvrknleegsqreleeiqrlhqEQLSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1697 ETQKKKNAEDELKRKSEA-EKEAARQKQKALDELQKHKMQAEEAE---RRLKQAEEEKVRQIKVVEEVAQ---------- 1762
Cdd:pfam07111 156 LTQAHEEALSSLTSKAEGlEKSLNSLETKRAGEAKQLAEAQKEAEllrKQLSKTQEELEAQVTLVESLRKyvgeqvppev 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1763 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK----QEEEANKARE-----------QAEKELETWRLKA 1827
Cdd:pfam07111 236 HSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHmlalQEEELTRKIQpsdslepefpkKCRSLLNRWREKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1828 NeALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIA-----------QQ 1896
Cdd:pfam07111 316 F-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMElsraqearrrqQQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1897 KLSAEQEYIRLKADFEHAEQQRglLDNELQRLKNEVNAAEKQRRQLEDELAKVRSeMDALLQMKIQAEKVSQSNTEKSKQ 1976
Cdd:pfam07111 395 QTASAEEQLKFVVNAMSSTQIW--LETTMTRVEQAVARIPSLSNRLSYAVRKVHT-IKGLMARKVALAQLRQESCPPPPP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1977 LLETEA---LKMKQLAEEAARLRSvaeEAKKQRQLAEDEA--ARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAE 2051
Cdd:pfam07111 472 APPVDAdlsLELEQLREERNRLDA---ELQLSAHLIQQEVgrAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2052 NERLKRQ--AEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRinfERASKE 2129
Cdd:pfam07111 549 VARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQ---HRATQE 625
|
650 660
....*....|....*....|
gi 1655220506 2130 KSDLEvELKKLKgiaDETQK 2149
Cdd:pfam07111 626 KERNQ-ELRRLQ---DEARK 641
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4225-4261 |
6.02e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.33 E-value: 6.02e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1655220506 4225 IRLLEAQIATGGIIDPQESHRLPVETAYERGLFDEEM 4261
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1314-2114 |
6.05e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.68 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1314 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDA--------------ELEHYRQLAGSLLERW 1379
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELkmekvfqgtdeqlnDLYHNHQRTVREKERE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1380 QAVFaqidlrQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKI-EAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIEN 1458
Cdd:TIGR00606 321 LVDC------QRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHqEHIRARDSLIQSLATRLELDGFERGPFSERQIKN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1459 CQKDAKAYIDSLKDYEFQILAyrALQDPIASPLK-----KPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQR 1533
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCA--DLQSKERLKQEqadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1534 RLEDDEKASEKLKEDEK-KRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQL- 1611
Cdd:TIGR00606 473 ILELDQELRKAERELSKaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIr 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1612 --------ELTQL-------KNLSE------QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD------ 1664
Cdd:TIGR00606 553 kiksrhsdELTSLlgyfpnkKQLEDwlhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvc 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1665 -------ELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1737
Cdd:TIGR00606 633 gsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1738 EAERRLKQAEEE-----------------KVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEA- 1799
Cdd:TIGR00606 713 STESELKKKEKRrdemlglapgrqsiidlKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVt 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1800 --EKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKE 1877
Cdd:TIGR00606 793 imERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1878 NAE--KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDA 1955
Cdd:TIGR00606 873 KLQigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1956 LLQMKIQAEKVSQSNTEKSKQLLETEALKMK-QLAEEAARLRSVAEEAKKQRQLAEDEAARqraeaEKILKEKLaainea 2034
Cdd:TIGR00606 953 IHGYMKDIENKIQDGKDDYLKQKETELNTVNaQLEECEKHQEKINEDMRLMRQDIDTQKIQ-----ERWLQDNL------ 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2035 TRLKTEAEValkaKEAENERlkRQAEDEAYQRKLLEDQAAQHKhdIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEE 2114
Cdd:TIGR00606 1022 TLRKRENEL----KEVEEEL--KQHLKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1769-2015 |
6.16e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1769 LQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRlRLRAEEEAQRKSLAQ 1848
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA----ALARRIR-ALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1849 EEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELE---KQRTFAEqiAQQKLSAEQEYIRlkADFEHAEQQRGLLDnEL 1925
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLD--AVRRLQYLKYLAP--ARREQAEELRADLA-EL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1926 QRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQ 2005
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1655220506 2006 RQLAEDEAAR 2015
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1594-1792 |
6.64e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.28 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1594 QRQGLAVDAEKQKQNIQleltqlknlsEQEIRSKNQQLEEAQVSRRKLEEEihliRIQLQTTIKQKSTADDELQKLRDQA 1673
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE----------QQQAEELQQKQAAEQERLKQLEKE----RLAAQEQKKQAEEAAKQAALKQKQA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1674 AEAEKV-----RKAAQEEAERLR---KQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ 1745
Cdd:PRK09510 135 EEAAAKaaaaaKAKAEAEAKRAAaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220506 1746 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEEslKKEQGTV 1792
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA--AKAAAEV 259
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1667-1860 |
6.92e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 58.64 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1667 QKLRDQAAEAEKVRKAAQEEAERLRKQvneetqKKKNAEDE-LKRKSEAEKEaARQKQKaldELQKhkmqaeeAERRLKQ 1745
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKE------ALLEAKEEiHKLRNEFEKE-LRERRN---ELQK-------LEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1746 AEEEKVRQikvveevaqktaatqlqamsfSEKTTKLEESLKKEQGTVLQLQEEAEklrKQEEEANKAREQAEKELETW-R 1824
Cdd:PRK12704 94 KEENLDRK---------------------LELLEKREEELEKKEKELEQKQQELE---KKEEELEELIEEQLQELERIsG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1655220506 1825 LKANEA---LRLRLRAEEEAQRKSLAQEEAEKQKTEAER 1860
Cdd:PRK12704 150 LTAEEAkeiLLEKVEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2387-2779 |
7.04e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 59.30 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2387 EELQRVKAQVNDAvkQKAQVEnELSKVKMQMDELLKLKVRIEEenlrlMQKNKDNTQKLLAEEAEKMKSLAEEaaRLSVE 2466
Cdd:PRK10929 30 QELEQAKAAKTPA--QAEIVE-ALQSALNWLEERKGSLERAKQ-----YQQVIDNFPKLSAELRQQLNNERDE--PRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2467 AEETArqrktaeAELaEQRAL--AEKMLKEKMQAIQEATKLKAEAEELQkQKNQAQEKAKKLLedkQEIQQRLdkETQGF 2544
Cdd:PRK10929 100 PNMST-------DAL-EQEILqvSSQLLEKSRQAQQEQDRAREISDSLS-QLPQQQTEARRQL---NEIERRL--QTLGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2545 QKSLEAERKRQLeISAEAEKLKLRVKELSSAQAKA--EEEATR-----FKKQADEAKVRLQETEKQTTETVVQKLEtQRL 2617
Cdd:PRK10929 166 PNTPLAQAQLTA-LQAESAALKALVDELELAQLSAnnRQELARlrselAKKRSQQLDAYLQALRNQLNSQRQREAE-RAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2618 QSTR----EADDLKKAI-AELEKERE---KLKRDAQELqnkskETASAQQEQMEQQKAMLQQTFLTekellLKRERDVED 2689
Cdd:PRK10929 244 ESTEllaeQSGDLPKSIvAQFKINRElsqALNQQAQRM-----DLIASQQRQAASQTLQVRQALNT-----LREQSQWLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2690 EKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQaiMDEAVKKQKEaeaEMKNKQKEMEALEKkrlEQEKLLADEN 2769
Cdd:PRK10929 314 VSNALGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLR--YEDLLNKQPQ---LRQIRQADGQPLTA---EQNRILDAQL 385
|
410
....*....|
gi 1655220506 2770 KKLREKLESL 2779
Cdd:PRK10929 386 RTQRELLNSL 395
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1630-1860 |
7.23e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 58.81 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1630 QLEEAQVSRRKLEEEIHLIRiqlQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQE-------EAERLRKQ-VNEETQKK 1701
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMR---RLEVERKRREQEEQRRLQQEQLERAEKMREELEleqqrrfEEIRLRKQrLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1702 KNAEDELKRKSEAEKEAARQKQ----KALDELQKHKMQaEEAERrlkqAEEEKVRQikvveevaqktaatqlqamsfsek 1777
Cdd:pfam15709 404 EEEERKQRLQLQAAQERARQQQeefrRKLQELQRKKQQ-EEAER----AEAEKQRQ------------------------ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1778 tTKLEESLKKEQGTVLQLQEEA--EKLRKQEEEANKAREQAEKeletwrlkanealrlRLRAEEEAQRksLAQEEAEKQK 1855
Cdd:pfam15709 455 -KELEMQLAEEQKRLMEMAEEErlEYQRQKQEAEEKARLEAEE---------------RRQKEEEAAR--LALEEAMKQA 516
|
....*
gi 1655220506 1856 TEAER 1860
Cdd:pfam15709 517 QEQAR 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2386-2605 |
7.89e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2386 DEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSV 2465
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2466 EAEETARQRKTAEA--------ELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRL 2537
Cdd:COG3883 94 ALYRSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2538 DK---ETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTT 2605
Cdd:COG3883 174 EAqqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1671-2025 |
7.90e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1671 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQ--KHKMQAEEaERRLKQAEE 1748
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEafLDRTAKRE-ERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1749 EKVRQIKVVEEVAQKTAATQLQAMsfSEKTTKLEESLKKEQ-GTVLQLQEEAEKLRKQEEEANKAREQAEKeletwrlka 1827
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKE--NNEEEENSSWEKEEKrDSRLGRYKEEETEIREKEYQENKWSTEVR--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1828 nealrlrlRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqEYIRL 1907
Cdd:pfam02029 151 --------QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNG-----EEEVT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1908 KADFEHAEQQRGLLDNELQRLKNEV-----NAAEKQRRQLEDelaKVRSEMDALLQMKIQA----EKVSQSNTEKSKqLL 1978
Cdd:pfam02029 218 KLKVTTKRRQGGLSQSQEREEEAEVfleaeQKLEELRRRRQE---KESEEFEKLRQKQQEAelelEELKKKREERRK-LL 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1655220506 1979 ETEALKMKQlaEEAARLRSVAEEAKKQRQlaedEAARQRAEA-EKILK 2025
Cdd:pfam02029 294 EEEEQRRKQ--EEAERKLREEEEKRRMKE----EIERRRAEAaEKRQK 335
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
202-313 |
8.62e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 53.27 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 202 QKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDLVRNVRLPrekgrmrFHKLQNVQIALDFLK 281
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMP-------FKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1655220506 282 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 313
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1653-2024 |
8.75e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1653 QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQvneetqkkKNAEDELKRKSEAEKEAArQKQKALDELQKH 1732
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER--------REALQRLAEYSWDEIDVA-SAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1733 KMQAEEAERRLKQAEEekvrqikvveevaqktaatQLQAmsfsekttkLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA 1812
Cdd:COG4913 677 LERLDASSDDLAALEE-------------------QLEE---------LEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1813 REQAEKELETWRLKANEALRLRLraeeEAQRKSLAQEEAEKQKTEAERDakkkakAEEAALKQKENAEKELEKQRT---- 1888
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALL----EERFAAALGDAVERELRENLEE------RIDALRARLNRAEEELERAMRafnr 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1889 ---FAEQIAQQKLSAEQEYIRL------------KADFEHA--EQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1951
Cdd:COG4913 799 ewpAETADLDADLESLPEYLALldrleedglpeyEERFKELlnENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPF 878
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 1952 EMDALLQMKIQAEKVSQSNTEKSkqlletealKMKQLAEEAARLRSVAEEAKKQR------QLAEDEAARQRAEAEKIL 2024
Cdd:COG4913 879 GPGRYLRLEARPRPDPEVREFRQ---------ELRAVTSGASLFDEELSEARFAAlkrlieRLRSEEEESDRRWRARVL 948
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
324-428 |
9.26e-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: 53.17 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 324 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGV 402
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*...
gi 1655220506 403 TRLLDPEDVdvAHPD--EKSIITYVSSL 428
Cdd:cd21313 80 PQVITPEEI--IHPDvdEHSVMTYLSQF 105
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1875-2075 |
9.74e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1875 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAK------ 1948
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1949 ----VRSEMDALLQMKIQAEKVSQSntekskQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIL 2024
Cdd:COG3883 97 rsggSVSYLDVLLGSESFSDFLDRL------SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2025 KEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQ 2075
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1700-2412 |
1.01e-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: 58.49 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1700 KKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQaeeekvrQIKVVEevaQKTAATQLQAMSFSEKTT 1779
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNN-------KIKILE---QQIKDLNDKLKKNKDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1780 KLEESLKKeqgTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlraEEEAQRKSLAQEEAEKQKTEAE 1859
Cdd:TIGR04523 100 KLNSDLSK---INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK----EKELEKLNNKYNDLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1860 RDAKKKAKAEEaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN-------ELQRLKNEV 1932
Cdd:TIGR04523 173 NELNLLEKEKL----NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDniekkqqEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1933 NAAEKQRRQLEDELAKVRsemDALLQMKIQAEKVSQSNTEKSKQL--LETEALKMKQLAEEAArLRSVAEEAKKQRqlae 2010
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKIKELEKQLnqLKSEISDLNNQKEQDW-NKELKSELKNQE---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2011 deaaRQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKhdiqEKITQLQSS 2090
Cdd:TIGR04523 321 ----KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK----QEIKNLESQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2091 SvSELDRQKNIVEETLRQKkvvEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEER 2170
Cdd:TIGR04523 393 I-NDLESKIQNQEKLNQQK---DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2171 KRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANK----LKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVL 2246
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEkvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2247 SKNKEdlLSQEKLRDEfenakklaqaaetakekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEA 2326
Cdd:TIGR04523 549 KDDFE--LKKENLEKE------------------------IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2327 AKRAAAEAAALKQKQEADAEMAKHKKEAEQALK---QKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQK 2403
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNiksKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELM 682
|
....*....
gi 1655220506 2404 AQVENELSK 2412
Cdd:TIGR04523 683 KDWLKELSL 691
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1504-1950 |
1.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1504 IQEYVTLRTRYSELSTLTSQYIKfILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAksvAKAELEAQE 1583
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---LEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1584 LKL-KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTA 1662
Cdd:COG4717 146 ERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1663 DDELQKLRDQAAEAEKVRKAAQEEAE-RLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAER 1741
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1742 RLKQAEEEkvrqikvvEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQgtVLQLQEEAEKLRKQEEEANKAREQAEKE-- 1819
Cdd:COG4717 306 ELQALPAL--------EELEEEELEELLAALGLPPDLSPEELLELLDR--IEELQELLREAEELEEELQLEELEQEIAal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1820 LETWRLKANEALRLRLRAEEEAQrkslaQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLS 1899
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQ-----ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 1900 AEQEYIRLKADFEHAEQqrgllDNELQRLKNEVNAAEKQRRQLEDELAKVR 1950
Cdd:COG4717 451 LREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALK 496
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2506-2757 |
1.14e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2506 KAEAEELQKQKNQAqEKAKKLLEDKQeiqQRLDKEtqgfqkslEAERKRQLEISAEAeklklRVKELSSAQAKAEEEATR 2585
Cdd:PRK05035 435 KAEIRAIEQEKKKA-EEAKARFEARQ---ARLERE--------KAAREARHKKAAEA-----RAAKDKDAVAAALARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2586 FKKQADEAKVRLQETEKQTTETV-------VQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETA--- 2655
Cdd:PRK05035 498 KKAAATQPIVIKAGARPDNSAVIaarearkAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEvdp 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2656 --SAQQEQMEQQKAMLQQTFLTEKElllKRERDVEDEKKKLQkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2733
Cdd:PRK05035 578 kkAAVAAAIARAKAKKAAQQAASAE---PEEQVAEVDPKKAA--VAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260
....*....|....*....|....*
gi 1655220506 2734 VK-KQKEAEAEMKNKQKEMEALEKK 2757
Cdd:PRK05035 653 ARaKARKAAQQQANAEPEEAEDPKK 677
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2338-2781 |
1.20e-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: 58.21 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2338 KQKQEADAEMAK-HKKEAEQALKQKSQVEkELGLVKLQLDETDKQkalmdeeLQRVKAQVNDAVKQKAQVENELSKVKMQ 2416
Cdd:pfam05557 48 DRNQELQKRIRLlEKREAEAEEALREQAE-LNRLKKKYLEALNKK-------LNEKESQLADAREVISCLKNELSELRRQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2417 -MDELLKLKvRIEEENLRLMQKNKDNTQKllAEEAEKMKSLAEEAARLSVEAEEtarQRKTAEAELA--EQRALAEKMLK 2493
Cdd:pfam05557 120 iQRAELELQ-STNSELEELQERLDLLKAK--ASEAEQLRQNLEKQQSSLAEAEQ---RIKELEFEIQsqEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2494 EKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEKLKLRVK--E 2571
Cdd:pfam05557 194 SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE----EKYREEAATLELEKEKLEQELQSWVKlaQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2572 LSSAQAKAEEEATRFKKQADEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnKS 2651
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQREIVLKE-ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-RR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2652 KETASAQQEQMeqqKAMLQQ--TFLTEKE---LLLKRERDVEDEKKKLQKHLEDEvnkakalkdEQQRQQKLMDEEKKKL 2726
Cdd:pfam05557 348 VLLLTKERDGY---RAILESydKELTMSNyspQLLERIEEAEDMTQKMQAHNEEM---------EAQLSVAEEELGGYKQ 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2727 QAIMDEA---VKKQKEAEAEMKNKQKEMEALekkRLEQEKLLAdENKKLREKLESLEV 2781
Cdd:pfam05557 416 QAQTLERelqALRQQESLADPSYSKEEVDSL---RRKLETLEL-ERQRLREQKNELEM 469
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2618-2766 |
1.62e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.48 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2618 QSTREADDLKK-AIAELEKEREKLKRDAqELQNKSKETASAQQEQMEQQKamlqqtflteKELLLKRERDVEDEKKKLQK 2696
Cdd:PRK12704 46 EAKKEAEAIKKeALLEAKEEIHKLRNEF-EKELRERRNELQKLEKRLLQK----------EENLDRKLELLEKREEELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2697 HLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIM----DEA-------VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2765
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQELERISgltaEEAkeillekVEEEARHEAAVLIKEIEEEAKEEADKKAKEIL 194
|
.
gi 1655220506 2766 A 2766
Cdd:PRK12704 195 A 195
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2191-2805 |
1.73e-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: 58.13 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEqkaqdvLSKNKEDLLsqeklrDEFENAKKLA 2270
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSRE------IVKSYENEL------DPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2271 QAAETAKEKAEKEAALLRQKAEEAEKLKKaaEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEaaalKQKQEADAEMAKH 2350
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNS--ELELKMEKVFQGTDEQLNDLYHNHQRTVREKE----RELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2351 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVN-DAVKQKAQVENELSKVKMQMDELLKLKVRIEE 2429
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2430 ENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIqeatklKAEA 2509
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR------KAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2510 EELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgfqkSLEAERKRQLEISAEAEKLKlRVKELSSAQAKAEEEATRFKKQ 2589
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDR-------KLRKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2590 ADEAKVRLQE--TEKQTTETVVQKLETQRLQSTREADDLKKAIAELE-------KEREKLKRDAQELQNKSKETASAQQE 2660
Cdd:TIGR00606 558 HSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEqnknhinNELESKEEQLSSYEDKLFDVCGSQDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2661 QMEQQKAMLQQTFLTEKELLLKRERDVEDEkkkLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEA 2740
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAMLAGATAVYSQ---FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2741 EAEMKNKQKEME---ALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKV-PEEQL 2805
Cdd:TIGR00606 715 ESELKKKEKRRDemlGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImPEEES 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1495-1805 |
2.17e-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: 57.77 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1495 KMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLE----DDEKASEKLKEDEKKrMAEIQAQLETQKQLAEGH 1570
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqEEEKLKERLEELEED-LSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1571 AKSVAKAELEAQELKLKMKE----------DASQRQGLAVDAEKQKQNIQL--------ELTQLKNLSEQEIRSKNQQLE 1632
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDlearlshsriPEIQAELSKLEEEVSRIEARLreieqklnRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1633 EAQVSRRKLEEEIHLIRIQ---LQTTIKQKSTADDELQK-----------LRDQAAEAEKVRKAAQEEAERLRKQVNEET 1698
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKkeeLEEELEELEAALRDLESrlgdlkkerdeLEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1699 QKKKNAEDELKRKSEAEKEAARQKQKALDeLQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamSFSEKT 1778
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD-------ELKEKR 995
|
330 340
....*....|....*....|....*..
gi 1655220506 1779 TKLEEslkkEQGTVLQLQEEAEKLRKQ 1805
Cdd:TIGR02169 996 AKLEE----ERKAILERIEEYEKKKRE 1018
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
329-426 |
2.21e-07 |
|
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: 52.48 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 329 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLD 407
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1655220506 408 PEDVDVAHPDEKSIITYVS 426
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1909-2765 |
2.41e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1909 ADF-EHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkIQAEKVSQSNTEKSKQLLetealkmkQ 1987
Cdd:PRK04863 272 ADYmRHANERRVHLEEALE-LRRELYTSRRQLAAEQYRLVEMARELAEL----NEAESDLEQDYQAASDHL--------N 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1988 LAEEAARLRSvaeeaKKQRQLAEDEAARQRAEaekilkEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDeaYQRK 2067
Cdd:PRK04863 339 LVQTALRQQE-----KIERYQADLEELEERLE------EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD--YQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2068 LLEDQ--AAQHKHDIQ--EKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGI 2143
Cdd:PRK04863 406 LDVQQtrAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2144 ADETQKSKAKAEEEAEKLKKLAAEEERKRREaeekvkkiaaaeeeaarQRKAAQDEVERLKQKAAEANKLKDKAEKELEK 2223
Cdd:PRK04863 486 AGEVSRSEAWDVARELLRRLREQRHLAEQLQ-----------------QLRMRLSELEQRLRQQQRAERLLAEFCKRLGK 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2224 QVILAKEAAQKSTAAEQKAQDvLSKNKEDLLSQ-EKLRDEFENAKKLAQAaetakekaekeaalLRQKAEEAEKLKKAAE 2302
Cdd:PRK04863 549 NLDDEDELEQLQEELEARLES-LSESVSEARERrMALRQQLEQLQARIQR--------------LAARAPAWLAAQDALA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2303 DEAAKQAKAQKDAERLRkeaeaeaakraaaeaaalkqkqEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLDETDKQK 2382
Cdd:PRK04863 614 RLREQSGEEFEDSQDVT----------------------EYMQQLLERERELTV---ERDELAARKQALDEEIERLSQPG 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2383 ALMDEELQRVKAQVN--------------DAV--------KQKAQVENELSKVKMQM----------------------- 2417
Cdd:PRK04863 669 GSEDPRLNALAERFGgvllseiyddvsleDAPyfsalygpARHAIVVPDLSDAAEQLagledcpedlyliegdpdsfdds 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2418 ----DELLK-LKVRIEEENLR---------LMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETARQRKTAEAELAE 2483
Cdd:PRK04863 749 vfsvEELEKaVVVKIADRQWRysrfpevplFGRAAREKRIEQLRAERE---ELAERYATLSFDVQKLQRLHQAFSRFIGS 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2484 QRALA-----EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQR---LDKETqgFQKSLEAERKrQ 2555
Cdd:PRK04863 826 HLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRlnlLADET--LADRVEEIRE-Q 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2556 LEISAEAEK--------LKLRVKELSSAQAKAEEEATrFKKQADEAKVRLQETEKQT---TEtVVQKLEtqRLQSTREAD 2624
Cdd:PRK04863 903 LDEAEEAKRfvqqhgnaLAQLEPIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAfalTE-VVQRRA--HFSYEDAAE 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2625 DLKKAIAELEKEREKLKRdAQELQNKSKETASAQQEQMEQQKAMLQQtfltekellLKRERDV-EDEKKKLQKHLE---- 2699
Cdd:PRK04863 979 MLAKNSDLNEKLRQRLEQ-AEQERTRAREQLRQAQAQLAQYNQVLAS---------LKSSYDAkRQMLQELKQELQdlgv 1048
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2700 --DEVNKAKALKDEQQRQQKLMDEEKKKlqaimDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2765
Cdd:PRK04863 1049 paDSGAEERARARRDELHARLSANRSRR-----NQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2344-2569 |
2.47e-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: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2344 DAEMAKHKKEAEQALKQKSQVEKELGLVKL--QLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELL 2421
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2422 klkvrieeenlrlmqkNKDNTQKLLAEEAEKMKSLAEEAARLSveaeETARQRKTAEAELAEQRALAEKMLKEKMQAIQ- 2500
Cdd:COG3206 261 ----------------QSPVIQQLRAQLAELEAELAELSARYT----PNHPDVIALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2501 EATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIqQRLDKETQGFQKSLEA--ERKRQLEISAEAEKLKLRV 2569
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAEL-RRLEREVEVARELYESllQRLEEARLAEALTVGNVRV 390
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2197-2695 |
2.67e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2197 QDEVERLKQKAAEANKLK-DKAEKELEKQvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEK--LRDEFENAKKLAQAA 2273
Cdd:pfam12128 374 TAKYNRRRSKIKEQNNRDiAGIKDKLAKI----REARDRQLAVAEDDLQALESELREQLEAGKleFNEEEYRLKSRLGEL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2274 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAK--AQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHK 2351
Cdd:pfam12128 450 KLRLNQATATPELLLQLENFDERIERAREEQEAANAEveRLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2352 KEAEQAL-----KQKSQVEKELGLV--KLQLDETDKQKALMDE-------------ELQRVkaQVNDAVKQKAQVENELS 2411
Cdd:pfam12128 530 FPQAGTLlhflrKEAPDWEQSIGKVisPELLHRTDLDPEVWDGsvggelnlygvklDLKRI--DVPEWAASEEELRERLD 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2412 KVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEetARQRKTAEAELAEQRALAEKM 2491
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQ-LVQANGELEKASREETFARTALKNARLDLRRLFDEKQ--SEKDKKNKALAERKDSANERL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2492 LKEKMQAIQEATKLKAEAEELQKQKNQA----QEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKrQLEISAEAEKLKL 2567
Cdd:pfam12128 685 NSLEAQLKQLDKKHQAWLEEQKEQKREArtekQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK-ALETWYKRDLASL 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2568 RVKELSSAQAKAE--------EEATRFKKQADEAKVRLQET-------EKQTTETVVQKLETQRLQSTREADDLKKAIAE 2632
Cdd:pfam12128 764 GVDPDVIAKLKREirtlerkiERIAVRRQEVLRYFDWYQETwlqrrprLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2633 LEKEREKLkRDAQELQNKSKETASAQQEQM---------EQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ 2695
Cdd:pfam12128 844 LEMERKAS-EKQQVRLSENLRGLRCEMSKLatlkedansEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1538-1747 |
2.71e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1538 DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGH-AKSVAKAELEAQELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQL 1616
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQErLKQLEKERLAAQEQK-KQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1617 KNLSEQeirsknQQLEEAQvsrRKLEEEihliriqlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE 1696
Cdd:PRK09510 148 KAEAEA------KRAAAAA---KKAAAE-------------AKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 1697 ETQKKKNAEDELKRKSEAEK--EAARQKQKALDELQKHKMQAEEAERRLKQAE 1747
Cdd:PRK09510 206 EAKKKAAAEAKKKAAAEAKAaaAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2443-2667 |
2.86e-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: 56.01 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2443 QKLLAEEAEKMKSLAEEAAR----LSVEAEETARQRKTAEAelAEQRALAEkmLKEKMQAIQEATKLKAEAEELQKQKNQ 2518
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKkeqeRQKKLEQQAEEAEKQRA--AEQARQKE--LEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2519 AQEKAKKLLED--KQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEAtrfKKQADEAKVR 2596
Cdd:TIGR02794 121 AEEAKAKQAAEakAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA---KAKAEEAKAK 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2597 LQETEKQTTETVVQKletqrlqstreADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2667
Cdd:TIGR02794 198 AEAAKAKAAAEAAAK-----------AEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAA 257
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2388-2794 |
3.03e-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: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2388 ELQRVKAQVndavkqkAQVENElskvKMQMDellklkvrIEEENLRLMQKNKDNTQKL-LAEEAEKMKSLAEEAARLSvE 2466
Cdd:pfam05557 3 ELIESKARL-------SQLQNE----KKQME--------LEHKRARIELEKKASALKRqLDRESDRNQELQKRIRLLE-K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2467 AEETARQRKTAEAELAEQRalaEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQK 2546
Cdd:pfam05557 63 REAEAEEALREQAELNRLK---KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2547 SLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEatrfkkqadEAKVRLQETEKQTTETVVQKLETqrlqstreaddl 2626
Cdd:pfam05557 140 RLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKEL---------EFEIQSQEQDSEIVKNSKSELAR------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2627 kkaIAELEKEREKLKRDAQELqNKSKETASAQQEQMEQQKAMLQQTFLTEKELLlkrerDVEDEKKKLQKHLEDEVNKAK 2706
Cdd:pfam05557 199 ---IPELEKELERLREHNKHL-NENIENKLLLKEEVEDLKRKLEREEKYREEAA-----TLELEKEKLEQELQSWVKLAQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2707 ALKDEQQRQQKLMDEEKKKLQaimDEAVKKQK--EAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSK 2784
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQ---REIVLKEEnsSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
410
....*....|
gi 1655220506 2785 QAASKTKEIE 2794
Cdd:pfam05557 347 RVLLLTKERD 356
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1216-1941 |
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 1655220506 1216 EQMKVQSELEGLKKDLNSItEKTEEILASPQQSSSAPM--LRSELDVTLKKMDHVYG-LSSVYLDKLKTIDIVirntKDA 1292
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASL-ERSIAEKERELEDAEERLakLEAEIDKLLAEIEELEReIEEERKRRDKLTEEY----AEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1293 EDTVKSYESRLRDVSKVPAEEK-EVEAHRSQLKAMRAEAEADQATFDRLQDELK-----------AATSVSDKMTRLHSE 1360
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRdELKDYREKLEKLKREINELKRELDRLQEELQrlseeladlnaAIAGIEAKINELEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1361 RD---AELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKE 1437
Cdd:TIGR02169 443 KEdkaLEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1438 QLTQEKKLLEEIEKNKDQIENC------------QKDAKAYIDSLKDYE---FQILAYRALQDPiASPLKKPKMESASDN 1502
Cdd:TIGR02169 523 VHGTVAQLGSVGERYATAIEVAagnrlnnvvvedDAVAKEAIELLKRRKagrATFLPLNKMRDE-RRDLSILSEDGVIGF 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1503 IIqEYVTLRTRYSELstltsqyIKFILETQRRLEDDEKASEKLkedEKKRMAEIQAQL------ETQKQLAEGHAKSVAK 1576
Cdd:TIGR02169 602 AV-DLVEFDPKYEPA-------FKYVFGDTLVVEDIEAARRLM---GKYRMVTLEGELfeksgaMTGGSRAPRGGILFSR 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1577 AEL-EAQELKLKMKEDASQRQGLAVDAEKQKQNIQlELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTT 1655
Cdd:TIGR02169 671 SEPaELQRLRERLEGLKRELSSLQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1656 IKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAA-RQKQKALDELQKHKM 1734
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlREIEQKLNRLTLEKE 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1735 QAEEAerrlKQAEEEKVRQIKV-VEEVAQKTAATQLqamsfseKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAR 1813
Cdd:TIGR02169 830 YLEKE----IQELQEQRIDLKEqIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1814 EQAEKELETWRLKANEAlrlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaeqI 1893
Cdd:TIGR02169 899 RELERKIEELEAQIEKK---RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA-----L 970
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1655220506 1894 AQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ 1941
Cdd:TIGR02169 971 EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2525-2796 |
3.33e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2525 KLLEDKQEIQQRLDKETQGFQKSLEAERKRQ---LEISAEA---EKLKLRVKELSSA---------QAKAEEEATRFKKQ 2589
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLRKNLTVEPVKGsnvIEISYTSpdpELAAAVANALAEAyleqnlelrREEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2590 ADEAKVRLQETEKQttetvVQKLETQR--LQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2667
Cdd:COG3206 184 LPELRKELEEAEAA-----LEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2668 MLQQTFLTEkelLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAimdeavkkqkEAEAEMKNK 2747
Cdd:COG3206 259 LLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA----------SLEAELEAL 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2748 QKEMEALEKKRLEQEKLLADENKKLRE------KLESLEVTSKQAASKTKEIEVQ 2796
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAElrrlerEVEVARELYESLLQRLEEARLA 380
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1783-2228 |
3.36e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1783 ESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANealRLRLRAEEEAQRKSLAQEEAEKQKTEAERDA 1862
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1863 KKKAKAeeaalkQKENAEKEL-EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ 1941
Cdd:COG4717 158 LRELEE------ELEELEAELaELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1942 LEDE--------------------------------LAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLA 1989
Cdd:COG4717 232 LENEleaaaleerlkearlllliaaallallglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1990 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEA--YQRK 2067
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2068 LLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQK-KVVEEEIHIIRINFERASKEKSDLEVELKKLKGiade 2146
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE---- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2147 tqkskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaarqrkaaQDEVERLKQKAAEA-NKLKDKAEKELEKQV 2225
Cdd:COG4717 468 --------------------------------------------------DGELAELLQELEELkAELRELAEEWAALKL 497
|
...
gi 1655220506 2226 ILA 2228
Cdd:COG4717 498 ALE 500
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1582-2139 |
3.51e-07 |
|
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: 56.58 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1582 QELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQ-EIRSKNQQLEEAQVsrrkleeeihliriqlqttiKQks 1660
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEAQA--------------------KQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1661 taDDELQKLRDQAAE---AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1737
Cdd:pfam05701 99 --DSELAKLRVEEMEqgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1738 EAErrlKQAEEEKVRQIKVVEEVAQKTAAtQLQAmsfSEKttKLEESLKKEQGTvLQLQEEaekLRKQEEEANKAREQ-- 1815
Cdd:pfam05701 177 EIE---KTVEELTIELIATKESLESAHAA-HLEA---EEH--RIGAALAREQDK-LNWEKE---LKQAEEELQRLNQQll 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1816 AEKELETwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAeeaalkqkENAEKELEKQRTFAEqiaq 1895
Cdd:pfam05701 244 SAKDLKS-KLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAAL--------ASAKKELEEVKANIE---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1896 qKLSAEQEYIRLKADFEHAEqqrglLDNE---LQRLKNEVNAAEKQRRQLEDELAKVRSEMdALLQMKiqaekvsqsnTE 1972
Cdd:pfam05701 311 -KAKDEVNCLRVAAASLRSE-----LEKEkaeLASLRQREGMASIAVSSLEAELNRTKSEI-ALVQAK----------EK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1973 KSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA-- 2050
Cdd:pfam05701 374 EAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlq 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2051 ENERLKRQAEDEAYQRKLL----------------EDQAaqhKHDIQEKITQLQSSSVSELdRQKNIVEETLRQKKVVEE 2114
Cdd:pfam05701 454 ESESSAESTNQEDSPRGVTlsleeyyelskraheaEELA---NKRVAEAVSQIEEAKESEL-RSLEKLEEVNREMEERKE 529
|
570 580
....*....|....*....|....*
gi 1655220506 2115 EIHIIRINFERASKEKSDLEVELKK 2139
Cdd:pfam05701 530 ALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2506-2748 |
3.57e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.62 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2506 KAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldKETQGFQKSLEAERKRQLEISAEAEKLKlrvkelsSAQAKAEEEATR 2585
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ--AEEAEKQRAAEQARQKELEQRAAAEKAA-------KQAEQAAKQAEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2586 FKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAqELQNKSKETASAQQEQMEQQ 2665
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA-EAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2666 KAMLQQTFLTEKELLLKRERD------VEDEKKKLQKHLEDEVNKAKALKDEQQRQ--QKLMDEEKKKLQAIMDEAVKKQ 2737
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEaaaaaaAEAERKADEAELGDIFGLASGSNAEKQGGarGAAAGSEVDKYAAIIQQAIQQN 275
|
250
....*....|.
gi 1655220506 2738 KEAEAEMKNKQ 2748
Cdd:TIGR02794 276 LYDDPSFRGKT 286
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2419-2780 |
3.92e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2419 ELLKLKVRIEEENLRLMqknkdNTQKLLAEEAEKMKSLAE--EAAR----LSVEAEETARQRKTAEAELAEqralAEKML 2492
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQdyQAASdhlnLVQTALRQQEKIERYQADLEE----LEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2493 KEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDkqeIQQRLD-KETQG--FQKSLEA-ERKRQL--EISAEAEKLK 2566
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD---YQQALDvQQTRAiqYQQAVQAlERAKQLcgLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2567 LRVKELssaQAKaEEEATRFKKQAdEAKVRLQETEKQTTETVVQKLetQRLQSTREADDLKKAIAELEKEREKLKRDAQE 2646
Cdd:PRK04863 442 DWLEEF---QAK-EQEATEELLSL-EQKLSVAQAAHSQFEQAYQLV--RKIAGEVSRSEAWDVARELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2647 LQNKSKETASAQQEQMEQQKAM-LQQTFLTEKELLLKRERDVED---EKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEE 2722
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAErLLAEFCKRLGKNLDDEDELEQlqeELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2723 KKKLQAI------MDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLE 2780
Cdd:PRK04863 595 IQRLAARapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALD 658
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1914-2100 |
4.06e-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: 54.55 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1914 AEQQRGLLDneLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQAEKVSQSNTEKSKQLLETEalkMKQLAEEAA 1993
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELE---IEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1994 RLRSVAEEAKKQRQLA-----EDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQrkl 2068
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE--- 153
|
170 180 190
....*....|....*....|....*....|..
gi 1655220506 2069 LEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 2100
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPELLALYERIRK 185
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1663-1821 |
5.16e-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: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1663 DDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKsEAEKEAARQKQKAL----------DELQKH 1732
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEARIKKYeeqlgnvrnnKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1733 KMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQlqamsfsEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEANKA 1812
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELE-------AELAELEAELEEKKA---ELDEELAELEAELEELEAE 164
|
....*....
gi 1655220506 1813 REQAEKELE 1821
Cdd:COG1579 165 REELAAKIP 173
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1515-1789 |
5.38e-07 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 56.38 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1515 SELSTLTSQYIKFILE---TQRRLEDDEKA---SEKLKEDEKKRMAEI---QAQLETQKQLA---EGHAKSVA-KAELEA 1581
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAeadRQRLEQEKQQQLAAIsgsQSQLESTDQNAletNGQAQRDAiLEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1582 --QELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQ--LKNLSEQEIRSKnqqleeaQVSRRKLEEeihliriqlqttIK 1657
Cdd:NF012221 1618 vtKELT-TLAQGLDALDSQATYAGESGDQWRNPFAGglLDRVQEQLDDAK-------KISGKQLAD------------AK 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1658 QKSTadDELQKLRDQAAEAEkvrkAAQEEAERLRKQVNEETQKKKNAEDelKRKseaeKEAARQKQKALDELQKHKMQAE 1737
Cdd:NF012221 1678 QRHV--DNQQKVKDAVAKSE----AGVAQGEQNQANAEQDIDDAKADAE--KRK----DDALAKQNEAQQAESDANAAAN 1745
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 1738 EAERRLKQaeeekvrqikvvEEVAQKTAATQLQAmsfSEKTTKLEESLKKEQ 1789
Cdd:NF012221 1746 DAQSRGEQ------------DASAAENKANQAQA---DAKGAKQDESDKPNR 1782
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1994-2805 |
5.48e-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: 56.59 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1994 RLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVAlKAKEAENERLK-RQAEDEAYQRKLledq 2072
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV-KSYENELDPLKnRLKEIEHNLSKI---- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2073 aaqhkHDIQEKITQLQSSsvsELDRQKNIVEETLRQKKV---VEEEIHIIRINFERASKEKSDLEVEL-KKLKGIADETQ 2148
Cdd:TIGR00606 265 -----MKLDNEIKALKSR---KKQMEKDNSELELKMEKVfqgTDEQLNDLYHNHQRTVREKERELVDCqRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2149 kskakaeeeAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILA 2228
Cdd:TIGR00606 337 ---------LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2229 KEAAQkstaaeqkaqdVLSKNKEDLLSQEKLRDEFENAKK-LAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAK 2307
Cdd:TIGR00606 408 KTAAQ-----------LCADLQSKERLKQEQADEIRDEKKgLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2308 QAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQeadAEMAKHKKEAEQALKQKSQVEKELGlvklQLDETDKQKALMDE 2387
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEK---ADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2388 ELQRVKAQVNDAV----------KQKAQVENELSKVKMQMDELLKlKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLA 2457
Cdd:TIGR00606 550 QIRKIKSRHSDELtsllgyfpnkKQLEDWLHSKSKEINQTRDRLA-KLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2458 EEAArlSVEAEETARQRKTAEAELA-EQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQR 2536
Cdd:TIGR00606 629 FDVC--GSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2537 LDKETQGFQKSLEAERKRQLEISAEAE----KLKLRVKELSSAQAKAEEEATRFKkqadEAKVRLQETEKQTtETVVQKL 2612
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPgrqsIIDLKEKEIPELRNKLQKVNRDIQ----RLKNDIEEQETLL-GTIMPEE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2613 ETQRLQSTrEADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLlkreRDVEDEKK 2692
Cdd:TIGR00606 782 ESAKVCLT-DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELN----RKLIQDQQ 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2693 KLQKHLEDEVNKAKALK-----DEQQRQQklMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD 2767
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEKlqigtNLQRRQQ--FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
810 820 830
....*....|....*....|....*....|....*...
gi 1655220506 2768 ENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2805
Cdd:TIGR00606 935 SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYL 972
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1529-1844 |
5.83e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.92 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1529 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQN 1608
Cdd:pfam13868 45 LDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1609 IQLELTQLKNLSEQEIRSKNQQleeaqvsrrKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1688
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELE---------KEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1689 RLRKQVNEETQKKKNAEDELKRKS-EAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAT 1767
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERKErQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1768 QLQamsfsekttkleeslKKEQGTVLQLQEEAEKLRKQEEEANKAREQA-EKELETWRLKANEALRLRLRAEEEAQRK 1844
Cdd:pfam13868 276 IEQ---------------EEAEKRRMKRLEHRRELEKQIEEREEQRAAErEEELEEGERLREEEAERRERIEEERQKK 338
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1312-1861 |
6.18e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.88 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1312 EEKEVEAHRSQLKaMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQR 1391
Cdd:pfam05483 200 EELRVQAENARLE-MHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1392 elsLLGRHMNSYKQSYEWLIQWLREARLRQEKieaaPVWDSKALKEQLTQEKKLLEEIEKNKD-QIENCQKDAKAYIDSL 1470
Cdd:pfam05483 279 ---LQDENLKELIEKKDHLTKELEDIKMSLQR----SMSTQKALEEDLQIATKTICQLTEEKEaQMEELNKAKAAHSFVV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1471 KDYEFQILAYRALQDPiasplKKPKMESASDNIIQEYVTLRTRYSELSTLTS---------QYIKFILETQRRLEDDEKA 1541
Cdd:pfam05483 352 TEFEATTCSLEELLRT-----EQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkevelEELKKILAEDEKLLDEKKQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1542 SEKLKEDEK--------------KRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAE---- 1603
Cdd:pfam05483 427 FEKIAEELKgkeqelifllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeltq 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1604 ---------------------------KQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTI 1656
Cdd:pfam05483 507 easdmtlelkkhqediinckkqeermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1657 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETqKKKNAEDELKRKSEAEKEAARQK-QKALDELQKH-KM 1734
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN-KQLNAYEIKVNKLELELASAKQKfEEIIDNYQKEiED 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1735 QAEEAERRLKQAEEEKV---RQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLqeeaekLRKQEEEANK 1811
Cdd:pfam05483 666 KKISEEKLLEEVEKAKAiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGL------YKNKEQEQSS 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1812 AREQAEKELETWRlkaNEALRLRLRAEEEaqrkslaQEEAEKQKTEAERD 1861
Cdd:pfam05483 740 AKAALEIELSNIK---AELLSLKKQLEIE-------KEEKEKLKMEAKEN 779
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1639-1959 |
6.31e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.92 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1639 RKLEEEIHLIRIQL----QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEA 1714
Cdd:pfam13868 9 RELNSKLLAAKCNKerdaQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1715 EKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIK--VVEEVAQKTAATQLQAMSFSEKTTKLEESLK-KEQGT 1791
Cdd:pfam13868 89 RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLReeIDEFNEEQAEWKELEKEEEREEDERILEYLKeKAERE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1792 VLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEA 1871
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKA--ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1872 ALKQKENAEKELEKQ------RTFAEQIAQQKLSAEQEYIRLKAdfEHAEQQRGLLDNELQRL---KNEVNAAEKQRRQL 1942
Cdd:pfam13868 247 LKERRLAEEAEREEEefermlRKQAEDEEIEQEEAEKRRMKRLE--HRRELEKQIEEREEQRAaerEEELEEGERLREEE 324
|
330
....*....|....*..
gi 1655220506 1943 EDELAKVRSEMDALLQM 1959
Cdd:pfam13868 325 AERRERIEEERQKKLKE 341
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4328-4356 |
6.38e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 6.38e-07
10 20
....*....|....*....|....*....
gi 1655220506 4328 IVDPESGKEMSVYEAYQKGLIDHQTYLEL 4356
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2433-2626 |
6.54e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2433 RLMQKNKDNT------QKLLAEEA-EKMKSLAEEAARL-SVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQ-EAT 2503
Cdd:PRK09510 66 RQQQQQKSAKraeeqrKKKEQQQAeELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAaAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2504 KLKAEAEE--LQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgfQKSLEAERKRQLEISAEAEKLKL-RVKELSSAQAKAE 2580
Cdd:PRK09510 146 KAKAEAEAkrAAAAAKKAAAEAKKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKKAEAEaKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1655220506 2581 EEATRFKKQADEAKVRLQETEKQTTEtvvqKLETQRLQSTREADDL 2626
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKA----AEKAAAAKAAAEVDDL 262
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1875-2074 |
6.65e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1875 QKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRglldneLQRLKNEVNAAEKQRRQLEDELAKvrsemd 1954
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER------LKQLEKERLAAQEQKKQAEEAAKQ------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1955 ALLQMKiQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARlrsVAEEAKKQrqlAEDEAARQRAEAEKILKEKLAAINEA 2034
Cdd:PRK09510 127 AALKQK-QAEEAAAKAAAAAKAKAEAEA---KRAAAAAKK---AAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220506 2035 TRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAA 2074
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1467-1771 |
7.52e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1467 IDSLKDYEFQILAYRALQDPIASPLKKPKMESASD-NIIQeyVTLRTRYSELS-----TLTSQYIKFILEtqRRLEDDEK 1540
Cdd:COG3206 100 VDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGsNVIE--ISYTSPDPELAaavanALAEAYLEQNLE--LRREEARK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1541 ASEKLKEdekkRMAEIQAQLEtqkqlaeghaksvaKAELEAQELKlkmkedasQRQGLaVDAEKQKQNIQLELTQLknls 1620
Cdd:COG3206 176 ALEFLEE----QLPELRKELE--------------EAEAALEEFR--------QKNGL-VDLSEEAKLLLQQLSEL---- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1621 eqeirskNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST--ADDELQKLRDQAAEAEKVRKAAQE-------EAERLR 1691
Cdd:COG3206 225 -------ESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1692 KQVNEETQKKKNAEDELKRKSEAEKEAARQK----QKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAT 1767
Cdd:COG3206 298 AQIAALRAQLQQEAQRILASLEAELEALQAReaslQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
....
gi 1655220506 1768 QLQA 1771
Cdd:COG3206 378 RLAE 381
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1721-1938 |
7.65e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1721 QKQKALDELQKHKMQAEEAERRLKQ---AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQE 1797
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQkqaAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1798 EAEKLRkQEEEANKAREQAEKELETWRLKANEAlRLRLRAEEEAQRKslAQEEAEKQKTEAERDAKKKAKAEEAALKQKE 1877
Cdd:PRK09510 150 EAEAKR-AAAAAKKAAAEAKKKAEAEAAKKAAA-EAKKKAEAEAAAK--AAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 1878 NAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRGLLDNELQRLKNEVNAAEKQ 1938
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAA----------AAKAAAEVDDLFGGLDSGKNAPKTG 276
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1603-2014 |
7.70e-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: 55.29 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1603 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1682
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1683 AQEEAERLRKQVNEETQKKKNAEDELKRKSEaekeaarQKQKALDELQKHKMQAEEAERRLKQAEEEKvrqikvvEEVAQ 1762
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQ-------RVLERETELERMKERAKKAGAQRKEEEAER-------KQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1763 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkaneALRLRLRAEE--- 1839
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR-----SLQERLNASErkv 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1840 EAQRKSLAQEEAEKQKTEAErdakkkakaeeAALKQKENAEKELE-KQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQR 1918
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAE-----------LHQARLQAAQLTLQlADASLALREGRARWAQERETLQQSAEADKDRIEK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1919 glLDNELQRLKNEVNAAEKQRRQLEDELAKVR-------SEMDALLQMKIQAEKVSQSntEKSKQLLETEALkMKQLAEE 1991
Cdd:pfam07888 323 --LSAELQRLEERLQEERMEREKLEVELGREKdcnrvqlSESRRELQELKASLRVAQK--EKEQLQAEKQEL-LEYIRQL 397
|
410 420
....*....|....*....|...
gi 1655220506 1992 AARLRSVAEEAKKQRQLAEDEAA 2014
Cdd:pfam07888 398 EQRLETVADAKWSEAALTSTERP 420
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1306-1986 |
7.72e-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: 56.00 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1306 VSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSvsDKMTRLHSERDAELEHYRQLAGSLL---ERWQAV 1382
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA--ELNQLLRTLDDQWKEKRDELNGELSaadAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1383 FAQID-LRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQK 1461
Cdd:pfam12128 321 RSELEaLEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1462 DAKAYIDSLKDYEFQILAYRALQDPIasplkKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIkfiletqrrLEDDEKA 1541
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESEL-----REQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT---------ATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1542 SEKLKEDEKKRMAEIQAQlETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAvDAEKQKQNIQLELTQLKNLSE 1621
Cdd:pfam12128 465 QLENFDERIERAREEQEA-ANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA-LDELELQLFPQAGTLLHFLRK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1622 QEI---RSKNQQLEEAQVSRRKLEEEI----------------HLIRIQlqttIKQKSTADDELQKLRDQAAEAekvRKA 1682
Cdd:pfam12128 543 EAPdweQSIGKVISPELLHRTDLDPEVwdgsvggelnlygvklDLKRID----VPEWAASEEELRERLDKAEEA---LQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1683 AQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIkvveEVAQ 1762
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL----EAQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1763 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAE---KELETWR------LKANEALRL 1833
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKaelKALETWYkrdlasLGVDPDVIA 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1834 RLRAEEEAQRKSLAQEEAEKQKTEAERDakkkaKAEEAALKQKENAEKELEKQRTFAEQIaQQKLSAEQEYIRLKadfeh 1913
Cdd:pfam12128 772 KLKREIRTLERKIERIAVRRQEVLRYFD-----WYQETWLQRRPRLATQLSNIERAISEL-QQQLARLIADTKLR----- 840
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 1914 aeqqrglldneLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEkVSQSNTEKSKQLLETEALKMK 1986
Cdd:pfam12128 841 -----------RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDAN-SEQAQGSIGERLAQLEDLKLK 901
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2399-2603 |
8.22e-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: 54.77 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2399 AVKQKAQVENELSKVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAE 2478
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2479 AELAEQRALAEKMLKE--KM----------------QAIQEATKLKAEAEELQKQKNQAQEKAKKLledkQEIQQRLDKE 2540
Cdd:COG4942 97 AELEAQKEELAELLRAlyRLgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAEL----AALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2541 TQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2603
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2499-2712 |
8.34e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2499 IQEATKLKAEAEelQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKLRVKElssAQAK 2578
Cdd:PRK09510 67 QQQQQKSAKRAE--EQRKKKEQQQAEELQQKQAAEQERL--------KQLEKERLAAQEQKKQAEEAAKQAAL---KQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2579 AEEEAtrfKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQ 2658
Cdd:PRK09510 134 AEEAA---AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2659 QEQMEQQKAmlqqtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQ 2712
Cdd:PRK09510 211 AAAEAKKKA--------AAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1620-1819 |
8.97e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1620 SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE--- 1696
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1697 ETQKKKNAEDELK------------RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKT 1764
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 1765 AATQLQAmsfsektTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKE 1819
Cdd:COG3883 174 EAQQAEQ-------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1676-2117 |
1.06e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.15 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1676 AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAArQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIK 1755
Cdd:pfam09731 43 GEEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEK-KQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1756 VVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEqgTVLQLQEEAEKLRKQEEEANKAREqaeKELETWRLKANealrlrl 1835
Cdd:pfam09731 122 SEQEKEKALEEVLKEAISKAESATAVAKEAKDD--AIQAVKAHTDSLKEASDTAEISRE---KATDSALQKAE------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1836 RAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAAlkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAE 1915
Cdd:pfam09731 190 ALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPE--HLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1916 qqrglldNELQRLKNEVNAAEKQRrqLEDELAKVRSEMDALlqmkiqaekvsqsntekSKQLLEtealkmKQLAEEAARL 1995
Cdd:pfam09731 268 -------PDIIPVLKEDNLLSNDD--LNSLIAHAHREIDQL-----------------SKKLAE------LKKREEKHIE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1996 RSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaaineatRLKTEAEVALKAKEAENE---RLKRQAED-EAYQRKLLED 2071
Cdd:pfam09731 316 RALEKQKEELDKLAEELSARLEEVRAADEAQL--------RLEFEREREEIRESYEEKlrtELERQAEAhEEHLKDVLVE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2072 QAAQ----HKHDIQEKITQ---LQSSSVSELDRQKNIVEETLRQKKVVEEEIH 2117
Cdd:pfam09731 388 QEIElqreFLQDIKEKVEEeraGRLLKLNELLANLKGLEKATSSHSEVEDENR 440
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1738-2149 |
1.08e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.13 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1738 EAERRLKQAEEEKVRQikvveEVAQKTAATQLQAmsfseKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA-REQA 1816
Cdd:pfam05557 6 ESKARLSQLQNEKKQM-----ELEHKRARIELEK-----KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAlREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1817 ekeletwrlkanEALRLRLRAEEEAQRKslaQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1896
Cdd:pfam05557 76 ------------ELNRLKKKYLEALNKK---LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1897 klsaEQEYirlKADFEHAEQQRGLLDNELQRLKnevnAAEKQRRQLEDELAKvrSEMDALLQMKIQAEKVSQSNTEKSKQ 1976
Cdd:pfam05557 141 ----LDLL---KAKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQS--QEQDSEIVKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1977 LLETEALKMKQLAEEAARLRSVAEEAKkqRQLAEDEAARQRAEAEKILKEKLAA-INEATRLKTEAEVALKAKEAENERL 2055
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEEVEDLK--RKLEREEKYREEAATLELEKEKLEQeLQSWVKLAQDTGLNLRSPEDLSRRI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2056 KR-QAEDEAY-QRKLLEDQAAQHKH----DIQEKITQLQSSSVSE---LDRQKNIVEETLRQKKVVEEEIHIIRINFERA 2126
Cdd:pfam05557 286 EQlQQREIVLkEENSSLTSSARQLEkarrELEQELAQYLKKIEDLnkkLKRHKALVRRLQRRVLLLTKERDGYRAILESY 365
|
410 420
....*....|....*....|....*.
gi 1655220506 2127 SKEKSDLEVELKKL---KGIADETQK 2149
Cdd:pfam05557 366 DKELTMSNYSPQLLeriEEAEDMTQK 391
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
197-317 |
1.10e-06 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 50.37 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 197 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDLVRNVRLPREKGRMRfhKLQNVQIA 276
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220506 277 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 317
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2191-2589 |
1.12e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAK-EAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFEN--AK 2267
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELEAelAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2268 KLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAE--DEAAKQAKAQKDA--ERLRKEAEAEAAKRAAAEAAALKQKQEA 2343
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAelEEELEEAQEELEEleEELEQLENELEAAALEERLKEARLLLLI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2344 DAEMAKHKKEAEQALKQKSQVEK----ELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKV----KM 2415
Cdd:COG4717 255 AAALLALLGLGGSLLSLILTIAGvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2416 QMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSL-------AEEAARLSVEAEETARQRKTAEAELAEQRALA 2488
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEEL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2489 EKMLKEKMQAIQEATkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdkETQGFQKSLEAERKRQLEISAEAEKLKLR 2568
Cdd:COG4717 415 LGELEELLEALDEEE-LEEELEELEEELEELEEELEELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEE 491
|
410 420
....*....|....*....|.
gi 1655220506 2569 VKELSSAQAKAEEEATRFKKQ 2589
Cdd:COG4717 492 WAALKLALELLEEAREEYREE 512
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2192-2369 |
1.13e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2192 QRKAAQDEVERL-----KQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdllsqeklrdefENA 2266
Cdd:PRK09510 100 QERLKQLEKERLaaqeqKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA------------AEA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2267 KKLAQAAETAKEKAEKeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAaAEAAALKQKQEADAE 2346
Cdd:PRK09510 168 KKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA-AAKAAAEAKAAAEKA 241
|
170 180
....*....|....*....|...
gi 1655220506 2347 MAKHKKEAEQALKQKSQVEKELG 2369
Cdd:PRK09510 242 AAAKAAEKAAAAKAAAEVDDLFG 264
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1713-2077 |
1.30e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1713 EAEKEAARQKQKaldelqkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEqgtv 1792
Cdd:pfam02029 2 EDEEEAARERRR----------RAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDR---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1793 LQLQEEAEKLRKQEEEankareQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEaekqKTEAERDAKKKAKAEEAA 1872
Cdd:pfam02029 68 TAKREERRQKRLQEAL------ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEE----KRDSRLGRYKEEETEIRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1873 LKQKENAEKELEKQRtfAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSE 1952
Cdd:pfam02029 138 KEYQENKWSTEVRQA--EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKK-VKYESKVFLDQKRGHPEVKSQNGEE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1953 MDALLQMKIQAEKVSQSNT----EKSKQLLETEaLKMKQLAEEAARLRSVAEEAKKQRQLaedEAARQRAEAEKILKEKL 2028
Cdd:pfam02029 215 EVTKLKVTTKRRQGGLSQSqereEEAEVFLEAE-QKLEELRRRRQEKESEEFEKLRQKQQ---EAELELEELKKKREERR 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2029 AAINEATRLKTEAEVALKAKEAENERL------KRQAEDEAYQRKLLEDQAAQHK 2077
Cdd:pfam02029 291 KLLEEEEQRRKQEEAERKLREEEEKRRmkeeieRRRAEAAEKRQKLPEDSSSEGK 345
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1912-2038 |
1.46e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.02 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1912 EHAEQQ-RGLLdnELQRLKNEVnAAEKQRRqledelakvrsemdALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAE 1990
Cdd:PTZ00491 673 ELLEQEaRGRL--ERQKMHDKA-KAEEQRT--------------KLLELQAESAAVESSGQSRAEALAEAEARLIEAEAE 735
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 1991 -EAARLRSVAE--------EAKKQRQLAEDEAARQRAEAEkILKEKLAAINEATRLK 2038
Cdd:PTZ00491 736 vEQAELRAKALrieaeaelEKLRKRQELELEYEQAQNELE-IAKAKELADIEATKFE 791
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2448-2776 |
1.51e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2448 EEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEatKLKAEAEELQKQKNQAQEKAKKLL 2527
Cdd:pfam13868 6 DELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2528 EDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEakvRLQETEKQTTET 2607
Cdd:pfam13868 84 EREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EEREEDERILEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2608 VVQKLETQrlqstreaddlkkaiAELEKEREKLKRDAQELQNKsketASAQQEQMEQQKAMLQqtfltekELLLKRERDv 2687
Cdd:pfam13868 161 LKEKAERE---------------EEREAEREEIEEEKEREIAR----LRAQQEKAQDEKAERD-------ELRAKLYQE- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2688 EDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQaimdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD 2767
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLA----EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
....*....
gi 1655220506 2768 ENKKLREKL 2776
Cdd:pfam13868 290 EHRRELEKQ 298
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2341-2566 |
1.54e-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: 54.65 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2341 QEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVndavkqkAQVENELSKVKMQMDEL 2420
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNEEL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2421 LKlKVRIEEENLRLMQKNKDNTQKL---LAEEAEKMKSLAE--EAARLSVEAEETARQRKTAEAELAEQRALAE-KMLKE 2494
Cdd:pfam05667 383 EK-QYKVKKKTLDLLPDAEENIAKLqalVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiKELRE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2495 KMQAIQEATKLKaeaEELQKQKNQAQEKAKKlleDKQ---------EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2565
Cdd:pfam05667 462 KIKEVAEEAKQK---EELYKQLVAEYERLPK---DVSrsaytrrilEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
.
gi 1655220506 2566 K 2566
Cdd:pfam05667 536 D 536
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1303-1861 |
1.69e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1303 LRDVSKVPAEEKEVEAHRSQLKAMRAEAEAdQATFDRLQDELKAATSVS----DKMTRLHSERDAELEHYRQLAGSLLER 1378
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNlddeDELEQLQEELEARLESLSESVSEARER 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1379 wqavfaQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapVWDSKALKEQLTQEKKLLEEIEKNKDQIEN 1458
Cdd:PRK04863 581 ------RMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEE--FEDSQDVTEYMQQLLERERELTVERDELAA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1459 CQKDAKAYIDSL------KDYEFQILAYR----------------------ALQDPIASPLKKPKMESASDNIIQEYVTL 1510
Cdd:PRK04863 653 RKQALDEEIERLsqpggsEDPRLNALAERfggvllseiyddvsledapyfsALYGPARHAIVVPDLSDAAEQLAGLEDCP 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1511 RTRYselstltsqyikFILETQRRLEDDEKASEKLKEDEKKRMAEIQ------------------AQLETQKQLAEGHAK 1572
Cdd:PRK04863 733 EDLY------------LIEGDPDSFDDSVFSVEELEKAVVVKIADRQwrysrfpevplfgraareKRIEQLRAEREELAE 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1573 SVAKAELEAQELKlKMKEDASQRQG--LAV-----------DAEKQKQNIQLELTQLKNlSEQEIRSKNQQLEEAQVSRR 1639
Cdd:PRK04863 801 RYATLSFDVQKLQ-RLHQAFSRFIGshLAVafeadpeaelrQLNRRRVELERALADHES-QEQQQRSQLEQAKEGLSALN 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1640 KLEEEIHLIriqlqttikqkstADDELQklrDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE---------DELKR 1710
Cdd:PRK04863 879 RLLPRLNLL-------------ADETLA---DRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSvlqsdpeqfEQLKQ 942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1711 K---SEAEKEAARQKQKALDEL--QKHKMQAEEAERRLKQAEE--EKVRQIKVVEEVAQKTAATQL-----QAMSFSEKT 1778
Cdd:PRK04863 943 DyqqAQQTQRDAKQQAFALTEVvqRRAHFSYEDAAEMLAKNSDlnEKLRQRLEQAEQERTRAREQLrqaqaQLAQYNQVL 1022
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1779 TKLEESLKKEQGTVLQLQEEAEKLRKQ-----EEEANKAREQAEKELETWRLKANEALRLRLRAEEEAqrkslaqEEAEK 1853
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQELQDLGVPadsgaEERARARRDELHARLSANRSRRNQLEKQLTFCEAEM-------DNLTK 1095
|
....*...
gi 1655220506 1854 QKTEAERD 1861
Cdd:PRK04863 1096 KLRKLERD 1103
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1601-1859 |
1.75e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1601 DAEKQKQNIQLELTQLKnlseQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR 1680
Cdd:COG1340 12 ELEEKIEELREEIEELK----EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1681 KAAQEEAERLRKQVNEETQKKKNaEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1760
Cdd:COG1340 88 NELREELDELRKELAELNKAGGS-IDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1761 AQkTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR-------- 1832
Cdd:COG1340 167 AE-LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKelrelrke 245
|
250 260
....*....|....*....|....*...
gi 1655220506 1833 -LRLRAEEEAQRKSLAQEEAEKQKTEAE 1859
Cdd:COG1340 246 lKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2580-2774 |
1.78e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.19 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2580 EEEATRFKKQADEAKVRLQETEKQTTETvvqklETQRLQSTREADDLKKAIAELEKERE---------KLKRDAQELQNK 2650
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVERKRREQ-----EEQRRLQQEQLERAEKMREELELEQQrrfeeirlrKQRLEEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2651 SKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEdekkklqkhledEVNKAKALKDEQQRQQKLMDEEKKKLQAIM 2730
Cdd:pfam15709 405 EEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE------------EAERAEAEKQRQKELEMQLAEEQKRLMEMA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1655220506 2731 DEA-VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLRE 2774
Cdd:pfam15709 473 EEErLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2387-2632 |
2.10e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2387 EELQRVKAQVNDAVKQKAQveneLSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVE 2466
Cdd:COG4913 235 DDLERAHEALEDAREQIEL----LEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2467 AEETARQRKTAEAELaeqRALAEKMLKEKMQAIQEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQk 2546
Cdd:COG4913 311 LERLEARLDALREEL---DELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2547 sleaerkrqleisAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvVQKLETQRLQSTREADDL 2626
Cdd:COG4913 384 -------------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE-----IASLERRKSNIPARLLAL 445
|
....*.
gi 1655220506 2627 KKAIAE 2632
Cdd:COG4913 446 RDALAE 451
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2508-2794 |
2.46e-06 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 52.65 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2508 EAEELQKQKNQAQEKAKKLLEDKQEIQQrLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE---EAT 2584
Cdd:pfam09728 2 AARELMQLLNKLDSPEEKLAALCKKYAE-LLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKlcrELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2585 RFKKQADEAKVRLQETEKQTTETVVQKLETqrlqstrEADDLKKAIAELEKEREKLKRDAQELQNKSKETAsAQQEQMEQ 2664
Cdd:pfam09728 81 KQNKKLKEESKKLAKEEEEKRKELSEKFQS-------TLKDIQDKMEEKSEKNNKLREENEELREKLKSLI-EQYELREL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2665 Q-KAMLQQTFLTEKELLLKRERDVEDEKKKLQkhlEDEVNKAKALkdeqQRQQKLMDEEKKKLQAIMDEAVKKQKEAE-- 2741
Cdd:pfam09728 153 HfEKLLKTKELEVQLAEAKLQQATEEEEKKAQ---EKEVAKAREL----KAQVQTLSETEKELREQLNLYVEKFEEFQdt 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2742 ------------AEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2794
Cdd:pfam09728 226 lnksnevfttfkKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLE 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2289-2739 |
2.49e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2289 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKraaaeaaalKQKQEADAEMAKHKKEAEQALKQKSQVEKEL 2368
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---------LEELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2369 GLVKLQLDETDKQKalmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAE 2448
Cdd:COG4717 142 AELPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2449 EAEKMKSLAEEAARLSVEAEETARQRKTAEAE--------------LAEQRALAEKMLKEKMQAIQEATKLKAEAEELQK 2514
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2515 QKNQAQEKAKKLLEDKQEIQQRldkETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRfKKQADEAK 2594
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEE---ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-EELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2595 VRLQETEKQTTETVVQKLETQrlqstREADDLKKAIAELEKEREKLKRDAQE-LQNKSKETASAQQEQMEQQKAMLQQtf 2673
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQA-----EEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEEELEELEE-- 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2674 ltEKELLLKRERDVEDEKKKLQKhlEDEVNKAKALKDEQQRQQKLMDEE---KKKLQAIMDEAVKKQKE 2739
Cdd:COG4717 447 --ELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEwaaLKLALELLEEAREEYRE 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1708-1969 |
2.53e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1708 LKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEeKVRQIKvveevaqktaaTQLQAMSFSEKTTKLEESLKk 1787
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE------QLPELRKELEEAEA-ALEEFR-----------QKNGLVDLSEEAKLLLQQLS- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1788 eqgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKak 1867
Cdd:COG3206 223 ------ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1868 aeeaalkqkeNAEKELEKQRtfaEQIAQQklsAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEV---NAAEKQRRQLED 1944
Cdd:COG3206 295 ----------ALRAQIAALR---AQLQQE---AQRILASLEAELEALQAREASLQAQLAQLEARLaelPELEAELRRLER 358
|
250 260
....*....|....*....|....*
gi 1655220506 1945 ELAKVRSEMDALLQmKIQAEKVSQS 1969
Cdd:COG3206 359 EVEVARELYESLLQ-RLEEARLAEA 382
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1953-2404 |
2.81e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1953 MDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE-AKKQRQLAEDEAARQRAEAEKILKEKLAAI 2031
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2032 NEATRLKTEAEVALKAKEAENERLKRQAED-EAYQRKL--LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQ 2108
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2109 KKVVEEEIHIIRINFERASKEKSDLEVELKKLK----------------------GIADETQKSKAKAEEEAEKLKKLAA 2166
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAAleerlkearlllliaaallallGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2167 EEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEA-AQKSTAAEQKAQDV 2245
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2246 LSKNKEDLLSQEKLRDEFEnakklaqaaetakekaekeaalLRQKAEEAEKLKKAaedeaakQAKAQKDAERLRKEAEAE 2325
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEE----------------------LRAALEQAEEYQEL-------KEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2326 AAKRAAAEAAALKQK-QEADAEMAKHKKEAEQALKQKSQVEKELGLVklqldETDKQKALMDEELQRVKAQVNDAVKQKA 2404
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWA 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1794-2038 |
2.87e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1794 QLQEEAEKLRKQEEEANKAREQAEKELEtwrlkanealrlrlraeeeaQRKSLAQEEAEKQKTEAERDakkkakaeeaal 1873
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDARE--------------------QIELLEPIRELAERYAAARE------------ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1874 kQKENAEKELEKQRTFAEQIAQQKLSAEQEyiRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLE-DELAKVRSE 1952
Cdd:COG4913 270 -RLAELEYLRAALRLWFAQRRLELLEAELE--ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1953 MDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAIN 2032
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*.
gi 1655220506 2033 EATRLK 2038
Cdd:COG4913 427 EIASLE 432
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2338-2727 |
3.11e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 53.14 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2338 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQM 2417
Cdd:pfam15742 6 KLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2418 dELLKLKVR-IEEENLRLMQKNKdnTQKLLAEE--AEKMKSLAEEAARLSVEAE-ETARQRKTAEAELAEQRALAEKM-- 2491
Cdd:pfam15742 86 -KHCQQKIReLELEVLKQAQSIK--SQNSLQEKlaQEKSRVADAEEKILELQQKlEHAHKVCLTDTCILEKKQLEERIke 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2492 -------LKEKMQAIQEATK-LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdKETQGFQKSLEAERKRQLEISAEAE 2563
Cdd:pfam15742 163 aseneakLKQQYQEEQQKRKlLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRI-QQQEAQLKQLENEKRKSDEHLKSNQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2564 KLKlrvKELSSAQAKAE---EEATRFKKQADeAKVRlQETEKQTTETVvqKLETQRLQSTREADDLKKAIAELEKEREKL 2640
Cdd:pfam15742 242 ELS---EKLSSLQQEKEalqEELQQVLKQLD-VHVR-KYNEKHHHHKA--KLRRAKDRLVHEVEQRDERIKQLENEIGIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2641 krdaqelqnksketasaqQEQMEQQKAMlQQTFLTEKELLLKrerdvedEKKKLQKHLEDE---VNKAKALKDEQQRQQK 2717
Cdd:pfam15742 315 ------------------QQQSEKEKAF-QKQVTAQNEILLL-------EKRKLLEQLTEQeelIKNNKRTISSVQNRVN 368
|
410
....*....|
gi 1655220506 2718 LMDEEKKKLQ 2727
Cdd:pfam15742 369 FLDEENKQLQ 378
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1524-2061 |
3.30e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1524 YIKFILETQRRLEDDEKaSEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEdasqrqglavdAE 1603
Cdd:PRK01156 195 SNLELENIKKQIADDEK-SHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKT-----------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1604 KQKQNIQLELTQLKNLSEQEIRSKNqqlEEAQVSRRKLEEEIHLIRiQLQTTIKQKSTADDELQKLRDQaaeaekVRKAA 1683
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHAI------IKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1684 QEEAERlrkqvnEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVV----EE 1759
Cdd:PRK01156 333 VLQKDY------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1760 VAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ-----------EEEANKAREQAEKELETWRLKAN 1828
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1829 EALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK 1908
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1909 -ADFEHAEQQRGLLDNE-LQRLKNEVNA----AEKQRRQLEDELAKVRSEMDALLQmKIQAEkvsQSNTEKSKQLLETEA 1982
Cdd:PRK01156 567 rTSWLNALAVISLIDIEtNRSRSNEIKKqlndLESRLQEIEIGFPDDKSYIDKSIR-EIENE---ANNLNNKYNEIQENK 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 1983 LKMKQLAEEAARLRSVAEEaKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAED 2061
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2591-2809 |
3.60e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 53.68 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2591 DEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQ 2670
Cdd:PRK00409 505 EEAKKLIGE-DKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2671 QtfltEKELLLKRERDVEDEKKKLQkhledevnKAKALKDEQQRqqklMDEEKKKLQAIMDEAVKKQKEAEAEMKNK--- 2747
Cdd:PRK00409 584 K----EADEIIKELRQLQKGGYASV--------KAHELIEARKR----LNKANEKKEKKKKKQKEKQEELKVGDEVKyls 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2748 --QKeMEALEKKRlEQEKLLADENKKLREKLESLEVTSKQaasKTKEIEVQTDKVPEEQLVSMT 2809
Cdd:PRK00409 648 lgQK-GEVLSIPD-DKEAIVQAGIMKMKVPLSDLEKIQKP---KKKKKKKPKTVKPKPRTVSLE 706
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1464-1787 |
3.98e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1464 KAYIDSLKDYEFQILAYRalqdpIASPLKKPKMESASDNIIQEYV---TLRTRYSELstltsQYIKFILETQRRLEDDEK 1540
Cdd:COG5022 813 RSYLACIIKLQKTIKREK-----KLRETEEVEFSLKAEVLIQKFGrslKAKKRFSLL-----KKETIYLQSAQRVELAER 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1541 ASEKLKEDEKKRMAEIQAQLETQKQLAEgHAKSVAKAELEaqelKLKMKEDASQRqglavdAEKQKQNIQLELTQLKNLS 1620
Cdd:COG5022 883 QLQELKIDVKSISSLKLVNLELESEIIE-LKKSLSSDLIE----NLEFKTELIAR------LKKLLNNIDLEEGPSIEYV 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1621 EQEIRsknQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLR--------- 1691
Cdd:COG5022 952 KLPEL---NKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKelpvevael 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1692 ----KQVNEETQKKK--NAEDELKRKSEAEKEAARQKQKALdELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTa 1765
Cdd:COG5022 1029 qsasKIISSESTELSilKPLQKLKGLLLLENNQLQARYKAL-KLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNR- 1106
|
330 340
....*....|....*....|..
gi 1655220506 1766 atqlQAMSFSEKTTKLEESLKK 1787
Cdd:COG5022 1107 ----NLVKPANVLQFIVAQMIK 1124
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2339-2761 |
4.00e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2339 QKQEADAEMAKHKKEAEQAlkqKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVndavkqkAQVENELSKVKMQMD 2418
Cdd:pfam07888 35 RLEECLQERAELLQAQEAA---NRQREKEKERYKRDREQWERQRRELESRVAELKEEL-------RQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2419 ELLKLKVRIEEENLRLMQKNKDNTQKLLaEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlAEKMLKEKMQA 2498
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA-ERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2499 IQEatKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRqleisaeaeklklrvKELSSAQAK 2578
Cdd:pfam07888 183 TEE--ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALL---------------EELRSLQER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2579 AEeeatrfkkqadeakvrlqeTEKQTTETVVQKLETQRLQSTReaddlkkAIAELEKEReklkRDAQELQNKSKETASAQ 2658
Cdd:pfam07888 246 LN-------------------ASERKVEGLGEELSSMAAQRDR-------TQAELHQAR----LQAAQLTLQLADASLAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2659 QE---QMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVK 2735
Cdd:pfam07888 296 REgraRWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV 375
|
410 420
....*....|....*....|....*.
gi 1655220506 2736 KQKEAEAEMKNKQKEMEALekKRLEQ 2761
Cdd:pfam07888 376 AQKEKEQLQAEKQELLEYI--RQLEQ 399
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2419-2585 |
4.01e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 53.08 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2419 ELLKLKVRIEEENLRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA 2498
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKK-QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2499 IQeatklKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDK--ETQGFQKSLEAERKRqLEISAEAEKLKLRVKelssAQ 2576
Cdd:pfam05262 278 NQ-----KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKasEKEAEDKELEAQKKR-EPVAEDLQKTKPQVE----AQ 347
|
....*....
gi 1655220506 2577 AKAEEEATR 2585
Cdd:pfam05262 348 PTSLNEDAI 356
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1554-1810 |
4.15e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1554 AEIQAQLET---QKQLAEghAKSVAKAELEaQELKL-----KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIR 1625
Cdd:PRK11281 39 ADVQAQLDAlnkQKLLEA--EDKLVQQDLE-QTLALldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1626 SKNQQLEEAQVSRRkLEEeihlIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE 1705
Cdd:PRK11281 116 ETLSTLSLRQLESR-LAQ----TLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1706 DELKRKSEAE------KEAARQK------------QKALDELQKHKMQAEEA---------ERRLKQAEeekvrqiKVVE 1758
Cdd:PRK11281 191 PSQRVLLQAEqallnaQNDLQRKslegntqlqdllQKQRDYLTARIQRLEHQlqllqeainSKRLTLSE-------KTVQ 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 1759 EVAQKTAATQLQAMSFsekttkleesLKKEQGTVLQLqeeAEKLRKQEEEAN 1810
Cdd:PRK11281 264 EAQSQDEAARIQANPL----------VAQELEINLQL---SQRLLKATEKLN 302
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1899-2099 |
4.23e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.54 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1899 SAEQEYIRLKAdfehaeQQRGLLDNELQRLKNEVNAAE--KQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQ 1976
Cdd:TIGR02794 47 AVAQQANRIQQ------QKKPAAKKEQERQKKLEQQAEeaEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1977 LLETEA--LKMKQLAEEAARLRSVAEEAKKQRQL-----AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKE 2049
Cdd:TIGR02794 121 AEEAKAkqAAEAKAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEA 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2050 AENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQK 2099
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2451-2766 |
4.39e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2451 EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK 2530
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAE-------KRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2531 QEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEatrfkkqadeakvrlQETEKQTTE---T 2607
Cdd:COG1340 81 DELNEKL--------NELREELDELRKELAELNKAGGSIDKLRKEIERLEWR---------------QQTEVLSPEeekE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2608 VVQKLE--TQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETAsaqqEQMEQQKAMLQQTFLTEKELllkreR 2685
Cdd:COG1340 138 LVEKIKelEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELA----EEAQELHEEMIELYKEADEL-----R 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2686 DVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2765
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEELK 288
|
.
gi 1655220506 2766 A 2766
Cdd:COG1340 289 L 289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2609-2780 |
4.41e-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: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2609 VQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETasaqqeqmeqqkamlqQTFLTEKELLLKrerDVE 2688
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL----------------EKEIKRLELEIE---EVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2689 DEKKKLQKHLeDEVNKAKALK------DEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQE 2762
Cdd:COG1579 73 ARIKKYEEQL-GNVRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....*...
gi 1655220506 2763 KLLADENKKLREKLESLE 2780
Cdd:COG1579 152 AELEAELEELEAEREELA 169
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2610-2805 |
4.54e-06 |
|
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: 53.52 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2610 QKLETQ-RLQSTREA-DDLKKAIAELEKEREKLKRDA------QELQNKSKET-----------ASAQQEQMEQQKAMLQ 2670
Cdd:TIGR02168 173 RRKETErKLERTRENlDRLEDILNELERQLKSLERQAekaeryKELKAELRELelallvlrleeLREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2671 QTFLTEKELLLKRERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKN---- 2746
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEElesk 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2747 ---KQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2805
Cdd:TIGR02168 332 ldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2208-2764 |
4.60e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2208 AEANKLKDKAEKELEKQVI-LAKEAAQKSTAA--EQKAQDVLSKNKE---DLLSQEKLRDEFENAKKLAQAAETAKekae 2281
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRtLDDQWKEKRDELngELSAADAAVAKDRselEALEDQHGAFLDADIETAAADQEQLP---- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2282 keaaLLRQKAEEAEKLKKAAED-----EAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH----KK 2352
Cdd:pfam12128 351 ----SWQSELENLEERLKALTGkhqdvTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeselRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2353 EAEQALK----QKSQVEKELGLVKLQLD------ETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDE--- 2419
Cdd:pfam12128 427 QLEAGKLefneEEYRLKSRLGELKLRLNqatatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQase 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2420 --------LLKLKVRIEEENLRLMQKN--------------KDNTQKLLAEEAEKMKSLAEEAARLSVEAEETAR----- 2472
Cdd:pfam12128 507 alrqasrrLEERQSALDELELQLFPQAgtllhflrkeapdwEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYgvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2473 -QRKTAEAELAEQRALAEKMLKEKmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQeiqqrldketQGFQKSleAE 2551
Cdd:pfam12128 587 lKRIDVPEWAASEEELRERLDKAE-EALQSAREKQAAAEEQLVQANGELEKASREETFAR----------TALKNA--RL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2552 RKRQLEISAEAEKLKLRvKELSSAQAKAEEEATRFKKQAD----EAKVRLQETEKQTTETVVQKLETQRLQSTREADDLK 2627
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKN-KALAERKDSANERLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLA 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2628 KAIAELEKEREKLKR--DAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVED-----------EKKKL 2694
Cdd:pfam12128 733 LLKAAIAARRSGAKAelKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRL 812
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2695 QKHLEDEVNKAKALKDEQQRQQKlmdEEKKKLQAIMdeavkkqKEAEAEMKNKQKEMEALEKKRLEQEKL 2764
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIA---DTKLRRAKLE-------MERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
795-887 |
4.76e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.09 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 795 HTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGVQTTGDKLLRDGHPGRKTIEAFTA 874
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1655220506 875 ALQTQWSWILQLC 887
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1408-1822 |
5.04e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 53.04 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1408 EWLIQWLREARLRQEKIEAAPvwDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAY------- 1480
Cdd:COG5185 157 ETGIIKDIFGKLTQELNQNLK--KLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEiinieea 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1481 -RALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRleDDEKASEKLKEDEKKRMAEI-QA 1558
Cdd:COG5185 235 lKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK--QFENTKEKIAEYTKSIDIKKaTE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1559 QLETQKQLAEGHAK-SVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEA--- 1634
Cdd:COG5185 313 SLEEQLAAAEAEQElEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTkes 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1635 -QVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQ----KLRDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaedelK 1709
Cdd:COG5185 393 lDEIPQNQRGYAQEILATLEDTLKAADRQIEELQrqieQATSSNEEVSKLLNELISELNKVMREADEESQ---------S 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1710 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKE- 1788
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEn 543
|
410 420 430
....*....|....*....|....*....|....*.
gi 1655220506 1789 --QGTVLQLQEEAEKLRKQEEEANKAREQAEKELET 1822
Cdd:COG5185 544 liPASELIQASNAKTDGQAANLRTAVIDELTQYLST 579
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1595-1943 |
5.34e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1595 RQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAA 1674
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1675 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQI 1754
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1755 KVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR 1834
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1835 LRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHA 1914
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
330 340
....*....|....*....|....*....
gi 1655220506 1915 EQQRGLLDNELQRLKNEVNAAEKQRRQLE 1943
Cdd:COG4372 338 ELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2441-2816 |
5.35e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2441 NTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKtAEAELAEQRalaEKMLKEKMQAIQEATKLKAEAEELQKQKNqAQ 2520
Cdd:pfam15709 170 HAERELIDKAKRRKGTKTDKTKTPKREREGKVHGE-AEAAVGKSR---ESKAEKKSELISKGKKTGAKRKRTQKERN-LE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2521 EKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQakaeeeatrfkkQADEAKVRLQET 2600
Cdd:pfam15709 245 VAAELSGPDVINSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPT------------QTFVVTGNMESE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2601 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELl 2680
Cdd:pfam15709 313 EERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRL- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2681 lkRERDVEDEKkklQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEmeaLEKKRLE 2760
Cdd:pfam15709 392 --RKQRLEEER---QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKE---LEMQLAE 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2761 QEKLLADENKKlrEKLESLEvtSKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKK 2816
Cdd:pfam15709 464 EQKRLMEMAEE--ERLEYQR--QKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2195-2408 |
5.37e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2195 AAQDEVERLKQKAAEANKLKDKAEKELEKQvilAKEAAQKSTAAEQKAQDVlskNKEDLLSQEKLRDEFENAKKLAQAAE 2274
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQ---AEELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQAALKQK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2275 TAKEKAEKEAALLRQKAEEAEK----LKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAemakh 2350
Cdd:PRK09510 133 QAEEAAAKAAAAAKAKAEAEAKraaaAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA----- 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2351 KKEAEQALKQKSQVEKELGLVKlqldETDKQKALMDEELQRVKAQVNDAVKQKAQVEN 2408
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAK----AAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1532-1729 |
5.42e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1532 QRRLEDDEKasEKLKEDEKKRMAEIQAQL--ETQKQLAEGHAKSVAKAeleaqelKLKMKEDASQRQGLAVDAEKQKQNI 1609
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAKQaaLKQKQAEEAAAKAAAAA-------KAKAEAEAKRAAAAAKKAAAEAKKK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1610 QLELTQLKnlseQEIRSKNQQLEEAQVsrrKLEEEihliriqlqttIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAEr 1689
Cdd:PRK09510 171 AEAEAAKK----AAAEAKKKAEAEAAA---KAAAE-----------AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAA- 231
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220506 1690 lrkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDEL 1729
Cdd:PRK09510 232 ---------AEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2439-2672 |
5.59e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2439 KDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQ 2518
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2519 AQEKAKKLLEDKQEIQQRLDK-----ETQGFQ------KSLEAERKRQLEISAEAEKLKlrvKELSSAQAKAEEEATRFK 2587
Cdd:COG3883 84 RREELGERARALYRSGGSVSYldvllGSESFSdfldrlSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2588 KQADEAKVRLQEtekqttetvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2667
Cdd:COG3883 161 ALKAELEAAKAE------------LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
....*
gi 1655220506 2668 MLQQT 2672
Cdd:COG3883 229 AAAAA 233
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2337-2588 |
5.68e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2337 LKQKQEADAEMAKHKKE----AEQALKQKSQVEKELGLVKLQLDETDKQKALMDE---ELQRVKAQVNDAVKQKAQVENE 2409
Cdd:COG1340 14 EEKIEELREEIEELKEKrdelNEELKELAEKRDELNAQVKELREEAQELREKRDElneKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2410 LSKVKMQMDELL-------KLKVRIE-------------EENLRLMQKNKDNTQKLlaEEAEKMKSLAEEAARLSVEAEE 2469
Cdd:COG1340 94 LDELRKELAELNkaggsidKLRKEIErlewrqqtevlspEEEKELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2470 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLE 2549
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1655220506 2550 AERKRQLEISaeaeklklRVKELSSAQAKAEEEATRFKK 2588
Cdd:COG1340 248 KLRKKQRALK--------REKEKEELEEKAEEIFEKLKK 278
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2352-2713 |
5.82e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.65 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2352 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMD-EELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE 2430
Cdd:COG5185 196 KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINiEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2431 NLRLMQKNKDNTQKLLAEEAEKMKSLAEE---------------AARLSVEAEETARQRKTAEAELAEQRALAEKMLKEK 2495
Cdd:COG5185 276 SSKRLNENANNLIKQFENTKEKIAEYTKSidikkatesleeqlaAAEAEQELEESKRETETGIQNLTAEIEQGQESLTEN 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2496 MQAIQEATK---LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEisaeaeklklRVKEL 2572
Cdd:COG5185 356 LEAIKEEIEnivGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR----------QIEEL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2573 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREaddLKKAIAELEKEREKLKRDAQELQNKSK 2652
Cdd:COG5185 426 QRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS---VRSKKEDLNEELTQIESRVSTLKATLE 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2653 ETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhlEDEVNKAKALKDEQQ 2713
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIP--ASELIQASNAKTDGQ 561
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1876-2064 |
6.03e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1876 KENAEKELEKQRTFAEQIAQQKLS-AEQEYIRLKADFEhaeqqrglldNELQRLKNEVNAAEKQRRQLEDELAKvrsEMD 1954
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE----------KELRERRNELQKLEKRLLQKEENLDR---KLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1955 ALLQMKIQAEKVSQSNTEKSKQLletealkmKQLAEEAARLRsvaeeaKKQRQLAEDEAARQRAEAEKILKEKLaainea 2034
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQEL--------EKKEEELEELI------EEQLQELERISGLTAEEAKEILLEKV------ 163
|
170 180 190
....*....|....*....|....*....|
gi 1655220506 2035 tRLKTEAEVALKAKEAENErLKRQAEDEAY 2064
Cdd:PRK12704 164 -EEEARHEAAVLIKEIEEE-AKEEADKKAK 191
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1220-1749 |
6.07e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.92 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1220 VQSELEGLKKDLNSITEKTE--EILASPQQSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKT-----IDIVIRNTKDA 1292
Cdd:pfam12128 359 LEERLKALTGKHQDVTAKYNrrRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelreqLEAGKLEFNEE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1293 EDTVKSYES----RLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEhy 1368
Cdd:pfam12128 439 EYRLKSRLGelklRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE-- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1369 rQLAGSLLERWQAVFAQidlRQRELSLLGRHMNSYKQSYEWLI---QWLRE-------------------ARLRQEKIEA 1426
Cdd:pfam12128 517 -ERQSALDELELQLFPQ---AGTLLHFLRKEAPDWEQSIGKVIspeLLHRTdldpevwdgsvggelnlygVKLDLKRIDV 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1427 aPVW--DSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqILAYRALQDpiasplkkpkmesASDNII 1504
Cdd:pfam12128 593 -PEWaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREE--TFARTALKN-------------ARLDLR 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1505 QEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEK----LKEDEKKRMAEIQAQLETQKQLAEGhAKSVA----K 1576
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKkhqaWLEEQKEQKREARTEKQAYWQVVEG-ALDAQlallK 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1577 AELEAQELKLKMKEDASQRQ------GLAVDAE---KQKQNIQLELTQLKNLS--EQEIRSKNQQLEEAQVSRR------ 1639
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWykrdlaSLGVDPDviaKLKREIRTLERKIERIAvrRQEVLRYFDWYQETWLQRRprlatq 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1640 --KLEEEIHLIRIQL-------QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE----- 1705
Cdd:pfam12128 816 lsNIERAISELQQQLarliadtKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGErlaql 895
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1655220506 1706 DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1749
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREED 939
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1426-1694 |
6.27e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1426 AAPVWDSKALKEQLTQE-KKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRAlqdpiasplkkpkmesasdnii 1504
Cdd:COG4942 12 ALAAAAQADAAAEAEAElEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1505 qeyvTLRTRYSELSTLTSQyikfILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQEL 1584
Cdd:COG4942 70 ----RIRALEQELAALEAE----LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1585 KLKMKEDASQRQGLAVDAEkqkqniqlELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD 1664
Cdd:COG4942 142 KYLAPARREQAEELRADLA--------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
250 260 270
....*....|....*....|....*....|
gi 1655220506 1665 ELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1694
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1530-1822 |
6.69e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.53 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQ-----LAEGHAKSVAKAELEAQ----ELKLKMKEDASQrQGLAV 1600
Cdd:PRK04778 116 LIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElrkslLANRFSFGPALDELEKQlenlEEEFSQFVELTE-SGDYV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1601 DAEKQKQNIQLELTQLKNLSEQ--EIRSKNQ-----QLEEAQVSRRKLEEE-IHLIRIQLQTTIKQKSTADDELQKL--R 1670
Cdd:PRK04778 195 EAREILDQLEEELAALEQIMEEipELLKELQtelpdQLQELKAGYRELVEEgYHLDHLDIEKEIQDLKEQIDENLALleE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1671 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDEL----QKHKMQAEEAERRlKQA 1746
Cdd:PRK04778 275 LDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkQSYTLNESELESV-RQL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1747 EEEKVRQIKVVEEVAQKTAAtqlQAMSFSEKTTKLEESLK------KEQgtvLQLQEEAEKLRKQEEEANKAREQAEKEL 1820
Cdd:PRK04778 354 EKQLESLEKQYDEITERIAE---QEIAYSELQEELEEILKqleeieKEQ---EKLSEMLQGLRKDELEAREKLERYRNKL 427
|
..
gi 1655220506 1821 ET 1822
Cdd:PRK04778 428 HE 429
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1718-1887 |
7.11e-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: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1718 AARQKQKALDELQKHKMQAEEAERRLKQAEEEkvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQE 1797
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1798 EAEKLRKQEEEANKARE--QAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQ 1875
Cdd:COG1579 74 RIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|..
gi 1655220506 1876 KENAEKELEKQR 1887
Cdd:COG1579 154 LEAELEELEAER 165
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2287-2794 |
7.49e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2287 LRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAakraaaeaaalKQKQEADAEMAKHKKEAEQALKQKSQVEK 2366
Cdd:PRK01156 192 LKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAM-----------DDYNNLKSALNELSSLEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2367 ELGLVKLQLDETDKQKALmDEELQRVkaqVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnlrlMQKNKDNTQKLl 2446
Cdd:PRK01156 261 AESDLSMELEKNNYYKEL-EERHMKI---INDPVYKNRNYINDYFKYKNDIENKKQILSNIDAE----INKYHAIIKKL- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2447 aEEAEKMKSLAEEAARlsvEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2526
Cdd:PRK01156 332 -SVLQKDYNDYIKKKS---RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2527 LEDKQEIQQRLDK---ETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQEtekq 2603
Cdd:PRK01156 408 KKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEE---- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2604 ttetvvqkletqrlqstrEADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKR 2683
Cdd:PRK01156 484 ------------------KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2684 ERDVEDEKKKLQKHLED------EVNKAKALKD--EQQRQQKLMDEEKKKLQAI---MDEAVKKQKEAEAEMKNKQKEME 2752
Cdd:PRK01156 546 DKYEEIKNRYKSLKLEDldskrtSWLNALAVISliDIETNRSRSNEIKKQLNDLesrLQEIEIGFPDDKSYIDKSIREIE 625
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1655220506 2753 AlEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2794
Cdd:PRK01156 626 N-EANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSII 666
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2337-2680 |
8.79e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2337 LKQK-QEADAEMAKHKKEAEQALKQKSQVEKElglVKLQLDETDKQKALMDE------ELQRVKAQVNDAVKQ--KAQVE 2407
Cdd:PRK10929 28 ITQElEQAKAAKTPAQAEIVEALQSALNWLEE---RKGSLERAKQYQQVIDNfpklsaELRQQLNNERDEPRSvpPNMST 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2408 NELSKvkmqmdELLKLKVRIEEENlRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAL 2487
Cdd:PRK10929 105 DALEQ------EILQVSSQLLEKS-RQAQQEQDRAREI-SDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2488 AekmlkekMQAiqEATKLKAEAEEL---QKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE-AE 2563
Cdd:PRK10929 177 A-------LQA--ESAALKALVDELelaQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2564 KL-------------KLRV-KELSSA---QAKAEEEATRFKKQADEAKVRLQETEKQTTETvVQKL-------ETQRLQS 2619
Cdd:PRK10929 248 LLaeqsgdlpksivaQFKInRELSQAlnqQAQRMDLIASQQRQAASQTLQVRQALNTLREQ-SQWLgvsnalgEALRAQV 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2620 TREAD-----DLKKAIAELEKER-------EKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtflTEKELL 2680
Cdd:PRK10929 327 ARLPEmpkpqQLDTEMAQLRVQRlryedllNKQPQLRQIRQADGQPLTAEQNRILDAQLR-------TQRELL 392
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2463-2801 |
8.98e-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: 52.06 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2463 LSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKL----------KAEAEELQK--------QKNQAQEKAK 2524
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELdalavaekagQAEAEGLRAalagaemvRKNLEEGSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2525 KLLEDKQEIQQRLDKETQGFQKSLE--AERKRQLEISAEAEKLKL--RVKELSSAQAKAEEEATRFKKQAD--EAKVRLQ 2598
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEALSslTSKAEGLEKSLNSLETKRagEAKQLAEAQKEAELLRKQLSKTQEelEAQVTLV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2599 ET-EKQTTETVVQKLETQRLQSTREadDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEK 2677
Cdd:pfam07111 221 ESlRKYVGEQVPPEVHSQTWELERQ--ELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2678 EL------LLKRERD-VEDEKKKLQKHLEDEVNKAKALKDE-QQRQQKLMDEEKKklQAIMDEAVK-KQKEAEAE---MK 2745
Cdd:pfam07111 299 EFpkkcrsLLNRWREkVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQVTSQSQE--QAILQRALQdKAAEVEVErmsAK 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2746 NKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVP 2801
Cdd:pfam07111 377 GLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIP 432
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2392-2755 |
9.48e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2392 VKAQVNDAVKQKAQVENELSKVKMQMDELLKlkvriEEENLRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETA 2471
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIR-----DIQAIAGIMKIRPEFTKL-QQEFNTLESAELRLSHLHFGYKSDE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2472 RQrktaEAELAEQRALAEKMLKEKMQAiqeatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQK----S 2547
Cdd:pfam12128 272 TL----IASRQEERQETSAELNQLLRT------LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDadieT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2548 LEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVvqkLETQRLQSTREADDLK 2627
Cdd:pfam12128 342 AAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI---REARDRQLAVAEDDLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2628 KAIAELEKEREKLKRDAQELQNKSKETAsaqqeqmEQQKAMLQQTFLTEKELLLKRERDvedekkklqkhleDEVNKAKA 2707
Cdd:pfam12128 419 ALESELREQLEAGKLEFNEEEYRLKSRL-------GELKLRLNQATATPELLLQLENFD-------------ERIERARE 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2708 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALE 2755
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2371-2619 |
9.66e-06 |
|
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: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2371 VKLQLDETDKQKALMDEELQRVKAQVNDAvkqkaqvENELSKVKMQMDEllklkVRIEEENLRLMQKNKDNTQKLLAEEA 2450
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFRQKNGL-----VDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2451 EkmksLAEEAARLSvEAEETARQRKTAEAELAEQRALAekmlkekmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK 2530
Cdd:COG3206 234 E----LAEAEARLA-ALRAQLGSGPDALPELLQSPVIQ--------QLRAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2531 QEIQQRLDKETQGFQKSLEAERkrqleisaeaEKLKLRVKELSSAQAKAEEEATRFKKQADEAKV--RLQETEKQTTETV 2608
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAEL----------EALQAREASLQAQLAQLEARLAELPELEAELRRleREVEVARELYESL 370
|
250
....*....|.
gi 1655220506 2609 VQKLETQRLQS 2619
Cdd:COG3206 371 LQRLEEARLAE 381
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1628-1816 |
9.92e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.38 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1628 NQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKnAEDE 1707
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK-QAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1708 LKRKSEAEKEaarqkQKALDELQKhkmQAEEaERRLKQAEEEKVRQikvvEEVAQKTAATQLQAMSFSEKTTKLEESLKK 1787
Cdd:TIGR02794 132 AKAKAEAEAE-----RKAKEEAAK---QAEE-EAKAKAAAEAKKKA----EEAKKKAEAEAKAKAEAEAKAKAEEAKAKA 198
|
170 180
....*....|....*....|....*....
gi 1655220506 1788 EQGTVLQLQEEAEKLRKQEEEANKAREQA 1816
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4113-4151 |
1.03e-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: 1.03e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1655220506 4113 YLEGVSCIAGVFVESTKERLSIYQAMKKNMIRPGTAFEL 4151
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1389-1940 |
1.06e-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: 52.05 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1389 RQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLT---QEKKLLEEIEKNKDQIENCQKDAKA 1465
Cdd:pfam05557 25 HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrLKKKYLEALNKKLNEKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1466 YIDSLKD--YEFQILAYRALQDPIASPLKKPKMESASDNI---IQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEK 1540
Cdd:pfam05557 105 VISCLKNelSELRRQIQRAELELQSTNSELEELQERLDLLkakASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1541 ASEKLK--EDEKKRMAEIQAQLETQ----KQLAEGHA-KSVAKAELEAQELKLKMKEDAsqrQGLAVDAEKQKQNIQLEL 1613
Cdd:pfam05557 185 DSEIVKnsKSELARIPELEKELERLrehnKHLNENIEnKLLLKEEVEDLKRKLEREEKY---REEAATLELEKEKLEQEL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1614 TQLKNLSEQ---EIRSK---NQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1687
Cdd:pfam05557 262 QSWVKLAQDtglNLRSPedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1688 ERLRKQVNEETQKK-------KNAEDELKrKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1760
Cdd:pfam05557 342 RRLQRRVLLLTKERdgyrailESYDKELT-MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1761 AQKTAATQLQAMSFSEKTTKLE-ESLKKEQGTvLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKAnealrLRLRAEE 1839
Cdd:pfam05557 421 ERELQALRQQESLADPSYSKEEvDSLRRKLET-LELERQRLREQKNELEMELERRCLQGDYDPKKTKV-----LHLSMNP 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1840 EAQRKSLAQEEAEKQKTEAERdakkkakaeeaALKQKENAEKELEKQRTFAEQIAQQklsAEQEYIRLKADFEHAEQQrg 1919
Cdd:pfam05557 495 AAEAYQQRKNQLEKLQAEIER-----------LKRLLKKLEDDLEQVLRLPETTSTM---NFKEVLDLRKELESAELK-- 558
|
570 580
....*....|....*....|.
gi 1655220506 1920 lldneLQRLKNEVNAAEKQRR 1940
Cdd:pfam05557 559 -----NQRLKEVFQAKIQEFR 574
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2447-2672 |
1.12e-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: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2447 AEEAEKMKSLAEEAARLSVEAEETARQRKTAEAE--LAEQRALAEKMLKEKMQAIQE------ATKLKAEAEELQKQKNQ 2518
Cdd:COG3206 144 SPDPELAAAVANALAEAYLEQNLELRREEARKALefLEEQLPELRKELEEAEAALEEfrqkngLVDLSEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2519 AQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLEISAEAEKLKLRvKELSSAQAKAEEEATRFK------KQADE 2592
Cdd:COG3206 224 LESQLAEARAELAEAEARLAA----LRAQLGSGPDALPELLQSPVIQQLR-AQLAELEAELAELSARYTpnhpdvIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2593 AKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQ--EQMEQQKAMLQ 2670
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARElyESLLQRLEEAR 378
|
..
gi 1655220506 2671 QT 2672
Cdd:COG3206 379 LA 380
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1667-1853 |
1.13e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1667 QKLRDQAAEAEKVRKaaqeEAERLRKQVNEETQKKKNAEDELKRKSEAE--------KEAARQKQKALDELQKHKM---- 1734
Cdd:PRK00409 530 RELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQKGGYasvk 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1735 --QAEEAERRLKQAEEEKVRQIKVveevaQKTAATQLQA------MSFSEKTTKLEESLKKEqgtvLQLQEEAEKLR--- 1803
Cdd:PRK00409 606 ahELIEARKRLNKANEKKEKKKKK-----QKEKQEELKVgdevkyLSLGQKGEVLSIPDDKE----AIVQAGIMKMKvpl 676
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 1804 KQEEEANKAREQAEKELETWRLKANEA---LRLR-LRAEEeaqrkslAQEEAEK 1853
Cdd:PRK00409 677 SDLEKIQKPKKKKKKKPKTVKPKPRTVsleLDLRgMRYEE-------ALERLDK 723
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2466-2606 |
1.20e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2466 EAEETARQRKTAEAELAEQRalaekmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD-----KE 2540
Cdd:COG1579 18 ELDRLEHRLKELPAELAELE-------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2541 TQGFQKSLEAERKRQ-------LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE 2606
Cdd:COG1579 91 YEALQKEIESLKRRIsdledeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2338-2525 |
1.25e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2338 KQKQEADAEMAKHKKEAEQA--LKQKSQVE----KELGLVKLQLDETDKQKAlmDEELQRVKAQVNDAVKQKAQVENELS 2411
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEqerlKQLEKERLAAQEQKKQAE--EAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2412 KVKMQMDELLKLKVRIEEENLRL----MQKNKDNTQKLLAEEAEKMKSLAEEAARlsveAEETARQRKTAEaelAEQRAL 2487
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKaeaeAAKKAAAEAKKKAEAEAAAKAAAEAKKK----AEAEAKKKAAAE---AKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1655220506 2488 AEKmlkeKMQAIQEATKLKAEAEELQKQKNQAQEKAKK 2525
Cdd:PRK09510 221 AEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1571-1765 |
1.25e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1571 AKSVAKAEL-EAQELKLKMKEDASQRqglavdAEKQKQNIQL----ELTQLKNLSEQEIRSKNQQLEeaqvsrrkleeei 1645
Cdd:PRK12704 25 RKKIAEAKIkEAEEEAKRILEEAKKE------AEAIKKEALLeakeEIHKLRNEFEKELRERRNELQ------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1646 hliriQLQTTIKQK-STADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQkqk 1724
Cdd:PRK12704 86 -----KLEKRLLQKeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKE--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1655220506 1725 aldelqkhkMQAEEAErrlKQAEEEKVRQIKVVEEVAQKTA 1765
Cdd:PRK12704 158 ---------ILLEKVE---EEARHEAAVLIKEIEEEAKEEA 186
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1844-2045 |
1.25e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1844 KSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN 1923
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1924 ELQ--RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALK-------MKQLAEEAAR 1994
Cdd:COG4717 124 LLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslateeeLQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 1995 LRSVAEEAKKQRQLAEDEAARQRAEAEKiLKEKLAAINEATRLKTEAEVAL 2045
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQ-LENELEAAALEERLKEARLLLL 253
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1575-1771 |
1.28e-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: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1575 AKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEI-HLIRIQ-- 1651
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELgERARALyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1652 -------LQTTIKQKSTAD-----DELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAA 1719
Cdd:COG3883 98 sggsvsyLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 1720 RQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQA 1771
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2652-2794 |
1.31e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2652 KETASAQQEQMEQQ-KAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKalKDEQQRQQKLMDEE---KKKLQ 2727
Cdd:PRK12704 26 KKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEenlDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2728 AImdeaVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLrEKLESL--------------EVTSKQAASKTKEI 2793
Cdd:PRK12704 104 LL----EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaeeakeillekveEEARHEAAVLIKEI 178
|
.
gi 1655220506 2794 E 2794
Cdd:PRK12704 179 E 179
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2486-2744 |
1.33e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2486 ALAEKMLKEKMQAIQEATK-----LKAEAEELQKQKNQAQEKAKKLLEDKQEIQqrLDKETQGFQKSLEAERKRQLEISA 2560
Cdd:COG3206 156 ALAEAYLEQNLELRREEARkalefLEEQLPELRKELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2561 EAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvvQKLETQRLQSTREADDLKkaiaELEKEREKL 2640
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE------AELAELSARYTPNHPDVI----ALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2641 KRDAQELQNKSKETASAQQEQMEQQKAMLQQTfltekelllkrerdvedekkklqkhLEDEVNKAKALKDEQQRQQKLMd 2720
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQ-------------------------LAQLEARLAELPELEAELRRLE- 357
|
250 260
....*....|....*....|....
gi 1655220506 2721 EEKKKLQAIMDEAVKKQKEAEAEM 2744
Cdd:COG3206 358 REVEVARELYESLLQRLEEARLAE 381
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1794-2068 |
1.36e-05 |
|
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: 50.81 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1794 QLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQktEAERdakkkakAEEAAL 1873
Cdd:pfam15558 43 KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQ--ENQR-------QEKLER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1874 KQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEM 1953
Cdd:pfam15558 114 ARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1954 DALLqMKIQAEKVSQSNTEKSKQLLETEALKMKQLA----EEAARLRSVAEEAKKQRQ--------LAEDEAARQRAEAE 2021
Cdd:pfam15558 194 EELL-RRLSLEQSLQRSQENYEQLVEERHRELREKAqkeeEQFQRAKWRAEEKEEERQehkealaeLADRKIQQARQVAH 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1655220506 2022 KILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKL 2068
Cdd:pfam15558 273 KTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKE 319
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2470-2793 |
1.37e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.00 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2470 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK-LLEDKQEI----QQRL-DKETQG 2543
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRfSLLKKETIylqsAQRVeLAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2544 FQKSLEAERKRQL-EISAEAEKLKLRVK--ELSSAQAKAE---EEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRL 2617
Cdd:COG5022 885 QELKIDVKSISSLkLVNLELESEIIELKksLSSDLIENLEfktELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVES 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2618 QSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEqqkamlqqtfLTEKELLLKRERDVEDEKKKLQKH 2697
Cdd:COG5022 965 KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGA----------LQESTKQLKELPVEVAELQSASKI 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2698 LEDEVNKAKALKDEQQrQQKLMDEEKKKLQAIMdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLE 2777
Cdd:COG5022 1035 ISSESTELSILKPLQK-LKGLLLLENNQLQARY-KALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPA 1112
|
330
....*....|....*.
gi 1655220506 2778 SLEVTSKQAASKTKEI 2793
Cdd:COG5022 1113 NVLQFIVAQMIKLNLL 1128
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1593-1803 |
1.46e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1593 SQRQGLAVD----AEKQKQNIQLELTQL-KNLSEQEIRSKnQQLEEAQvsrrKLEEEIHLIRIQLQttiKQKSTADDELQ 1667
Cdd:PRK00409 494 AKRLGLPENiieeAKKLIGEDKEKLNELiASLEELERELE-QKAEEAE----ALLKEAEKLKEELE---EKKEKLQEEED 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1668 KLRDQAA-EAEKVRKAAQEEAERLRKQVNEETQKKKNAedelkRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQA 1746
Cdd:PRK00409 566 KLLEEAEkEAQQAIKEAKKEADEIIKELRQLQKGGYAS-----VKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 1747 EEEKVRQIK----VVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLR 1803
Cdd:PRK00409 641 DEVKYLSLGqkgeVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1892-2109 |
1.47e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.61 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1892 QIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRqlEDELAKVrsemdALLQMKIQAEKVSQSNT 1971
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ--AEQAAKQ-----AEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1972 EKSKQLletEALKMKQLAEEAAR------LRSVAEEAKKQRQLAEDEA---ARQRAEAE-KILKEKLAAINEATRLKTEA 2041
Cdd:TIGR02794 131 EAKAKA---EAEAERKAKEEAAKqaeeeaKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEaKAKAEEAKAKAEAAKAKAAA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2042 EVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQK 2109
Cdd:TIGR02794 208 EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1720-1904 |
1.48e-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: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1720 RQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVvEEVAQKTAATQLQAmsfsekttkleeslKKEQGTVLQLQEEA 1799
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAI-AQANREAEEAELEQ--------------EREIETARIAEAEA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1800 EKLRKQEE---EANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK 1876
Cdd:COG2268 245 ELAKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324
|
170 180
....*....|....*....|....*....
gi 1655220506 1877 ENAEKELEKQRTFAEQIAQQKLS-AEQEY 1904
Cdd:COG2268 325 AEAEAEAIRAKGLAEAEGKRALAeAWNKL 353
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1214-1757 |
1.63e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1214 TAEQMK--VQSELEGLKKDLNSITEKTEEILASPQQSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKTI--------- 1282
Cdd:TIGR00606 602 SLEQNKnhINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLtdenqsccp 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1283 --DIVIRNTKDAEDTVKSYESRLRDV-SKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHS 1359
Cdd:TIGR00606 682 vcQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1360 ERDAELEHYRQLAGSL---LERWQAVFAQIDLRQRelslLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapvwdSKALK 1436
Cdd:TIGR00606 762 RLKNDIEEQETLLGTImpeEESAKVCLTDVTIMER----FQMELKDVERKIAQQAAKLQGSDLDRTVQQV-----NQEKQ 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1437 EQLTQEKKLLEEIEKNKDQIENCQKDA---KAYIDSLKDYEFQILAYRALQDPIAsplkkpkmesasdniiQEYVTLRTR 1513
Cdd:TIGR00606 833 EKQHELDTVVSKIELNRKLIQDQQEQIqhlKSKTNELKSEKLQIGTNLQRRQQFE----------------EQLVELSTE 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1514 YSELSTLTSQYIKFILETQRRLEDDEKASEKL--KEDEKKRMAEIQAQLetqkqlaeghaksvakaeleaqelklkMKED 1591
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELisSKETSNKKAQDKVND---------------------------IKEK 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1592 ASQRQGLAVDAEKQkqnIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRD 1671
Cdd:TIGR00606 950 VKNIHGYMKDIENK---IQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKR 1026
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1672 QAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRkseaekeAARQKQKALDELQKHKMQAEEAERRLKQAE---- 1747
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKRNHVLALGRQKGYEKEIKHFKKELREPQfrda 1099
|
570
....*....|
gi 1655220506 1748 EEKVRQIKVV 1757
Cdd:TIGR00606 1100 EEKYREMMIV 1109
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1454-1727 |
1.65e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 51.16 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1454 DQIENCQKDAKAYIDSLKDYEFQ--------ILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYI 1525
Cdd:pfam05262 79 DHILNLRRILAGYLMAAYGYERSdaetiakfITIYNAVYRGDLDYFKEFYKEVVTKSLTKENAGLARRYDQWPGKTQIVI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1526 KFileTQRRLED-----------DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKsvaKAELEAQELKLKMKEDASQ 1594
Cdd:pfam05262 159 PL---KKNILSGnvsdvdtdsisDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAK---RAQQLKEELDKKQIDADKA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1595 RQGLAV---DAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliriQLQTTIKQKstaDDELQKLRD 1671
Cdd:pfam05262 233 QQKADFaqdNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIE-------KAQIEIKKN---DEEALKAKD 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 1672 QAAEAEKvRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALD 1727
Cdd:pfam05262 303 HKAFDLK-QESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1923-2083 |
1.76e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1923 NELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQA-EKVSQSNTEKSKQLLET---EALKMKQLAEEAARLRSV 1998
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQlEKERLAAQEQKKQAEEAakqAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1999 AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKH 2078
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
....*
gi 1655220506 2079 DIQEK 2083
Cdd:PRK09510 225 AAAAK 229
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1620-2107 |
1.79e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1620 SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLrKQVNEETQ 1699
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-SMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1700 KKKNAEDELKRkseAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEekvrQIKVVEEVAQKTAATQLQAMSFSEKTT 1779
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA----EINKYHAIIKKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1780 KLEEsLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR------LRAEEEAQRKSLAQEEAEK 1853
Cdd:PRK01156 347 RYDD-LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpdaIKKELNEINVKLQDISSKV 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1854 QKTEAERDAKKKAKAEEAALKQKENAEKEL---------EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNE 1924
Cdd:PRK01156 426 SSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1925 LQRL-KNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKqlLETEALKMKqlaeeaarlRSVAEEAK 2003
Cdd:PRK01156 506 KEYLeSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS--LKLEDLDSK---------RTSWLNAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2004 KQRQLAEDEAARQRAEaekilkEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAY----QRKLLEDQAAQhKHD 2079
Cdd:PRK01156 575 AVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQENKIL-IEK 647
|
490 500
....*....|....*....|....*...
gi 1655220506 2080 IQEKITQLQSSSVSELDRQKNIVEETLR 2107
Cdd:PRK01156 648 LRGKIDNYKKQIAEIDSIIPDLKEITSR 675
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3244-3277 |
1.82e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.82e-05
10 20 30
....*....|....*....|....*....|....
gi 1655220506 3244 LLEAQAATGFVIDPVKNEKVSVDDAVKSGLVGPE 3277
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2691-2800 |
1.86e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2691 KKKLQKHLEDEVNKAKALKDEQQRQQKlmDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENK 2770
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAE--AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|
gi 1655220506 2771 KLREKLESLEVTSKQAASKTKEIEVQTDKV 2800
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEEL 133
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4111-4148 |
1.97e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.97e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220506 4111 KKYLEGVSCIAGVFVESTKERLSIYQAMKKNMIRPGTA 4148
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1551-1838 |
2.04e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1551 KRMAEIQAQLEtqkQLAEGHAKSVAKaeleaqelKLKMKEDASQRQGLAvdaEKQKQNIQLELT----QLKNLSEQEIRS 1626
Cdd:COG2268 116 RDPEEIEELAE---EKLEGALRAVAA--------QMTVEELNEDREKFA---EKVQEVAGTDLAknglELESVAITDLED 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1627 KNQQLEeAQvSRRKLEEeihLIRIQlqttIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKnAED 1706
Cdd:COG2268 182 ENNYLD-AL-GRRKIAE---IIRDA----RIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAK-KKA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1707 ELKRKSEAEKeaArqkqkaldelqkhkmqaeEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsekttkLEESLK 1786
Cdd:COG2268 252 EERREAETAR--A------------------EAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-------AEREEA 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 1787 KEQGTVlQLQEEAEKLRKQEE---EANKAREQAEKELETWRLKA------NEALRLRLRAE 1838
Cdd:COG2268 305 ELEADV-RKPAEAEKQAAEAEaeaEAEAIRAKGLAEAEGKRALAeawnklGDAAILLMLIE 364
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2991-3027 |
2.09e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 2.09e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1655220506 2991 TKFLDVQLATGGIIDPVNSHRLPLQTAYKQGQFDPDM 3027
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1433-1822 |
2.10e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 50.62 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1433 KALKEQLTQEKKLLEEIEKNKDQIENCQKdakayidslkdyefQILAYRALQDPIASPLkkpkmesasDNIIQEYVTLRT 1512
Cdd:pfam06160 107 EELDELLESEEKNREEVEELKDKYRELRK--------------TLLANRFSYGPAIDEL---------EKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1513 RYSELSTlTSQYIK---FILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtqkQLAEGHAksvakaELEAQELKLKmk 1589
Cdd:pfam06160 164 QFEELTE-SGDYLEareVLEKLEEETDALEELMEDIPPLYEELKTELPDQLE---ELKEGYR------EMEEEGYALE-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1590 edasqrqglavdaekqKQNIQLELTQLKN-LSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQK 1668
Cdd:pfam06160 232 ----------------HLNVDKEIQQLEEqLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1669 LRDQAAEAEKVRKAAQEEAERLRK--QVNEEtqkkknaedelkrkseaEKEAARQKQKALDELQKhkmqaeeaerrlkqa 1746
Cdd:pfam06160 296 IEDYLEHAEEQNKELKEELERVQQsyTLNEN-----------------ELERVRGLEKQLEELEK--------------- 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 1747 eeekvRQIKVVEEVAQKTAA-TQLQAMsFSEKTTKLEEsLKKEQgtvLQLQEEAEKLRKQEEEANKAREQAEKELET 1822
Cdd:pfam06160 344 -----RYDEIVERLEEKEVAySELQEE-LEEILEQLEE-IEEEQ---EEFKESLQSLRKDELEAREKLDEFKLELRE 410
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2339-2603 |
2.35e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 50.72 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2339 QKQEAD-AEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKAlmdeelQRVKAQVNDAVKQ-----KAQVENELSK 2412
Cdd:PRK05035 441 IEQEKKkAEEAKARFEARQARLEREKAARE---------ARHKKAA------EARAAKDKDAVAAalarvKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2413 VKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSlAEEAARLSVEAEETARQRKTAEAELAE-----QRAL 2487
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKA-AVAAAIARAKAKKAAQQAANAEAEEEVdpkkaAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2488 AEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfqKSLEAERKRQLEISAEAEKLKL 2567
Cdd:PRK05035 585 AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEP-----EEPVDPRKAAVAAAIARAKARK 659
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655220506 2568 RVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2603
Cdd:PRK05035 660 AAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1622-1892 |
2.41e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1622 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEaekVRKAAQEEAERlRKQVNEETQKK 1701
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---LREEAQELREK-RDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1702 KNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE-------KVRQIKVVEEVAQKtaATQLQAMsf 1774
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqqtevlsPEEEKELVEKIKEL--EKELEKA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1775 sEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ----EEEANKAREQ---AEKELETWRLKANEALRLRLRAEEEAQRksLA 1847
Cdd:COG1340 153 -KKALEKNEKLKELRAELKELRKEAEEIHKKikelAEEAQELHEEmieLYKEADELRKEADELHKEIVEAQEKADE--LH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1655220506 1848 QEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQ 1892
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
202-321 |
2.43e-05 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 47.35 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 202 QKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRNVRLPrekgrmrFHKLQN 272
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTISEN 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1655220506 273 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 321
Cdd:cd21323 97 LNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1796-1931 |
2.46e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1796 QEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKS---LAQEEAEKQKTEAERDakkKAKAEEAA 1872
Cdd:COG2268 210 RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETaraEAEAAYEIAEANAERE---VQRQLEIA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 1873 LKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADfEHAEQQ----RGLLDNELQRLKNE 1931
Cdd:COG2268 287 EREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE-AEAEAEairaKGLAEAEGKRALAE 348
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2524-2790 |
2.65e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.46 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2524 KKLLEDKQEIQQR---LDKetqgfQKSLEAERKRQLEisAEAEKLKLRVKELSSAQAKAEEEATRF---KKQADEakvrL 2597
Cdd:pfam05622 3 SEAQEEKDELAQRcheLDQ-----QVSLLQEEKNSLQ--QENKKLQERLDQLESGDDSGTPGGKKYlllQKQLEQ----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2598 QEtekqttetvvqklETQRLQSTReaDDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE-----QMEQQKAMLQQT 2672
Cdd:pfam05622 72 QE-------------ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEmdilrESSDKVKKLEAT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2673 FLTEKELL-----LKR------ERDVEDEKKKLQkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKkqkeAE 2741
Cdd:pfam05622 137 VETYKKKLedlgdLRRqvklleERNAEYMQRTLQ--LEEELKKANALRGQLETYKRQVQELHGKLSEESKKADK----LE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1655220506 2742 AEMKNKQKEMEALEKkrlEQEKLLAdENKKLREKLESLEVTSKQAASKT 2790
Cdd:pfam05622 211 FEYKKLEEKLEALQK---EKERLII-ERDTLRETNEELRCAQLQQAELS 255
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2442-2751 |
2.72e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2442 TQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQE 2521
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2522 KAKKLLEDKQEIQQRLdKETQGFQKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETE 2601
Cdd:COG4372 102 ELESLQEEAEELQEEL-EELQKERQDLEQQRK---QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2602 KQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLL 2681
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2682 KRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM 2751
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2404-2856 |
2.74e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2404 AQVENELSKVKMQMDELLKLKVRIEEENLRL--MQKNKDNTQKLLAEE-AEKMKSLAEEAARLSVE--AEETARQRKTAE 2478
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIasRQEERQETSAELNQLlRTLDDQWKEKRDELNGElsAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2479 AELAEQRALA------EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEA-- 2550
Cdd:pfam12128 324 LEALEDQHGAfldadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKir 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2551 -ERKRQL-EISAEAEKLK--LRvKELSSAQAKAEEEATRFKKQADEAKVRL---QETEKQTTETVVQKLETQRLQSTREA 2623
Cdd:pfam12128 404 eARDRQLaVAEDDLQALEseLR-EQLEAGKLEFNEEEYRLKSRLGELKLRLnqaTATPELLLQLENFDERIERAREEQEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2624 -----DDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQ--------------QKAMLQQTF--LTEKELLLK 2682
Cdd:pfam12128 483 anaevERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflrkEAPDWEQSIgkVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2683 RERDVE------------------------DEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK 2738
Cdd:pfam12128 563 TDLDPEvwdgsvggelnlygvkldlkridvPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2739 EAEAEMKNKQKEMEAL----EKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMTT---- 2810
Cdd:pfam12128 643 FARTALKNARLDLRRLfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAywqv 722
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2811 VETTKKVFNGSV---------------EAVKKDGASPLAFEGIRESVPAERLLEIGVLTKK 2856
Cdd:pfam12128 723 VEGALDAQLALLkaaiaarrsgakaelKALETWYKRDLASLGVDPDVIAKLKREIRTLERK 783
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4571-4608 |
2.81e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.81e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220506 4571 QRFLEVQYLTGGLIEPDTTGRVSIDEAVKKGSLDARTA 4608
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
197-317 |
2.88e-05 |
|
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: 46.52 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 197 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDLVRNVRLPREKGRMRfhKLQNVQIA 276
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLENCNYA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220506 277 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 317
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1836-2037 |
2.94e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1836 RAEEEAQRKSLAQEEAEKQKTEAERDAkkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAE 1915
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQER------------LKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1916 QQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAllqMKIQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARL 1995
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1655220506 1996 RSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRL 2037
Cdd:PRK09510 218 KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1671-2016 |
2.96e-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: 50.34 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1671 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE---AEKEAARQKQKALDELQKHKMQAEEAERRLKqaE 1747
Cdd:pfam15709 218 EKKSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVINSKETedaSERGAFSSDSVVEDPWLSSKYDAEESQVSID--G 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1748 EEKVRQIKVV-------EEVAQKTAATQLQAMSFSEKTTKleESLKKEQGTVLQLQEEaeklRKQEEEANKAREQAEKEL 1820
Cdd:pfam15709 296 RSSPTQTFVVtgnmeseEERSEEDPSKALLEKREQEKASR--DRLRAERAEMRRLEVE----RKRREQEEQRRLQQEQLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1821 ETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEaerdakkkakaeeaalkqkenaekelEKQRTFAEQIAQQKLSA 1900
Cdd:pfam15709 370 RAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEE--------------------------ERKQRLQLQAAQERARQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1901 EQEYIRLKAdfehAEQQRGLLDNELQRLknevnAAEKQRR-QLEDELAKvrsEMDALLQMKIQAEKVSQSNTEKSKQLLE 1979
Cdd:pfam15709 424 QQEEFRRKL----QELQRKKQQEEAERA-----EAEKQRQkELEMQLAE---EQKRLMEMAEEERLEYQRQKQEAEEKAR 491
|
330 340 350
....*....|....*....|....*....|....*..
gi 1655220506 1980 TEALKMKQLAEEAARLrsVAEEAKKQRQlaedEAARQ 2016
Cdd:pfam15709 492 LEAEERRQKEEEAARL--ALEEAMKQAQ----EQARQ 522
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2489-2667 |
3.11e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2489 EKMLKEKMQAI---QEATKLKA-EAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEK 2564
Cdd:pfam05262 184 EALREDNEKGVnfrRDMTDLKErESQEDAKRAQQLKEELDKKQIDADKAQQKADFA----QDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2565 lklrvkelssAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvQKLETQRLQSTREADDLKKAIAELEKEREKLKRDA 2644
Cdd:pfam05262 260 ----------LPKPADTSSPKEDKQVAENQKREIEKAQIEIK---KNDEEALKAKDHKAFDLKQESKASEKEAEDKELEA 326
|
170 180
....*....|....*....|...
gi 1655220506 2645 QElqnKSKETASAQQEQMEQQKA 2667
Cdd:pfam05262 327 QK---KREPVAEDLQKTKPQVEA 346
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1631-2610 |
3.49e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1631 LEEAQVSRRKLEEEIHLIriqlqtTIKQKSTADD------ELQKLRDQAAEAEKVRKAAqeeaerlRKQVNEETQKKKNA 1704
Cdd:COG3096 245 LEAIRVTQSDRDLFKHLI------TEATNYVAADymrhanERRELSERALELRRELFGA-------RRQLAEEQYRLVEM 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1705 EDELKRKSEAEKEAARQKQKALDELQKHKM---QAEEAERR---LKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKT 1778
Cdd:COG3096 312 ARELEELSARESDLEQDYQAASDHLNLVQTalrQQEKIERYqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1779 TKL-------EESLKKEQGTVLQLQEEAEKLRKQE---EEANKAREQAEKELETWRLKANEALRLRLRAEeeaQRKSLAQ 1848
Cdd:COG3096 392 DSLksqladyQQALDVQQTRAIQYQQAVQALEKARalcGLPDLTPENAEDYLAAFRAKEQQATEEVLELE---QKLSVAD 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1849 EEAEkqkteaerdakkkakaeeaalkQKENAEKELEK-----QRTFAEQIAQQKLSaeqEYIRLKADFEHAEQQRGLLdN 1923
Cdd:COG3096 469 AARR----------------------QFEKAYELVCKiagevERSQAWQTARELLR---RYRSQQALAQRLQQLRAQL-A 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1924 ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKvsqsntekskqlletealkmkQLAEEAARLRSVAEEAK 2003
Cdd:COG3096 523 ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEA---------------------QLEELEEQAAEAVEQRS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2004 KQRQlAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAyQRKLLEDQAAQHKHDIQEK 2083
Cdd:COG3096 582 ELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER-EATVERDELAARKQALESQ 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2084 ITQLQSSSVSELDRQKNIVEetlRQKKVVEEEIhiirinFERASKEK-----------------SDLEVELKKLKGIADe 2146
Cdd:COG3096 660 IERLSQPGGAEDPRLLALAE---RLGGVLLSEI------YDDVTLEDapyfsalygparhaivvPDLSAVKEQLAGLED- 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2147 tqkSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAaeeeaaRQ-RKAAQDEVERLKQKAAEANKLKDKAEKElekqv 2225
Cdd:COG3096 730 ---CPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSD------RQwRYSRFPEVPLFGRAAREKRLEELRAERD----- 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2226 ILAKEAAQksTAAEQKAQDVLSKNKEDLLSQEkLRDEFEnakklaqaaetakekaekeaallrqkaeeaeklkkaAEDEA 2305
Cdd:COG3096 796 ELAEQYAK--ASFDVQKLQRLHQAFSQFVGGH-LAVAFA------------------------------------PDPEA 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2306 AKQAKAQK--DAERlrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKA 2383
Cdd:COG3096 837 ELAALRQRrsELER---------------------ELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRL 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2384 lmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvR---IEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEA 2460
Cdd:COG3096 896 ---EELREELDAAQEAQAFIQQHGKALAQLEPLVAVL-----QsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRR 967
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2461 ARLSVEaeetarqrkTAEAELAEQRALAEKmLKEKM-QAIQEATKLKAEAEELQK---QKNQAQEKAKKLLEDKQEIQQR 2536
Cdd:COG3096 968 PHFSYE---------DAVGLLGENSDLNEK-LRARLeQAEEARREAREQLRQAQAqysQYNQVLASLKSSRDAKQQTLQE 1037
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2537 LDKETQ--GFQKSLEAE---RKRQLEISAEAEKLKLRVKELssaqakaEEEATRFKKQADEAKVRLQETEK---QTTETV 2608
Cdd:COG3096 1038 LEQELEelGVQADAEAEeraRIRRDELHEELSQNRSRRSQL-------EKQLTRCEAEMDSLQKRLRKAERdykQEREQV 1110
|
..
gi 1655220506 2609 VQ 2610
Cdd:COG3096 1111 VQ 1112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1875-2060 |
3.56e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1875 QKENAEKELEKqrtfAEQiAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMD 1954
Cdd:COG3206 183 QLPELRKELEE----AEA-ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1955 ALLQmkiqaekvSQSNTEKSKQLLETEAlkmkQLAEEAARL-------RSVAEEAKKQRQLAEDEAARQRAEAE---KIL 2024
Cdd:COG3206 258 ELLQ--------SPVIQQLRAQLAELEA----ELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEaelEAL 325
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220506 2025 KEKLAAINEA-TRLKTEAEvALKAKEAENERLKRQAE 2060
Cdd:COG3206 326 QAREASLQAQlAQLEARLA-ELPELEAELRRLEREVE 361
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4321-4349 |
3.66e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.66e-05
10 20
....*....|....*....|....*....
gi 1655220506 4321 VRKRRVVIVDPESGKEMSVYEAYQKGLID 4349
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2635-2780 |
3.78e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 49.21 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2635 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMlQQTFLTEKELLLKRERDVEDEKKKlqkhlEDEVNKAKALKDEQQR 2714
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQSKEAV-EEAILQTDQALTAKEKAIEAERAK-----AEAAEAEQELLREKQK 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2715 QQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMeALEKKRLEQEKLLadeNKKLREKLESLE 2780
Cdd:pfam02841 229 EEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQER-MLEHKLQEQEELL---KEGFKTEAESLQ 290
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1651-2066 |
3.82e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.91 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1651 QLQTTIKQKSTADDELQKLRDQ----AAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAL 1726
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAggleAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1727 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQE 1806
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1807 EEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQ 1886
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1887 RTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKV 1966
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1967 SQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALK 2046
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
410 420
....*....|....*....|
gi 1655220506 2047 AKEAENERLKRQAEDEAYQR 2066
Cdd:COG5278 511 AAAEAALAAALAAALASAEL 530
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1677-1852 |
4.05e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.62 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1677 EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKV 1756
Cdd:pfam05262 180 KKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1757 VEEVAQKTAA---TQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRl 1833
Cdd:pfam05262 260 LPKPADTSSPkedKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ- 338
|
170
....*....|....*....
gi 1655220506 1834 RLRAEEEAQRKSLAQEEAE 1852
Cdd:pfam05262 339 KTKPQVEAQPTSLNEDAID 357
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1729-2508 |
4.07e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1729 LQKHKMQAEEAERRLKQA-EEEKVRQIKVVEEVAQ-KTAATQLQAMSFSEKTTK-LEESLKKEQGTvlQLQEEAEKLRKQ 1805
Cdd:pfam12128 218 LNRQQVEHWIRDIQAIAGiMKIRPEFTKLQQEFNTlESAELRLSHLHFGYKSDEtLIASRQEERQE--TSAELNQLLRTL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1806 EEEANKAREQAEKELETWRLKANEAlRLRLRAEEEaQRKSLAQEEAEKQKTEAERdakkkakaEEAALKQKENAEKELEK 1885
Cdd:pfam12128 296 DDQWKEKRDELNGELSAADAAVAKD-RSELEALED-QHGAFLDADIETAAADQEQ--------LPSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1886 QRTfaeqiAQQKLSAEQEYIRLKADFEHAeqqRGLLDNElQRLKNEVNAAEKQRRQLEDELAKVRSEMDallqmkiqaEK 1965
Cdd:pfam12128 366 LTG-----KHQDVTAKYNRRRSKIKEQNN---RDIAGIK-DKLAKIREARDRQLAVAEDDLQALESELR---------EQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1966 VSQSNTEKSKQLLETEAlkmkQLAEEAARLRSV--AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEV 2043
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKS----RLGELKLRLNQAtaTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2044 ALKAKEAENERL-KRQAEDEAYQRKLleDQAAQHKHDIQEKITQLQSSSV-----SELDRQKNIVEETLRQKKVVEEEIH 2117
Cdd:pfam12128 504 ASEALRQASRRLeERQSALDELELQL--FPQAGTLLHFLRKEAPDWEQSIgkvisPELLHRTDLDPEVWDGSVGGELNLY 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2118 IIRINFERAS-KEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAeeerkrreaeekvKKIAAAEEEAARQRKAA 2196
Cdd:pfam12128 582 GVKLDLKRIDvPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAN-------------GELEKASREETFARTAL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2197 QDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKsTAAEQKAQDvlskNKEDLLSQEKLRDEFENAKKLAQAaeta 2276
Cdd:pfam12128 649 KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS-LEAQLKQLD----KKHQAWLEEQKEQKREARTEKQAY---- 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2277 kekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAErlrkeaeaeaakraaaeaaaLKQ-KQEADAEMAKHKKEAE 2355
Cdd:pfam12128 720 -----------WQVVEGALDAQLALLKAAIAARRSGAKAE--------------------LKAlETWYKRDLASLGVDPD 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2356 QALKQKSQVeKELgLVKLQLDETDKQKAL-MDEELQRVKAQVNDAVK-QKAQVENELSKVKMQMDELLKlKVRIEEENLR 2433
Cdd:pfam12128 769 VIAKLKREI-RTL-ERKIERIAVRRQEVLrYFDWYQETWLQRRPRLAtQLSNIERAISELQQQLARLIA-DTKLRRAKLE 845
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2434 LMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEEtarqrKTAEAELAEQRALAEKmLKEKMQAIQEATKLKAE 2508
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLRCEMSKLATLKEDANS-----EQAQGSIGERLAQLED-LKLKRDYLSESVKKYVE 914
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1836-2027 |
4.13e-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: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1836 RAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK-----ELEKQRTFAE-QIAQQKLSAEQE------ 1903
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKmreelELEQQRRFEEiRLRKQRLEEERQrqeeee 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1904 ---YIRLKADFEHAEQQRGLLDNELQRLknevnaaEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLlet 1980
Cdd:pfam15709 408 rkqRLQLQAAQERARQQQEEFRRKLQEL-------QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERL--- 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220506 1981 EALKMKQLAEEAARLrsvaeEAKKQRQLAEDEAARQRAEAEKILKEK 2027
Cdd:pfam15709 478 EYQRQKQEAEEKARL-----EAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2497-2805 |
4.43e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2497 QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEI---SAEAEKLKLRVKELS 2573
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELeslQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2574 SAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKE 2653
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2654 TASAQQEQMEQQkamlqqtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2733
Cdd:COG4372 202 LAEAEKLIESLP----------RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2734 VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2805
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1551-1962 |
4.57e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1551 KRMAEIQAQLEtqkQLAEGHAKsvakAELEAQELKlKMKEDASQ--RQGLAV----DAEKQKQNIQLELTQLKNL----- 1619
Cdd:COG3096 785 KRLEELRAERD---ELAEQYAK----ASFDVQKLQ-RLHQAFSQfvGGHLAVafapDPEAELAALRQRRSELERElaqhr 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1620 -SEQEIRSKNQQLEEAQVSRRKLEEEIHLIriqlqttikqkstADDELQklrDQAAEAEKVRKAAQEeAERlrkqvneET 1698
Cdd:COG3096 857 aQEQQLRQQLDQLKEQLQLLNKLLPQANLL-------------ADETLA---DRLEELREELDAAQE-AQA-------FI 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1699 QKKKNAEDELKRKSEAekeaARQKQKALDELQKHKMQAEEAERRLKQaeeekvrQIKVVEEVAQKtaatqLQAMSFSEKT 1778
Cdd:COG3096 913 QQHGKALAQLEPLVAV----LQSDPEQFEQLQADYLQAKEQQRRLKQ-------QIFALSEVVQR-----RPHFSYEDAV 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1779 TKLEESlkkeqgtvlqlQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR--LRAEEEAQRKSLAQEEAEKQK- 1855
Cdd:COG3096 977 GLLGEN-----------SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLasLKSSRDAKQQTLQELEQELEEl 1045
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1856 -----TEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAE---QIAQQKLS-AEQEY-----------------IRLKA 1909
Cdd:COG3096 1046 gvqadAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEaemDSLQKRLRkAERDYkqereqvvqakagwcavLRLAR 1125
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1910 D-------------FEHAEQQRGLLDNELQRLKNEVNAAEKQR---RQLED------------------------ELAKV 1949
Cdd:COG3096 1126 DndverrlhrrelaYLSADELRSMSDKALGALRLAVADNEHLRdalRLSEDprrperkvqfyiavyqhlrerirqDIIRT 1205
|
490
....*....|...
gi 1655220506 1950 RSEMDALLQMKIQ 1962
Cdd:COG3096 1206 DDPVEAIEQMEIE 1218
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2433-2607 |
4.65e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2433 RLMQKNKDNTQKLLAEEaeKMKSLAEEAARlsvEAEETARQRKT-AEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEE 2511
Cdd:PRK12704 22 YFVRKKIAEAKIKEAEE--EAKRILEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2512 LQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKA------EEEATR 2585
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQK-------QQELEKKEEELEELIEEQLQELERISGLTAEEAKEillekvEEEARH 169
|
170 180
....*....|....*....|..
gi 1655220506 2586 fkkqadEAKVRLQETEKQTTET 2607
Cdd:PRK12704 170 ------EAAVLIKEIEEEAKEE 185
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1313-1706 |
4.71e-05 |
|
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: 50.06 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1313 EKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWqavfAQIDLRQRE 1392
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI----AQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1393 LsllgrhmnsykqsyewliqwlrearlrQEKIEAApvwdSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAyidslkd 1472
Cdd:TIGR02168 759 L---------------------------EAEIEEL----EERLEEAEEELAEAEAEIEELEAQIEQLKEELKA------- 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1473 yefQILAYRALQDpiasplkkpkmesasdniiqEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKE----- 1547
Cdd:TIGR02168 801 ---LREALDELRA--------------------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdiesl 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1548 -----DEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDAEKQKQNIQLELTQLkNLSEQ 1622
Cdd:TIGR02168 858 aaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS----ELRRELEELREKLAQL-ELRLE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1623 EIRSKNQQLEEAQVSRRKLEEEIHliriqlqttIKQKSTADDELQKLRDQAAEAEKVRKA-----------AQEEAER-- 1689
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEEA---------EALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeYEELKERyd 1003
|
410
....*....|....*...
gi 1655220506 1690 -LRKQVNEETQKKKNAED 1706
Cdd:TIGR02168 1004 fLTAQKEDLTEAKETLEE 1021
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2467-2753 |
5.03e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2467 AEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQK 2546
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARF--------------EARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2547 SLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE----EATRFKK---QADEAKVRLQETEKQTTETvvqkletqrlqS 2619
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREARKAQARARQAEkqaaAAADPKKaavAAAIARAKAKKAAQQAANA-----------E 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2620 TREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhLE 2699
Cdd:PRK05035 571 AEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-VA 649
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2700 DEVNKAKALKDEQQRQQklmdeekkkLQAIMDEAVKKQKEAEAEMKNKQKEMEA 2753
Cdd:PRK05035 650 AAIARAKARKAAQQQAN---------AEPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1618-2073 |
5.06e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.57 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1618 NLSEQEIRSKNQQLEEAQVSRRKLEEE----IHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQ 1693
Cdd:COG5185 130 IVALKDELIKVEKLDEIADIEASYGEVetgiIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1694 VNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS 1773
Cdd:COG5185 210 SETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1774 FSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlraeeeaqrKSLAQEEAEK 1853
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIE-------------QGQESLTENL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1854 QKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR-LKADFEHAEQQRGLLDNELQRLKNEV 1932
Cdd:COG5185 357 EAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQIEELQRQIEQATSSN 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1933 NAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKqlLETEALKMKQLAEEAARLRSVAEE--AKKQRQL-- 2008
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSK--KEDLNEELTQIESRVSTLKATLEKlrAKLERQLeg 514
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2009 ---AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAK---EAENERLKRQAEDEAYQRKLLEDQA 2073
Cdd:COG5185 515 vrsKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKtdgQAANLRTAVIDELTQYLSTIESQQA 585
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2341-2494 |
5.33e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2341 QEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVK------ 2414
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2415 ---MQMDELLKLKVRIEEENLRLMQKnKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKM 2491
Cdd:COG1579 93 alqKEIESLKRRISDLEDEILELMER-IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
...
gi 1655220506 2492 LKE 2494
Cdd:COG1579 172 IPP 174
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2443-2590 |
5.50e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.32 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2443 QKLLAEEAEKMKSLAEEAARLSVEAEETARQ---RKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQA 2519
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKellLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2520 QEKAKKLLEDKQEIQQRLDKETQGFQK--SLEAERKRQ-----LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQA 2590
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKlllklLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2548-2781 |
5.58e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.10 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2548 LEAERKRQL-EISAEAEKLKlrvkelSSAQAKAEEEATRFKKQADEAKVRlQETEKQTTETVVQKLETQRlqstreaddl 2626
Cdd:COG2268 186 LDALGRRKIaEIIRDARIAE------AEAERETEIAIAQANREAEEAELE-QEREIETARIAEAEAELAK---------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2627 KKAIAELEKEREKLKRDAQelqnksketASAQQEQMEQQKAMLQQTFLTEKELLLKRERdvedEKKKLQKHLEDEVNKAK 2706
Cdd:COG2268 249 KKAEERREAETARAEAEAA---------YEIAEANAEREVQRQLEIAEREREIELQEKE----AEREEAELEADVRKPAE 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2707 ALKDEQQRQQKLmDEEKKKLQAIMdEAVKKQKEAEAEMKNKQkemEALEKKRLEQEKLLADENKKLREKLESLEV 2781
Cdd:COG2268 316 AEKQAAEAEAEA-EAEAIRAKGLA-EAEGKRALAEAWNKLGD---AAILLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2530-2762 |
5.64e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2530 KQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLrvKELSSAQAKAEEEatrfKKQADEAKVRLQETEKQTTETVV 2609
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERL--KQLEKERLAAQEQ----KKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2610 QKLETQRLqstrEADDLKKAIAELEK--EREKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtfltekelllkrerdv 2687
Cdd:PRK09510 140 KAAAAAKA----KAEAEAKRAAAAAKkaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKA-------------------- 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2688 edekkklqkhleDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQE 2762
Cdd:PRK09510 196 ------------AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1512-2068 |
5.64e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.80 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1512 TRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQ-LAEGHAKSVAKAELEA-QELKLKMK 1589
Cdd:PRK10246 297 ERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGwRAQFSQQT 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1590 EDASQRQGLA--VDAEKQKQNIQLELTQlkNLSEQEIRSKNQQLEEAQVSRRKLeeeihlirIQLQTTIKQkstaddeLQ 1667
Cdd:PRK10246 377 SDREQLRQWQqqLTHAEQKLNALPAITL--TLTADEVAAALAQHAEQRPLRQRL--------VALHGQIVP-------QQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1668 KLRDQAAEAekvRKAAQEEaerlrkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDELqkhkmqaeeaERRLKQAE 1747
Cdd:PRK10246 440 KRLAQLQVA---IQNVTQE------------QTQRNAALNEMRQRYKEKTQQLADVKTICEQ----------EARIKDLE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1748 EEKVR----QIKVVEEVAQKTAATQLQAMSFSEKTTKLE------ESLKKEQGTVL-QLQEEAEKLRKQEEEANKAREQA 1816
Cdd:PRK10246 495 AQRAQlqagQPCPLCGSTSHPAVEAYQALEPGVNQSRLDalekevKKLGEEGAALRgQLDALTKQLQRDESEAQSLRQEE 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1817 EKELETWRlKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAeRDAKKKAKAEEAALKQKENAEKELEKQR-TFAEQIAQ 1895
Cdd:PRK10246 575 QALTQQWQ-AVCASLNITLQPQDDIQPWLDAQEEHERQLRLL-SQRHELQGQIAAHNQQIIQYQQQIEQRQqQLLTALAG 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1896 QKLS-----AEQEYIRLKADFEHAEQQRgllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQ--MKIQAEKVS- 1967
Cdd:PRK10246 653 YALTlpqedEEASWLATRQQEAQSWQQR---QNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDnwRQVHEQCLSl 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1968 --QSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaAINEATRLKTEAEVAL 2045
Cdd:PRK10246 730 hsQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLEN--QRQQAQTLVTQTAQAL 807
|
570 580
....*....|....*....|....
gi 1655220506 2046 KAKEAEN-ERLKRQAEDEAYQRKL 2068
Cdd:PRK10246 808 AQHQQHRpDGLDLTVTVEQIQQEL 831
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
199-310 |
6.15e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 45.34 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 199 DRVQKKTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPRERDLVRNvrlprekgrmRFHKLQNVQIA 276
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKN----------RSQMIENIDAC 77
|
90 100 110
....*....|....*....|....*....|....
gi 1655220506 277 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 310
Cdd:cd21285 78 LSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1602-1771 |
6.40e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1602 AEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRK 1681
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1682 AAQE-----EAERLRKQvNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKhkmqAEEAERrlKQAEEEKVRQIKV 1756
Cdd:TIGR02794 128 QAAEakakaEAEAERKA-KEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA----KAEAEA--KAKAEEAKAKAEA 200
|
170
....*....|....*
gi 1655220506 1757 VEEVAQKTAATQLQA 1771
Cdd:TIGR02794 201 AKAKAAAEAAAKAEA 215
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2345-2790 |
7.00e-05 |
|
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: 49.26 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2345 AEMAKHKKEAEQALKQKSQVEKEL----GLV---KLQLD--ETDKQKALMDEELQRVKAQ-------VNDAVKQKAQVEN 2408
Cdd:pfam05701 49 EEIPEYKKQSEAAEAAKAQVLEELestkRLIeelKLNLEraQTEEAQAKQDSELAKLRVEemeqgiaDEASVAAKAQLEV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2409 ELSKVKMQMDELLKLKvrieeENLRLMQKNKDntqkLLAEEAEKMKSLAEEAARLSVEAEETARQrktAEAELAEQRALA 2488
Cdd:pfam05701 129 AKARHAAAVAELKSVK-----EELESLRKEYA----SLVSERDIAIKRAEEAVSASKEIEKTVEE---LTIELIATKESL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2489 EKM----LKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLledKQEIQQRLDKETQgfqksLEAERKRQLEISAE-AE 2563
Cdd:pfam05701 197 ESAhaahLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRL---NQQLLSAKDLKSK-----LETASALLLDLKAElAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2564 KLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQET----EKQTTETVVQKLETQRLQStreaddlkkaiaELEKEREK 2639
Cdd:pfam05701 269 YMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVkaniEKAKDEVNCLRVAAASLRS------------ELEKEKAE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2640 LKrDAQELQNKSKETASAQQEQMEQQKamlqqtflTEKELLLKRERDVEDEKKKLQKHLED---EVNKAKALKDEQQrqq 2716
Cdd:pfam05701 337 LA-SLRQREGMASIAVSSLEAELNRTK--------SEIALVQAKEKEAREKMVELPKQLQQaaqEAEEAKSLAQAAR--- 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2717 klmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEkkrlEQEKLLADENKKLREKLESLEVTSKQAASKT 2790
Cdd:pfam05701 405 ----EELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAK----ASEKLALAAIKALQESESSAESTNQEDSPRG 470
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1416-1855 |
7.24e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.87 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1416 EARLRQEKIEAAPVWDSKALKEqLTQEKKLLEEIEKNKDQIENCQKDAKayidslKDYEFQILAYRALQDPIA---SPLK 1492
Cdd:pfam05701 50 EIPEYKKQSEAAEAAKAQVLEE-LESTKRLIEELKLNLERAQTEEAQAK------QDSELAKLRVEEMEQGIAdeaSVAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1493 KPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKkRMAEIQAQLETQKQL------ 1566
Cdd:pfam05701 123 KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEK-TVEELTIELIATKESlesaha 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1567 ----AEGHAKSVA---------------KAELEAQELK--------LKMKEDASQRQGLAVDAE---------KQKQNIQ 1610
Cdd:pfam05701 202 ahleAEEHRIGAAlareqdklnwekelkQAEEELQRLNqqllsakdLKSKLETASALLLDLKAElaaymesklKEEADGE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1611 LELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRI---QLQ----------TTIKQKSTA--------DDELQKL 1669
Cdd:pfam05701 282 GNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVaaaSLRselekekaelASLRQREGMasiavsslEAELNRT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1670 RDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaedelkrksEAEkEAARQKQKALDELQKHKMQAEEAERRLKQAE-- 1747
Cdd:pfam05701 362 KSEIALVQAKEKEAREKMVELPKQLQQAAQ-------------EAE-EAKSLAQAAREELRKAKEEAEQAKAAASTVEsr 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1748 -EEKVRQIKVVEEvAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAE---KLRKQEEEANKAREQAEKELETW 1823
Cdd:pfam05701 428 lEAVLKEIEAAKA-SEKLALAAIKALQESESSAESTNQEDSPRGVTLSLEEYYElskRAHEAEELANKRVAEAVSQIEEA 506
|
490 500 510
....*....|....*....|....*....|....*.
gi 1655220506 1824 RLKANEAL-RLRLRAEEEAQRKS---LAQEEAEKQK 1855
Cdd:pfam05701 507 KESELRSLeKLEEVNREMEERKEalkIALEKAEKAK 542
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1657-1964 |
7.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1657 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQA 1736
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1737 EEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1816
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1817 EKELetwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1896
Cdd:COG4372 191 EANR---NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1897 KLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE 1964
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3649-3686 |
7.42e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 7.42e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220506 3649 LPLLEAQFATGGIIDPVSSHRVPNDVAIQRGYLSKQMV 3686
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1539-1777 |
7.55e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1539 EKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksvaKAELEAQELKLKMKEDASQrqglavdAEKQKQNIQLEltqlkn 1618
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAE-------QARQKELEQRAAAEKAAKQ-------AEQAAKQAEEK------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1619 lSEQEIRSKNQQLEEAqvsrrkleeeihliriqlqttiKQKSTADDELQKLRDQAAEAEKVRKA-----AQEEAERLRKQ 1693
Cdd:TIGR02794 118 -QKQAEEAKAKQAAEA----------------------KAKAEAEAERKAKEEAAKQAEEEAKAkaaaeAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1694 VNEETQKKKNAE-----DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQ 1768
Cdd:TIGR02794 175 AEAEAKAKAEAEakakaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
....*....
gi 1655220506 1769 LQAMSFSEK 1777
Cdd:TIGR02794 255 AAAGSEVDK 263
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1613-1858 |
7.76e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1613 LTQLKNLSEQEIRSKNQQLEEAQVsRRKLEEEIHLIRI--QLQTTIKQKSTADDELQKLRDQaaEAEKVRKAAQEEAERL 1690
Cdd:PRK05771 22 LEALHELGVVHIEDLKEELSNERL-RKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVK--SLEELIKDVEEELEKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1691 RKQVNEETQKKKNAEDELKRKsEAEKEAArQKQKALD-ELQK--------------HKMQAEEAERRLKQAEEEKVRQIK 1755
Cdd:PRK05771 99 EKEIKELEEEISELENEIKEL-EQEIERL-EPWGNFDlDLSLllgfkyvsvfvgtvPEDKLEELKLESDVENVEYISTDK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1756 -------VVEEVAQKTAATQLQAMSFSEKTTKLEESLKkeqgtvlqlqEEAEKLRKQEEEANKAREQAEKELETWrlkAN 1828
Cdd:PRK05771 177 gyvyvvvVVLKELSDEVEEELKKLGFERLELEEEGTPS----------ELIREIKEELEEIEKERESLLEELKEL---AK 243
|
250 260 270
....*....|....*....|....*....|
gi 1655220506 1829 EALRLRLRAEEEAqrkslaqeEAEKQKTEA 1858
Cdd:PRK05771 244 KYLEELLALYEYL--------EIELERAEA 265
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1571-2048 |
7.84e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.98 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1571 AKSVAKAELEAQELKLKMKEDASQRQGLAVdaekqkQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHL-IR 1649
Cdd:pfam09731 43 GEEVVLYALGEDPPLAPKPKTFRPLQPSVV------SAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAeAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1650 IQLQTTIKQKSTADDELQKlrDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDEL 1729
Cdd:pfam09731 117 AQLPKSEQEKEKALEEVLK--EAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1730 QKHKM-------------QAEEAERRLKQAEEEKVRQIKVVEEVAQKTA-ATQLQAMSFSEKTTKLEESLKKEQGTVLQL 1795
Cdd:pfam09731 195 LKEVInlakqseeeaappLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKlVDQYKELVASERIVFQQELVSIFPDIIPVL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1796 QE----EAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKslaQEEAEKQKTEAERDAkkkakaeea 1871
Cdd:pfam09731 275 KEdnllSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDK---LAEELSARLEEVRAA--------- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1872 alkQKENAEKELEKQRTFAEQIAQQKLSAEQeyirlkadfehaEQQRGLLDnelQRLKNEV--NAAEKQRRQLEDELAKV 1949
Cdd:pfam09731 343 ---DEAQLRLEFEREREEIRESYEEKLRTEL------------ERQAEAHE---EHLKDVLveQEIELQREFLQDIKEKV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1950 RSE-------MDALLQMKIQAEKVSQSNTEkskqlLETEALKMKQLAEEAARLRSVAEEAKKQRQLA----EDEAARQRA 2018
Cdd:pfam09731 405 EEEragrllkLNELLANLKGLEKATSSHSE-----VEDENRKAQQLWLAVEALRSTLEDGSADSRPRplvrELKALKELA 479
|
490 500 510
....*....|....*....|....*....|.
gi 1655220506 2019 EAEKILKEKLAAINEATRLK-TEAEVALKAK 2048
Cdd:pfam09731 480 SDDEVVKAALASLPEEAYQRgVYTEAALRER 510
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1703-2024 |
8.01e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1703 NAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLkQAEEEKVRQIKV---------VEEVAQKTAATQlQAMS 1773
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL-SALNRLLPRLNLladetladrVEEIREQLDEAE-EAKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1774 FSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKeletwrlkanealRLRLRAEEEAQRKSLAQEEAEK 1853
Cdd:PRK04863 912 FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQ-------------QAFALTEVVQRRAHFSYEDAAE 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1854 QKTEAerdakkkAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQ------- 1926
Cdd:PRK04863 979 MLAKN-------SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpad 1051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1927 ------------RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmkiQAEKVsqsnTEKSKQLLE--TEALKMKQLAEEA 1992
Cdd:PRK04863 1052 sgaeerararrdELHARLSANRSRRNQLEKQLTFCEAEMDNLTK---KLRKL----ERDYHEMREqvVNAKAGWCAVLRL 1124
|
330 340 350
....*....|....*....|....*....|..
gi 1655220506 1993 ARLRSVaEEAKKQRQLAEDEAARQRAEAEKIL 2024
Cdd:PRK04863 1125 VKDNGV-ERRLHRRELAYLSADELRSMSDKAL 1155
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1431-1731 |
8.25e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1431 DSKALKEQLTQEKKLLEEIEKNKDQIENCQK----------DAKAYIDSLKDYE-------FQILAYRALQDPIASPLKK 1493
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQqlaqapaklrQAQAELEALKDDNdeetretLSTLSLRQLESRLAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1494 pkMESASDNIIQ---EYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRM-AE---IQAQLETQKQL 1566
Cdd:PRK11281 137 --LQNAQNDLAEynsQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLqAEqalLNAQNDLQRKS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1567 AEGH--------------AKSVAKAELEAQEL-------KLKMKE----------DASQRQGLAVDAEKQKQNIQL---- 1611
Cdd:PRK11281 215 LEGNtqlqdllqkqrdylTARIQRLEHQLQLLqeainskRLTLSEktvqeaqsqdEAARIQANPLVAQELEINLQLsqrl 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1612 -ELTQLKN-LSEQEIRSKNQqLEEAQVSRRKLEEEIH-------LIRIQLQTtiKQKSTADDELQKLRDQAAEaekvrka 1682
Cdd:PRK11281 295 lKATEKLNtLTQQNLRVKNW-LDRLTQSERNIKEQISvlkgsllLSRILYQQ--QQALPSADLIEGLADRIAD------- 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1683 aqeeaerLRKQVNEETQKKknaeDELKRKSE-AEKEAARQKQKALDELQK 1731
Cdd:PRK11281 365 -------LRLEQFEINQQR----DALFQPDAyIDKLEAGHKSEVTDEVRD 403
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2500-2672 |
8.90e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 46.49 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2500 QEATKLKAEAEELQKQ-KNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKR-QLEISAEAEKLKLRVKELssaqa 2577
Cdd:pfam01442 4 DSLDELSTYAEELQEQlGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEElQAKLGQNVEELRQRLEPY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2578 kAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAE-LEKEREKLKRDAQELQNKSKETAS 2656
Cdd:pfam01442 79 -TEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAErLEELKESLAPYAEEVQAQLSQRLQ 157
|
170
....*....|....*.
gi 1655220506 2657 AQQEQMEQQKAMLQQT 2672
Cdd:pfam01442 158 ELREKLEPQAEDLREK 173
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1526-1718 |
9.06e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1526 KFILETQrrLEDDEKASEKLKEDEKKRMaeiqaqlETQKQlaeghaksvaKAELEAQELKLKMKEdasqrqglavDAEKQ 1605
Cdd:PRK12704 26 KKIAEAK--IKEAEEEAKRILEEAKKEA-------EAIKK----------EALLEAKEEIHKLRN----------EFEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1606 KQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKlrdQAAEAEKVRKAAQE 1685
Cdd:PRK12704 77 LRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERISGLTAE 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220506 1686 EA-ERLRKQVNEETQKKKNA---EDELKRKSEAEKEA 1718
Cdd:PRK12704 154 EAkEILLEKVEEEARHEAAVlikEIEEEAKEEADKKA 190
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2621-2796 |
9.11e-05 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 48.03 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2621 READDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQqtfltekellLKRERDvedekkklqkHLED 2700
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQ----------LQKEKD----------QLQS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2701 EVNKAKALKD-------EQQRQQKLMDEEKKKLqaiMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLR 2773
Cdd:pfam09728 61 ELSKAILAKSkleklcrELQKQNKKLKEESKKL---AKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELR 137
|
170 180
....*....|....*....|....*....
gi 1655220506 2774 EKLESL----EVTSKQAAS--KTKEIEVQ 2796
Cdd:pfam09728 138 EKLKSLieqyELRELHFEKllKTKELEVQ 166
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1953-2269 |
9.73e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1953 MDALLQMKIQAEKVSQSNTEKSKQLLETEalKMKQLAEEAARlrsvaeEAKKQRQLAEDEAARQRAeaekiLKEKLAAIN 2032
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQAE-----MDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2033 EATRLKTEAE-----VALKAKEAENERLKRQ--AEDEAYQRKL--LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVE 2103
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQEeiAMEISRMRELerLQMERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2104 ETLRQKKVVEEEIHIIRINFERASKEKsdlevelkklkgiADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIA 2183
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEER-------------AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2184 AAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELE-KQVILAKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDE 2262
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEMEERRR---IQEQMRKA 561
|
....*..
gi 1655220506 2263 FENAKKL 2269
Cdd:pfam17380 562 TEERSRL 568
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1648-1787 |
9.84e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1648 IRIQLQTTIKQKSTADDELQKLRDQAAEAEK-VRKAAQEEAERLRKQVneetQKKKNAEDELKRKSEAEKEAARQKQKAL 1726
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKeQDEASFERLAELRDEL----AELEEELEALKARWEAEKELIEEIQELK 477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 1727 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEE----------VAQKTA--ATQLQAmSFSEKTTKLEESLKK 1787
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREevteediaevVSRWTGipVGKLLE-GEREKLLNLEEELHE 549
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2500-2792 |
9.98e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2500 QEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfqKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKA 2579
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEEL--------KELAEKRD---ELNAQVKELREEAQELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2580 EEEATRFKKQADEAKVRLQETEKQTTEtvVQKLETQRLQSTREADDLKKAIAELEK--EREKLKRDAQ-ELQNKSKETAs 2656
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDE--LRKELAELNKAGGSIDKLRKEIERLEWrqQTEVLSPEEEkELVEKIKELE- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2657 aqqEQMEQQKAMLQQtfltEKELllkreRDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAvkk 2736
Cdd:COG1340 147 ---KELEKAKKALEK----NEKL-----KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA--- 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2737 qKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKE 2792
Cdd:COG1340 212 -DELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2443-2804 |
1.00e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.60 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2443 QKLLAEEAEKMKSLAEEaaRLSVEAEETarqRKTAEAELAEQRALAEKMLKEKMQAIQEAtklkaeAEELQKQKNQAQEK 2522
Cdd:pfam09731 79 SKEPKEEKKQVKIPRQS--GVSSEVAEE---EKEATKDAAEAKAQLPKSEQEKEKALEEV------LKEAISKAESATAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2523 AKKLLEDKQE-IQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQAdeakvrLQETE 2601
Cdd:pfam09731 148 AKEAKDDAIQaVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDA------APETP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2602 KQTTETvvqklETQRLQSTREADDLKKAIAELEKEREKLKRD-AQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELL 2680
Cdd:pfam09731 222 PKLPEH-----LDNVEEKVEKAQSLAKLVDQYKELVASERIVfQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2681 LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAimdeaVKKQKEAEAEMKNKQKEMEalEKKRLE 2760
Cdd:pfam09731 297 DQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADE-----AQLRLEFEREREEIRESYE--EKLRTE 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1655220506 2761 QEKLLADENKKLREKLESLEVTSKQAAskTKEIEvqtDKVPEEQ 2804
Cdd:pfam09731 370 LERQAEAHEEHLKDVLVEQEIELQREF--LQDIK---EKVEEER 408
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1797-2018 |
1.01e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1797 EEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK 1876
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLE----QQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1877 ENAEKELEKQR-TFAEQIAQQKLSAEQEYIRLKADFEHAEQQRgllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEmda 1955
Cdd:TIGR02794 126 AKQAAEAKAKAeAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA---EEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE--- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 1956 llQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRA 2018
Cdd:TIGR02794 200 --AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1574-1818 |
1.05e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.79 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1574 VAKAELEAQELKLKMKEDASQR--------------------QGLAVDAEKQKQNIQ--LELTQLKNLSEQEIRSKNQQL 1631
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEAKARfearqarlerekaarearhkKAAEARAAKDKDAVAaaLARVKAKKAAATQPIVIKAGA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1632 EEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLrdQAAEAE-KVRKAAQEEAErlRKQVNEETQKKKNAEDEL-- 1708
Cdd:PRK05035 513 RPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAV--AAAIARaKAKKAAQQAAN--AEAEEEVDPKKAAVAAAIar 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1709 -KRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAtqLQAMSFSEKTTkleeslKK 1787
Cdd:PRK05035 589 aKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA--VAAAIARAKAR------KA 660
|
250 260 270
....*....|....*....|....*....|.
gi 1655220506 1788 EQGTVLQLQEEAEKLRKQEEEANKAREQAEK 1818
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2449-2663 |
1.10e-04 |
|
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: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2449 EAEKMKSLAE---EAARLSVEAE-ETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKnQAQEKAK 2524
Cdd:COG2268 187 DALGRRKIAEiirDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAE-TARAEAE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2525 KLLEDKQEIQQRldketqgfqksleaERKRQLEIsAEAEKlKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQt 2604
Cdd:COG2268 266 AAYEIAEANAER--------------EVQRQLEI-AERER-EIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE- 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2605 tetvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAqeLQNKSKETASAQQEQME 2663
Cdd:COG2268 329 -------AEAIRAKGLAEAEGKRALAEAWNKLGDAAILLM--LIEKLPEIAEAAAKPLE 378
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1444-2821 |
1.11e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1444 KLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPiasplkkpkmESASDNIIQEyvTLRTRYSElstlTSQ 1523
Cdd:TIGR01612 755 KILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND----------QINIDNIKDE--DAKQNYDK----SKE 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1524 YIKFIletqrRLEDDEkaSEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQ------- 1596
Cdd:TIGR01612 819 YIKTI-----SIKEDE--IFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKlndyekk 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1597 ---------GLAVDAEKQKQNIQ--------LELTQLKNLSEQEIRSKNQQLEEaqvsrrKLEEEIHLIRiqlQTTIKQK 1659
Cdd:TIGR01612 892 fndskslinEINKSIEEEYQNINtlkkvdeyIKICENTKESIEKFHNKQNILKE------ILNKNIDTIK---ESNLIEK 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1660 STADDELQKLRDQAAEAEKVRKAAQEEAERLRKqvNEETQKKKNAEDEL-KRKSEAEKEAARQKQKALDELQKhkmQAEE 1738
Cdd:TIGR01612 963 SYKDKFDNTLIDKINELDKAFKDASLNDYEAKN--NELIKYFNDLKANLgKNKENMLYHQFDEKEKATNDIEQ---KIED 1037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1739 AERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsekttklEESLKKEQGTVLQLQEEAEKLR-------------KQ 1805
Cdd:TIGR01612 1038 ANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLN--------KEILEEAEINITNFNEIKEKLKhynfddfgkeeniKY 1109
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1806 EEEANKAREQAEkeletwrlKANEALRLRLRAEEEAQRKSlaqeeaekqkteaerdakkkakaeeaalkqkENAEKELEK 1885
Cdd:TIGR01612 1110 ADEINKIKDDIK--------NLDQKIDHHIKALEEIKKKS-------------------------------ENYIDEIKA 1150
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1886 QRTFAEQIAQQKLSAE--------QEYIRLKADfehaeqQRGLLDNELQRLKNEVNAAEKQRRQLEdelaKVRS------ 1951
Cdd:TIGR01612 1151 QINDLEDVADKAISNDdpeeiekkIENIVTKID------KKKNIYDEIKKLLNEIAEIEKDKTSLE----EVKGinlsyg 1220
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1952 -EMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRaeaekilKEKLAA 2030
Cdd:TIGR01612 1221 kNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDK-------DHHIIS 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2031 INEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQaaQHKHDIQEKITQLQS-SSVSELDRQKNIVEETLRQK 2109
Cdd:TIGR01612 1294 KKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQ--KHNSDINLYLNEIANiYNILKLNKIKKIIDEVKEYT 1371
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2110 KVVEEEIHIIRINFERAS------KEKSDLE---------VELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE 2174
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEklikkiKDDINLEeckskiestLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEN 1451
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2175 AEEKVKKIAAAEEEAARQRKAAQD--------EVERLKQKAAEANKLKDKAE---KELEKQVILAKEAAQKSTAAEQKAQ 2243
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQHILKIKKDnatndhdfNINELKEHIDKSKGCKDEADknaKAIEKNKELFEQYKKDVTELLNKYS 1531
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2244 DVLSKNKEDLLSQ--EKLRDEFENAKKLAQAAETAKekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrke 2321
Cdd:TIGR01612 1532 ALAIKNKFAKTKKdsEIIIKEIKDAHKKFILEAEKS----------EQKIKEIKKEKFRIEDDAAKNDKSNKAAIDI--- 1598
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2322 aeaeaakraaaeAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDET------DKQKALMD--EELQRVK 2393
Cdd:TIGR01612 1599 ------------QLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTelkengDNLNSLQEflESLKDQK 1666
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2394 AQVNDAVKQKAQVENELSKVKMQMDELLK-LKVRIEEENLRLMQKNK---DNTQKLLAEEAEKMKSLAEEAARLSVEAEE 2469
Cdd:TIGR01612 1667 KNIEDKKKELDELDSEIEKIEIDVDQHKKnYEIGIIEKIKEIAIANKeeiESIKELIEPTIENLISSFNTNDLEGIDPNE 1746
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2470 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEA---------TKLKAEAEELqkqKN-QAQEKAKKLLEDKQ-------- 2531
Cdd:TIGR01612 1747 KLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEpitydeiknTRINAQNEFL---KIiEIEKKSKSYLDDIEakefdrii 1823
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2532 -EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELS---------------------SAQAKAEEEATRFKKQ 2589
Cdd:TIGR01612 1824 nHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENLlfdilnktkdayagiigkkyySYKDEAEKIFINISKL 1903
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2590 ADEAKVRLQETE-----KQTTETVVQKLETqrlqstrEADDLKKAIAELEKERE---KLKRDAQELQNKSKETASAQQEQ 2661
Cdd:TIGR01612 1904 ANSINIQIQNNSgidlfDNINIAILSSLDS-------EKEDTLKFIPSPEKEPEiytKIRDSYDTLLDIFKKSQDLHKKE 1976
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2662 MEQQKAMLQQTFLTEK------------ELLLKRERDVEDekKKLQKHLEDEVNKAKA----------LKDEQQRQQKLM 2719
Cdd:TIGR01612 1977 QDTLNIIFENQQLYEKiqasnelkdtlsDLKYKKEKILND--VKLLLHKFDELNKLSCdsqnydtileLSKQDKIKEKID 2054
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2720 DEEKKKLQAIMDEAVKKQKEaeaEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDK 2799
Cdd:TIGR01612 2055 NYEKEKEKFGIDFDVKAMEE---KFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDK 2131
|
1530 1540 1550
....*....|....*....|....*....|....*...
gi 1655220506 2800 VPEE-----QLVSM----------TTVETTK-KVFNGS 2821
Cdd:TIGR01612 2132 IIEKndlidKLIEMrkecllfsyaTLVETLKsKVINHS 2169
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2587-2792 |
1.20e-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: 48.47 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2587 KKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLK-KAIAELEKEREKLKrdaQELQNKSKETASAQQEQMEQQ 2665
Cdd:NF033838 57 KEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKtEYLYELNVLKEKSE---AELTSKTKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2666 KAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALK-DEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEM 2744
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKV 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2745 KNKQKEMEALEKKRLEQEKllADENKKLREKLESLEVTSKQAASKTKE 2792
Cdd:NF033838 214 ESKKAEATRLEKIKTDREK--AEEEAKRRADAKLKEAVEKNVATSEQD 259
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2420-2594 |
1.22e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2420 LLKLKVRIEEENLRLmQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQrKTAEAELAEQRALAEKMLKEKMQAI 2499
Cdd:PRK00409 525 LEELERELEQKAEEA-EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ-AIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2500 QEATKlkaEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD-----KETQGFQKS--LEAERKRQLEISAEAEKLKLRVKEL 2572
Cdd:PRK00409 603 SVKAH---ELIEARKRLNKANEKKEKKKKKQKEKQEELKvgdevKYLSLGQKGevLSIPDDKEAIVQAGIMKMKVPLSDL 679
|
170 180
....*....|....*....|..
gi 1655220506 2573 SSAQAKAEEEATRFKKQADEAK 2594
Cdd:PRK00409 680 EKIQKPKKKKKKKPKTVKPKPR 701
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
1666-1860 |
1.30e-04 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 48.45 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1666 LQKLRDQAAEAEKVRK----AAQEEAERLRKQVNEETQKKknAEDELKRKSEAEKEAARQKqkaldelqKHKMQAEEAer 1741
Cdd:PRK14900 834 LAGVIDLAAETARVDKeigkVDQDLAVLERKLQNPSFVQN--APPAVVEKDRARAEELREK--------RGKLEAHRA-- 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1742 RLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEA--------EKLRKQEEEANK-- 1811
Cdd:PRK14900 902 MLSGSEANSARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAatavasgiEKVAEAVRKTVRrs 981
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1655220506 1812 AREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKqKTEAER 1860
Cdd:PRK14900 982 VKKAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAK-KAPAKK 1029
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1589-1831 |
1.35e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 48.31 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1589 KEDASQRqgLAVDAEKqkqnIQLELTQLKNLsEQEIRSKNQQLEEAQVSRR----KLEEEIHLIRIQLQTTIKQKstadd 1664
Cdd:pfam09726 393 KPDALVR--LEQDIKK----LKAELQASRQT-EQELRSQISSLTSLERSLKselgQLRQENDLLQTKLHNAVSAK----- 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1665 elQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETqkkknaedelKRKSEAEKEAARQKQKALD------ELQKHKMQAEE 1738
Cdd:pfam09726 461 --QKDKQTVQQLEKRLKAEQEARASAEKQLAEEK----------KRKKEEEATAARAVALAAAsrgectESLKQRKRELE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1739 AERRLKQAE----EEKVRQIKV-VEEVAQ--------KTAATQLQAMsfSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ 1805
Cdd:pfam09726 529 SEIKKLTHDiklkEEQIRELEIkVQELRKykesekdtEVLMSALSAM--QDKNQHLENSLSAETRIKLDLFSALGDAKRQ 606
|
250 260
....*....|....*....|....*.
gi 1655220506 1806 EEEANKAREQAEKELETWRLKANEAL 1831
Cdd:pfam09726 607 LEIAQGQIYQKDQEIKDLKQKIAEVM 632
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
202-322 |
1.39e-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: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 202 QKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRNVRLPrekgrmrFHKLQN 272
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FIIQEN 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 273 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 322
Cdd:cd21325 97 LNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
201-314 |
1.39e-04 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 44.33 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 201 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlVRNVRLPREKGRmrfHKLQNVQIALDFL 280
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVP-----LHSFHLTPTSFE---QKVHNVQFAFELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 1655220506 281 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 314
Cdd:cd21306 88 QDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1688-1883 |
1.39e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.08 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1688 ERLRKQVNEETQKKKNAEDELKRKSEaekEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvaqktaat 1767
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQ---EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ-------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1768 QLQAMSFSEKTTKLEESLKKEQgtvlqLQEEaeklrkQEEEANKAREQAEKeletwrlKANEALRLRLRAEEEAQRKSLA 1847
Cdd:pfam05262 253 KQQEAKNLPKPADTSSPKEDKQ-----VAEN------QKREIEKAQIEIKK-------NDEEALKAKDHKAFDLKQESKA 314
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220506 1848 QEEAEKQKT-EAERDAKKKAKAEEAALKQKENAEKEL 1883
Cdd:pfam05262 315 SEKEAEDKElEAQKKREPVAEDLQKTKPQVEAQPTSL 351
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1662-1956 |
1.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1662 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAER 1741
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1742 RLKQAEEEkvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELE 1821
Cdd:COG4372 81 ELEELNEQ-------LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1822 TWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAE 1901
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 1902 QEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1956
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2292-2444 |
1.45e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 48.21 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2292 EEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAAL-KQKQEADAEMAKHKKEAEQA---LKQKSQVEKE 2367
Cdd:COG1193 521 EELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILeKAREEAEEILREARKEAEELireLREAQAEEEE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2368 LGLVKLQLDETDKQkalMDEELQRVKA-----------QVNDAVK-----QKAQVENELSK--VKMQMDEllkLKVRIEE 2429
Cdd:COG1193 601 LKEARKKLEELKQE---LEEKLEKPKKkakpakppeelKVGDRVRvlslgQKGEVLEIPKGgeAEVQVGI---LKMTVKL 674
|
170
....*....|....*
gi 1655220506 2430 ENLRLMQKNKDNTQK 2444
Cdd:COG1193 675 SDLEKVEKKKPKKPK 689
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1746-2087 |
1.49e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1746 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1825
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1826 KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYI 1905
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1906 RLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKM 1985
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1986 KQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ 2065
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|..
gi 1655220506 2066 RKLLEDQAAQHKHDIQEKITQL 2087
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVADG 370
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1794-2024 |
1.51e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1794 QLQEEAEKLRKQEEEANKAREQAEKELETwrlKANEALRLRlraEEEAQRksLAQEEAEKQKTEAERdakkkakaeeaal 1873
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQK---QAAEQERLK---QLEKER--LAAQEQKKQAEEAAK------------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1874 kQKENAEKELEKQRtfAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQrrqleDELAKVRSEM 1953
Cdd:PRK09510 126 -QAALKQKQAEEAA--AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA-----EAEAAAKAAA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 1954 DALLQMKIQAEKVSQSNTEKskqllETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIL 2024
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKK-----KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
224-311 |
1.53e-04 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 44.36 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 224 LYEDLRDGHNLISLLEVLSGETLPRErdlVRNVRLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLT 303
Cdd:cd21294 38 LFDECKDGLVLSKLINDSVPDTIDER---VLNKPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLI 114
|
....*...
gi 1655220506 304 LGLIWTII 311
Cdd:cd21294 115 LGLIWQII 122
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1777-1937 |
1.58e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1777 KTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEeeAQRKSLAQEEAEKQKT 1856
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPAD--TSSPKEDKQVAENQKR 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1857 EAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqeyirlkadfeHAEQQRGLLD--NELQRLKNEVNA 1934
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK---------------ELEAQKKREPvaEDLQKTKPQVEA 346
|
...
gi 1655220506 1935 AEK 1937
Cdd:pfam05262 347 QPT 349
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1909-2753 |
1.61e-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: 48.41 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1909 ADF-EHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkiqaekvsqsntEKSKQLLETE---ALK 1984
Cdd:COG3096 271 ADYmRHANERRELSERALE-LRRELFGARRQLAEEQYRLVEMARELEEL---------------SARESDLEQDyqaASD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1985 MKQLAEEAARlrsvAEEAKKQRQLAEDEAARQRAEAEKILKEklaaineATRLKTEAEVALKAKEAENERLKRQAEDeaY 2064
Cdd:COG3096 335 HLNLVQTALR----QQEKIERYQEDLEELTERLEEQEEVVEE-------AAEQLAEAEARLEAAEEEVDSLKSQLAD--Y 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2065 QRKLLEDQ--AAQHKHDIQ--EKITQLqsSSVSELDrQKNIvEETLRQKKVVEEEIHIIRINFER----ASKEKSDLEVE 2136
Cdd:COG3096 402 QQALDVQQtrAIQYQQAVQalEKARAL--CGLPDLT-PENA-EDYLAAFRAKEQQATEEVLELEQklsvADAARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2137 LKKLKGIADETQKSKAKAEEEAEKLKKlaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERLKQKAAEANKLKDK 2216
Cdd:COG3096 478 YELVCKIAGEVERSQAWQTARELLRRY---------------------------RSQQALAQRLQQLRAQLAELEQRLRQ 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2217 AEKELEKQVILAKEAAQKSTAAEQKaqdvlsknkEDLLS-QEKLRDEFENAKKLAQAAETAkekaekeaalLRQKAEEAE 2295
Cdd:COG3096 531 QQNAERLLEEFCQRIGQQLDAAEEL---------EELLAeLEAQLEELEEQAAEAVEQRSE----------LRQQLEQLR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2296 KLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakrAAAEAAALKQKQEADAEMAkhkkEAEQALKQKSQVEKELGLVKLQL 2375
Cdd:COG3096 592 ARIKELAARAPAWLAAQDALERL-----------REQSGEALADSQEVTAAMQ----QLLEREREATVERDELAARKQAL 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2376 DETDKQKAL----MDEELQRVKAQ--------------VNDAV--------KQKAQVENELSKVKMQMDEL--------- 2420
Cdd:COG3096 657 ESQIERLSQpggaEDPRLLALAERlggvllseiyddvtLEDAPyfsalygpARHAIVVPDLSAVKEQLAGLedcpedlyl 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2421 -------------------LKLKVRIEEENLR---------LMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETAR 2472
Cdd:COG3096 737 iegdpdsfddsvfdaeeleDAVVVKLSDRQWRysrfpevplFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQR 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2473 QRKTAEAELAEQRALA-----EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK-------------LLEDkQEIQ 2534
Cdd:COG3096 814 LHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEqlqllnkllpqanLLAD-ETLA 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2535 QRLDKETQGFQKSLEAERkrqlEISAEAEKLKLRVKELSSAQAKAEEEAtRFKKQADEAKVRLQETEKQT--TETVVQKL 2612
Cdd:COG3096 893 DRLEELREELDAAQEAQA----FIQQHGKALAQLEPLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIfaLSEVVQRR 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2613 ETqrlQSTREADDLKKAIAEL-EKEREKLkRDAQELQNKSKETASAQQEQMEQQKAMLQQ---TFLTEKELLlkreRDVE 2688
Cdd:COG3096 968 PH---FSYEDAVGLLGENSDLnEKLRARL-EQAEEARREAREQLRQAQAQYSQYNQVLASlksSRDAKQQTL----QELE 1039
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2689 DEKKKLQKHLEDE-VNKAKALKDE------QQRQQKlmDEEKKKLQAI---MDEAVKKQKEAEAEMKNKQKEMEA 2753
Cdd:COG3096 1040 QELEELGVQADAEaEERARIRRDElheelsQNRSRR--SQLEKQLTRCeaeMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1882-2521 |
1.63e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1882 ELEKQRTFAEQIAQQKLSAEQEYIRlKADFEHAEQQRGLLDNELQRLKNEVNAAEKQrrqLEDELAKVRSEMDALlqmKI 1961
Cdd:pfam12128 257 ELRLSHLHFGYKSDETLIASRQEER-QETSAELNQLLRTLDDQWKEKRDELNGELSA---ADAAVAKDRSELEAL---ED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1962 QAEKVSQSNTEKSKQLLETEALKMKQLAEEAARL-------RSVAEEAKKQRQLAEDEAARQRAEaekiLKEKLAAINEA 2034
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLPSWQSELENLEERLkaltgkhQDVTAKYNRRRSKIKEQNNRDIAG----IKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2035 -TRLKTEAEVALKAKEAEnerlkrqaedeayqrklLEDQAAQHKHDIQEKITQLQSSsVSELDRQKN---IVEETLRQKK 2110
Cdd:pfam12128 406 rDRQLAVAEDDLQALESE-----------------LREQLEAGKLEFNEEEYRLKSR-LGELKLRLNqatATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2111 VVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAA 2190
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDW 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRK---------------------------------------------AAQDEVERLKQKAAEANKLKDKAEKELEKQV 2225
Cdd:pfam12128 548 EQSIgkvispellhrtdldpevwdgsvggelnlygvkldlkridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2226 ILAKEAAQKSTAAEQKAQDVLSKNKEDLlsqEKLRDEFENAKklaqaaetakekaekeaallRQKAEEAEKLKKAAEDEA 2305
Cdd:pfam12128 628 VQANGELEKASREETFARTALKNARLDL---RRLFDEKQSEK--------------------DKKNKALAERKDSANERL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2306 AKQAKAQKdaerlrkeaeaeaakraaaeaAALKQKQEADAEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKALM 2385
Cdd:pfam12128 685 NSLEAQLK---------------------QLDKKHQAWLEEQKEQKREARTEKQAYWQVVEG---------ALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2386 DEELQrvkaqvndavKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLlaEEAEKMKSlaeEAARLSV 2465
Cdd:pfam12128 735 KAAIA----------ARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKI--ERIAVRRQ---EVLRYFD 799
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2466 EAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQE 2521
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1603-1738 |
1.64e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1603 EKQKQNIQLELTQLKNL---SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD---------ELQKLR 1670
Cdd:COG1579 23 EHRLKELPAELAELEDElaaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1671 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE 1738
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1730-1903 |
1.65e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1730 QKHKMQAEEAERRLKQAEEEKvrqikvvEEVAQKTAATQlqamsfsekttkleESLKKEQGTVLQLQEEaeklRKQEEEA 1809
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQA-------EELQQKQAAEQ--------------ERLKQLEKERLAAQEQ----KKQAEEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1810 NKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQrtf 1889
Cdd:PRK09510 124 AKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA--------------EAAKKAAAEAKKK--- 186
|
170
....*....|....
gi 1655220506 1890 AEQIAQQKLSAEQE 1903
Cdd:PRK09510 187 AEAEAAAKAAAEAK 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2557-2780 |
1.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2557 EISAEAEKLKLRVKELSSAQAKAEEEatrfKKQAdEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKE 2636
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDA----REQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2637 REKLKRDAQELQnksketasaqqEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQ 2716
Cdd:COG4913 297 LEELRAELARLE-----------AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 2717 KLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREK---LESLE 2780
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeIASLE 432
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1975-2132 |
1.81e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1975 KQLLETEALKMKQLAE---EAARLRsvAEEAKKQRQL-AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 2050
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKE--AEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2051 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQS--SSVSELDRQ--KNIVEETLRqKKVVEEEIHIIRiNFERA 2126
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLTAEeaKEILLEKVE-EEARHEAAVLIK-EIEEE 181
|
....*.
gi 1655220506 2127 SKEKSD 2132
Cdd:PRK12704 182 AKEEAD 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2337-2660 |
1.84e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2337 LKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQ 2416
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2417 MDELLKLKVRIEEENLRLMQKNKDnTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQrALAEKMLKEKM 2496
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ-ALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2497 QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ 2576
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2577 AKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETAS 2656
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
....
gi 1655220506 2657 AQQE 2660
Cdd:COG4372 355 VLEL 358
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2497-2637 |
1.86e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.09 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2497 QAIQEATKLKAEAEElQKQKNQAQEKAKKLledKQEIQQRLDKetQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ 2576
Cdd:PTZ00491 647 DSLQKSVQLAIEITT-KSQEAAARHQAELL---EQEARGRLER--QKMHDKAKAEEQRTKLLELQAESAAVESSGQSRAE 720
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2577 AKAEEEATRFKKQA--DEAKVRLqETEKQTTETVVQKLETQR---LQSTREADDL----KKAIAELEKER 2637
Cdd:PTZ00491 721 ALAEAEARLIEAEAevEQAELRA-KALRIEAEAELEKLRKRQeleLEYEQAQNELeiakAKELADIEATK 789
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2288-2665 |
1.87e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2288 RQKaEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALKQK-SQVEK 2366
Cdd:PRK11281 77 RQK-EETEQLKQQLAQAPAKLRQAQAELEAL--------------------KDDNDEETRETLSTLSLRQLESRlAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2367 ELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKmqmdellklkvrIEEENLRLMQKNKDNT-QKL 2445
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGK------------VGGKALRPSQRVLLQAeQAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2446 LAEEAEKMKSLAEEAARLSVEAEEtarQRktaeAELAEQRALAEKMLkekmQAIQEA--TKLKAEAEELQKQKNQAQEKA 2523
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQDLLQK---QR----DYLTARIQRLEHQL----QLLQEAinSKRLTLSEKTVQEAQSQDEAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2524 K--------KLLEDKQEIQQRLDKETQG----FQKSLEAerKRQLEISAEAEK-LKLRVKELSSA---------QAKAEE 2581
Cdd:PRK11281 273 RiqanplvaQELEINLQLSQRLLKATEKlntlTQQNLRV--KNWLDRLTQSERnIKEQISVLKGSlllsrilyqQQQALP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2582 EATRFKKQADE-AKVRLQ--ETEKQ-----TTETVVQKLETQrlQSTREADDLKKAIAELEKEREKLKRD---------- 2643
Cdd:PRK11281 351 SADLIEGLADRiADLRLEqfEINQQrdalfQPDAYIDKLEAG--HKSEVTDEVRDALLQLLDERRELLDQlnkqlnnqln 428
|
410 420
....*....|....*....|....*.
gi 1655220506 2644 -AQELQNKSKE---TASAQQEQMEQQ 2665
Cdd:PRK11281 429 lAINLQLNQQQllsVSDSLQSTLTQQ 454
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2956-2990 |
2.00e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.00e-04
10 20 30
....*....|....*....|....*....|....*
gi 1655220506 2956 LSAERAATGFKDPYTGAKISVFEAMQKGLIEKDLA 2990
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2485-2777 |
2.26e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2485 RALAEKMLKEKMQAIQEATKLkaeaeelQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEK 2564
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIA-------EKKRIKAEEKEEERRLDEMMEEERERAL----EEEEEKEEERKEERKRYRQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2565 LKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvvqKLETQRLQSTREADDLKKAIAELEKEREKLKRDA 2644
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQA-------EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2645 QELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELL------LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKL 2718
Cdd:pfam13868 151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2719 MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLE 2777
Cdd:pfam13868 231 ARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1748-1997 |
2.38e-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: 46.35 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1748 EEKVRQIKVVeeVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKA 1827
Cdd:pfam17045 9 QELMKQIDIM--VAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1828 NEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK--ENAEKELEKQRTFAEQIAQQKLSAEQEYI 1905
Cdd:pfam17045 87 QEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKslEWEQQRLQYQQQVASLEAQRKALAEQSSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1906 RLKADF----EHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMD--ALLQMKIQAEKvsqsntEKSKQLLE 1979
Cdd:pfam17045 167 IQSAAYqvqlEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSelGDSNRKLLEEQ------QRLLEELR 240
|
250
....*....|....*...
gi 1655220506 1980 TEALKMKQLAEEAARLRS 1997
Cdd:pfam17045 241 MSQRQLQVLQNELMELKA 258
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2521-2773 |
2.47e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2521 EKAKKLL-EDKQEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKlrvkelssaqakaeEEATRFKKQADEAKVRLQE 2599
Cdd:PRK00409 505 EEAKKLIgEDKEKLNELI--------ASLEELERELEQKAEEAEALL--------------KEAEKLKEELEEKKEKLQE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2600 TEKQttetVVQKLEtqrlqstREAddlKKAIAELEKEREKLKRDAQELQnksKETASAQQEQmeqqkamlqqtfltekel 2679
Cdd:PRK00409 563 EEDK----LLEEAE-------KEA---QQAIKEAKKEADEIIKELRQLQ---KGGYASVKAH------------------ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2680 llkrerDVEDEKKKLQKHLEdEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAE-------MKNKQKEME 2752
Cdd:PRK00409 608 ------ELIEARKRLNKANE-KKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVLSIPDDKEAIvqagimkMKVPLSDLE 680
|
250 260
....*....|....*....|.
gi 1655220506 2753 ALEKKRLEQEKLLADENKKLR 2773
Cdd:PRK00409 681 KIQKPKKKKKKKPKTVKPKPR 701
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3906-3941 |
2.58e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.58e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1655220506 3906 LNLLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPE 3941
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2192-2403 |
2.68e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2192 QRKAAQDEVERLKQKAAEANKlKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLlsQEKLRDEFENAKKLAQ 2271
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEK-QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE--EAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2272 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQ---AKAQKDAER-----LRKEAEAEAAKRAAaeaaalkqkQEA 2343
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEAkakaeEAKAKAEAAKAKAA---------AEA 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2344 DAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQK------ALMDEELQRVKAQVNDAVKQK 2403
Cdd:TIGR02794 210 AAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAGSEVDKYAAIIQQAIQQN 275
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1675-2019 |
2.68e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.21 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1675 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEEKVRQI 1754
Cdd:pfam15964 357 QCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ------NVAQLEAQVEKVTREKNSLV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1755 KVVEEVAQKTAAtqlQAMSFSEKTTKLEESLKKEQgtvlQLQEEAEK-LRKQEEEANKAREQAEKELETWRLKANEAlrl 1833
Cdd:pfam15964 431 SQLEEAQKQLAS---QEMDVTKVCGEMRYQLNQTK----MKKDEAEKeHREYRTKTGRQLEIKDQEIEKLGLELSES--- 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1834 RLRAEEEAQRKSLAQEEAEKQK---TEAERDAKKKAKaeeaalkqkenaEKElEKQRTFAEQIAQQKLSAEQEYIRLKAD 1910
Cdd:pfam15964 501 KQRLEQAQQDAARAREECLKLTellGESEHQLHLTRL------------EKE-SIQQSFSNEAKAQALQAQQREQELTQK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1911 FEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ--------LEDELAKVRSEMDALLQ----MKIQAEKVSQSNTEKSKQLL 1978
Cdd:pfam15964 568 MQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEecctlakkLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQCV 647
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 1979 ------ETEALKMKQL-------AEEAARLRSVAEEAKKQRQLAEDEAARQRAE 2019
Cdd:pfam15964 648 qhgrmhERMKQRLRQLdkhcqatAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
2425-2765 |
2.77e-04 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 47.35 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2425 VRIEEENLRLMQKNKDNTQKLLAE-EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAT 2503
Cdd:pfam14817 50 VRKIRGNLLWYGGLQDKGKAESRQsAAARRLELQKEIERLRAEISRLDKQLEARELELSREEAERERALDEISDSRHRQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2504 KLKAeaeelqkQKNQAQEKAKKLLEDKQEIQQRLDketqgfqksleaeRKRQLEISAEAEKLKLRVKELSSAQAKAEEEA 2583
Cdd:pfam14817 130 LLEA-------YDQQCEEARKILAEDHQRLQGQLQ-------------QLRDAARKAEKEVVFGDSKGSKSSVIALEPQV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2584 TRFKKQADEAKVR----LQETE-KQTTETVVQKLETQR----LQSTREADDLK-----------------KAIAELEKER 2637
Cdd:pfam14817 190 LRDVREACELRAQflqeLLESSlKAYEGSGIHMNRDQRraviQHWLSAVETLLtshppshllqalehlaaREKTAIQEET 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2638 EKL--KRDAQELQNK---------SKETASAQQEQ---MEQQKAMLQQtFLTEKELLLKRERdvedekkKLQKHLE---D 2700
Cdd:pfam14817 270 ESLdvRADAEALRFRyesnhlldvSSDESSDLPSVrqlLERQWAHVQQ-FLNELAETRSRCQ-------QLQARLQglkD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2701 EVNK-----AKALKDEQQRQQKLMDE-----EKKKLQAIMDE------AVKKQKEAEAEMKNKQKEMEALEKKRLEQEKL 2764
Cdd:pfam14817 342 EAELeslgiGDTSQNDSLLRQVLELElqaagLAASRDTLRSEcqqlnkLARERQEALRSLQKKWQRILDFRQLVSELQEQ 421
|
.
gi 1655220506 2765 L 2765
Cdd:pfam14817 422 I 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2080-2536 |
2.78e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2080 IQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLkgiadETQKSKAKAEEEAE 2159
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2160 KLKKLAAEEERKRREAEEKVKKIaaaeEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2239
Cdd:COG4717 136 ALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2240 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2319
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2320 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKL--QLDETDKQKALMDEELQRVKA-QV 2396
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieELQELLREAEELEEELQLEELeQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2397 NDAVKQKAQVENE--LSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETARQR 2474
Cdd:COG4717 372 IAALLAEAGVEDEeeLRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2475 KTAEAELAEQRALAEKMLKEK--MQAIQEATKLKAEAEELQKQkNQAQEKAKKLLEDKQEIQQR 2536
Cdd:COG4717 449 EELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE-WAALKLALELLEEAREEYRE 511
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
318-428 |
2.83e-04 |
|
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: 43.64 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 318 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-ENLEQAFSVA 396
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPvTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|..
gi 1655220506 397 ERELGVTRLLDPEDVDVAHPDEKSIITYVSSL 428
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2464-2717 |
2.84e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2464 SVEAEETARQRKTAEAELAEQRALAEKmlkekmqAIQEATKLKAEaeelQKQKNQAQEKAKKLLEDKQEIQQRLDKETQG 2543
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK-------ERAEADRQRLE----QEKQQQLAAISGSQSQLESTDQNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2544 FQKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQ-ADEAKVRLQETEKQTTETVVQKLETQRLQSTRE 2622
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2623 ADDLKKAIAELE---KEREKLKRDAQelQNKSKETASAQQEQMEqqkAMLQQTFLTEKEllLKRERDVEDEKKKLQKHLE 2699
Cdd:NF012221 1684 QQKVKDAVAKSEagvAQGEQNQANAE--QDIDDAKADAEKRKDD---ALAKQNEAQQAE--SDANAAANDAQSRGEQDAS 1756
|
250
....*....|....*....
gi 1655220506 2700 DEVNKA-KALKDEQQRQQK 2717
Cdd:NF012221 1757 AAENKAnQAQADAKGAKQD 1775
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1849-2146 |
2.91e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1849 EEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRL 1928
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1929 KNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE-AKKQRQ 2007
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2008 LAEDEAARQR---AEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKI 2084
Cdd:COG4372 166 LAALEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2085 TQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 2146
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1621-1731 |
2.95e-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: 43.97 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1621 EQEIRsknQQLEEAQVSRRKLEEeihliriqlqttikQKSTADDELQKLRdqaAEAEKVRKAAQEEAERLRKQVNEETQK 1700
Cdd:cd06503 32 EEKIA---ESLEEAEKAKEEAEE--------------LLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKE 91
|
90 100 110
....*....|....*....|....*....|.
gi 1655220506 1701 KKNaedelKRKSEAEKEAARQKQKALDELQK 1731
Cdd:cd06503 92 EAE-----RILEQAKAEIEQEKEKALAELRK 117
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1787-2113 |
2.97e-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: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1787 KEQGTVLQLQEEAEKLRKQEEEANKA-REQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKteAERDAKKK 1865
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERAlEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQER--EQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1866 AKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDE 1945
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1946 LAKV-------RSEMDALLQMKIQAEkvsqsNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQlaEDEAARQRA 2018
Cdd:pfam13868 189 LRAQqekaqdeKAERDELRAKLYQEE-----QERKERQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2019 EAEKILKEKlaaineatrlkteAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQ 2098
Cdd:pfam13868 262 EFERMLRKQ-------------AEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERR 328
|
330
....*....|....*
gi 1655220506 2099 KNIVEEtlRQKKVVE 2113
Cdd:pfam13868 329 ERIEEE--RQKKLKE 341
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1842-2061 |
3.07e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1842 QRKSLAQEEAEKQKTEAERdakkkakaeeaalkQKENAEKELEKQRTFaEQIAQQKLSAEQEYirlkadfEHAEQQRGll 1921
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQ--------------AEELQQKQAAEQERL-KQLEKERLAAQEQK-------KQAEEAAK-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1922 dnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQllETEALKMKQLAEEAARLRSVAEE 2001
Cdd:PRK09510 126 ----QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA--KKAAAEAKKKAEAEAAAKAAAEA 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2002 AKKQRQLAEDEA---ARQRAEAEKilkeKLAAINEATRLKTEAEVALKAKEAENERLKRQAED 2061
Cdd:PRK09510 200 KKKAEAEAKKKAaaeAKKKAAAEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3281-3312 |
3.08e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.08e-04
10 20 30
....*....|....*....|....*....|..
gi 1655220506 3281 QLLSAERAVSGYKDPYTGKTVSLFEAMNKGLI 3312
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2575-2763 |
3.22e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2575 AQAKAEEEATRFKKQADEAKVRL-QE----------TEKQTTETVVQKLET----QRLQSTREADDLKKAIAELEKEREK 2639
Cdd:NF012221 1552 KQDDAAQNALADKERAEADRQRLeQEkqqqlaaisgSQSQLESTDQNALETngqaQRDAILEESRAVTKELTTLAQGLDA 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2640 LKRDAQ-------------------ELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDV---EDEKKKLQKH 2697
Cdd:NF012221 1632 LDSQATyagesgdqwrnpfagglldRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVaqgEQNQANAEQD 1711
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 2698 LEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKK--QKEAEAEMKNKQKEMEALEKKRLEQEK 2763
Cdd:NF012221 1712 IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgeQDASAAENKANQAQADAKGAKQDESDK 1779
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2594-2794 |
3.26e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2594 KVRLQETEKQTTEtVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQK--AMLQQ 2671
Cdd:pfam07888 33 QNRLEECLQERAE-LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKelSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2672 TFLTEKELLLkrerDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM 2751
Cdd:pfam07888 112 ELSEEKDALL----AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1655220506 2752 EALEKKRLEQEKLLADENK---KLREKLESLEVTSKQAASKTKEIE 2794
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTqvlQLQDTITTLTQKLTTAHRKEAENE 233
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2917-2950 |
3.33e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.33e-04
10 20 30
....*....|....*....|....*....|....
gi 1655220506 2917 LLEAQAASGYIVDPVKNKLLTVDEAVKEELIGPE 2950
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1825-2239 |
3.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1825 LKANEALRLRLRaEEEAQRKSLAQEEAEKQKTEAERDAKKKakaeeaalkQKENAEKELEKQRTF--AEQIAQQKLSAEQ 1902
Cdd:COG4717 70 LKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEA---------ELEELREELEKLEKLlqLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1903 EYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA 1982
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1983 LKMKQLAEEAARLRSVAEEAKKQRQLAEdEAARQRAEAEKILKEKLAAINEATRLKTEAEVAL-----------KAKEAE 2051
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgllallfllLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2052 NERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKS 2131
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2132 DLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKK-IAAAEEEAARQRKAAQDEVERLKQKAAEA 2210
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAEL 458
|
410 420
....*....|....*....|....*....
gi 1655220506 2211 NKLKDKAEKELEKQVILAKEAAQKSTAAE 2239
Cdd:COG4717 459 EAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1698-1899 |
3.49e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1698 TQKKKNAEDELKR-KSEAEKEAARQKQKALdelqkhkMQAEEAERRLKQAEEEKVRQIKvveevaqktaatqlqamsfsE 1776
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEAKKEAEAIKKEAL-------LEAKEEIHKLRNEFEKELRERR--------------------N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1777 KTTKLEESLK-KEQgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKS-LAQEEAEKQ 1854
Cdd:PRK12704 83 ELQKLEKRLLqKEE----NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1855 ---KTEAErdakkkAKAEEAALKQ------KENAEKELEK------QRTFAEQIAQQKLS 1899
Cdd:PRK12704 159 lleKVEEE------ARHEAAVLIKeieeeaKEEADKKAKEilaqaiQRCAADHVAETTVS 212
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1817-2059 |
3.78e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.51 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1817 EKELETWRLKANEalrlrlRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1896
Cdd:PRK07735 4 EKDLEDLKKEAAR------RAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1897 KLSAEQEYI---RLKADFEHAEQQRGlldnELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEK 1973
Cdd:PRK07735 78 KREGTEEVTeeeKAKAKAKAAAAAKA----KAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1974 SKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED-------EAARQRAEAEKILKEKLAAI-----------NEAT 2035
Cdd:PRK07735 154 TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGteevteeEKAKAKAKAAAAAKAKAAALakqkasqgngdSGDE 233
|
250 260
....*....|....*....|....
gi 1655220506 2036 RLKTEAEVALKAKEAENERLKRQA 2059
Cdd:PRK07735 234 DAKAKAIAAAKAKAAAAARAKTKG 257
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2453-2794 |
3.83e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.61 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2453 MKSLAEEAARLsveaeETARQRKTAEAELAEqRALAEKMLK--EKMQAIQEATKLKAEAEELQ------KQKNQAQEKAK 2524
Cdd:pfam05622 68 LEQLQEENFRL-----ETARDDYRIKCEELE-KEVLELQHRneELTSLAEEAQALKDEMDILRessdkvKKLEATVETYK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2525 KLLED----KQEIQQRLDKETQGFQK--SLEAERKRQLEISAEAEKLKLRVKELssaQAKAEEEATRFKKQADEAKvRLQ 2598
Cdd:pfam05622 142 KKLEDlgdlRRQVKLLEERNAEYMQRtlQLEEELKKANALRGQLETYKRQVQEL---HGKLSEESKKADKLEFEYK-KLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2599 ETEKqttetVVQKlETQRLQSTReaDDLKKAIAELE----KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFL 2674
Cdd:pfam05622 218 EKLE-----ALQK-EKERLIIER--DTLRETNEELRcaqlQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2675 TEKELLLKRERDVEDEKKKLQKHLEDevnkAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMK---NKQKEM 2751
Cdd:pfam05622 290 ENKMLRLGQEGSYRERLTELQQLLED----ANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEdssLLKQKL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1655220506 2752 EALEKKRLEqeklLADENKKLREKLESLEVT-SKQAASKTKEIE 2794
Cdd:pfam05622 366 EEHLEKLHE----AQSELQKKKEQIEELEPKqDSNLAQKIDELQ 405
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1599-1752 |
3.83e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.56 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1599 AVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDELQKLRDQAAEAEK 1678
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIK----KLESSIKQVEEELEELKEQNEELEKQYK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1679 VRKA-------AQEEAERLRKQVNEETQKKKNAEDE-------LKRKSEAEKEAARQK----QKALDELQKHKMQAEEAE 1740
Cdd:pfam05667 388 VKKKtldllpdAEENIAKLQALVDASAQRLVELAGQwekhrvpLIEEYRALKEAKSNKedesQRKLEEIKELREKIKEVA 467
|
170
....*....|..
gi 1655220506 1741 RRLKQAEEEKVR 1752
Cdd:pfam05667 468 EEAKQKEELYKQ 479
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1550-2011 |
3.92e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1550 KKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKlkmkedasqrQGLAVDAEKQKQNIQlELTQLKNLSEQEIRSKNQ 1629
Cdd:PRK10246 425 RQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN----------AALNEMRQRYKEKTQ-QLADVKTICEQEARIKDL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1630 qleEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKvrKAAQEEAERLRKQVNEETQKKKNAEDELK 1709
Cdd:PRK10246 494 ---EAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEV--KKLGEEGAALRGQLDALTKQLQRDESEAQ 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1710 RKSEAEKEAARQKQKAL----------DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQlqamSFSEKTT 1779
Cdd:PRK10246 569 SLRQEEQALTQQWQAVCaslnitlqpqDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQ----QIEQRQQ 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1780 KLEESLKKEQGTVLQLQEEAEKLRKQEEEAN--KAREQAEKELETwRLKANEALRLRLRAEEEAQrkslaqEEAEKQKTE 1857
Cdd:PRK10246 645 QLLTALAGYALTLPQEDEEASWLATRQQEAQswQQRQNELTALQN-RIQQLTPLLETLPQSDDLP------HSEETVALD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1858 AER---DAKKKAKAEEAALKQKENAEKE--LEKQRTFAEQIAQQKLSAEQEYIRLKADfehaEQQRGLLDNELQRLKNEV 1932
Cdd:PRK10246 718 NWRqvhEQCLSLHSQLQTLQQQDVLEAQrlQKAQAQFDTALQASVFDDQQAFLAALLD----EETLTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1933 NAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA------LKMKQLAEEAARLRSVAEEAKKQR 2006
Cdd:PRK10246 794 QQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTrqgeirQQLKQDADNRQQQQALMQQIAQAT 873
|
....*
gi 1655220506 2007 QLAED 2011
Cdd:PRK10246 874 QQVED 878
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4461-4494 |
3.94e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.94e-04
10 20 30
....*....|....*....|....*....|....
gi 1655220506 4461 EESGPVAGILDTDTLEKVSVTEAIHRNLVDNITG 4494
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1658-2097 |
3.95e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1658 QKSTADDELQKLRDQAAeaeKVRKAAQEEAERLRKQVNEETqkkknaeDELKRKSEAEKEAARQKQ--KALDELQKHKMQ 1735
Cdd:PRK10246 192 QHKSARTELEKLQAQAS---GVALLTPEQVQSLTASLQVLT-------DEEKQLLTAQQQQQQSLNwlTRLDELQQEASR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1736 AEEAERRLKQAEEEKVRQIKVVEeVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAE---KLRKQEEEANKA 1812
Cdd:PRK10246 262 RQQALQQALAAEEKAQPQLAALS-LAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMAlraRIRHHAAKQSAE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1813 REQAEKELETWrLKANEALRLrLRAEEEAQRKSLAQEEAEKQKTEAERdakkkakAEEAALKQKENAEKELEKQRTFAEQ 1892
Cdd:PRK10246 341 LQAQQQSLNTW-LAEHDRFRQ-WNNELAGWRAQFSQQTSDREQLRQWQ-------QQLTHAEQKLNALPAITLTLTADEV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1893 IAQQKLSAEQEYIR-----LKADFEHAEQQRGLLDNELQRLKNEV---NAAEKQRRQL----EDELAKVRS--------- 1951
Cdd:PRK10246 412 AAALAQHAEQRPLRqrlvaLHGQIVPQQKRLAQLQVAIQNVTQEQtqrNAALNEMRQRykekTQQLADVKTiceqearik 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1952 ---EMDALLQM----------------KIQAEKVSQSNTEKSKqlLETEalkMKQLAEEAARLRSVAEEAKKQRQLAEDE 2012
Cdd:PRK10246 492 dleAQRAQLQAgqpcplcgstshpaveAYQALEPGVNQSRLDA--LEKE---VKKLGEEGAALRGQLDALTKQLQRDESE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2013 AARQRAEaEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAeDEAYQRKLLEDQAAQHKHDI---QEKITQLQS 2089
Cdd:PRK10246 567 AQSLRQE-EQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQL-RLLSQRHELQGQIAAHNQQIiqyQQQIEQRQQ 644
|
....*...
gi 1655220506 2090 SSVSELDR 2097
Cdd:PRK10246 645 QLLTALAG 652
|
|
| MAP70 |
pfam07058 |
Microtubule-associated protein 70; This family represents a family of plant ... |
2504-2787 |
4.01e-04 |
|
Microtubule-associated protein 70; This family represents a family of plant microtubule-associated proteins of size 70 kDa. The proteins contain four predicted coiled-coil domains, and truncation studies identify a central domain that targets the proteins to microtubules. It has no predicted trans-membrane domains, and the region between the coils from approximately residues 240-483 is the targetting region.
Pssm-ID: 399798 [Multi-domain] Cd Length: 544 Bit Score: 46.73 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2504 KLKAEAEEL---QKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEIsaeaEKLKLRVKELSSAQAKAE 2580
Cdd:pfam07058 15 EVRDKDRELgeaLAEIKALRLSERLKEKAVEELTDELLKLDEKLKASENLLESKNLEI----KKINDEKKAALAAQFAAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2581 EEATRFKK-QADEAKVRLQETE-KQTTETVVQKLETQRLQSTREADD---LKKAIAELEKEREK--LKRDAQ---ELQNK 2650
Cdd:pfam07058 91 ATLRRVHAaQKDEDMPPIEAILaPLEAELKLARQEINKLQDDNKALDrltKSKEAALLEAERAVqiALAKASlvdDLQNK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2651 S----KETASAQQEQMEQQKAMLQQTFLTEKELLLKRErdvedekkkLQKHLEDEVNKAKALKDEQqRQQKLMDEEKKKL 2726
Cdd:pfam07058 171 NqelmKQIEICQEENKILDKAHRQKVAEVEKLSQTVRE---------LEEAVLAGGAAANAVRDYQ-RKVKEMNEERRTL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2727 QAIMDEAVKKQKEAEAEMKNKQKE-----MEalEKKRLEQEKLLADENKKLREKLESLEVTSKQAA 2787
Cdd:pfam07058 241 ERELARAKVVANRVATVVANEWKDandkvMP--VKQWLEERRFLQGEMQQLRDKLAISERTAKAEA 304
|
|
| I-BAR_IMD |
cd07605 |
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ... |
2658-2801 |
4.04e-04 |
|
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.
Pssm-ID: 153289 [Multi-domain] Cd Length: 223 Bit Score: 45.05 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2658 QQEQMEQQKAMLQQTFLteKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQR-QQKLMDEEKKKLQAIMDEAVKK 2736
Cdd:cd07605 76 THKSIEASLEQVAKAFH--GELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKaRSELKKLQKKSQKSGTGKYQEK 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 2737 QKEAEAEMKNKQKEMEALEKkrLEQEKLLADENKKLREKLESL-EVTSKQAASKTKEIEVQTDKVP 2801
Cdd:cd07605 154 LDQALEELNDKQKELEAFVS--QGLRDALLEERRRYCFLVDKHcSVAKHEIAYHAKAMTLLSTRLP 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1552-1725 |
4.13e-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: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1552 RMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDAEKQKQNIQLELTQLknlsEQEIRSKNQQL 1631
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1632 EEAQVSRrkleeEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKrK 1711
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE-A 156
|
170
....*....|....
gi 1655220506 1712 SEAEKEAARQKQKA 1725
Cdd:COG1579 157 ELEELEAEREELAA 170
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
202-321 |
4.22e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 43.84 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 202 QKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRNVRLPrekgrmrFHKLQN 272
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTIQEN 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1655220506 273 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 321
Cdd:cd21324 97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2622-2732 |
4.54e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.61 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2622 EADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLlkrerdveDEKKKLQKHLEDE 2701
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELI--------EEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|.
gi 1655220506 2702 VNKAKALKDEQQRQQKLMDEEKKKLQAIMDE 2732
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2545-2878 |
4.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2545 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRL--QSTRE 2622
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEleSLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2623 ADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEV 2702
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2703 NKAKalKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVT 2782
Cdd:COG4372 190 KEAN--RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2783 SKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNGSVEAVKKDGASPLAFEGIRESVPAERLLEIGVLTKKDVDKLK 2862
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330
....*....|....*.
gi 1655220506 2863 KGKVSAQDLSKADKVK 2878
Cdd:COG4372 348 VGLLDNDVLELLSKGA 363
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1801-2056 |
4.66e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1801 KLRKQEEEANKAREQAEKEletwrlkanealrlrlrAEEEAQRKSL-AQEEAEKQKTEAERDAKkkakaeeaalkQKENA 1879
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKE-----------------AEAIKKEALLeAKEEIHKLRNEFEKELR-----------ERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1880 EKELEKqrtfaeqiaqqklsaeqeyiRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEdelaKVRSEMDALLQM 1959
Cdd:PRK12704 84 LQKLEK--------------------RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE----KKEEELEELIEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1960 KIQA-EKVSQSNTEKSKQLLetealkMKQLAEEAarlrsvAEEAKKQRQLAEDEAarqRAEAEKILKEKLA-AIneaTRL 2037
Cdd:PRK12704 140 QLQElERISGLTAEEAKEIL------LEKVEEEA------RHEAAVLIKEIEEEA---KEEADKKAKEILAqAI---QRC 201
|
250 260
....*....|....*....|.
gi 1655220506 2038 KTE--AEVALKAKEAENERLK 2056
Cdd:PRK12704 202 AADhvAETTVSVVNLPNDEMK 222
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2338-2686 |
4.67e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2338 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEE------LQRVKAQVNDAVKQKAQVENELS 2411
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDdhnrasMQRDEAIAAIDNEQQTNSKDGEQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2412 KVKMQMDELLKLKVRIEEENLRLMQ-------------KNKDNTQK-------LLAEEAEKMKSLAEEAARLSVEAEETA 2471
Cdd:PLN02939 125 LSDFQLEDLVGMIQNAEKNILLLNQarlqaledlekilTEKEALQGkinilemRLSETDARIKLAAQEKIHVEILEEQLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2472 RQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLedkqeiqqRLDKETQGFQKSLeae 2551
Cdd:PLN02939 205 KLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVF--------KLEKERSLLDASL--- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2552 rkRQLE---ISAEAEKLKLRVKELSSAQAKAEEEAT---RFKKQADEAKVRLQetEKQTTETVVQKLEtqrlQSTREADD 2625
Cdd:PLN02939 274 --RELEskfIVAQEDVSKLSPLQYDCWWEKVENLQDlldRATNQVEKAALVLD--QNQDLRDKVDKLE----ASLKEANV 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2626 LKKAIAELEKEREKLKRDAQELQNKSKETASaQQEQMEQQKAMLQQTFLTEKELLLKRERD 2686
Cdd:PLN02939 346 SKFSSYKVELLQQKLKLLEERLQASDHEIHS-YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1530-1854 |
4.73e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.18 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDasqrqglavdaEKQKQNI 1609
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLE-----------RARQEAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1610 QLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIH---LIRIQLQTTIKQKSTAD----DELQKLRDQAAEAEKVRKA 1682
Cdd:pfam15558 120 QRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHkrqLKEREEQKKVQENNLSEllnhQARKVLVDCQAKAEELLRR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1683 AQEEAERLRKQVNEETQKKKNAEdELKRKSEAEKEAARQKQ----KALDELQKHK-MQAEEAERRLKQAEEekvrqikVV 1757
Cdd:pfam15558 200 LSLEQSLQRSQENYEQLVEERHR-ELREKAQKEEEQFQRAKwraeEKEEERQEHKeALAELADRKIQQARQ-------VA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1758 EEVAQKTAATQLQAMSFSEKTTKLEEsLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRA 1837
Cdd:pfam15558 272 HKTVQDKAQRARELNLEREKNHHILK-LKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKV 350
|
330
....*....|....*..
gi 1655220506 1838 EEEAQRKSLAQEEAEKQ 1854
Cdd:pfam15558 351 REETNNRTFDKMALEAQ 367
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2396-2691 |
5.25e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.29 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2396 VNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRK 2475
Cdd:pfam09731 109 TKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2476 TAEAELAEQRALAEKmlkekmqaIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQ 2555
Cdd:pfam09731 189 EALAEKLKEVINLAK--------QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2556 LE--------ISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTRE----- 2622
Cdd:pfam09731 261 QElvsifpdiIPVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARleevr 340
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2623 ADDLKKAIAELEKEREKLKRDAQ-----ELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEK 2691
Cdd:pfam09731 341 AADEAQLRLEFEREREEIRESYEeklrtELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1891-2306 |
5.81e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.05 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1891 EQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSN 1970
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1971 TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 2050
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2051 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEK 2130
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2131 SDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA 2210
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2211 NKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQK 2290
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAA 512
|
410
....*....|....*.
gi 1655220506 2291 AEEAEKLKKAAEDEAA 2306
Cdd:COG5278 513 AEAALAAALAAALASA 528
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1543-1810 |
6.01e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.39 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1543 EKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLeltqLKNLSEQ 1622
Cdd:PLN03229 514 EKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEA----LKAEVAS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1623 EIRSKNQQLEEA---QVSRRKLEEEIHLIRIQlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQ 1699
Cdd:PLN03229 590 SGASSGDELDDDlkeKVEKMKKEIELELAGVL------KSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKIE 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1700 KKKNAEDeLKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKvveevaQKTAATQLQAMSFSEKTT 1779
Cdd:PLN03229 664 RVIRSSD-LKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELK------EKFEELEAELAAARETAA 736
|
250 260 270
....*....|....*....|....*....|.
gi 1655220506 1780 KLEESLKKEqgtvlQLQEEAEKLRKQEEEAN 1810
Cdd:PLN03229 737 ESNGSLKND-----DDKEEDSKEDGSRVEVN 762
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2576-2796 |
6.51e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2576 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrlqstreaddlkkaIAELEKEREKLKRDAQELQNKSKETA 2655
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR--------------AAEQARQKELEQRAAAEKAAKQAEQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2656 SAQQEqmEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQ----KLMDEEKKKlqaimD 2731
Cdd:TIGR02794 111 AKQAE--EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEeakkKAEAEAKAK-----A 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 2732 EAVKKQKEAEAEMKNKQ--KEMEALEKKRLEQEKLLADENKKLReKLESLEVTSKQAASKTKEIEVQ 2796
Cdd:TIGR02794 184 EAEAKAKAEEAKAKAEAakAKAAAEAAAKAEAEAAAAAAAEAER-KADEAELGDIFGLASGSNAEKQ 249
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1435-1750 |
6.74e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1435 LKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDY---------EFQILAYRALQDPIASPLKKPKMESASDNIIQ 1505
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelesrvaELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1506 EYVTL-------RTRYSEL----STLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmaeiqAQLETQKQLAEGHAKSV 1574
Cdd:pfam07888 116 EKDALlaqraahEARIRELeediKTLTQRVLERETELERMKERAKKAGAQRKEEEAER-----KQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1575 AKaelEAQELKLKMKEDASQRQGLAVDAEKQKQNI------QLELTQLK----------NLSEQEIRSKNQQLEEAQVSR 1638
Cdd:pfam07888 191 SK---EFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLeelrslqerlNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1639 RKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQ-AAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKE 1717
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350
....*....|....*....|....*....|...
gi 1655220506 1718 AARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1750
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2435-2667 |
6.78e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.74 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2435 MQKNKDnTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAtklKAEAEELQK 2514
Cdd:PRK07735 1 MDPEKD-LEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAA---KAKAAALAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2515 QKNQAQEKAKKllEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEeatrFKKQADEAK 2594
Cdd:PRK07735 77 QKREGTEEVTE--EEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAA----LAKQKREGT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2595 VRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2667
Cdd:PRK07735 151 EEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKA 223
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2542-2803 |
7.13e-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: 45.19 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2542 QGFQKSLEAERKRQLEISAEAEKL----KLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ-----TTETVVQKL 2612
Cdd:pfam15905 27 QRFRKQKAAESQPNLNNSKDASTPatarKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQdkrlqALEEELEKV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2613 ETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM-LQQTFLTEKELLLKRERDVEDEK 2691
Cdd:pfam15905 107 EAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSMELMkLRNKLEAKMKEVMAKQEGMEGKL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2692 KKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEaEMKNKQKEMEALEKKRLEQEKLLADENKK 2771
Cdd:pfam15905 187 QVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-QVEKYKLDIAQLEELLKEKNDEIESLKQS 265
|
250 260 270
....*....|....*....|....*....|..
gi 1655220506 2772 LREKLESLEVTSKQAASKTKEIEVQTDKVPEE 2803
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2290-2555 |
7.21e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2290 KAEEAEKLKKAAEDEAAKQA---KAQKDAERlrkeaeaeaakraaaeaAALKQ-KQEADAEMAKHKKEAE----QALKQK 2361
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQNAladKERAEADR-----------------QRLEQeKQQQLAAISGSQSQLEstdqNALETN 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2362 SQVEKELglVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENE-----LSKVKMQMDELlKLKVRIEEENLRlmQ 2436
Cdd:NF012221 1604 GQAQRDA--ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDA-KKISGKQLADAK--Q 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2437 KNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTaEAELAEQRALAEKmlkekmqaiQEATKLKAEAEELQKQK 2516
Cdd:NF012221 1679 RHVDNQQKV-KDAVAKSEAGVAQGEQNQANAEQDIDDAKA-DAEKRKDDALAKQ---------NEAQQAESDANAAANDA 1747
|
250 260 270
....*....|....*....|....*....|....*....
gi 1655220506 2517 NQAQEKAKKLLEDKQEIQQrldKETQGFQKSLEAERKRQ 2555
Cdd:NF012221 1748 QSRGEQDASAAENKANQAQ---ADAKGAKQDESDKPNRQ 1783
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2457-2720 |
7.88e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2457 AEEAARLSVEAE-----ETARQRKTAEAElaeqRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKakkLLEDKQ 2531
Cdd:PRK11281 29 AASNGDLPTEADvqaqlDALNKQKLLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAK---LRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2532 EIQQRLDKETQGFQKSLEAERKRQLEisaeaEKLKLRVKELSSAQAKAEEEAT----------RFKKQADEAKVRLQETE 2601
Cdd:PRK11281 102 ELEALKDDNDEETRETLSTLSLRQLE-----SRLAQTLDQLQNAQNDLAEYNSqlvslqtqpeRAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2602 KQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDA--QELQNKSKETASAQQEQMEQQKAMLQQtfltekel 2679
Cdd:PRK11281 177 NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlQDLLQKQRDYLTARIQRLEHQLQLLQE-------- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1655220506 2680 LLKRERDVEDEKKKLQKHLEDEVNKAKA---LKDEQQRQQKLMD 2720
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQAnplVAQELEINLQLSQ 292
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1443-2108 |
8.12e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1443 KKLLEEIEKNKDQIENCQKDAKAYIDSLKDyefQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTS 1522
Cdd:TIGR01612 1121 KNLDQKIDHHIKALEEIKKKSENYIDEIKA---QINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLN 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1523 QyIKFILETQRRLEDDEKASEKLKEDEKKRMAEiqaQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQrQGLAVDA 1602
Cdd:TIGR01612 1198 E-IAEIEKDKTSLEEVKGINLSYGKNLGKLFLE---KIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENE-MGIEMDI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1603 EKQKQNIQLE---------LTQLKNLSEQEIRSKNQQLEEAQVSrrklEEEIHLIRIQLQTTIKQKSTADDELQKLRDQA 1673
Cdd:TIGR01612 1273 KAEMETFNIShdddkdhhiISKKHDENISDIREKSLKIIEDFSE----ESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1674 AEAEKVRK--AAQEEAERLRKQVNEETQKKKNAEDELkrkSEAEKEAARQKQKALDELQKHKMQA-------EEAERRLK 1744
Cdd:TIGR01612 1349 ANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDEL---DKSEKLIKKIKDDINLEECKSKIEStlddkdiDECIKKIK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1745 Q------AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGT------VLQLQEEAEKLRKQEEEANKA 1812
Cdd:TIGR01612 1426 ElknhilSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATndhdfnINELKEHIDKSKGCKDEADKN 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1813 REQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQkteaerdakkkakaeeaalkQKENAEKELEKQRTFAEQ 1892
Cdd:TIGR01612 1506 AKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSE--------------------IIIKEIKDAHKKFILEAE 1565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1893 IAQQKlsaeqeyirlkadfehaeqqrglldnelqrlkneVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKvsqsnte 1972
Cdd:TIGR01612 1566 KSEQK----------------------------------IKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEN------- 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1973 kskqlLETEALKMKQLAEEAARLRSVAEEAKKqrQLAEDEAARQRAEaekiLKEKLAAINEatrLKTEAEvALKAKEAEN 2052
Cdd:TIGR01612 1605 -----FENKFLKISDIKKKINDCLKETESIEK--KISSFSIDSQDTE----LKENGDNLNS---LQEFLE-SLKDQKKNI 1669
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2053 ERLKRQAEDEAYQRKLLEDQAAQHKHD----IQEKITQLQSSSVSELDRQKNIVEETLRQ 2108
Cdd:TIGR01612 1670 EDKKKELDELDSEIEKIEIDVDQHKKNyeigIIEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2628-2804 |
8.37e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2628 KAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELllkreRDVEDEKKKLQKHLedevnkaKA 2707
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAEL-------AE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2708 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKkRLEQEKLLADENKK----LREKLESLEVTS 2783
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREqaeeLRADLAELAALR 166
|
170 180
....*....|....*....|.
gi 1655220506 2784 KQAASKTKEIEVQTDKVPEEQ 2804
Cdd:COG4942 167 AELEAERAELEALLAELEEER 187
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
204-308 |
8.42e-04 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 45.70 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 204 KTFTKWVNKHLMKAQrhITDLYEDLRDGhnlISLLEVLSGETLPRERDLVR-NVRLPREKGRMRFHKLQNVQIALDFLKH 282
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLvKKQPASGIEENRFKAFENENYAVDLGIT 456
|
90 100
....*....|....*....|....*.
gi 1655220506 283 RQVKLVNIRNDDIADGNpKLTLGLIW 308
Cdd:COG5069 457 EGFSLVGIKGLEILDGI-RLKLTLVW 481
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1681-2075 |
8.70e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.40 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1681 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAarqKQKALDELQKHKMQAEEAERRLKQAEEEKvRQIKVVEEV 1760
Cdd:pfam05701 27 KAHRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAA---KAQVLEELESTKRLIEELKLNLERAQTEE-AQAKQDSEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1761 AQktaaTQLQAMsfsekttklEESLKKEQGTVLQLQEEAEKLRKQE--EEANKAREqaekELETWRLKANEALRLRLRAE 1838
Cdd:pfam05701 103 AK----LRVEEM---------EQGIADEASVAAKAQLEVAKARHAAavAELKSVKE----ELESLRKEYASLVSERDIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1839 EEAQRKSLAQEEAEKQKTEAerdakkkakaeeaalKQKENAEKE-LEKQRTFAEQIAQQKLSA----EQEYIRLKADFEH 1913
Cdd:pfam05701 166 KRAEEAVSASKEIEKTVEEL---------------TIELIATKEsLESAHAAHLEAEEHRIGAalarEQDKLNWEKELKQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1914 AEQqrglldnELQRLKNEVNAAEKQRRQLE---DELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLL-ETEALKMKQLA 1989
Cdd:pfam05701 231 AEE-------ELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIqAALASAKKELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1990 E----------EAARLRSVAE--EAKKQRQLAEDEAARQRAEAEKILKEKLAAinEATRLKTEAEVA-LKAKEAENERLK 2056
Cdd:pfam05701 304 EvkaniekakdEVNCLRVAAAslRSELEKEKAELASLRQREGMASIAVSSLEA--ELNRTKSEIALVqAKEKEAREKMVE 381
|
410 420
....*....|....*....|....
gi 1655220506 2057 -----RQAEDEAYQRKLLEdQAAQ 2075
Cdd:pfam05701 382 lpkqlQQAAQEAEEAKSLA-QAAR 404
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1662-1813 |
9.13e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.80 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1662 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKhKMQAEEAER 1741
Cdd:PRK10811 625 DNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQAQQEA-KALNVEEQS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1742 RLKQAEEEKVRQI-----------KV-VEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEA 1809
Cdd:PRK10811 704 VQETEQEERVQQVqprrkqrqlnqKVrIEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEEN 783
|
....
gi 1655220506 1810 NKAR 1813
Cdd:PRK10811 784 NAEN 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1212-1803 |
9.19e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1212 QKTAEQMKVQSELEGLKKDLNSITEKTEEILASPQqsssapmlrseldvtlkkmdhvyglssvyldKLKTIDIVIRNTKD 1291
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEG-------------------------------SKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1292 AEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQL 1371
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1372 AGSLLERWQAVFAQIDLRQRELSLLGRhMNSYKQsyewliqwlREARLRQEKIEAAPVWDSKAlKEQLTQEkklLEEIEK 1451
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEE-LERLKK---------RLTGLTPEKLEKELEELEKA-KEEIEEE---ISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1452 NKDQIENCQKDAKAYIDSLK---------------DYEFQILA-YRALQDPIASPLKkpKMESASDNIIQEYVTLRTRYS 1515
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKkakgkcpvcgrelteEHRKELLEeYTAELKRIEKELK--EIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1516 ELSTLTSQY--IKFILETQRRLE--DDEKASEKLKEDE--KKRMAEIQAQLETQKQLAEghaksvakaelEAQELKLKMK 1589
Cdd:PRK03918 491 KESELIKLKelAEQLKELEEKLKkyNLEELEKKAEEYEklKEKLIKLKGEIKSLKKELE-----------KLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1590 EDASQRQglavDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL 1669
Cdd:PRK03918 560 ELEKKLD----ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1670 RDQAAEAEKVRKaaqeEAERLRKQVNEETQKKKNAE-----DELKRKSEAEKEAARQKQ---KALDELQKHKMQAEEAER 1741
Cdd:PRK03918 636 AETEKRLEELRK----ELEELEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREeikKTLEKLKEELEEREKAKK 711
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 1742 RLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS-FSEKTTKLEESLKKEQGTVLQLQEEAEKLR 1803
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKALLKERALSkVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
2430-2803 |
9.22e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 45.44 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2430 ENLRLMQKNKDNTQKLLAEEA----EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA----IQE 2501
Cdd:pfam15070 4 ESLKQLQTERDQYAENLKEEGavwqQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPpagpSEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2502 ATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQqRLDKETQgfQKSLEAERkrQLEISAEAEKLKLRVkeLSSAQAkaeE 2581
Cdd:pfam15070 84 EQRLQEEAEQLQKELEALAGQLQAQVQDNEQLS-RLNQEQE--QRLLELER--AAERWGEQAEDRKQI--LEDMQS---D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2582 EAT--RFKKQADEAKVRLQETEKQTTETVVQKLE-TQRLQSTREA-DDLKKAIAELEKEREKLKrdaQELQNKSKEtASA 2657
Cdd:pfam15070 154 RATisRALSQNRELKEQLAELQNGFVKLTNENMElTSALQSEQHVkKELAKKLGQLQEELGELK---ETLELKSQE-AQS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2658 QQEQMEQQKAMLQQ------TFLTEKELLLKRERDVEDEKKKLQ-KHLEDEVNKAKALKDEQQRQQKL--MDEEKKKLQA 2728
Cdd:pfam15070 230 LQEQRDQYLAHLQQyvaayqQLASEKEELHKQYLLQTQLMDRLQhEEVQGKVAAEMARQELQETQERLeaLTQQNQQLQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2729 -----------------IMDEAVKKQKEAEAEMKNKQKEMEA--------LEKKRLEQEKLLADENKKLREKLESLEVTS 2783
Cdd:pfam15070 310 qlsllanpgegdgleseEEEEEAPRPSLSIPEDFESREAMVAffnsalaqAEEERAELRRQLKEQKRRCRRLAQQAAPAQ 389
|
410 420
....*....|....*....|
gi 1655220506 2784 KQAASKTKEIEVQTDKVPEE 2803
Cdd:pfam15070 390 EEPEHEAHAPGTGGDSVPVE 409
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1670-1858 |
9.28e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1670 RDQAAEAEKVRKAAQEEAErlrkqvnEETQKKKNAEDELKRKSEAEKEAARQKQKALD-------ELQKHKMQAEEAERR 1742
Cdd:PRK05035 464 REKAAREARHKKAAEARAA-------KDKDAVAAALARVKAKKAAATQPIVIKAGARPdnsaviaAREARKAQARARQAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1743 LKQAEEEKVRQIKVVEEVAQKTAATQLQAmsfsEKTTKLEESLKKEQGTVLQLQEEAeKLRKQEEEANKAREQAEKELET 1822
Cdd:PRK05035 537 KQAAAAADPKKAAVAAAIARAKAKKAAQQ----AANAEAEEEVDPKKAAVAAAIARA-KAKKAAQQAASAEPEEQVAEVD 611
|
170 180 190
....*....|....*....|....*....|....*.
gi 1655220506 1823 WRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEA 1858
Cdd:PRK05035 612 PKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA 647
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2426-2610 |
9.29e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2426 RIEEENLRLMQKNKDNTQKLLAEEAEKMKslaEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKL 2505
Cdd:pfam15709 347 RLEVERKRREQEEQRRLQQEQLERAEKMR---EELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2506 KAEA---EELQKQKNQAQEKAKKLLEDKqeiQQRLDKETQgfqksLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE 2582
Cdd:pfam15709 424 QQEEfrrKLQELQRKKQQEEAERAEAEK---QRQKELEMQ-----LAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAE 495
|
170 180
....*....|....*....|....*...
gi 1655220506 2583 ATRfKKQADEAKVRLQETEKQTTETVVQ 2610
Cdd:pfam15709 496 ERR-QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2345-2602 |
9.48e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.39 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2345 AEMAKHKKEAEQalKQKSQVEKEL--------GLVKLQLDETDKQKALMDEELQRVKAQV---NDAVKQ-KAQVENE--- 2409
Cdd:NF033838 142 AEATKKVEEAEK--KAKDQKEEDRrnyptntyKTLELEIAESDVEVKKAELELVKEEAKEprdEEKIKQaKAKVESKkae 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2410 ---LSKVKMQMDELL-KLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQR 2485
Cdd:NF033838 220 atrLEKIKTDREKAEeEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2486 ALAEKMLKEKMQAIQEATKlKAEAEELQKQKNQAQEKAKKL-LE------DKQEIQQRLDKETQgfQKSLEAERKRQLEI 2558
Cdd:NF033838 300 LKPEKKVAEAEKKVEEAKK-KAKDQKEEDRRNYPTNTYKTLeLEiaesdvKVKEAELELVKEEA--KEPRNEEKIKQAKA 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1655220506 2559 SAEAEKLK-LRVKELSSAQAKAEEEATRfkKQADEAKVRLQETEK 2602
Cdd:NF033838 377 KVESKKAEaTRLEKIKTDRKKAEEEAKR--KAAEEDKVKEKPAEQ 419
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1525-1754 |
9.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1525 IKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksVAKAELEAQELklkmkedasqRQGLAvDAEK 1604
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-----YSWDEIDVASA----------EREIA-ELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1605 QKQNIQLELTQLKNLSEQ------EIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEA-- 1676
Cdd:COG4913 676 ELERLDASSDDLAALEEQleeleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErf 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1677 --EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRK--------------SEAEKEAARQKQKALDELQKHKM--QAEE 1738
Cdd:COG4913 756 aaALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewpaetadLDADLESLPEYLALLDRLEEDGLpeYEER 835
|
250
....*....|....*.
gi 1655220506 1739 AERRLKQAEEEKVRQI 1754
Cdd:COG4913 836 FKELLNENSIEFVADL 851
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1433-1818 |
9.75e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1433 KALKEQLTQEKKLLEEIEKNKDQIENCQKDakayidslkdyefqILAYRALQDPIASPLKKpKMESASDNiIQEYVTLrt 1512
Cdd:PRK04778 126 EELQELLESEEKNREEVEQLKDLYRELRKS--------------LLANRFSFGPALDELEK-QLENLEEE-FSQFVEL-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1513 ryselsTLTSQYI---KFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtqkQLAEGHAKSVAKA--------ELEA 1581
Cdd:PRK04778 188 ------TESGDYVearEILDQLEEELAALEQIMEEIPELLKELQTELPDQLQ---ELKAGYRELVEEGyhldhldiEKEI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1582 QELKLKMKEDASQRQGLAVD-AEKQKQNIQLELTQLKNLSEQEIRSKN----------QQLEEAQVSRRKLEEEIHLIR- 1649
Cdd:PRK04778 259 QDLKEQIDENLALLEELDLDeAEEKNEEIQERIDQLYDILEREVKARKyveknsdtlpDFLEHAKEQNKELKEEIDRVKq 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1650 --------IQLQTTI-KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVN--EETQKKKNaeDELK--RKSEAEk 1716
Cdd:PRK04778 339 sytlneseLESVRQLeKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEeiEKEQEKLS--EMLQglRKDELE- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1717 eaARQKqkaLDELQ------KHKMQA--------------EEAERRLKQAEEEkVRQIKV-VEEVAQKTAATQLQAMSFS 1775
Cdd:PRK04778 416 --AREK---LERYRnklheiKRYLEKsnlpglpedylemfFEVSDEIEALAEE-LEEKPInMEAVNRLLEEATEDVETLE 489
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1655220506 1776 EKTTKLEESlkkeqgTVL--QLQEEAEKLRKQEEEANKAREQAEK 1818
Cdd:PRK04778 490 EETEELVEN------ATLteQLIQYANRYRSDNEEVAEALNEAER 528
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1677-1834 |
9.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1677 EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQkaldELQKHKMQAEEAERRLKQAEEEKVRQIkv 1756
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKE----ELEEKKEKLQEEEDKLLEEAEKEAQQA-- 578
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1757 VEEvAQKTAATQLQAMSFSEkttKLEESLKKEQgtvlQLQEEAEKLRKQEEEANKarEQAEKELETWRLKANEALRLR 1834
Cdd:PRK00409 579 IKE-AKKEADEIIKELRQLQ---KGGYASVKAH----ELIEARKRLNKANEKKEK--KKKKQKEKQEELKVGDEVKYL 646
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1651-1934 |
9.92e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.60 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1651 QLQTTIKQKSTADDELQKLRDQA-AEAEKvRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAL-DE 1728
Cdd:NF012221 1543 QADAVSKHAKQDDAAQNALADKErAEADR-QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAVtKE 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1729 LQKhKMQAEEAERRLKQAEEEKVRQ---------IKVVEEV---AQKTAATQLQAMS--FSEKTTKLEESLKKEQGTVLQ 1794
Cdd:NF012221 1622 LTT-LAQGLDALDSQATYAGESGDQwrnpfagglLDRVQEQlddAKKISGKQLADAKqrHVDNQQKVKDAVAKSEAGVAQ 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1795 lqeeAEKLRKQEEEA-NKAREQAEKeletwrlKANEALRLRLRAEEEAQRKSLAQEEAEKQ-KTEAERDAKKKAKAEEAA 1872
Cdd:NF012221 1701 ----GEQNQANAEQDiDDAKADAEK-------RKDDALAKQNEAQQAESDANAAANDAQSRgEQDASAAENKANQAQADA 1769
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1873 LKQKENAEKELEKQRTFAEQIAQQKLSAE---QEYIRLKADFEHAEQQR---GLLDNELQRLKNEVNA 1934
Cdd:NF012221 1770 KGAKQDESDKPNRQGAAGSGLSGKAYSVEgvaEPGSHINPDSPAAADGRfseGLTEQEQEALEGATNA 1837
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2525-2777 |
1.02e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 45.05 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2525 KLLEDKQEIQQRLDKETQgfqksleaeRKRQLEISAEAEKLKLRVKELSSAQAKA--EEEATRFKKQADEAKVRLQETEK 2602
Cdd:pfam15742 6 KLKYQQQEEVQQLRQNLQ---------RLQILCTSAEKELRYERGKNLDLKQHNSllQEENIKIKAELKQAQQKLLDSTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2603 QTT------ETVVQKLETQRLQSTREADDLKkAIAELEKEREKLKRDAQELQNKSKETasaqQEQMEQ-QKAMLQQTFLT 2675
Cdd:pfam15742 77 MCSsltaewKHCQQKIRELELEVLKQAQSIK-SQNSLQEKLAQEKSRVADAEEKILEL----QQKLEHaHKVCLTDTCIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2676 EKELLLKRERDVEDEKKKLQKHLEdevnkakalkdEQQRQQKLMDEEKKKLQaiMDEAVKKQKEAEAEMKNKQ-----KE 2750
Cdd:pfam15742 152 EKKQLEERIKEASENEAKLKQQYQ-----------EEQQKRKLLDQNVNELQ--QQVRSLQDKEAQLEMTNSQqqlriQQ 218
|
250 260
....*....|....*....|....*..
gi 1655220506 2751 MEALEKKrLEQEKLLADENKKLREKLE 2777
Cdd:pfam15742 219 QEAQLKQ-LENEKRKSDEHLKSNQELS 244
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2492-2798 |
1.02e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2492 LKEKMQAI-QEATKLKAEAEELQ---KQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEA-ERK---RQLEISAEAE 2563
Cdd:pfam10174 329 LKESLTAKeQRAAILQTEVDALRlrlEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVkERKinvLQKKIENLQE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2564 KLKLRVKELSSAQAKAEEEATRfKKQADEAKVRLQE--TEKqttETVVQKLETQRLQSTR----EADDLKKAIAELEKER 2637
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTD-SSNTDTALTTLEEalSEK---ERIIERLKEQREREDRerleELESLKKENKDLKEKV 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2638 EKLKRDAQELQ---NKSKETASAQQEQMEQQKAMLQQTfltEKELLLKRER--DVEDEKKKLQKHLEDE------VNKAK 2706
Cdd:pfam10174 485 SALQPELTEKEsslIDLKEHASSLASSGLKKDSKLKSL---EIAVEQKKEEcsKLENQLKKAHNAEEAVrtnpeiNDRIR 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2707 ALKDEQQRQQklmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKllaDENKKLREKLESLEVTSKQA 2786
Cdd:pfam10174 562 LLEQEVARYK----EESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMK---EQNKKVANIKHGQQEMKKKG 634
|
330
....*....|..
gi 1655220506 2787 ASKTKEIEVQTD 2798
Cdd:pfam10174 635 AQLLEEARRRED 646
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1786-1949 |
1.04e-03 |
|
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: 44.84 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1786 KKEQGTVLQLQEEAEKL---RKQEEE----------ANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLA----- 1847
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAekqRAAEQArqkeleqraaAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAeaerk 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1848 -QEEAEKQKtEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRglldnelq 1926
Cdd:TIGR02794 144 aKEEAAKQA-EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAE-------- 214
|
170 180
....*....|....*....|...
gi 1655220506 1927 RLKNEVNAAEKQRRQLEDELAKV 1949
Cdd:TIGR02794 215 AEAAAAAAAEAERKADEAELGDI 237
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2191-2369 |
1.04e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRKAAQDEVERLKQKA-AEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKL 2269
Cdd:COG2268 199 RDARIAEAEAERETEIAiAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2270 AQAAETAKEKAEKEaallrqKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaakraaaeaAALKQKQEADAEMAK 2349
Cdd:COG2268 279 VQRQLEIAEREREI------ELQEKEAEREEAELEADVRKPAEAEKQA-----------------AEAEAEAEAEAIRAK 335
|
170 180
....*....|....*....|
gi 1655220506 2350 HKKEAEqALKQKSQVEKELG 2369
Cdd:COG2268 336 GLAEAE-GKRALAEAWNKLG 354
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1545-1750 |
1.07e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1545 LKEDEKKRMAEIQ-AQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQE 1623
Cdd:pfam06008 33 SPENAHKIQIEILeKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGEND 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1624 IRSKNQQLEEAQVSRRKLEEEIhliriQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNeetQKKKN 1703
Cdd:pfam06008 113 FALPSSDLSRMLAEAQRMLGEI-----RSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALR---DSLAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220506 1704 AEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1750
Cdd:pfam06008 185 YEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQK 231
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1710-2063 |
1.11e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.23 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1710 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ-AEEEKVRQIKvvEEVAQKTAATqLQAMSFSEKTTKLEESLKK- 1787
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKESSSKPSElALNEMIEKLK--KEIDLEYTEA-VIAMGLQERLENLREEFSKa 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1788 ---EQGTVLQLQEEAEKLrKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKK 1864
Cdd:PLN03229 499 nsqDQLMHPVLMEKIEKL-KDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIK 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1865 kakaeeaalkqkenaekelEKQRTFAEQIAQQKLSAEQEyirlkadfehaeqqrglLDNELqrlkneVNAAEKQRRQLED 1944
Cdd:PLN03229 578 -------------------EKMEALKAEVASSGASSGDE-----------------LDDDL------KEKVEKMKKEIEL 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1945 ELAKVRSEMDallqmkIQAEKVSQSNTEKSKQLLETE-ALKMKQLAEE----------AARLRSVAEEAKKQRQLA---E 2010
Cdd:PLN03229 616 ELAGVLKSMG------LEVIGVTKKNKDTAEQTPPPNlQEKIESLNEEinkkiervirSSDLKSKIELLKLEVAKAsktP 689
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2011 DEAARQRAEA-EKILKEKLAAINEATRLKT-----EAEVALKAK--EAENERLKRQAEDEA 2063
Cdd:PLN03229 690 DVTEKEKIEAlEQQIKQKIAEALNSSELKEkfeelEAELAAAREtaAESNGSLKNDDDKEE 750
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1543-1858 |
1.17e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.97 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1543 EKLKEDEKKRMAEiQAQLETQKQLAEGHAKSVAKAELEAQElklkmKEDASQRQGlAVDAEKQKQniqleltqlknlseq 1622
Cdd:PRK07735 4 EKDLEDLKKEAAR-RAKEEARKRLVAKHGAEISKLEEENRE-----KEKALPKND-DMTIEEAKR--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1623 eiRSKNQQLEEAQVSRRKLEEEIhliriqlqttikqKSTADDELQKLRDQAAEAEKVRKAAqeeaerLRKQVNEETQKKK 1702
Cdd:PRK07735 62 --RAAAAAKAKAAALAKQKREGT-------------EEVTEEEKAKAKAKAAAAAKAKAAA------LAKQKREGTEEVT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1703 naEDELKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEEKvrqikvVEEVAQKTAATQLQAMSFSEKTTKLE 1782
Cdd:PRK07735 121 --EEEKAAAKAKAAAAAKAKAAALAK------QKREGTEEVTEEEEET------DKEKAKAKAAAAAKAKAAALAKQKAA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1783 ESlkkEQGTVLQLQEEAEKLRKQEEEANKAREQA-----------EKELETWRLKANEALRLRLRAEEEAQRKSLAQEEA 1851
Cdd:PRK07735 187 EA---GEGTEEVTEEEKAKAKAKAAAAAKAKAAAlakqkasqgngDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKE 263
|
....*..
gi 1655220506 1852 EKQKTEA 1858
Cdd:PRK07735 264 EEPKQEE 270
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1923-2086 |
1.18e-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: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1923 NELQRlKNEVNAAEKQRRQledELAKVRSEMDalLQMKIQAEkvSQSNTEKSKQLLETEALKMKQLAEEAARLRSV---- 1998
Cdd:COG2268 206 AEAER-ETEIAIAQANREA---EEAELEQERE--IETARIAE--AEAELAKKKAEERREAETARAEAEAAYEIAEAnaer 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1999 -----AEEAKKQRQ--LAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEV-ALKAK---EAENERLKRQAEdEAYQRK 2067
Cdd:COG2268 278 evqrqLEIAEREREieLQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAeAIRAKglaEAEGKRALAEAW-NKLGDA 356
|
170
....*....|....*....
gi 1655220506 2068 LLEDQAAQHKHDIQEKITQ 2086
Cdd:COG2268 357 AILLMLIEKLPEIAEAAAK 375
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
349-430 |
1.21e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 41.52 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 349 RCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQ-AFSVAE--RELGVTRLLDPEdvDVAHPDEKSIITYV 425
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTPE--DIVSGNPRLNLAFV 109
|
....*
gi 1655220506 426 SSLYD 430
Cdd:cd21218 110 ATLFN 114
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1582-1746 |
1.24e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1582 QELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST 1661
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1662 AD------DELQKLRDQAAEAEKVRKAAQEEAERLR----------KQVNEETQKKKNAE--------------DELKRK 1711
Cdd:PRK00409 603 SVkaheliEARKRLNKANEKKEKKKKKQKEKQEELKvgdevkylslGQKGEVLSIPDDKEaivqagimkmkvplSDLEKI 682
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1655220506 1712 SEAEKEAARQKQKALDELQK-------HKMQAEEAERRLKQA 1746
Cdd:PRK00409 683 QKPKKKKKKKPKTVKPKPRTvsleldlRGMRYEEALERLDKY 724
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1915-2513 |
1.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1915 EQQRGLLDN--------ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLEtealkmk 1986
Cdd:PRK02224 183 SDQRGSLDQlkaqieekEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1987 qLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEklaaiNEATRLKTEAEvalkakEAENERLKRQAEDEAYQR 2066
Cdd:PRK02224 256 -LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-----RDDLLAEAGLD------DADAEAVEARREELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2067 KLLEDQAAQHKHDIQEKITQLqsssvseldrqkniveETLRqkkvveEEIHIIRINFERASKEKSDLEVELKKLKGIADE 2146
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEA----------------ESLR------EDADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2147 TQkskakaeeeaeklkKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVI 2226
Cdd:PRK02224 382 RR--------------EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2227 LAkeAAQKSTAAEQKAQD--VLSKNKEDLLSQEKLRDEFENAKklaqaaetakekaeKEAALLRQKAEEAEKLKKaAEDE 2304
Cdd:PRK02224 448 LL--EAGKCPECGQPVEGspHVETIEEDRERVEELEAELEDLE--------------EEVEEVEERLERAEDLVE-AEDR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2305 AAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEqalKQKSQVEKELGLVKlqldETDKQKAL 2384
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA---EAEEEAEEAREEVA----ELNSKLAE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2385 MDEELQRvkaqvndavkqkaqveneLSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQK--LLAEEAEKMKSLAEEaar 2462
Cdd:PRK02224 584 LKERIES------------------LERIRTLLAAIADAEDEIERLREKREALAELNDERreRLAEKRERKRELEAE--- 642
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2463 LSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQ-EATKLKAEAEELQ 2513
Cdd:PRK02224 643 FDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQaEIGAVENELEELE 694
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2446-2573 |
1.41e-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: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2446 LAEEAEKMKSLAEEAARLSVEAEETARQRKtaEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK 2525
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEE--EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1655220506 2526 LLEDKQEIqQRLDKETQGFQKSLEAERKRQLEISAEAEKLK-LRVKELS 2573
Cdd:COG2433 460 EIRKDREI-SRLDREIERLERELEEERERIEELKRKLERLKeLWKLEHS 507
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1530-1749 |
1.41e-03 |
|
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: 44.45 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQL--AEGHAKSVAKAELEAQELKLKMKEDASQRQglAVDAEKQKQ 1607
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAkqAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA--EAEAERKAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1608 niqlelTQLKNLSEQEirsknQQLEEAQVSRRKLEEeihliriqlqttIKQKSTADDELQKLRDQAAEAEKvrkaAQEEA 1687
Cdd:TIGR02794 146 ------EEAAKQAEEE-----AKAKAAAEAKKKAEE------------AKKKAEAEAKAKAEAEAKAKAEE----AKAKA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 1688 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1749
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2446-2559 |
1.42e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2446 LAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAE---KMLKEKMQAIQEATkLKAEAEELQKQKNQAQEK 2522
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEekqQELEAQLEQLQEKA-AETSQERKQKRKEITDQA 225
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1655220506 2523 AKKLLEDKQE----IQQRL-------DKETQGFQKSLEAERKRQLEIS 2559
Cdd:PRK11448 226 AKRLELSEEEtrilIDQQLrkagweaDSKTLRFSKGARPEKGRNLAIA 273
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1664-1732 |
1.43e-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: 42.08 E-value: 1.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 1664 DELQKLRDQA----AEAEKVRKAAQEEAERLRKQVNEETQK-----KKNAEDELKR-KSEAEKEAARQKQKALDELQKH 1732
Cdd:COG0711 41 AEAERAKEEAeaalAEYEEKLAEARAEAAEIIAEARKEAEAiaeeaKAEAEAEAERiIAQAEAEIEQERAKALAELRAE 119
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1576-2268 |
1.48e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1576 KAELEAQELKLKMKEDasqrqgLAVDAEKQKQNIQlelTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTT 1655
Cdd:TIGR04523 46 KNELKNKEKELKNLDK------NLNKDEEKINNSN---NKIKIL-EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1656 IKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKkknAEDELKRKSEAEKEaarqkqkaLDELQKHKMQ 1735
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK---YNDLKKQKEELENE--------LNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1736 AEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEANKAREQ 1815
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1816 AEKELETWRLKANEAlrlrlraeeEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQ 1895
Cdd:TIGR04523 262 QNKIKKQLSEKQKEL---------EQNNKKIKELEKQLNQLKSE--------------ISDLNNQKEQDWNKELKSELKN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1896 QklsaEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDaLLQMKIQAEKVSQSNTEKSK 1975
Cdd:TIGR04523 319 Q----EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1976 QLLETEALKMKQLAEEaarlrsvaeeakKQRQLaedeaarQRAEAEKILKEKlaaineatrlkteaevalkakeaENERL 2055
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQ------------KDEQI-------KKLQQEKELLEK-----------------------EIERL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2056 KRQAEDEAYQRKLLEDQAAQHKHDIQ--EKITQLQSSSVSELDRQKNIVEETLRQKKvveEEIHIIRINFERASKEKSDL 2133
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKnlDNTRESLETQLKVLSRSINKIKQNLEQKQ---KELKSKEKELKKLNEEKKEL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2134 EVELKKLKgiadetqKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAA--RQRKAAQDEVERLKQkaaEAN 2211
Cdd:TIGR04523 509 EEKVKDLT-------KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQ---TQK 578
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 2212 KLKDKAEkelEKQVILAKEAAQKstaaeqkaQDVLSKNKEDLLSQEKLRDEFENAKK 2268
Cdd:TIGR04523 579 SLKKKQE---EKQELIDQKEKEK--------KDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2524-2763 |
1.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2524 KKLLEDKQEIQ--QRLDKetqgFQKSLEAERKRQL-----EISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVR 2596
Cdd:PHA02562 153 RKLVEDLLDISvlSEMDK----LNKDKIRELNQQIqtldmKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2597 LQETEKQTTEtvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSK-----ETASAQQEQMEQQKAMLQ- 2670
Cdd:PHA02562 229 AKTIKAEIEE-----LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekgGVCPTCTQQISEGPDRITk 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2671 -QTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKD--EQQRQQ-KLMDEEKKKLQAIMDEAVKKQKEAEAEMKN 2746
Cdd:PHA02562 304 iKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNkiSTNKQSlITLVDKAKKVKAAIEELQAEFVDNAEELAK 383
|
250
....*....|....*....
gi 1655220506 2747 KQKEMEALEKKR--LEQEK 2763
Cdd:PHA02562 384 LQDELDKIVKTKseLVKEK 402
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2287-2455 |
1.53e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2287 LRQKAEEAEKLKKAAEDEAAKQaKAQKDAERlrkeaeaeaakraaaeaaaLKQKQEADAEMAKHKKEAEQALKQKSQVEK 2366
Cdd:PRK00409 539 AEALLKEAEKLKEELEEKKEKL-QEEEDKLL-------------------EEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2367 ELGL-VKLQlDETDKQKALMD-----EELQRVKAQVNDAVK-----------QKAQVeneLSKVK-----MQMDeLLKLK 2424
Cdd:PRK00409 599 GGYAsVKAH-ELIEARKRLNKanekkEKKKKKQKEKQEELKvgdevkylslgQKGEV---LSIPDdkeaiVQAG-IMKMK 673
|
170 180 190
....*....|....*....|....*....|.
gi 1655220506 2425 VRIEEenLRLMQKNKDNTQKLLAEEAEKMKS 2455
Cdd:PRK00409 674 VPLSD--LEKIQKPKKKKKKKPKTVKPKPRT 702
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2447-2766 |
1.56e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2447 AEEAEKMKSlAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2526
Cdd:COG3064 1 AQEALEEKA-AEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2527 LE---DKQEIQQRLDKETQgfQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2603
Cdd:COG3064 80 AEaekAAAEAEKKAAAEKA--KAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2604 TTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKR 2683
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2684 ERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2763
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAV 317
|
...
gi 1655220506 2764 LLA 2766
Cdd:COG3064 318 LAA 320
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
2554-2671 |
1.57e-03 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 44.68 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2554 RQLEISAEAEKLKlrvKELSSAQAKAEEEATRFKKQADEAKVrLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAEL 2633
Cdd:PTZ00186 537 RDSEQHAEADRVK---RELVEVRNNAETQLTTAERQLGEWKY-VSDAEKENVKTLVAELRKAMENPNVAKDDLAAATDKL 612
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1655220506 2634 EKE-----REKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQ 2671
Cdd:PTZ00186 613 QKAvmecgRTEYQQAAAANSGSSSNSGEQQQQQQQQQQQNSEE 655
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2214-2598 |
1.60e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2214 KDKAEKELEKQVILAKEAAQKSTAAEQKAQdvlSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAallrQKAEE 2293
Cdd:pfam09731 78 ESKEPKEEKKQVKIPRQSGVSSEVAEEEKE---ATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESAT----AVAKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2294 AEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEK---ELGL 2370
Cdd:pfam09731 151 AKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKlpeHLDN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2371 VKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKV-----KMQMDELLKLkvrIEEENLRLMQKNKDNTQKL 2445
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVlkednLLSNDDLNSL---IAHAHREIDQLSKKLAELK 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2446 LAEEAEKMKSLAEEAARLSVEAEETARQrktAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAeELQKQKNQAQEKAKK 2525
Cdd:pfam09731 308 KREEKHIERALEKQKEELDKLAEELSAR---LEEVRAADEAQLRLEFEREREEIRESYEEKLRT-ELERQAEAHEEHLKD 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2526 -LLEDKQEIQQRLDKEtqgFQKSLEAERKRQLEisaEAEKLKLRVKELssaqakaeEEATRFKKQADEAKVRLQ 2598
Cdd:pfam09731 384 vLVEQEIELQREFLQD---IKEKVEEERAGRLL---KLNELLANLKGL--------EKATSSHSEVEDENRKAQ 443
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1758-1939 |
1.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1758 EEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRLRLRA 1837
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----ERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1838 E--------------------------------EEAQRKSL-----AQEEAEKQKTEAERDAKKKAKAEEAALKQKENAE 1880
Cdd:COG3883 95 LyrsggsvsyldvllgsesfsdfldrlsalskiADADADLLeelkaDKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 1881 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQR 1939
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1657-1731 |
1.62e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.91 E-value: 1.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 1657 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAedelkRKSEAEKEAARQKQKALDELQK 1731
Cdd:PRK07353 54 EAEKLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQA-----SKEKARREIEQQKQAALAQLEQ 123
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
202-311 |
1.73e-03 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 41.88 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 202 QKKTFTKWVN---------KHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRnvrlpreKGRMRFHKLQN 272
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTID-ERAINK-------KKLTVFTIHEN 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220506 273 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 311
Cdd:cd21292 97 LTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2535-2694 |
1.78e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2535 QRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ----TTETVVQ 2610
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2611 KLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDE 2690
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
....
gi 1655220506 2691 KKKL 2694
Cdd:COG1579 173 PPEL 176
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
208-310 |
1.90e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 41.13 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 208 KWVNKHLMKAQR---HITDLYEDLRDGHNLISLLEVLSGETLPR--------ERDLVRNVRlprekgrmrfHKLQNVQiA 276
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKelvlevlsEEDLEKRAE----------KVLQAAE-K 85
|
90 100 110
....*....|....*....|....*....|....
gi 1655220506 277 LDFLKHrqvklvnIRNDDIADGNPKLTLGLIWTI 310
Cdd:cd21218 86 LGCKYF-------LTPEDIVSGNPRLNLAFVATL 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2013-2253 |
1.92e-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: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2013 AARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSv 2092
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2093 SELDRQKNIVEETLRqkkVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKR 2172
Cdd:COG4942 97 AELEAQKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2173 REAEEKVKKIAAAEEEAARQRKAAQDEVERL-KQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKE 2251
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 1655220506 2252 DL 2253
Cdd:COG4942 254 KL 255
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
195-315 |
1.94e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.52 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 195 ADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlVRNVRLPREKGRmrfHKLQNVQ 274
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVP-----LHSFFLTPDSFE---QKVLNVS 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655220506 275 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 315
Cdd:cd21337 86 FAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2349-2649 |
1.96e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 43.79 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2349 KHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIE 2428
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2429 EENLRLMQKNKdntqKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQralaEKMLKEKMQAIQEATKLKAE 2508
Cdd:pfam09728 81 KQNKKLKEESK----KLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREE----NEELREKLKSLIEQYELREL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2509 -------AEELQKQKNQAqeKAKKLLEDKQEIQQ-----RLDKETQGFQKSLEAERKRQLEISAEAEKLKlrvkELSSAQ 2576
Cdd:pfam09728 153 hfekllkTKELEVQLAEA--KLQQATEEEEKKAQekevaKARELKAQVQTLSETEKELREQLNLYVEKFE----EFQDTL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2577 AKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQR--LQSTREADDLKKAIAELEKEREKLKRDAQELQN 2649
Cdd:pfam09728 227 NKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKalLEMAEERQKLKEELEKLQKKLEKLENLCRALQA 301
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1666-1861 |
2.00e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1666 LQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaeDELKRKSEAEKEAARQKQKALDelqkhkmqaeEAERRLKQ 1745
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK------ELLLRERNQQRQEARREREELQ----------REEERLVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1746 AEEekvrqikvveevaqktaatQLQAMsfSEKTTKLEEslkkeqgtvlQLQEEAEKLRKQEEEANKAREQAEKEL-ETWR 1824
Cdd:PRK12705 89 KEE-------------------QLDAR--AEKLDNLEN----------QLEEREKALSARELELEELEKQLDNELyRVAG 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220506 1825 LKANEALRL---RLRAEEEAQRKSLAQEEAEKQKTEAERD 1861
Cdd:PRK12705 138 LTPEQARKLllkLLDAELEEEKAQRVKKIEEEADLEAERK 177
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1662-1738 |
2.02e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 41.27 E-value: 2.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 1662 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNaedelKRKSEAEKEAARQKQKALDELQKHKMQAEE 1738
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKE-----EILAEAKEEAERILEQAKAEIEQEKEKALA 113
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1543-1755 |
2.07e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1543 EKLKEDEKKRmAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAV------DAEKQKQNIQLELTQL 1616
Cdd:COG1340 57 EEAQELREKR-DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkeieRLEWRQQTEVLSPEEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1617 KNLSEQeIRSKNQQLEEAQVSRrKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE 1696
Cdd:COG1340 136 KELVEK-IKELEKELEKAKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1697 ETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAE-EEKVRQIK 1755
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEElEEKAEEIF 273
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2352-2728 |
2.07e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.28 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2352 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVND--AVKQKAQVENELSkvkmQMDELLKLKVRIEE 2429
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDecWKKIKRKKNSALS----EALNGFKYEANFKS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2430 ENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEqrALAEKMLKeKMQAIQEATKLKAEA 2509
Cdd:pfam13166 165 RLLREIEKDNFNAGVLLSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAE--ILIQKVIG-KSSAIEELIKNPDLA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2510 EELQkqknQAQEKAKKLLED----KQEIQQRL--------DKETQGFQKSLEaERKRQLE--ISAEAEKLKLRVKELSSA 2575
Cdd:pfam13166 242 DWVE----QGLELHKAHLDTcpfcGQPLPAERkaaleahfDDEFTEFQNRLQ-KLIEKVEsaISSLLAQLPAVSDLASLL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2576 QAkaeeeatrFKKQADEAKVRLQETEKQTtETVVQKLETQRLQSTREADdLKKAIAELEKEREKLKRdAQELQNKSKETA 2655
Cdd:pfam13166 317 SA--------FELDVEDIESEAEVLNSQL-DGLRRALEAKRKDPFKSIE-LDSVDAKIESINDLVAS-INELIAKHNEIT 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2656 SAQQEQMEQQKAMLQQTFLTEkellLKRERDVEDEKKKLqkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQA 2728
Cdd:pfam13166 386 DNFEEEKNKAKKKLRLHLVEE----FKSEIDEYKDKYAG---LEKAINSLEKEIKNLEAEIKKLREEIKELEA 451
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
2452-2672 |
2.08e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 44.18 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2452 KMKSLAEEAARLSVEAEETARQRKTAEAELAE-------QRALA--EKMLKEKMQAIQEATKLK---------AEAEELQ 2513
Cdd:PTZ00332 138 KMEKVEEELRRSQLDATQLAQVPTATLKNIEDimnvtqiQNALAstDDQIKTQLAQLEKTNEIQnvamhdgemQVAEEQM 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2514 KQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEiSAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEA 2593
Cdd:PTZ00332 218 WTKVQLQERLIELVADKFRLIGKCEEENKSFSKIHEVQKQANQE-TSQMKDAKRRLKQRCETDLKHIHDAIQKADLEDAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2594 KVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKER-EKLKRDAQELQNKSKETASAQQ--EQMEQQKAMLQ 2670
Cdd:PTZ00332 297 AMKRYATNKEKSERFIRENEDRQEEAWNKIQDLERQLQRLGTERfEEVKRRIEENDREEKRRVEYQQflEVAGQHKKLLE 376
|
..
gi 1655220506 2671 QT 2672
Cdd:PTZ00332 377 LT 378
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1673-2137 |
2.09e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1673 AAEAEKVRKAAQEEAERLRKQvneETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVR 1752
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQA---EAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1753 QIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR 1832
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1833 LRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFE 1912
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1913 HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEA 1992
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1993 ARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQ 2072
Cdd:COG3064 318 LAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2073 AAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVEL 2137
Cdd:COG3064 398 GGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADAL 462
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1445-1749 |
2.12e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.54 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1445 LLEEIEKNKDQIEncqkdakAYIDS-----LKDYEFQILAYrALQDPIASPL---KKPKMESASDNIIQEyvtlRTRYSE 1516
Cdd:PLN03188 991 LLEEIQDLRSQLQ-------YYIDSslpsaRKRNSLLKLTY-SCEPSQAPPLntiPESTDESPEKKLEQE----RLRWTE 1058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1517 LStltSQYIKFILETQRRLEDDEKASEKLKE--DEKKRMAEiqaQLETQKQLA-EGHAKSVAK-AELEAQELKL-----K 1587
Cdd:PLN03188 1059 AE---SKWISLAEELRTELDASRALAEKQKHelDTEKRCAE---ELKEAMQMAmEGHARMLEQyADLEEKHIQLlarhrR 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1588 MKE------DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEirsknqqleeaqvsRRKLEEEIHLIRIQLQTTIKQKST 1661
Cdd:PLN03188 1133 IQEgiddvkKAAARAGVRGAESKFINALAAEISALKVEREKE--------------RRYLRDENKSLQAQLRDTAEAVQA 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1662 ADDELQKLRDQ---AAEAEKVRKAAQEEAERLRKQVNeetQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE 1738
Cdd:PLN03188 1199 AGELLVRLKEAeeaLTVAQKRAMDAEQEAAEAYKQID---KLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCMAKYD 1275
|
330
....*....|.
gi 1655220506 1739 AERRLKQAEEE 1749
Cdd:PLN03188 1276 AGEPLSEGDQQ 1286
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1811-1972 |
2.12e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1811 KAREQAEKELETWR----LKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERdAKKKAKAEEAALKQKENAEKELEKQ 1886
Cdd:pfam05262 185 ALREDNEKGVNFRRdmtdLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADF-AQDNADKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1887 RTFAEQIAQQKLSAEQEYIRLKADFE---HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQA 1963
Cdd:pfam05262 264 ADTSSPKEDKQVAENQKREIEKAQIEikkNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ-KTKP 342
|
....*....
gi 1655220506 1964 EKVSQSNTE 1972
Cdd:pfam05262 343 QVEAQPTSL 351
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1529-1755 |
2.16e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 44.05 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1529 LETQRRLEDDEKASE---KLKEDEKKRMAEIQ---------------AQLETQKQlaEGHAKSVAKAELEAQEL---KLK 1587
Cdd:pfam15066 304 FESLQPLEEDMALNEvlqKLKHTNRKQQMQIQdlqcsnlylekkvkeLQMKITKQ--QVFVDIINKLKENVEELiedKYN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1588 MKEDASqrqglavDAEKQKQNIQ--LELTQlKNLSEQEIRSKNQQLEEAQVsrrkleeEIHLIRIQLQ--TTIKQKStad 1663
Cdd:pfam15066 382 VILEKN-------DINKTLQNLQeiLANTQ-KHLQESRKEKETLQLELKKI-------KVNYVHLQERyiTEMQQKN--- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1664 delqKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRkseaEKEAARQKQKAL-DELQKHKMQAEEAERR 1742
Cdd:pfam15066 444 ----KSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSALDLLKR----EKETREQEFLSLqEEFQKHEKENLEERQK 515
|
250
....*....|...
gi 1655220506 1743 LKQAEEEKVRQIK 1755
Cdd:pfam15066 516 LKSRLEKLVAQVK 528
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1435-1665 |
2.22e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1435 LKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYidsLKDYEFQILAYRALQdpIASPLKKPKMEsaSDNIIQEYVTLRTRY 1514
Cdd:TIGR01612 1488 LKEHIDKSKGCKDEADKNAKAIEKNKELFEQY---KKDVTELLNKYSALA--IKNKFAKTKKD--SEIIIKEIKDAHKKF 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1515 SELSTLTSQYIKFILETQRRLEDDEKASEK-----------LKEDEKK--RMAEIQAQLETQKQLAEGHAKSVAKAELEA 1581
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKKEKFRIEDDAAKNDKsnkaaidiqlsLENFENKflKISDIKKKINDCLKETESIEKKISSFSIDS 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1582 QELKLKMKEDASQR-QGLAVDAEKQKQNIQLELTQLKNLsEQEIRS---------KNQQL-------EEAQVSRRKLEEE 1644
Cdd:TIGR01612 1641 QDTELKENGDNLNSlQEFLESLKDQKKNIEDKKKELDEL-DSEIEKieidvdqhkKNYEIgiiekikEIAIANKEEIESI 1719
|
250 260
....*....|....*....|.
gi 1655220506 1645 IHLIRIQLQTTIKQKSTADDE 1665
Cdd:TIGR01612 1720 KELIEPTIENLISSFNTNDLE 1740
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1587-1844 |
2.26e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1587 KMKEDASQRQGLAVDAEKQKQNIQLELTqlknlsEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDEL 1666
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEE------EEEIRRLEEQVERLEAEVEELEAELE----EKDERIERLERELSEA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1667 QKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQ---KALDELQKhkmqaeEAERRL 1743
Cdd:COG2433 454 RSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELvpvKVVEKFTK------EAIRRL 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1744 KQAEEEKVRQIKVVEEV--AQKTAATQL-----QAMSFSEKT-TKLEESLKKEQGTVL-----QLQEEAEKLRKQEEEAN 1810
Cdd:COG2433 528 EEEYGLKEGDVVYLRDAsgAGRSTAELLaeagpRAVIVPGELsEAADEVLFEEGIPVLpaedvTIQEVDDLAVVDEEELE 607
|
250 260 270
....*....|....*....|....*....|....
gi 1655220506 1811 KAREQAEKELETWRLKANEALRLRLRAEEEAQRK 1844
Cdd:COG2433 608 AAIEDWEERAEERRREKKAEMLERLISEYRAERR 641
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1311-1469 |
2.28e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1311 AEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQlagSLLERWQAVFAQIDLRQ 1390
Cdd:cd00176 23 LSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE---ELNQRWEELRELAEERR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 1391 RELSLLGRHMNSYKQSYEwLIQWLREARLRQEKIEAAPvwDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDS 1469
Cdd:cd00176 100 QRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE 175
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
2409-2666 |
2.29e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2409 ELSKVKM-----QMDELLK------------LKVRIEEENLRLMQKNKDNTQKLLA---EEAEKMKSLAEEAARLSVEAE 2468
Cdd:PRK05771 5 RMKKVLIvtlksYKDEVLEalhelgvvhiedLKEELSNERLRKLRSLLTKLSEALDklrSYLPKLNPLREEKKKVSVKSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2469 ETARQRktAEAELAEqralAEKMLKEKMQAIQEatkLKAEAEELQKQKNQAqEKAKKLledkqeiqqrldketqgfqkSL 2548
Cdd:PRK05771 85 EELIKD--VEEELEK----IEKEIKELEEEISE---LENEIKELEQEIERL-EPWGNF--------------------DL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2549 EAERKRQLE--------ISAEAEKLKLRVKELSSAQAKAEEEATRF------KKQADEAKVRLQETEkqttetvVQKLET 2614
Cdd:PRK05771 135 DLSLLLGFKyvsvfvgtVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlKELSDEVEEELKKLG-------FERLEL 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2615 QRLQSTREA-DDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQK 2666
Cdd:PRK05771 208 EEEGTPSELiREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIEL 260
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1581-2066 |
2.29e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1581 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQttIKQKS 1660
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--AAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1661 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAE 1740
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1741 RRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKEL 1820
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1821 ETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSA 1900
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1901 EQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLET 1980
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1981 EALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAE 2060
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLAD 479
|
....*.
gi 1655220506 2061 DEAYQR 2066
Cdd:COG3064 480 LLLLGG 485
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2586-2770 |
2.32e-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: 42.74 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2586 FKKQADEAKVRLQETEKQTtETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQME-- 2663
Cdd:pfam04012 9 VRANIHEGLDKAEDPEKML-EQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2664 --QQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhledevNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAE 2741
Cdd:pfam04012 88 alAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAA------LETKIQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSS 161
|
170 180 190
....*....|....*....|....*....|....
gi 1655220506 2742 A-----EMKNKQKEMEALEKKRLEQEKLLADENK 2770
Cdd:pfam04012 162 AtdsfeRIEEKIEEREARADAAAELASAVDLDAK 195
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2429-2537 |
2.34e-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: 41.06 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2429 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2508
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91
|
90 100
....*....|....*....|....*....
gi 1655220506 2509 AEELQKQKNQAQEKAKKLLEDKQEIQQRL 2537
Cdd:pfam20492 92 IARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1892-2063 |
2.44e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1892 QIAQQKLSAEQEYIRlkadFEhAEQQRgLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAllQMKIQAEKVSQSNT 1971
Cdd:PRK05035 440 AIEQEKKKAEEAKAR----FE-ARQAR-LEREKAAREARHKKAAEARAAKDKDAVAAALARVKA--KKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1972 EKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQlAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAE 2051
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAK 590
|
170
....*....|..
gi 1655220506 2052 NERLKRQAEDEA 2063
Cdd:PRK05035 591 AKKAAQQAASAE 602
|
|
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
1591-1733 |
2.48e-03 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 42.20 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1591 DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKN---QQLEEAQVSRRKLEEEIhliriqlqttikqkstaDDELQ 1667
Cdd:pfam09727 57 DSELLRDQSQDEDVYEAMYEKPLAELEKLVEKQRETQRrmlEQLAAAEKRHRRVIREL-----------------EEEKR 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 1668 KLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE-AEKEAARQKQKALDELQKHK 1733
Cdd:pfam09727 120 KHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKELKKLLEkLEEELSKQKQIALLLVKERK 186
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3207-3244 |
2.48e-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: 2.48e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1655220506 3207 LQGTPSIAGLLNEPTKEKMSFYQAMKKELLSPEAAVNL 3244
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2582-2780 |
2.52e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.43 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2582 EATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETA---SAQ 2658
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2659 QEQMEQQKAMLQQtfltekeLLLKRERDVEDEKKKLQKHLEDEvnkaKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK 2738
Cdd:cd00176 81 LEELNQRWEELRE-------LAEERRQRLEEALDLQQFFRDAD----DLEQWLEEKEAALASEDLGKDLESVEELLKKHK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655220506 2739 EAEAEMKNKQKEMEALEKKRLE-QEKLLADENKKLREKLESLE 2780
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEElLEEGHPDADEEIEEKLEELN 192
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2378-2574 |
2.56e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2378 TDKQKALMDEELQrvkaqvndAVKQKAQVENELS--KVKMQMDELLKLKVrieEENLRLMQKNKdntqKLLAEEAEKMKS 2455
Cdd:smart00787 108 SPDVKLLMDKQFQ--------LVKTFARLEAKKMwyEWRMKLLEGLKEGL---DENLEGLKEDY----KLLMKELELLNS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2456 LAEEAARLSVEAEETARQRKTAEAEL-----AEQRALAEKMLKEKMQAIQEATKLkaeaEELQKQKNQAQEKAKKLLEDK 2530
Cdd:smart00787 173 IKPKLRDRKDALEEELRQLKQLEDELedcdpTELDRAKEKLKKLLQEIMIKVKKL----EELEEELQELESKIEDLTNKK 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1655220506 2531 QEIQQRLDKETQGFQKSLEAERKrqleisaEAEKLKLRVKELSS 2574
Cdd:smart00787 249 SELNTEIAEAEKKLEQCRGFTFK-------EIEKLKEQLKLLQS 285
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2446-2625 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2446 LAEEAEKMKSLAEEAARL-SVEAEETARQRKTAEAElaeqralAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAK 2524
Cdd:pfam05262 186 LREDNEKGVNFRRDMTDLkERESQEDAKRAQQLKEE-------LDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2525 KlLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQT 2604
Cdd:pfam05262 259 N-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDL 337
|
170 180
....*....|....*....|.
gi 1655220506 2605 TETVVQKletqRLQSTREADD 2625
Cdd:pfam05262 338 QKTKPQV----EAQPTSLNED 354
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1530-2125 |
2.64e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1530 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAK--AELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1607
Cdd:pfam10174 116 ENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1608 NIQLELTQLKnlseqeirSKNQQLEEAQVSRRKLEEEIHLIRiQLQTTIKQKSTADDELQK-LRDQAAEAEKVRKAA--- 1683
Cdd:pfam10174 196 HLEVLLDQKE--------KENIHLREELHRRNQLQPDPAKTK-ALQTVIEMKDTKISSLERnIRDLEDEVQMLKTNGllh 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1684 QEEAERLRKQV---NEETQKKKNAEDELKR---KSEAEKEAARQKQKALD----------ELQKHKMQAEEAERRLKQAE 1747
Cdd:pfam10174 267 TEDREEEIKQMevyKSHSKFMKNKIDQLKQelsKKESELLALQTKLETLTnqnsdckqhiEVLKESLTAKEQRAAILQTE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1748 EEKVRQIKVVEEVAQKTAATQLQAMSfSEKTT------KLEESLKKEQGTVLQLQEEAEKLRKQEEEANKARE---QAEK 1818
Cdd:pfam10174 347 VDALRLRLEEKESFLNKKTKQLQDLT-EEKSTlageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAglkERVK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1819 ELETWRLKANEAlrlrLRAEEEAqrksLAQEE--AEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTfaeqiaqQ 1896
Cdd:pfam10174 426 SLQTDSSNTDTA----LTTLEEA----LSEKEriIERLKEQREREDRERLEELESLKKENKDLKEKVSALQP-------E 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1897 KLSAEQEYIRLKadfEHAEQQRGLLDNELQRLKnevnaaekqrrQLEDELAKVRSEMDALlqmkiQAEKVSQSNTEKSKQ 1976
Cdd:pfam10174 491 LTEKESSLIDLK---EHASSLASSGLKKDSKLK-----------SLEIAVEQKKEECSKL-----ENQLKKAHNAEEAVR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1977 LLETEALKMKQLAEEAARLRSvaEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRL---KTEAEVALKAKEAENE 2053
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKE--ESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLrqmKEQNKKVANIKHGQQE 629
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2054 RLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETlrQKKVVEEEIHIIRINFER 2125
Cdd:pfam10174 630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSST--QQSLAEKDGHLTNLRAER 699
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1699-1822 |
2.70e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1699 QKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQaeeekvrqikvvEEVAQKTAATQLQamsfsekt 1778
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYER------------ELVLHAEDIKALQ-------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220506 1779 tKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELET 1822
Cdd:pfam07926 61 -ALREELNELKAEIAELKAEAESAKAELEESEESWEEQKKELEK 103
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2194-2366 |
2.85e-03 |
|
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: 43.30 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2194 KAAQDEVERLKQKAAEANKLKDKAEKELEKQvilaKEAAQKSTAAEQKAQDVLSKNKEDllsqeklrdefENAKKLAQAA 2273
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ----AEEAEKQRAAEQARQKELEQRAAA-----------EKAAKQAEQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2274 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAErlrkeaeAEAAKRAAAEAAALKQKQEADAEM-AKHKK 2352
Cdd:TIGR02794 111 AKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE-------EEAKAKAAAEAKKKAEEAKKKAEAeAKAKA 183
|
170
....*....|....
gi 1655220506 2353 EAEQALKQKSQVEK 2366
Cdd:TIGR02794 184 EAEAKAKAEEAKAK 197
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1492-1725 |
2.96e-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: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1492 KKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDekkrMAEIQAQLETQKQLAEGHA 1571
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1572 KSVAKAELEAQELKL----KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihl 1647
Cdd:COG3883 93 RALYRSGGSVSYLDVllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA--- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1648 iRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKA 1725
Cdd:COG3883 170 -KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1498-1740 |
3.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1498 SASDNIIQEYVTLRTRYSELSTLTSQyikfILETQRRLEDDEKASEKLKEDEKKRMAEIQaqlETQKQLAEghaksvAKA 1577
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAE------AEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1578 ELEAQELKLKMKEDASQRQGLAVDAEKQ---KQNIQLELTQLKNLSeQEIRSKNQQLEEAQVSRRKLEEeihliriqlqt 1654
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDVllgSESFSDFLDRLSALS-KIADADADLLEELKADKAELEA----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1655 tikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKM 1734
Cdd:COG3883 148 ---KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
....*.
gi 1655220506 1735 QAEEAE 1740
Cdd:COG3883 225 AAAAAA 230
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2339-2503 |
3.10e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2339 QKQEADAEMAKHKKEAEQALKQKSQVEKELglvklQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMD 2418
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAALLEAKEL-----LLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2419 ELLKLKVRIEEENLRLMQKNKDNTQKLlaEEAEKMKS---LAEEAARLSVEAEETARQRKTAEAELA--EQRALAEKMLK 2493
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEEKAQRVKKIEEEAdlEAERKAQNILA 183
|
170
....*....|
gi 1655220506 2494 EKMQAIQEAT 2503
Cdd:PRK12705 184 QAMQRIASET 193
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2527-2721 |
3.11e-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: 42.36 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2527 LEDKQEIQQR-LDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTT 2605
Cdd:pfam04012 16 GLDKAEDPEKmLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2606 ETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELqnKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRER 2685
Cdd:pfam04012 96 EKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLL--KARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKI 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1655220506 2686 DVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDE 2721
Cdd:pfam04012 174 EEREARADAAAELASAVDLDAKLEQAGIQMEVSEDV 209
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
2366-2701 |
3.11e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2366 KELGLVKLQLDEtdKQKALMDEELQRVKAQVNDAVK-QKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNK--DNT 2442
Cdd:PTZ00108 983 KEFYLVRLDLYK--KRKEYLLGKLERELARLSNKVRfIKHVINGELVITNAKKKDLVKELKKLGYVRFKDIIKKKseKIT 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2443 QKLLAEEAEKMKSLAEEAARLSVEAEE------------TARQRKTAEAELAEQRALAEKMLK----------------- 2493
Cdd:PTZ00108 1061 AEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNttpkdmwledldkfeea 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2494 -EKMQAIQEATKLKAE---------AEELQKQKNQAQEKAKK-------------------LLEDKQEIQQRLDKETQGF 2544
Cdd:PTZ00108 1141 lEEQEEVEEKEIAKEQrlksktkgkASKLRKPKLKKKEKKKKkssadkskkasvvgnskrvDSDEKRKLDDKPDNKKSNS 1220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2545 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREAD 2624
Cdd:PTZ00108 1221 SGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGS 1300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2625 DLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE--QMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDE 2701
Cdd:PTZ00108 1301 KPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKskTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDE 1379
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
698-791 |
3.24e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 698 LRYIQDLLGWVEENQRRVDDGEWGSDLPAVESQLGSHRGLHQSVEEFRSKIERAKADESQI---SPASKAAYRDYLAKLE 774
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*..
gi 1655220506 775 LQYDKLLHDSKARLRYL 791
Cdd:smart00150 84 ERWEELKELAEERRQKL 100
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1313-1859 |
3.29e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1313 EKEVEAHRSQLKAMRAEAEADQATFD-------RLQDELKAAT-------SVSDKM----TRLHSERD---AELEHYRQL 1371
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEaleegkkRLQRELEALTqqleekaAAYDKLektkNRLQQELDdllVDLDHQRQL 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1372 AgSLLERWQAVFAQIDLRQRELSLlgrhmnsykQSYEWLIQWLREARlrqEKieaapvwDSKALkeQLTQEkklLEEIEK 1451
Cdd:pfam01576 596 V-SNLEKKQKKFDQMLAEEKAISA---------RYAEERDRAEAEAR---EK-------ETRAL--SLARA---LEEALE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1452 NKDQIENCQKDAKAYIDSL--------KDYEFQILAYRALQDPIASplKKPKMESASDNI-IQEYVTLRTRYSeLSTLTS 1522
Cdd:pfam01576 651 AKEELERTNKQLRAEMEDLvsskddvgKNVHELERSKRALEQQVEE--MKTQLEELEDELqATEDAKLRLEVN-MQALKA 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1523 QYikfiletQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDA 1602
Cdd:pfam01576 728 QF-------ERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRE----EA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1603 EKQKQNIQlelTQLKNLSeqeirsknQQLEEAQVSRRKleeeihlIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1682
Cdd:pfam01576 797 VKQLKKLQ---AQMKDLQ--------RELEEARASRDE-------ILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1683 AQEEAERLRKQVNEETQKKKNAEDELKR------KSEAEKEAARQKQKALDE-LQKHKMQAEE------AERRLKQAEEE 1749
Cdd:pfam01576 859 AQQERDELADEIASGASGKSALQDEKRRleariaQLEEELEEEQSNTELLNDrLRKSTLQVEQlttelaAERSTSQKSES 938
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1750 KVRQIkvveEVAQKTAATQLQAMSFSEKtTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANE 1829
Cdd:pfam01576 939 ARQQL----ERQNKELKAKLQEMEGTVK-SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVED 1013
|
570 580 590
....*....|....*....|....*....|
gi 1655220506 1830 ALRLRLRAEEEAQRKSLAQEEAEKQKTEAE 1859
Cdd:pfam01576 1014 ERRHADQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1837-1954 |
3.30e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1837 AEEEAQRKSL-AQEEAEKQKTEAERDakkkakaEEAALKQKENAEKELEKQRTFAEQ--IAQQKL-SAEQEYIRLKADFE 1912
Cdd:COG1566 93 AAAEAQLARLeAELGAEAEIAAAEAQ-------LAAAQAQLDLAQRELERYQALYKKgaVSQQELdEARAALDAAQAQLE 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1913 HAEQQRGLL------DNELQRLKNEVNAAEKQRRQLEDELAK--VRSEMD 1954
Cdd:COG1566 166 AAQAQLAQAqaglreEEELAAAQAQVAQAEAALAQAELNLARttIRAPVD 215
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1241-1612 |
3.38e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1241 ILASPQQSSSAPMLRS-------ELDVTLKKMDHVYGLSSVYLDKLKtidiviRNTKDAEDTVKSYESRLRDVSKVPAEE 1313
Cdd:TIGR02169 666 ILFSRSEPAELQRLRErleglkrELSSLQSELRRIENRLDELSQELS------DASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1314 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAAtsvsdkmtrLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL 1393
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEED---------LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1394 SLLGRHMNSYKQSYEWLIQWLREARlrQEKIEAAPVWDSKalKEQLTQEKKLLE-EIEKNKDQIENCQKDAKAYIDSLKD 1472
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQ--IKSIEKEIENLNgKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1473 YEFQILAYRAlqdpiasplKKPKMESASDNIIQEYVTLRTRYSELST---LTSQYIKFILETQRRLEDDEKAS---EKLK 1546
Cdd:TIGR02169 887 LKKERDELEA---------QLRELERKIEELEAQIEKKRKRLSELKAkleALEEELSEIEDPKGEDEEIPEEElslEDVQ 957
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 1547 EDEKKRMAEIQAqLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLE 1612
Cdd:TIGR02169 958 AELQRVEEEIRA-LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2605-2805 |
3.39e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2605 TETVVQKLETQRLQ--STREADDLKKAIAElEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLK 2682
Cdd:PRK09510 57 PGAVVEQYNRQQQQqkSAKRAEEQRKKKEQ-QQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2683 RERDVEDEKKKL-----QKHLEDEVNKAKA---LKDEQQRQQKLMDEEKKKLQAimdeAVKKQKEAEAEmknKQKEMEAL 2754
Cdd:PRK09510 136 EAAAKAAAAAKAkaeaeAKRAAAAAKKAAAeakKKAEAEAAKKAAAEAKKKAEA----EAAAKAAAEAK---KKAEAEAK 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1655220506 2755 EKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2805
Cdd:PRK09510 209 KKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2634-2755 |
3.46e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2634 EKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQqTFLTEkelLLKRERDVEDEKKKLQKHLEDEV--NKAKALKDE 2711
Cdd:cd22656 109 DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLT-DFENQ---TEKDQTALETLEKALKDLLTDEGgaIARKEIKDL 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220506 2712 QQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALE 2755
Cdd:cd22656 185 QKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3945-3979 |
3.64e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.64e-03
10 20 30
....*....|....*....|....*....|....*
gi 1655220506 3945 KLLSAERAVTGYKDPYSGKVISLFQAMKKGLVPED 3979
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3318-3355 |
3.67e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.67e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1655220506 3318 IRLLEAQLSTGGIIDPVKSYRVPQEVACKRGYFNEEMA 3355
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2475-2779 |
3.79e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.48 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2475 KTAEAELAEQRALAEKMLkEKMQaiQEATKLKAEAEELQKQKNQAQ---EKAKKLLEdkqEIQQRLDKetqgfqKSLEAE 2551
Cdd:pfam05701 27 KAHRIQTVERRKLVELEL-EKVQ--EEIPEYKKQSEAAEAAKAQVLeelESTKRLIE---ELKLNLER------AQTEEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2552 RKRQleisaEAEKLKLRVKEL-------SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREAD 2624
Cdd:pfam05701 95 QAKQ-----DSELAKLRVEEMeqgiadeASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2625 DLKKAIAELEKEREKLkrdAQELQN--KSKETASAQQEQMEQQK---AM-LQQTFLT-EKELllkreRDVEDEKKKLQkh 2697
Cdd:pfam05701 170 EAVSASKEIEKTVEEL---TIELIAtkESLESAHAAHLEAEEHRigaALaREQDKLNwEKEL-----KQAEEELQRLN-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2698 leDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMK---NKQKEMEALEKKRLEQEKL----LADENK 2770
Cdd:pfam05701 240 --QQLLSAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKktsTSIQAALASAKKELEEVKAniekAKDEVN 317
|
....*....
gi 1655220506 2771 KLREKLESL 2779
Cdd:pfam05701 318 CLRVAAASL 326
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1778-1902 |
3.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1778 TTKLEESLKKEQGTVLQLQEEAEKLRKQ-----EEEANKAREQAEKELETWRLKANEALRlRLRAEEEAQRKSLaqEEAE 1852
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEalleaKEEIHKLRNEFEKELRERRNELQKLEK-RLLQKEENLDRKL--ELLE 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1853 KQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQqkLSAEQ 1902
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE 154
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2604-2785 |
3.92e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2604 TTETVVQKLETQRLQSTRE-------ADDLKkaiAELEKER---EKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQ-T 2672
Cdd:PLN03188 1041 TDESPEKKLEQERLRWTEAeskwislAEELR---TELDASRalaEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQyA 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2673 FLTEKEL-LLKRERDVE---DEKKKL----------QKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMD---EAVK 2735
Cdd:PLN03188 1118 DLEEKHIqLLARHRRIQegiDDVKKAaaragvrgaeSKFINALAAEISALKVEREKERRYLRDENKSLQAQLRdtaEAVQ 1197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2736 KQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENK---KLREKLESLEVTSKQ 2785
Cdd:PLN03188 1198 AAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAYKqidKLKRKHENEISTLNQ 1250
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1883-2085 |
4.31e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1883 LEKQRTFAEQIAQQKLSaeqeyiRLKADFEHAEQQrgllDNELQRLKNEvNAAEKQRRQLEDELAKVRSEM--------- 1953
Cdd:PRK11448 35 LIKLRQFGEALAKHIAA------LLGIYEPPCENQ----HDLLRRLGKE-GFLPDEILDVFHKLRKIGNKAvhefhgdhr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1954 DALLQMKIQ-------AEKVSQSNTEKSKQLLETE--ALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIl 2024
Cdd:PRK11448 104 EALMGLKLAfrlavwfHRTYGKDWDFKPGPFVPPEdpENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAL- 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220506 2025 kEKLAAineatrlktEAEVALKAKEAENERLKRQAE----DEAYQRKLLEDQAAQhKHDIQEKIT 2085
Cdd:PRK11448 183 -EGLAA---------ELEEKQQELEAQLEQLQEKAAetsqERKQKRKEITDQAAK-RLELSEEET 236
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
195-318 |
4.42e-03 |
|
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409187 Cd Length: 130 Bit Score: 40.34 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 195 ADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlVRNVRLPREKGRMRFHklqNVQ 274
Cdd:cd21338 15 APDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVP-----LHNFYLTPESFDQKVH---NVS 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220506 275 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 318
Cdd:cd21338 87 FAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2634-2777 |
4.85e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.00 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2634 EKEREKLKRDAQElqnKSKETASAQQEQMEQQKAMLQQtfltEKElllKRERDVEDEKKKLQKHLEDEVNKaKALKDEQQ 2713
Cdd:pfam13904 43 KLEGLKLERQPLE---AYENWLAAKQRQRQKELQAQKE----ERE---KEEQEAELRKRLAKEKYQEWLQR-KARQQTKK 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 2714 RQQKLMDEEKKKLQAIMDEAVKKQKEAEAemKNKQKEMEaLEKKRLEQEKLLADENKKLREKLE 2777
Cdd:pfam13904 112 REESHKQKAAESASKSLAKPERKVSQEEA--KEVLQEWE-RKKLEQQQRKREEEQREQLKKEEE 172
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2289-2555 |
4.89e-03 |
|
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: 42.53 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2289 QKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkEAEAEAAKRAAAEAAALKQKQEADAEmaKHKKEAEQALKQKSQVEKEl 2368
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQRAAEQARQKELEQRAAAE--KAAKQAEQAAKQAEEKQKQ- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2369 glvklqldetdkqkalmDEELqrvKAQVNDAVKQKAQVENElskvkmqmdellklkvrieeenlrlmQKNKDNTQKllAE 2448
Cdd:TIGR02794 121 -----------------AEEA---KAKQAAEAKAKAEAEAE--------------------------RKAKEEAAK--QA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2449 EAEKMKSLAEEAARLSVEAEETARQRKTAEAElAEQRALAekmlkEKMQAIQEATKLKAEAEelQKQKNQAQEKAKKLLE 2528
Cdd:TIGR02794 153 EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE-AEAKAKA-----EEAKAKAEAAKAKAAAE--AAAKAEAEAAAAAAAE 224
|
250 260
....*....|....*....|....*..
gi 1655220506 2529 DKQEIQQRLDKETQGFQKSLEAERKRQ 2555
Cdd:TIGR02794 225 AERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2191-2521 |
4.94e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKN--------KEDLLSQEKLRDE 2262
Cdd:COG5185 194 ELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSdkleklveQNTDLRLEKLGEN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2263 FENAKKLAQAAETAKEKAEKEAALLRQKAEEAEklKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQE 2342
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKIAEYTKSID--IKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2343 ADAEMAKHKKEAEQ--ALKQKSQVEKELGLVKLQLDET----DKQKALMDEELQRVKAQVNDAVK----QKAQVENELSK 2412
Cdd:COG5185 352 LTENLEAIKEEIENivGEVELSKSSEELDSFKDTIESTkeslDEIPQNQRGYAQEILATLEDTLKaadrQIEELQRQIEQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2413 VKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMK-SLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKM 2491
Cdd:COG5185 432 ATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
330 340 350
....*....|....*....|....*....|
gi 1655220506 2492 LKEKMQAIQEATKLKAEAEELQKQKNQAQE 2521
Cdd:COG5185 512 LEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2286-2485 |
4.95e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2286 LLRQKAEEAEKLKKAAEDEAAKQAKAQKDaerlrkeaeaeaakraaaeaaalKQKQEADAEMAKHKKEAEQALKQKsqvE 2365
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKK-----------------------EALLEAKEEIHKLRNEFEKELRER---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2366 KELGlvklQLDETDKQK-ALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQK 2444
Cdd:PRK12704 82 NELQ----KLEKRLLQKeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1655220506 2445 LLAEEAEkmKSLAEEAARLSVEAEETARQRKTAEAE----LAEQR 2485
Cdd:PRK12704 158 ILLEKVE--EEARHEAAVLIKEIEEEAKEEADKKAKeilaQAIQR 200
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2372-2517 |
5.16e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2372 KLQLDETDkqkALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAE 2451
Cdd:smart00787 146 KEGLDENL---EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 2452 KMKSLAE---EAARLSVEAEETARQRKTAEAELAEQRalaEKMLKEKMQAIQEATKLKAEAEELQKQKN 2517
Cdd:smart00787 223 KVKKLEEleeELQELESKIEDLTNKKSELNTEIAEAE---KKLEQCRGFTFKEIEKLKEQLKLLQSLTG 288
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2196-2779 |
5.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2196 AQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAqaaet 2275
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL----- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2276 akekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKdaERLRKEAEAEAAKRaaaeaaalkQKQEADAEMAKHKKEAE 2355
Cdd:COG4913 322 ------------REELDELEAQIRGNGGDRLEQLEREI--ERLERELEERERRR---------ARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2356 QAlkqksQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVK----------MQMDELLKLKV 2425
Cdd:COG4913 379 AE-----EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparlLALRDALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2426 RIEEENLR----LMQ-KNKD-----------NTQK--LLAEEA--------------------EKMKSLAEEAARLSVEA 2467
Cdd:COG4913 454 GLDEAELPfvgeLIEvRPEEerwrgaiervlGGFAltLLVPPEhyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2468 EETARQ--------RKTAEAELAEQRALA----EKMLKEKMQAIQEA--TKLKAEAEELQKQKN---------QAQEKAK 2524
Cdd:COG4913 534 DSLAGKldfkphpfRAWLEAELGRRFDYVcvdsPEELRRHPRAITRAgqVKGNGTRHEKDDRRRirsryvlgfDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2525 KLLEDKQEIQQRLDkETQGFQKSLEAERKRQLEISAEAEKL-KLRVKELSSAQAKAE-EEATRFKKQADEAKVRLQETEK 2602
Cdd:COG4913 614 ALEAELAELEEELA-EAEERLEALEAELDALQERREALQRLaEYSWDEIDVASAEREiAELEAELERLDASSDDLAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2603 QttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnksKETASAQQEQMEQQKAMLQQTFltEKELLLK 2682
Cdd:COG4913 693 Q-----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ---DRLEAAEDLARLELRALLEERF--AAALGDA 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2683 RERDVedekkklqkhledevnkAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMknkQKEMEALEKKRLEQE 2762
Cdd:COG4913 763 VEREL-----------------RENLEERIDALRARLNRAEEELERAMRAFNREWPAETADL---DADLESLPEYLALLD 822
|
650
....*....|....*..
gi 1655220506 2763 KLLADENKKLREKLESL 2779
Cdd:COG4913 823 RLEEDGLPEYEERFKEL 839
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1901-2149 |
5.49e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1901 EQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQAEKVSQSNTEKSKQLLET 1980
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-KVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1981 EALKMKQLAEEAARLRsvAEEAKKQRQLAEDEAARQRA----EAEKILkeklaaINEATRLKTEAEVALKAKEAENERLK 2056
Cdd:COG1340 93 ELDELRKELAELNKAG--GSIDKLRKEIERLEWRQQTEvlspEEEKEL------VEKIKELEKELEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2057 RQAEDEAyqrklLEDQAAQHKHDIQEKITQLQS------SSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEK 2130
Cdd:COG1340 165 LRAELKE-----LRKEAEEIHKKIKELAEEAQElheemiELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250
....*....|....*....
gi 1655220506 2131 SDLEVELKKLKGIADETQK 2149
Cdd:COG1340 240 RELRKELKKLRKKQRALKR 258
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
351-428 |
5.53e-03 |
|
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: 39.21 E-value: 5.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 351 DNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSvAERELGVTRLLDPEDVDVAHPDEKSIITYVSSL 428
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1584-1819 |
5.62e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1584 LKLKMKEDASQRQGLAVDAEKQKQNIQlelTQLKNLSEQEIRSKN--QQLEEAQVSRRKLEEEIHLIRIQLQTTIK---- 1657
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIK---TYNKNIEEQRKKNGEniARKQNKYDELVEEAKTIKAEIEELTDELLnlvm 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1658 -QKSTADDeLQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKkNAEDELKRKSEAeKEAARQKQKALDELQKHkmQA 1736
Cdd:PHA02562 249 dIEDPSAA-LNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQ-QISEGPDRITKI-KDKLKELQHSLEKLDTA--ID 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1737 EEAERrlkqaEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1816
Cdd:PHA02562 324 ELEEI-----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 1655220506 1817 EKE 1819
Cdd:PHA02562 399 VKE 401
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3612-3648 |
5.67e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.67e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1655220506 3612 KLLSAEKAVTGYKDPYTGNKISLFQAMTKELVLREHA 3648
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2660-2764 |
5.79e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.28 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2660 EQMEQQKAMLQQTflTEKELLLkrERDVEDEKKKLQKHLEDEVNKAKAlkdeqQRQQKLMDEE-KKKLQAIMDEA-VKKQ 2737
Cdd:cd03406 169 EAMEAEKTKLLIA--EQHQKVV--EKEAETERKRAVIEAEKDAEVAKI-----QMQQKIMEKEaEKKISEIEDEMhLARE 239
|
90 100
....*....|....*....|....*...
gi 1655220506 2738 KE-AEAEMKNKQKEMEAlEKKRLEQEKL 2764
Cdd:cd03406 240 KArADAEYYRALREAEA-NKLKLTPEYL 266
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
2619-2810 |
5.85e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.65 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2619 STREADDLKKAIAELEKEREKLKRDAQELQNKSkETASAQQEQMEQQKAMLQQ------TFLTEKElllKRERDVEDEKK 2692
Cdd:pfam17078 1 STKVIESLHDQIDALTKTNLQLTVQSQNLLSKL-EIAQQKESKFLENLASLKHendnlsSMLNRKE---RRLKDLEDQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2693 KLQKHLEDEVNKAKALKDE----QQRQQKLMdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM-EALEKKRLEQEK---- 2763
Cdd:pfam17078 77 ELKNSYEELTESNKQLKKRlensSASETTLE-AELERLQIQYDALVDSQNEYKDHYQQEINTLqESLEDLKLENEKqlen 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2764 ---LLADENKKLREKLESLEVTSKQaaskTKEIEVQTDKVPEEQLVSMTT 2810
Cdd:pfam17078 156 yqqRISSNDKDIDTKLDSYNNKFKN----LDNIYVNKNNKLLTKLDSLAQ 201
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1320-1563 |
6.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1320 RSQLKAMRAEAEAdqatfdrLQDELKAATSVSDKMTRLHSERDAELEHYRQLAgsllerwQAVFAQIDLR--QRELSLLG 1397
Cdd:COG4913 609 RAKLAALEAELAE-------LEEELAEAEERLEALEAELDALQERREALQRLA-------EYSWDEIDVAsaEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1398 RHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQI 1477
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEEL----EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1478 LAYRaLQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIK-FILETQ----------------RRLEDD-- 1538
Cdd:COG4913 751 LEER-FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNReWPAETAdldadleslpeylallDRLEEDgl 829
|
250 260
....*....|....*....|....*....
gi 1655220506 1539 ----EKASEKLKEDEKKRMAEIQAQLETQ 1563
Cdd:COG4913 830 peyeERFKELLNENSIEFVADLLSKLRRA 858
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1875-2027 |
6.24e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1875 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN--ELQRLKNEVNAAEKQRRQLEDELAKVRSE 1952
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMER 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220506 1953 MDALlqmkiqaEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQ-LAEDEAARQRAEAEKILKEK 2027
Cdd:COG1579 119 IEEL-------EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREeLAAKIPPELLALYERIRKRK 187
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1535-1819 |
6.26e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1535 LEDDEKASEKLKEDEKKRMAEIQAQLET-QKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDA---EKQKQNIQ 1610
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAmglQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1611 LELTQLKnlseqeirSKNQQLEEAQVSR-RKLEEEIH--LIRIQLQTTIKQKstaddeLQKLRDqaAEAEKVRKAAQEEA 1687
Cdd:PLN03229 493 EEFSKAN--------SQDQLMHPVLMEKiEKLKDEFNkrLSRAPNYLSLKYK------LDMLNE--FSRAKALSEKKSKA 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1688 ERLRKQVNeetQKKKNAED--ELKRKSEAEK-EAARQKQKALDELQKHkmQAEEAERRLKQAEEEKVRQIKV----VEEV 1760
Cdd:PLN03229 557 EKLKAEIN---KKFKEVMDrpEIKEKMEALKaEVASSGASSGDELDDD--LKEKVEKMKKEIELELAGVLKSmgleVIGV 631
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220506 1761 AQKTAATQLQAM--SFSEKTTKLEESLKKEQGTVLQ---LQEEAEKLRKQEEEANKAREQAEKE 1819
Cdd:PLN03229 632 TKKNKDTAEQTPppNLQEKIESLNEEINKKIERVIRssdLKSKIELLKLEVAKASKTPDVTEKE 695
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1602-1805 |
6.57e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.72 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1602 AEKQKQNIQLELTQLKNLSEQEIRS---KNQQLEEAQVSRRkleeeIHLIRIQlqttiKQKSTadDELQKLRDQaaeaek 1678
Cdd:pfam10168 522 ADKLSSPSPQECLQLLSRATQVFREeylKKHDLAREEIQKR-----VKLLKLQ-----KEQQL--QELQSLEEE------ 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1679 vRKAAQEEAERLRKQVNE--ETQKK---------KNAEDELKRKSEAEKEAARqkqkaldELQKHKMQAEEAERRLKQAE 1747
Cdd:pfam10168 584 -RKSLSERAEKLAEKYEEikDKQEKlmrrckkvlQRLNSQLPVLSDAEREMKK-------ELETINEQLKHLANAIKQAK 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220506 1748 EEKVRQIKvveEVAQKTAATQLQAMSFSEKTTK-LEESLKKEQGTVLQLQEEAEKLRKQ 1805
Cdd:pfam10168 656 KKMNYQRY---QIAKSQSIRKKSSLSLSEKQRKtIKEILKQLGSEIDELIKQVKDINKH 711
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
203-249 |
6.57e-03 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 39.18 E-value: 6.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1655220506 203 KKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE 249
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVP 49
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2557-2779 |
6.99e-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: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2557 EISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREA--DDLKKAIAELE 2634
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAakEELRIELRDKT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2635 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERD--VEDEKKKLQKHLEDEVNKA------- 2705
Cdd:pfam19220 118 AQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLalLEQENRRLQALSEEQAAELaeltrrl 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2706 ----KALKDEQQR----QQKLMDE--EKKKLQAIMDEAVKKQKEAEAEMKNKqkeMEALEKKRLEQEKLLADENKKLREK 2775
Cdd:pfam19220 198 aeleTQLDATRARlralEGQLAAEqaERERAEAQLEEAVEAHRAERASLRMK---LEALTARAAATEQLLAEARNQLRDR 274
|
....
gi 1655220506 2776 LESL 2779
Cdd:pfam19220 275 DEAI 278
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1544-1753 |
7.05e-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: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1544 KLKEDEKKRMAEIQAQLETQKQLAE---GHAKSVAKAELEAQELK-----LKMKEDASQRQGLAVDaekqKQNIQLElTQ 1615
Cdd:pfam19220 196 RLAELETQLDATRARLRALEGQLAAeqaERERAEAQLEEAVEAHRaerasLRMKLEALTARAAATE----QLLAEAR-NQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1616 LKNLSEqEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTtikqkstaddELQKLRDQAAEAEKVRKAAQEEAERLRKQVN 1695
Cdd:pfam19220 271 LRDRDE-AIRAAERRLKEASIERDTLERRLA----GLEA----------DLERRTQQFQEMQRARAELEERAEMLTKALA 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220506 1696 EETQKKKNAE----------DELKRKSEAEKEAARQKQKALDElqkhKMQAEEAERRLKQAEEEKVRQ 1753
Cdd:pfam19220 336 AKDAALERAEeriaslsdriAELTKRFEVERAALEQANRRLKE----ELQRERAERALAQGALEIARE 399
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1667-1767 |
7.18e-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: 40.16 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1667 QKLRDQAAEAEKVRKAAQEEAERLRKQVNEetqkkknAEDELKR-KSEAEKEAARQKQKALDELQkhkmqaEEAERRLKQ 1745
Cdd:COG0711 34 EKIADGLAEAERAKEEAEAALAEYEEKLAE-------ARAEAAEiIAEARKEAEAIAEEAKAEAE------AEAERIIAQ 100
|
90 100
....*....|....*....|...
gi 1655220506 1746 AEEEKVRQI-KVVEEVAQKTAAT 1767
Cdd:COG0711 101 AEAEIEQERaKALAELRAEVADL 123
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
202-311 |
7.44e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 39.43 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 202 QKKTFTKWVNKHL---------MKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRNVRL-PREKgrmrfhkLQ 271
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTID-ERAINTKKVLnPWER-------NE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1655220506 272 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 311
Cdd:cd21293 74 NHTLCLNSAKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2191-2494 |
7.78e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2191 RQRKAAQDEVERLKQKAAEAnKLK---DKAEKELEKQvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAK 2267
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEA-KARfeaRQARLEREKA---AREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2268 KLAQAAETAKEKAEKEAALLRQKAEEAEKlKKAAEDEAAKQAKAQKDAERlrkeaeaeaakrAAAEAAALKQKQEADAEM 2347
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAE-KQAAAAADPKKAAVAAAIAR------------AKAKKAAQQAANAEAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2348 AKHKKEAEQALKQKSQVEKElglvklqldetdkQKALMDEELQRVKAQVNDavkQKAQVENELSKVKMQMDELLKLKVRI 2427
Cdd:PRK05035 575 VDPKKAAVAAAIARAKAKKA-------------AQQAASAEPEEQVAEVDP---KKAAVAAAIARAKAKKAEQQANAEPE 638
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220506 2428 EEEnlrlmqknkDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAElAEQRALAEKMLKE 2494
Cdd:PRK05035 639 EPV---------DPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAA-AIARAKAKKAAQQ 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1764-2021 |
7.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1764 TAATQLQAMSfsEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRlRLRAEEEAQR 1843
Cdd:COG3883 13 FADPQIQAKQ--KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID----KLQAEIA-EAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1844 KSLAQEEAEKQKTEAERDAKKKAKaeeaalkqkeNAE--KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEH----AEQQ 1917
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVLL----------GSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAkkaeLEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1918 RGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRS 1997
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
250 260
....*....|....*....|....
gi 1655220506 1998 VAEEAKKQRQLAEDEAARQRAEAE 2021
Cdd:COG3883 236 AAAAAAAAASAAGAGAAGAAGAAA 259
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2407-2672 |
7.86e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2407 ENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLL--AEEAEKMKSLAEEAARLSVEAEETARQRKTAEAElaeq 2484
Cdd:pfam17045 5 EAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELlsARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2485 ralaekmlkEKMQAIQEA-TKLKAEAEELQ-KQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKR---QLEIS 2559
Cdd:pfam17045 81 ---------QQLQKLQEElSKLKRSYEKLQrKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRlqyQQQVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2560 AEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTReaddLKKAIAELEKEREK 2639
Cdd:pfam17045 152 SLEAQRKALAEQSSLIQSAAYQVQLEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELER----LRMRVSELGDSNRK 227
|
250 260 270
....*....|....*....|....*....|...
gi 1655220506 2640 LKRDAQELQNKSKEtASAQQEQMEQQKAMLQQT 2672
Cdd:pfam17045 228 LLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2510-2708 |
7.91e-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: 41.18 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2510 EELQKQKNQAQEKAKKLLEDKQE-IQQRLDKETQgfqkslEAERKRQLEISAEAEKLKLRVKElssaQAKAEEEATRFKK 2588
Cdd:pfam15665 14 AEIQALKEAHEEEIQQILAETREkILQYKSKIGE------ELDLKRRIQTLEESLEQHERMKR----QALTEFEQYKRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2589 QADEAKVRLQETEKQTT------------ETVVQKLETQRLQSTREAddlKKAIAELekeREKLKRDAQELQNKSKetas 2656
Cdd:pfam15665 84 EERELKAEAEHRQRVVElsreveeakrafEEKLESFEQLQAQFEQEK---RKALEEL---RAKHRQEIQELLTTQR---- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1655220506 2657 AQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKAL 2708
Cdd:pfam15665 154 AQSASSLAEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQAF 205
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
2505-2625 |
7.92e-03 |
|
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.
Pssm-ID: 462906 Cd Length: 615 Bit Score: 42.31 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2505 LKAEAEELQKQKnqaQEKAKKLLEDKQEIQQRLDKETQGFQKSLEaerkrqleiSAEAEK--LKLRVKELSSAQAKAEEE 2582
Cdd:pfam09798 2 LRDKLELLQQEK---EKELEKLKNSYEELKSSHEEELEKLKQEVQ---------KLEDEKkfLLNELRSLSATSPASSQS 69
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1655220506 2583 ATRFKKQADEAKVRLQETEKQTTETVVQKLetQRLQSTREADD 2625
Cdd:pfam09798 70 HETDTDDSSSVSLKKRKIEESTAESLKQKY--IRLQNNRIVDE 110
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1669-1749 |
8.32e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 40.70 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1669 LRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDElKRKSEAEKEAARQKQKALDELQKHKMQAEEA--ERRLKQA 1746
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILE-KAEREAEREKRRIISSAELEARKELLEAKEEliEEVFEEA 90
|
...
gi 1655220506 1747 EEE 1749
Cdd:COG1390 91 LEK 93
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2544-2703 |
8.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2544 FQKSLEAERKRQlEISAEAEKLKlrvkelSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLEtqrlQSTREA 2623
Cdd:PRK12705 29 QRLAKEAERILQ-EAQKEAEEKL------EAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEE----QLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2624 DDLKKAIAELEKEREKLKRDAQELQNKSKetasaQQEQMEQQKAMLQQTFLteKELLLKR-ERDVEDEKKKLQKHLEDEV 2702
Cdd:PRK12705 98 EKLDNLENQLEEREKALSARELELEELEK-----QLDNELYRVAGLTPEQA--RKLLLKLlDAELEEEKAQRVKKIEEEA 170
|
.
gi 1655220506 2703 N 2703
Cdd:PRK12705 171 D 171
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2625-2791 |
8.74e-03 |
|
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: 41.75 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2625 DLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtfltEKELLLKRERDVEDEKKKLQkhlEDEVNK 2704
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA--------EQARQKELEQRAAAEKAAKQ---AEQAAK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2705 AKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAE--AEMKNKQKEMEALEKKRLEQEKLLADENKK---LREKLESL 2779
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAkqAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAkaeAEAKAKAE 192
|
170
....*....|..
gi 1655220506 2780 EVTSKQAASKTK 2791
Cdd:TIGR02794 193 EAKAKAEAAKAK 204
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2337-2606 |
8.74e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2337 LKQKQEADAEMAKHKKEAEQALKQksqvekelglvklqldetdkqkalMDEELQRVKAQVNDAVKQKAQVENElSKVKMQ 2416
Cdd:pfam02029 65 LDRTAKREERRQKRLQEALERQKE------------------------FDPTIADEKESVAERKENNEEEENS-SWEKEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2417 MDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMkslaEEAARLSVEAEETARQRKTAEaELAEQRALAEKMLKEKM 2496
Cdd:pfam02029 120 KRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEG----EEEEDKSEEAEEVPTENFAKE-EVKDEKIKKEKKVKYES 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2497 ----------------QAIQEATKLKAEAEELQKQKNQAQEK---AKKLLEDKQEI----QQRLDKETQGFQKSleaeRK 2553
Cdd:pfam02029 195 kvfldqkrghpevksqNGEEEVTKLKVTTKRRQGGLSQSQEReeeAEVFLEAEQKLeelrRRRQEKESEEFEKL----RQ 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1655220506 2554 RQLEISAEAEKLKLRVKELSSAQakaEEEATRFKKQADEAKVRLQETEKQTTE 2606
Cdd:pfam02029 271 KQQEAELELEELKKKREERRKLL---EEEEQRRKQEEAERKLREEEEKRRMKE 320
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4467-4497 |
8.93e-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: 8.93e-03
10 20 30
....*....|....*....|....*....|.
gi 1655220506 4467 AGILDTDTLEKVSVTEAIHRNLVDNITGQRL 4497
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2421-2522 |
9.04e-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: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2421 LKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEA----EETARQRKTAEAELAEQRALAEKM--LKE 2494
Cdd:pfam20492 11 LEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRqeaeEEKERLEESAEMEAEEKEQLEAELaeAQE 90
|
90 100
....*....|....*....|....*....
gi 1655220506 2495 KMQAIQEATKLK-AEAEELQKQKNQAQEK 2522
Cdd:pfam20492 91 EIARLEEEVERKeEEARRLQEELEEAREE 119
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1837-2093 |
9.17e-03 |
|
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: 42.51 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1837 AEEEAQRKSLAQEEAEKQKTEAERdakkkakaeEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR--LKADFEHA 1914
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEADR---------QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRdaILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1915 EQQRGLLDNELQRLKNEVNAAEKQRRQLEDELA-----KVRSEMDallqmkiQAEKVSQSNTEKSKQLLETEALKMKqla 1989
Cdd:NF012221 1619 TKELTTLAQGLDALDSQATYAGESGDQWRNPFAgglldRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVK--- 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1990 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKlL 2069
Cdd:NF012221 1689 DAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ-A 1767
|
250 260
....*....|....*....|....
gi 1655220506 2070 EDQAAQHKHDIQEKITQLQSSSVS 2093
Cdd:NF012221 1768 DAKGAKQDESDKPNRQGAAGSGLS 1791
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2578-2751 |
9.28e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.16 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2578 KAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLetqRLQSTREADDLKKAI-AELEKEREKLKRDAQELQNKS----- 2651
Cdd:PRK00106 39 NAEQEAVNLRGKAERDAEHIKKTAKRESKALKKEL---LLEAKEEARKYREEIeQEFKSERQELKQIESRLTERAtsldr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2652 KETASAQQEQMEQQKamlQQTFLTEKELLLKRERDVEdekkKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKklqaIMD 2731
Cdd:PRK00106 116 KDENLSSKEKTLESK---EQSLTDKSKHIDEREEQVE----KLEEQKKAELERVAALSQAEAREIILAETENK----LTH 184
|
170 180
....*....|....*....|
gi 1655220506 2732 EAVKKQKEAEAEMKNKQKEM 2751
Cdd:PRK00106 185 EIATRIREAEREVKDRSDKM 204
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1986-2224 |
9.98e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 1986 KQLAEEAARLRSVAEEAKKQRQLAEdEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAE----D 2061
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelraE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2062 EAYQRKLLEDQ-AAQHKHDIQEKITQL-QSSSVSELDRQKNIVEETLRQKKvveEEIHIIRINFERASKEKSDLEVELKK 2139
Cdd:COG4942 99 LEAQKEELAELlRALYRLGRQPPLALLlSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220506 2140 LKGIADETQKskakaeeeaeklkklaaeeerKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEK 2219
Cdd:COG4942 176 LEALLAELEE---------------------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*
gi 1655220506 2220 ELEKQ 2224
Cdd:COG4942 235 EAAAA 239
|
|
| |
