|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
1-641 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1165.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 1 MPKLPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDD 80
Cdd:PTZ00009 1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 81 ATVQSDMKHWPFEVFAE-NGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATK 159
Cdd:PTZ00009 81 SVVQSDMKHWPFKVTTGgDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 160 DAGAIAGLNVLRIINEPTAAAIAYGLDKQGTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 240 HFVQEFQRKHK-KDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVA 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 319 KALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNKSINPDEAVAYGAAVQAAILHGDKSEAVQDLLLLDVTP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 399 LSLGIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 479 DIDANGILNVTALEKSTGKENRITITNDKGRLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQLRSTLDDEHL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 559 SSRFSPADRETIQQRSSETIAWLDANQLAERQEFEHKQQELERICSPIITRLYQGAG----------MAPPPTAGGSNPG 628
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQAAGggmpggmpggMPGGMPGGAGPAG 640
|
650
....*....|...
gi 266308 629 ATGGSGPTIEEVD 641
Cdd:PTZ00009 641 AGASSGPTVEEVD 653
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
6-612 |
0e+00 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 940.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFEVFA-ENGKPRIRVEYKGErkSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:pfam00012 81 DIKHLPYKVVKlPNGDAGVEVRYLGE--TFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQGTsERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKTDK-ERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSS-STQASIEIDSLFE-GVDFYTSVTRARFEELNGDLFRGTMEPVAKALR 322
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 323 DAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDksEAVQDLLLLDVTPLSLG 402
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 403 IETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDIDA 482
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 483 NGILNVTALEKSTGKENRITITNDKGrLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQLRSTLDDEhlSSRF 562
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE--GDKV 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 266308 563 SPADRETIqqrsSETIAWL-DANQLAERQEFEHKQQELERICSPIITRLYQ 612
Cdd:pfam00012 552 PEAEKSKV----ESAIEWLkDELEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
6-380 |
0e+00 |
|
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466831 [Multi-domain] Cd Length: 375 Bit Score: 902.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFEVFAENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQGTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 245
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 246 QRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDAK 325
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 266308 326 MDKGQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-626 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 879.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 1 MPKlpAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTES-ERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFD 79
Cdd:PRK00290 1 MGK--IIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRRDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 80 DatVQSDMKHWPFEVF-AENGKPRirVEYKGerKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQAT 158
Cdd:PRK00290 79 E--VQKDIKLVPYKIVkADNGDAW--VEIDG--KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 159 KDAGAIAGLNVLRIINEPTAAAIAYGLDKQGtsERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:PRK00290 153 KDAGKIAGLEVLRIINEPTAAALAYGLDKKG--DEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 239 NHFVQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIeidSL-FEGVD------FYTSVTRARFEELNGDLFR 311
Cdd:PRK00290 231 DYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEI---NLpFITADasgpkhLEIKLTRAKFEELTEDLVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 312 GTMEPVAKALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDkseaVQDL 391
Cdd:PRK00290 308 RTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 392 LLLDVTPLSLGIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGV 471
Cdd:PRK00290 383 LLLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 472 PQVEVTFDIDANGILNVTALEKSTGKENRITITNDKGrLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQLRS 551
Cdd:PRK00290 463 PQIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEK 541
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 266308 552 TLDDehLSSRFSPADRETIQQRSSETIAWLDANQLAERQEfehKQQELERICSPIITRLYQGAGMAPPPTAGGSN 626
Cdd:PRK00290 542 TLKE--LGDKVPADEKEKIEAAIKELKEALKGEDKEAIKA---KTEELTQASQKLGEAMYQQAQAAQGAAGAAAK 611
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
6-612 |
0e+00 |
|
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274091 [Multi-domain] Cd Length: 595 Bit Score: 802.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTES-ERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDatVQ 84
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 85 SDMKHWPFEVFAENGKPRIRVEykgeRKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKVD----GKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQGTSERnVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVD----FYTSVTRARFEELNGDLFRGTMEPVAKA 320
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVRQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 321 LRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDkseaVQDLLLLDVTPLS 400
Cdd:TIGR02350 315 LKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTPLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 401 LGIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDI 480
Cdd:TIGR02350 390 LGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 481 DANGILNVTALEKSTGKENRITITNDKGrLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQLRSTLDDehLSS 560
Cdd:TIGR02350 470 DANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--AGD 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 266308 561 RFSPADRETIQQRSSETIAWLDANQLAerqEFEHKQQELERICSPIITRLYQ 612
Cdd:TIGR02350 547 KLPAEEKEKIEKAVAELKEALKGEDVE---EIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
5-380 |
0e+00 |
|
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 753.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 5 PAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQ 84
Cdd:cd10241 2 TVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 85 SDMKHWPFEVFAENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:cd10241 82 KDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQGTsERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:cd10241 162 AGLNVLRIINEPTAAAIAYGLDKKGG-EKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDA 324
Cdd:cd10241 241 FKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 266308 325 KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10241 321 GLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
6-380 |
0e+00 |
|
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The HSPA1-like family includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10), HSPA13 (also known as 70-kDa heat shock protein 13; STCH; microsomal stress-70 protein ATPase core; stress-70 protein chaperone microsome-associated 60 kDa protein), as well as Saccharmoyces cerevisiae Hsp70 chaperone Ssb1-2 and heat shock protein Ssa1-4. HSPA1A/1B, HSPA1L, HSPA2 and HSPA6-8 are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). HSPA13 has peptide-independent ATPase activity. All family members belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466878 [Multi-domain] Cd Length: 376 Bit Score: 751.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFEVFA-ENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:cd24028 81 DIKHWPFKVVEdEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQGTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDA 324
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 266308 325 KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
7-625 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 708.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTES-ERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDatVQS 85
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE--ISE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFEVfAENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:CHL00094 83 EAKQVSYKV-KTDSNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQgtSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 245
Cdd:CHL00094 162 GLEVLRIINEPTAASLAYGLDKK--NNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 246 QRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIE---IDSLFEG-VDFYTSVTRARFEELNGDLFRGTMEPVAKAL 321
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 322 RDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDkseaVQDLLLLDVTPLSL 401
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDVTPLSL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 402 GIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDID 481
Cdd:CHL00094 395 GVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 482 ANGILNVTALEKSTGKENRITITNdKGRLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQLRSTLDDehLSSR 561
Cdd:CHL00094 475 ANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE--LKDK 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 266308 562 FSPADRETIQqrssETIAWL-DANQLAERQEFEHKQQELERICSPIITRLYQGAGMAPPPTAGGS 625
Cdd:CHL00094 552 ISEEKKEKIE----NLIKKLrQALQNDNYESIKSLLEELQKALMEIGKEVYSSTSTTDPASNDDD 612
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
7-641 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 699.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTES-ERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQs 85
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTEEE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 dmkhwpfevfaengkpRIRVEYKGER------------KSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDS 153
Cdd:PRK13411 84 ----------------RSRVPYTCVKgrddtvnvqirgRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 154 QRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDKQGTsERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDF 233
Cdd:PRK13411 148 QRQATKDAGTIAGLEVLRIINEPTAAALAYGLDKQDQ-EQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 234 DNRLVNHFVQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDslFEGVD------FYTSVTRARFEELNG 307
Cdd:PRK13411 227 DNCIVDWLVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLP--FITADetgpkhLEMELTRAKFEELTK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 308 DLFRGTMEPVAKALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNKSINPDEAVAYGAAVQAAILHGDksea 387
Cdd:PRK13411 305 DLVEATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 388 VQDLLLLDVTPLSLGIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPA 467
Cdd:PRK13411 381 VKDLLLLDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 468 PRGVPQVEVTFDIDANGILNVTALEKSTGKENRITITNdKGRLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCF 547
Cdd:PRK13411 461 PRGVPQIEVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLY 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 548 QLRSTLDDEhlSSRFSPADRETIQQRSSETIAWLDANQLaERQEFEHKQQELERICSPIITRLYQGAG------MAPPPT 621
Cdd:PRK13411 540 SYESTLKEN--GELISEELKQRAEQKVEQLEAALTDPNI-SLEELKQQLEEFQQALLAIGAEVYQQGGsqttdtVEPTSD 616
|
650 660
....*....|....*....|
gi 266308 622 AGGSNPGATGGSGPTIEEVD 641
Cdd:PRK13411 617 TLITATMNSSNETTLIDEFN 636
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
7-641 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 688.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTES-ERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFE-VFAENGKPRirVEYKGERKSfyPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:PTZ00400 124 EQKILPYKiVRASNGDAW--IEAQGKKYS--PSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKqgTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:PTZ00400 200 AGLDVLRIINEPTAAALAFGMDK--NDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQasIEIDSLFEGVD------FYTSVTRARFEELNGDLFRGTMEPVA 318
Cdd:PTZ00400 278 FKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQ--TEINLPFITADqsgpkhLQIKLSRAKLEELTHDLLKKTIEPCE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 319 KALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDkseaVQDLLLLDVTP 398
Cdd:PTZ00400 356 KCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDLLLLDVTP 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 399 LSLGIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTF 478
Cdd:PTZ00400 431 LSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTF 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 479 DIDANGILNVTALEKSTGKENRITITNDKGrLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQLRSTLDDehL 558
Cdd:PTZ00400 511 DVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD--L 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 559 SSRFSPADRETIQQRSSETIAWLDANQLaerQEFEHKQQELERICSPIITRLYQGAGmappptAGGSNPGATGGSGPTIE 638
Cdd:PTZ00400 588 KDKISDADKDELKQKITKLRSTLSSEDV---DSIKDKTKQLQEASWKISQQAYKQGN------SDNQQSEQSTNSEESEE 658
|
...
gi 266308 639 EVD 641
Cdd:PTZ00400 659 KND 661
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
6-519 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 682.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-ESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDatvq 84
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 85 sdmkhwpfevfaengkprIRVEYKGERKSfyPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:COG0443 77 ------------------EATEVGGKRYS--PEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKqGTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDK-GKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDsLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDA 324
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 325 KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDKSEavqdlllLDVTPLSLGIE 404
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 405 TAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDIDANG 484
Cdd:COG0443 367 TLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANG 446
|
490 500 510
....*....|....*....|....*....|....*
gi 266308 485 ILNVTALEKSTGKENRITItndkgrlsKEDIERMV 519
Cdd:COG0443 447 ILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
7-600 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 664.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-ESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDELDPES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 dmKHWPFEVFA-ENGKprIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:PRK13410 85 --KRVPYTIRRnEQGN--VRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQgtSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDRS--SSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVD----FYTSVTRARFEELNGDLFRGTMEPVAKA 320
Cdd:PRK13410 239 FLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDgpkhIETRLDRKQFESLCGDLLDRLLRPVKRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 321 LRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDkseaVQDLLLLDVTPLS 400
Cdd:PRK13410 319 LKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 401 LGIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDI 480
Cdd:PRK13410 394 LGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 481 DANGILNVTALEKSTGKENRITITNdKGRLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQ----LR-STLDd 555
Cdd:PRK13410 474 DANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQaerrLRdAALE- 551
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 266308 556 ehLSSRFSPADRETIQQRSSETIAWLDANQLaerQEFEHKQQELE 600
Cdd:PRK13410 552 --FGPYFAERQRRAVESAMRDVQDSLEQDDD---RELDLAVADLQ 591
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
6-380 |
0e+00 |
|
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466943 [Multi-domain] Cd Length: 375 Bit Score: 638.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQhGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFEVFAENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLD-KQGTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDA 324
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 266308 325 KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
7-641 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 635.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTES-ERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDatVQS 85
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFEVFA-ENGKPRIRVEYKGerKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:PLN03184 120 ESKQVSYRVVRdENGNVKLDCPAIG--KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQgtSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKK--SNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVD----FYTSVTRARFEELNGDLFRGTMEPVAKA 320
Cdd:PLN03184 276 FKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADgpkhIDTTLTRAKFEELCSDLLDRCKTPVENA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 321 LRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFfNGKELNKSINPDEAVAYGAAVQAAILHGDkseaVQDLLLLDVTPLS 400
Cdd:PLN03184 356 LRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTPLS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 401 LGIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDI 480
Cdd:PLN03184 431 LGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDI 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 481 DANGILNVTALEKSTGKENRITITNdKGRLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQLRSTLddEHLSS 560
Cdd:PLN03184 511 DANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQL--KELGD 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 561 RFSPADRETIQQRSSETIAWLDANQLaerQEFEHKQQELERICSPIITRLYQGAGMA---PPPTAGGSNPGATGGSGPTI 637
Cdd:PLN03184 588 KVPADVKEKVEAKLKELKDAIASGST---QKMKDAMAALNQEVMQIGQSLYNQPGAGgagPAPGGEAGSSSSSSSGGDGD 664
|
....
gi 266308 638 EEVD 641
Cdd:PLN03184 665 DVID 668
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
7-634 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 600.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQSD 86
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 87 MKHWPFEVF-AENGKPRIRveyKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:PTZ00186 110 IKNVPYKIVrAGNGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKqgTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 245
Cdd:PTZ00186 187 GLNVIRVVNEPTAAALAYGMDK--TKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 246 QRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVD----FYTSVTRARFEELNGDLFRGTMEPVAKAL 321
Cdd:PTZ00186 265 RKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAPCKQCM 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 322 RDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDkseaVQDLLLLDVTPLSL 401
Cdd:PTZ00186 345 KDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVTPLSL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 402 GIETAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDID 481
Cdd:PTZ00186 420 GIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDID 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 482 ANGILNVTALEKSTGKENRITITNDKGrLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESycfqlRSTLDDEHLSS- 560
Cdd:PTZ00186 500 ANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAET-----QLTTAERQLGEw 573
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 266308 561 -RFSPADRETIQQRSSETIAWLDaNQLAERQEFEHKQQELERICSPIITRLYQGAGMAppptaggsNPGATGGSG 634
Cdd:PTZ00186 574 kYVSDAEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQKAVMECGRTEYQQAAAA--------NSGSSSNSG 639
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
6-572 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 563.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDatVQS 85
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFE-VFAENGKPRIRVeyKGERKSfyPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:PRK05183 99 RYPHLPYQfVASENGMPLIRT--AQGLKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQgtSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDSG--QEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNkralRRLRTACERAKRTLSSSTQASIEIdSLFEGvdfytSVTRARFEELNGDLFRGTMEPVAKALRDA 324
Cdd:PRK05183 253 AGLSPRLDPEDQ----RLLLDAARAAKEALSDADSVEVSV-ALWQG-----EITREQFNALIAPLVKRTLLACRRALRDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 325 KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDKSEAvqDLLLLDVTPLSLGIE 404
Cdd:PRK05183 323 GVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 405 TAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDIDANG 484
Cdd:PRK05183 400 TMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 485 ILNVTALEKSTGKENRITITNDKGrLSKEDIERMVNDAEAYRQADEQQR----DRINAKNQLESycfqLRSTLD-DEHLs 559
Cdd:PRK05183 480 LLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEA----LQAALAaDGDL- 553
|
570
....*....|...
gi 266308 560 srFSPADRETIQQ 572
Cdd:PRK05183 554 --LSAAERAAIDA 564
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
7-380 |
0e+00 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar proteins; This subfamily includes Escherichia coli chaperone protein DnaK (also known as heat shock 70 kDa protein/HSP70), human mitochondrial heat shock 70 kDa protein HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74), Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466832 [Multi-domain] Cd Length: 373 Bit Score: 553.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTES-ERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFeVFAENGKPRIRVEykgeRKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd10234 82 KQVPYPV-VSAGNGDAWVEIG----GKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQGtsERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 245
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDKKK--DEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 246 QRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIeidSL-FEGVD------FYTSVTRARFEELNGDLFRGTMEPVA 318
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEI---NLpFITADasgpkhLEMKLTRAKFEELTEDLVERTIEPVE 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 266308 319 KALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10234 312 QALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVL 372
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
6-573 |
0e+00 |
|
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK. [Protein fate, Protein folding and stabilization]
Pssm-ID: 273915 [Multi-domain] Cd Length: 599 Bit Score: 541.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTE-SERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQ 84
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKdGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 85 SDMkhwPFEvFAENGKPRIRVEYKGERKSfyPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:TIGR01991 81 SIL---PYR-FVDGPGEMVRLRTVQGTVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKqgTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDK--ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAkrtlssSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDA 324
Cdd:TIGR01991 233 LGISADLNPEDQRLLLQAARAAKEAL------TDAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 325 KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHGDKSEavQDLLLLDVTPLSLGIE 404
Cdd:TIGR01991 307 GLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIG--NDLLLLDVTPLSLGIE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 405 TAGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDIDANG 484
Cdd:TIGR01991 384 TMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 485 ILNVTALEKSTGKENRITITNDKGrLSKEDIERMVNDAEAYRQADEQQRDRINAKNQLESYCFQLRSTLDDEhlSSRFSP 564
Cdd:TIGR01991 464 LLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAAD--GDLLSE 540
|
....*....
gi 266308 565 ADRETIQQR 573
Cdd:TIGR01991 541 DERAAIDAA 549
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
7-380 |
1.13e-173 |
|
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466839 [Multi-domain] Cd Length: 377 Bit Score: 498.71 E-value: 1.13e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-ESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFE-VFAENGKPRirVEYKGERKSfyPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:cd11733 84 DIKMVPYKiVKASNGDAW--VEAHGKKYS--PSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKqgTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:cd11733 160 AGLNVLRIINEPTAAALAYGLDK--KDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQAsiEIDSLFEGVD------FYTSVTRARFEELNGDLFRGTMEPVA 318
Cdd:cd11733 238 FKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 266308 319 KALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11733 316 KCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
5-382 |
5.93e-156 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins; This subgroup includes Saccharomyces cerevisiae Stress-Seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space.
Pssm-ID: 466840 [Multi-domain] Cd Length: 378 Bit Score: 453.83 E-value: 5.93e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 5 PAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTES-ERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATV 83
Cdd:cd11734 2 PVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDgERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 84 QSDMKHWPFEVFAE-NGKPRirVEYKGerKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAG 162
Cdd:cd11734 82 QRDIKEVPYKIVKHsNGDAW--VEARG--QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 163 AIAGLNVLRIINEPTAAAIAYGLDKQGtsERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFV 242
Cdd:cd11734 158 QIAGLNVLRVINEPTAAALAYGLDKSG--DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 243 QEFQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVD----FYTSVTRARFEELNGDLFRGTMEPVA 318
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKLTRAQFESLVKPLVDRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 266308 319 KALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHG 382
Cdd:cd11734 316 KALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
1-382 |
4.98e-150 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187.
Pssm-ID: 466835 [Multi-domain] Cd Length: 409 Bit Score: 439.85 E-value: 4.98e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 1 MPKLPAVGIDLGTTYSCVGVFQH--GKVEIIANDQGNRTTPSYVAFTESER-LIGDAAKNQVAMNPNNTIFDAKRLIGRR 77
Cdd:cd10237 19 PPKPKIVGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 78 FDDATVQSDMKHWPFEVFAEN-GKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQ 156
Cdd:cd10237 99 FTKEELEEEAKRYPFKVVNDNiGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 157 ATKDAGAIAGLNVLRIINEPTAAAIAYGLDKQGTSErNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNR 236
Cdd:cd10237 179 ATRKAANLAGLEVLRVINEPTAAAMAYGLHKKSDVN-NVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 237 LVNHFVQEFQRKHKKDLgQNKRALRRLRTACERAKRTLSSSTQASIEID-----SLFEGVDFYTSVTRARFEELNGDLFR 311
Cdd:cd10237 258 LFQYLIDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqislPSAFKVKFKEEITRDLFETLNEDLFQ 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 266308 312 GTMEPVAKALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHG 382
Cdd:cd10237 337 RVLEPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
7-380 |
5.69e-147 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466879 [Multi-domain] Cd Length: 351 Bit Score: 429.69 E-value: 5.69e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVF-QHGKVEIIANDQGNRTTPSYVAFTESER-LIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDatvq 84
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDKDGEvLVGEEAKNQALLDPENTIYSVKRLMGRDTKD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 85 sdmkhwpfevfaengkprirvEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:cd24029 77 ---------------------KEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKqGTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDK-EGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQRKH-KKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRD 323
Cdd:cd24029 215 IGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 266308 324 AKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
6-382 |
2.46e-146 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.
Pssm-ID: 466834 [Multi-domain] Cd Length: 367 Bit Score: 428.56 E-value: 2.46e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLI-GDAAKNQVAMNPNNTIFDAKRLIGRRFDDatVQ 84
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 85 SDMKHWPFEvFAENGKPRIRVEYKGERKSfyPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:cd10236 82 EELPLLPYR-LVGDENELPRFRTGAGNLT--PVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQgtSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 244
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQK--KEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 245 FQrkhkKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDslFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDA 324
Cdd:cd10236 237 IG----IDARLDPAVQQALLQAARRAKEALSDADSASIEVE--VEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 266308 325 KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAILHG 382
Cdd:cd10236 311 GLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-380 |
9.71e-144 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; HSPA14, also called HSP70-like protein 1 (Hsp70L1), or heat shock protein HSP60, is a component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, HSPA14 binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466836 [Multi-domain] Cd Length: 377 Bit Score: 422.42 E-value: 9.71e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 5 PAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQ 84
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 85 SDMKHWPFEVFAENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQGTSE-RNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQ 243
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPTEnSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 244 EFQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRD 323
Cdd:cd10238 241 EFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 266308 324 AKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10238 321 AGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
7-378 |
1.20e-142 |
|
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466838 [Multi-domain] Cd Length: 377 Bit Score: 419.66 E-value: 1.20e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQSD 86
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 87 MKHWPFEVFA-ENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQG-----TSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDlleseEKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 241 FVQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKA 320
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 266308 321 LRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAA 378
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
6-380 |
2.30e-139 |
|
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and similar proteins; The subgroup includes Arabidopsis thaliana Hsp70-14, also known as heat shock 70 kDa protein 14; heat shock protein 91), Hsp70-15 (also known as heat shock 70 kDa protein 15), and Hsp70-16 (also known as heat shock 70 kDa protein 16). In cooperation with other chaperones, they are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. Members in this subgroup belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466945 [Multi-domain] Cd Length: 389 Bit Score: 411.70 E-value: 2.30e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQS 85
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFEVFA-ENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAI 164
Cdd:cd24095 83 DLKLFPFKVTEgPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYGLDKQGTSE---RNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHF 241
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIYKTDLPEtdpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 242 VQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKAL 321
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKAL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 266308 322 RDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24095 323 ADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
7-378 |
2.05e-133 |
|
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25). They belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466826 [Multi-domain] Cd Length: 378 Bit Score: 396.26 E-value: 2.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQSD 86
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 87 MKHWPFEVFA-ENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQGTSE-----RNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDLPAeeekpRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 241 FVQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSS-STQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAK 319
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 266308 320 ALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAA 378
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
7-379 |
1.21e-122 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar proteins; Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. Members in this subfamily belong to the heat shock protein 70 (Hsp70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, Hsp70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Two genes in the vicinity of the HscC gene code for potential cochaperones: J-domain containing proteins, DjlB/YbeS and DjlC/YbeV. HscC and its co-chaperone partners may play a role in the SOS DNA damage response. HscC does not appear to require a NEF.
Pssm-ID: 466833 [Multi-domain] Cd Length: 343 Bit Score: 367.34 E-value: 1.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTE-SERLIGDAAKNQVAMNPNNTIFDAKRLIGrrfDDATVqs 85
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEdGSILVGRAAKERLVTHPDRTAASFKRFMG---TDKQY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 dmkhwpfevfaengkpRIRveykgeRKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd10235 76 ----------------RLG------NHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQGtSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQef 245
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKRE-DETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLK-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 246 qrKHKKD-LGQNKRALRRLRTACERAKRTLSSstQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDA 324
Cdd:cd10235 211 --KHRLDfTSLSPSELAALRKRAEQAKRQLSS--QDSAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 266308 325 KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAI 379
Cdd:cd10235 287 GLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
7-380 |
7.75e-122 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and similar proteins; The subgroup includes two Saccharomyces cerevisiae heat shock protein homologs, Sse1 and Sse2. They may have calcium-dependent calmodulin-binding activities. Both Sse1 and Sse2 belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466944 [Multi-domain] Cd Length: 385 Bit Score: 366.70 E-value: 7.75e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQSD 86
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 87 MKHWPFEVFAENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIAG 166
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 167 LNVLRIINEPTAAAIAYGLDK-----QGTSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHF 241
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKtdlpePEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 242 VQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKAL 321
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 266308 322 RDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
7-378 |
6.31e-116 |
|
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, 170 kDa glucose-regulated protein/GRP170; HSP12A; 150 kDa oxygen-regulated protein/ORP150; GRP-170; ORP-150) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (also known as BiP, Grp78 or HspA5) and may also act as a HSPA5-independent chaperone. S. cerevisiae Lhs1p, does not have a detectable endogenous ATPase activity like canonical HSP70s, but functions as a NEF for Kar2p; it's interaction with Kar2p is stimulated by nucleotide-binding. In addition, Lhs1p has a nucleotide-independent holdase activity that prevents heat-induced aggregation of proteins in vitro. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466828 [Multi-domain] Cd Length: 353 Bit Score: 350.26 E-value: 6.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGK-VEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGrrfddatvqs 85
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 dmkhwpfevfaengkprirveykgerksFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQGTSE--RNVLIFDLGGGTFDVSVLTI------EDGI------FEVKATAGDTHLGGE 231
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRRFENNepQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 232 DFDNRLVNHFVQEFQRKHKKDLG--QNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDL 309
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKDKDvrTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 266308 310 FRGTMEPVAKALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNKSINPDEAVAYGAAVQAA 378
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
6-522 |
1.69e-107 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 336.83 E-value: 1.69e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDaaknqvamnpNNTIFDAKRLIGRRFDDATVQS 85
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTLKEILNTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 86 DMKHWPFEVFAENGKpriRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:PRK01433 91 ALFSLVKDYLDVNSS---ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQGTSerNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 245
Cdd:PRK01433 168 GFEVLRLIAEPTAAAYAYGLNKNQKG--CYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNKF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 246 qrkhkkDLGQNKRALRrlrtACERAKRTLSSstQASIEIDSLfegvdfytSVTRARFEELNGDLFRGTMEPVAKALRDAK 325
Cdd:PRK01433 246 ------DLPNSIDTLQ----LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQECLEQAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 326 MDkgQIHDIVLVGGSTRIPKVQRLLQDFFNGKELNkSINPDEAVAYGAAVQAAILhgdkSEAVQDLLLLDVTPLSLGIET 405
Cdd:PRK01433 306 NP--NIDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENL----IAPHTNSLLIDVVPLSLGMEL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 406 AGGVMTTLIKRNTTIPTKQTQIFTTYADNQPGVLIQVFEGERAMTRDNNSLGKFELSAIPPAPRGVPQVEVTFDIDANGI 485
Cdd:PRK01433 379 YGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGI 458
|
490 500 510
....*....|....*....|....*....|....*..
gi 266308 486 LNVTALEKSTGKENRITITNDKGrLSKEDIERMVNDA 522
Cdd:PRK01433 459 LSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENA 494
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
7-379 |
7.48e-101 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; HSPA4, also called HSP70RY, , HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466843 [Multi-domain] Cd Length: 381 Bit Score: 312.64 E-value: 7.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQSD 86
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 87 MKHWPFEVFA-ENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd11737 83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQG-----TSERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQDlpapeEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 241 FVQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSS-STQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAK 319
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 320 ALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAI 379
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
5-380 |
3.96e-100 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex subunit Ssz1 and similar proteins; Ssz1, also called DnaK-related protein Ssz1, heat shock protein 70 homolog Ssz1, or pleiotropic drug resistance protein 13 (PDR13), is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones Ssb1/Ssb2 that bind to the nascent polypeptide chain. Ssz1 is required for Zuo1 to function efficiently as a J-protein for Ssb1/Ssb2. It is also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466830 [Multi-domain] Cd Length: 349 Bit Score: 309.29 E-value: 3.96e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 5 PAVGIDLGTTYSCVG-VFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRrfddatv 83
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGT------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 84 qsdmkhwpfevfaengkprirveykgerKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGA 163
Cdd:cd10232 74 ----------------------------TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 164 IAGLNVLRIINEPTAAAIAYGLDKQGTS----ERNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGdtikDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 240 HFVQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAK 319
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 266308 320 ALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFNG---KELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10232 286 AIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEstiIRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
7-380 |
2.06e-96 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466844 [Multi-domain] Cd Length: 383 Bit Score: 301.07 E-value: 2.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQSD 86
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 87 MKHWPFEVFA-ENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd11738 83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQG--TSE---RNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQDlpALEekpRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 241 FVQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSS-STQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAK 319
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 266308 320 ALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
7-378 |
4.16e-94 |
|
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar proteins; HSPH1, also called heat shock protein 105 kDa, antigen NY-CO-25, heat shock 110 kDa protein, acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. It prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. It inhibits HSPA8/HSC70 ATPase and chaperone activities. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466845 [Multi-domain] Cd Length: 380 Bit Score: 294.85 E-value: 4.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESERLIGDAAKNQVAMNPNNTIFDAKRLIGRRFDDATVQSD 86
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 87 MKHWPFE-VFAENGKPRIRVEYKGERKSFYPEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIA 165
Cdd:cd11739 83 KENLSYDlVPLKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 GLNVLRIINEPTAAAIAYGLDKQ---GTSE--RNVLIFDLGGGTFDVSVLTIEDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQdlpAPDEkpRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 241 FVQEFQRKHKKDLGQNKRALRRLRTACERAKRTLSS-STQASIEIDSLFEGVDFYTSVTRARFEELNGDLFRGTMEPVAK 319
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 266308 320 ALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAVAYGAAVQAA 378
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
118-375 |
6.05e-61 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 206.19 E-value: 6.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 118 EVSSMVLTKMRETAEAYLG-------GTVTDAVVTVPAYFNDSQRQATKDAGAIAGL----NVLRIINEPTAAAIAYGLD 186
Cdd:cd10170 46 EVVADFLRALLEHAKAELGdriweleKAPIEVVITVPAGWSDAAREALREAARAAGFgsdsDNVRLVSEPEAAALYALED 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 187 KQGTSE----RNVLIFDLGGGTFDVSVLTIEDGIFEVK---ATAGDTHLGGEDFDNRLVNHFVQEFQRKHKKDLGQNKRA 259
Cdd:cd10170 126 KGDLLPlkpgDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 260 LRRLRTACERAKRTLSSSTQASIEIDSLFEGVD---FYTSVTRARFEELNGDLFRGTMEPVAKALRDA--KMDKGQIHDI 334
Cdd:cd10170 206 LAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQleAKSGTPPDAV 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 266308 335 VLVGGSTRIPKVQRLLQDFFNGKELN---KSINPDEAVAYGAAV 375
Cdd:cd10170 286 VLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
7-354 |
1.72e-33 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.
Pssm-ID: 466829 [Multi-domain] Cd Length: 409 Bit Score: 132.78 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESE------RLIGDAAKNQVAMNPNNTIF--DAKRLIG-RR 77
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLGsSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 78 FDDATVqsdmkhwpfevfaengkprirveyKGERKSFypEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQA 157
Cdd:cd10231 81 FDETTI------------------------FGRRYPF--EDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 158 T-------KDAGAIAGLNVLRIINEPTAAAIAYglDKQGTSERNVLIFDLGGGTFDVSVL----TIEDGIFEVKATAGDt 226
Cdd:cd10231 135 DaqaesrlRDAARRAGFRNVEFQYEPIAAALDY--EQRLDREELVLVVDFGGGTSDFSVLrlgpNRTDRRADILATSGV- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 227 HLGGEDFDNRLVNHFV-QEFQRKH------------------------------------KKDL---GQNKRALRRLRT- 265
Cdd:cd10231 212 GIGGDDFDRELALKKVmPHLGRGStyvsgdkglpvpawlyadlsnwhaisllytkktlrlLLDLrrdAADPEKIERLLSl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 266 -----------ACERAKRTLSSSTQASIEIDslFEGVDFYTSVTRARFEELNGDLFRGTMEPVAKALRDAKMDKGQIHDI 334
Cdd:cd10231 292 vedqlghrlfrAVEQAKIALSSADEATLSFD--FIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420
....*....|....*....|
gi 266308 335 VLVGGSTRIPKVQRLLQDFF 354
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLF 389
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
7-374 |
2.13e-22 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 99.27 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVG-VFQH--GKVEIIANDQG------NRTTPSYVAFTESERLIG---DAAKNQVAMNPNNtifDAKRLI 74
Cdd:cd10229 3 VAIDFGTTYSGYAySFITdpGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDE---EHQWLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 75 GRRFDDATVQSDMKHWPFEVFAENGKprirveykgerkSFYPEEVSSMVLTKMRETAEAYL----GGTVTDA----VVTV 146
Cdd:cd10229 80 FFKFKMMLLSEKELTRDTKVKAVNGK------------SMPALEVFAEALRYLKDHALKELrdrsGSSLDEDdirwVLTV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 147 PAYFNDSQ----RQATKDAGAIAGLN--VLRIINEPTAAAIAY------GLDKQGTSERNVLIFDLGGGTFDVSVLTI-E 213
Cdd:cd10229 148 PAIWSDAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCqkllaeGEEKELKPGDKYLVVDCGGGTVDITVHEVlE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 214 DGIFE--VKATAGdtHLGGEDFDNRLVN--------HFVQEFQRKHkkdlgqnKRALRRLRTACERAKRTlssstqASIE 283
Cdd:cd10229 228 DGKLEelLKASGG--PWGSTSVDEEFEElleeifgdDFMEAFKQKY-------PSDYLDLLQAFERKKRS------FKLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 284 IdslfegvdfytsvTRARFEELNGDLFRGTMEPVAKALRDAKMDKgqIHDIVLVGGSTRIPKVQRLLQDFFNGKelNKSI 363
Cdd:cd10229 293 L-------------SPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAFSTK--VKII 355
|
410
....*....|....
gi 266308 364 ---NPDEAVAYGAA 374
Cdd:cd10229 356 ippEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
7-375 |
1.16e-13 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 72.12 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVgvFQHGKvEIIANDqgnrttPSYVAF-TESERLI--GDaaknqvamnpnntifDAKRLIGRRFDDATV 83
Cdd:cd10225 2 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 84 qsdmkHWPFE--VFAEngkprirveykgerksfypEEVSSMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDA 161
Cdd:cd10225 58 -----IRPLRdgVIAD-------------------FEATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 162 GAIAGLNVLRIINEPTAAAIAYGLD---KQGtsernVLIFDLGGGTFDVSVLTIeDGIFEVKAtagdTHLGGEDFDNRLV 238
Cdd:cd10225 114 AEHAGAREVYLIEEPMAAAIGAGLPieePRG-----SMVVDIGGGTTEIAVISL-GGIVTSRS----VRVAGDEMDEAII 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 239 NHfvqeFQRKHKKDLGqnkralrrLRTAcERAKRTLSSstqASIEIDSL---FEGVDFYTSVTRARfeELNGDLFRGTME 315
Cdd:cd10225 184 NY----VRRKYNLLIG--------ERTA-ERIKIEIGS---AYPLDEELsmeVRGRDLVTGLPRTI--EITSEEVREALE 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 266308 316 P--------VAKALRDAK-------MDKGqihdIVLVGGSTRIPKVQRLLQdffngKELNKSI----NPDEAVAYGAAV 375
Cdd:cd10225 246 EpvnaiveaVRSTLERTPpelaadiVDRG----IVLTGGGALLRGLDELLR-----EETGLPVhvadDPLTCVAKGAGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
142-374 |
5.12e-11 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 64.38 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 142 AVVTVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLD---KQGTsernvLIFDLGGGTFDVSVLTIeDGIfe 218
Cdd:PRK13930 103 IVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPvtePVGN-----MVVDIGGGTTEVAVISL-GGI-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 219 vkATAGDTHLGGEDFDNRLVNHfvqeFQRKHKKDLGQnkralrrlRTAcERAKRTLSSSTQA----SIEIdslfEGVDFY 294
Cdd:PRK13930 175 --VYSESIRVAGDEMDEAIVQY----VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLdeeeSMEV----RGRDLV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 295 TSvtRARFEELNGDLFRGTMEP--------VAKALRDAK-------MDKGqihdIVLVGGSTRIPKVQRLLQDFFnGKEL 359
Cdd:PRK13930 236 TG--LPKTIEISSEEVREALAEplqqiveaVKSVLEKTPpelaadiIDRG----IVLTGGGALLRGLDKLLSEET-GLPV 308
|
250
....*....|....*
gi 266308 360 NKSINPDEAVAYGAA 374
Cdd:PRK13930 309 HIAEDPLTCVARGTG 323
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
143-374 |
3.28e-10 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 62.02 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 143 VVTVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDKqgTSERNVLIFDLGGGTFDVSVLTIeDGIfeVKAT 222
Cdd:COG1077 103 VICVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPI--EEPTGNMVVDIGGGTTEVAVISL-GGI--VVSR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 223 AgdTHLGGEDFDNRLVNHfvqeFQRKHKKDLGQnkralrrlRTAcERAKRTLSS----STQASIEIdslfEGVDFYTSVT 298
Cdd:COG1077 178 S--IRVAGDELDEAIIQY----VRKKYNLLIGE--------RTA-EEIKIEIGSayplEEELTMEV----RGRDLVTGLP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 299 RARfeELNGDLFRGTMEP--------VAKALRDAK-------MDKGqihdIVLVGGSTRIPKVQRLLQDFFNgkeLNKSI 363
Cdd:COG1077 239 KTI--TITSEEIREALEEplnaiveaIKSVLEKTPpelaadiVDRG----IVLTGGGALLRGLDKLLSEETG---LPVHV 309
|
250
....*....|...
gi 266308 364 --NPDEAVAYGAA 374
Cdd:COG1077 310 aeDPLTCVARGTG 322
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
142-373 |
2.98e-08 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 56.02 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 142 AVVTVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLD---KQGTsernvLIFDLGGGTFDVSVLTIeDGIfe 218
Cdd:pfam06723 96 VVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPveePTGN-----MVVDIGGGTTEVAVISL-GGI-- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 219 vkATAGDTHLGGEDFDNRLVNHFvqefQRKHKKDLGQnkralrrlRTAcERAKrtlssstqasIEIDSLFEGVDFYTSVT 298
Cdd:pfam06723 168 --VTSKSVRVAGDEFDEAIIKYI----RKKYNLLIGE--------RTA-ERIK----------IEIGSAYPTEEEEKMEI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 299 RAR-----------------FEELNgDLFRGTMEPVAKALRDAK-------MDKGqihdIVLVGGSTRIPKVQRLLQDFF 354
Cdd:pfam06723 223 RGRdlvtglpktieisseevREALK-EPVSAIVEAVKEVLEKTPpelaadiVDRG----IVLTGGGALLRGLDKLLSDET 297
|
250
....*....|....*....
gi 266308 355 nGKELNKSINPDEAVAYGA 373
Cdd:pfam06723 298 -GLPVHIAEDPLTCVALGT 315
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
116-355 |
8.17e-08 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 54.22 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 116 PEEVSsMVLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKdagaiAGLNVLRIINEPTAAAiaYGLDKQGTSERNV 195
Cdd:cd24004 45 ISKVA-ESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAA--NLLIPYDMRDLNI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 196 LIFDLGGGTFDVSVltIEDGifEVKATaGDTHLGGEDFDNRLVNHFVQEFQrkhkkdlgqnkralrrlrtACERAKRTLS 275
Cdd:cd24004 117 ALVDIGAGTTDIAL--IRNG--GIEAY-RMVPLGGDDFTKAIAEGFLISFE-------------------EAEKIKRTYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 276 SST--QASIEIDSLFEGVDFYtSVTRARFEELngdlfrgtMEPVAKALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDF 353
Cdd:cd24004 173 IFLliEAKDQLGFTINKKEVY-DIIKPVLEEL--------ASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEK 243
|
..
gi 266308 354 FN 355
Cdd:cd24004 244 LG 245
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
7-357 |
1.67e-07 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 53.86 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYS-----------CVGVFQHGKveiiANDQG--NRTTPSYVAFTESERL--IGDAAKNQVA-MNPNNT---- 66
Cdd:cd11735 3 VAIDFGTTSSgyaysftkepeCIHVMRRWE----GGDPGvsNQKTPTTILLTPERKFhsFGYAARDFYHdLDPNESkqwl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 67 IFDAKRLIGRRFDDATVQSDMKhwpfevfAENGKPRIRVEYKGERKSFYPEEVssmvLTKMRETAEAYLGGTVTDAVVTV 146
Cdd:cd11735 79 YFEKFKMKLHTTGNLTMETDLT-------AANGKKVKALEIFAYALQFFKEQA----LKELSDQAGSEFDNSDVRWVITV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 147 PAYFNDSQRQATKDAGAIAGLNV------LRIINEPTAAAIAYGLDKQGTSERNVLIfDLGGGTFDVSVLTI---EDGIF 217
Cdd:cd11735 148 PAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIYCRKLRLHQMDRYVVV-DCGGGTVDLTVHQIrlpEGHLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 218 EV-KATAGDTHLGGED--FDNRLVNHFVQEFQRKHKKdlgQNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGVDFY 294
Cdd:cd11735 227 ELyKASGGPYGSLGVDyeFEKLLCKIFGEDFIDQFKI---KRPAAWVDLMIAFESRKRAAAPDRTNPLNITLPFSFIDYY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 295 T-----SVTRARFE--------------ELNGD----LFRGTMEPVAKALRD--AKMDKGQIHDIVLVGGSTRIPKVQRL 349
Cdd:cd11735 304 KkfrghSVEHALRKsnvdfvkwssqgmlRMSPDamnaLFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAESPLLQQA 383
|
....*...
gi 266308 350 LQDFFNGK 357
Cdd:cd11735 384 VQNAFGDQ 391
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
123-228 |
2.40e-07 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 52.27 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 123 VLTKMRETAEAYLGGTVTDAVVTVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLdkqgtseRNVLIFDLGG 202
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI-------RDGAVVDIGG 120
|
90 100 110
....*....|....*....|....*....|
gi 266308 203 GTFDVSVltIEDGifEVKATA----GDTHL 228
Cdd:cd24047 121 GTTGIAV--LKDG--KVVYTAdeptGGTHL 146
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
123-228 |
5.11e-07 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 51.37 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 123 VLTKMRETAEAYLGGTVTDAVVTVPAyfndsqrqAT--KDAGAI------AGLNVLRIINEPTAAAIAYGLDkqgtserN 194
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGID-------N 136
|
90 100 110
....*....|....*....|....*....|....*...
gi 266308 195 VLIFDLGGGTFDVSVLtiEDGifEVKATA----GDTHL 228
Cdd:PRK15080 137 GAVVDIGGGTTGISIL--KDG--KVVYSAdeptGGTHM 170
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
288-391 |
5.73e-07 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 52.53 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 288 FEGVDFYTsvTRArfeelngDLFRGTMEPVAKALRDAkMD-----KGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKS 362
Cdd:COG1070 358 FFGLTLSH--TRA-------HLARAVLEGVAFALRDG-LEaleeaGVKIDRIRATGGGARSPLWRQILADVL-GRPVEVP 426
|
90 100 110
....*....|....*....|....*....|..
gi 266308 363 iNPDEAVAYGAAVQAAI---LHGDKSEAVQDL 391
Cdd:COG1070 427 -EAEEGGALGAALLAAVglgLYDDLEEAAAAM 457
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
7-354 |
7.97e-07 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 51.51 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEII-------ANDQG--NRTTPSYVAFTESERL--IGDAAKNQVA-MNPNNT----IFDA 70
Cdd:cd11736 3 VAIDFGTTSSGYAFSFSSDPEAIhmmrkweGGDPGvaNQKTPTSLLLTPDGAFhsFGYTARDYYHdLDPEEArdwlYFEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 71 KRLIGRRFDDATVQSDMKhwpfevfAENGKPRIRVEYKGERKSFYPEEVssmvLTKMRETAEAYLGGTVTDAVVTVPAYF 150
Cdd:cd11736 83 FKMKIHSTSDLTMETELE-------AVNGKKVQALEVFAHALRFFKEHA----LQELKDQSPSLPEKDAVRWVLTVPAIW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 151 NDSQRQATKDAGAIAGL------NVLRIINEPTAAAI-AYGLDKqgtsernVLIFDLGGGTFDVSVLTIED--GIFE--V 219
Cdd:cd11736 152 KQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR-------YIVADCGGGTVDLTVHQIEQpqGTLKelY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 220 KATAGDTHLGGED--FDNRLVNHFVQEFQRKHKKdlgQNKRALRRLRTACERAKRT--LSSSTQASIEidslfegvdfyt 295
Cdd:cd11736 225 KASGGPYGAVGVDlaFEKLLCQIFGEDFIATFKA---KRPAAWVDLTIAFEARKRTaaLRMSSEAMNE------------ 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 266308 296 svtrarfeelngdLFRGTMEPVAKALrDAKMDKGQIHDI---VLVGGSTRIPKVQRLLQDFF 354
Cdd:cd11736 290 -------------LFQPTISQIIQHI-DDLMKKPEVKGIkflFLVGGFAESPMLQRAVQAAF 337
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
143-250 |
3.20e-06 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 49.52 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 143 VVTVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDKQGTSERnvLIFDLGGGTFDVSVLTIEDGIfevkaT 222
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGN--MVVDIGGGTTDIAVLSLGGIV-----T 171
|
90 100
....*....|....*....|....*...
gi 266308 223 AGDTHLGGEDFDNRLVNHfvqeFQRKHK 250
Cdd:PRK13928 172 SSSIKVAGDKFDEAIIRY----IRKKYK 195
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
7-210 |
3.36e-06 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 49.86 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTESErLIGDAAKNQVAMNPNNTIFDA--KRLI-GRRFDDATV 83
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTRE-AVSEWLYRHLDVPAYDDERQAllRRAIrYNREEDIDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 84 QSD--------MKH---WPFEVFaengkprirveYKGERKSFY------PEEVS-------SMVLtKMRETAEAYLGGTV 139
Cdd:PRK11678 82 TAQsvffglaaLAQyleDPEEVY-----------FVKSPKSFLgasglkPQQVAlfedlvcAMML-HIKQQAEAQLQAAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 140 TDAVVTVPAYFN-----DSQRQAT---KDAGAIAGLNVLRIINEPTAAaiayGLDKQGT--SERNVLIFDLGGGTFDVSV 209
Cdd:PRK11678 150 TQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDFEATltEEKRVLVVDIGGGTTDCSM 225
|
.
gi 266308 210 L 210
Cdd:PRK11678 226 L 226
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
165-355 |
3.47e-06 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 49.75 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYgLDKqgtSER--NVLIFDLGGGTFDVSVltIEDGIfeVKATAGDThLGGedfdnrlvNHFV 242
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTE---DEKelGVALVDIGGGTTDIAV--FKDGA--LRHTAVIP-VGG--------DHIT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 243 qefqrkhkKDLgqnKRALR-RLRTAcERAKRTLSSSTQASIEIDSLFE----GVDFYTSVTR--------ARFEELngdl 309
Cdd:COG0849 237 --------NDI---AIGLRtPLEEA-ERLKIKYGSALASLADEDETIEvpgiGGRPPREISRkelaeiieARVEEI---- 300
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 266308 310 frgtMEPVAKALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFN 355
Cdd:COG0849 301 ----FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
7-255 |
5.47e-06 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 48.29 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCVgVFQHGKVEIIandqgnrttPSYVAFTESERLIGDAAKNQVAMNPNNTIFdakrLIGrrfDDAtvqsd 86
Cdd:cd10227 1 IGIDIGNGNTKV-VTGGGKEFKF---------PSAVAEARESSLDDGLLEDDIIVEYNGKRY----LVG---ELA----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 87 mkhwpfevFAENGKPRIRVEYKGERKSFYPeevssMVLTKMRETAEAYlgGTVTDAVVTVP-AYFNDSQRQATKDAGAIA 165
Cdd:cd10227 59 --------LREGGGGRSTGDDKKKSEDALL-----LLLAALALLGDDE--EVDVNLVVGLPiSEYKEEKKELKKKLLKGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 166 G------------LNVLRIINEPTAAAIAYGLDKQGTSERNVLIFDLGGGTfdVSVLTIEDGIFEVKatAGDTHLGGEDF 233
Cdd:cd10227 124 HeftfngkerritINDVKVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENGKPIEE--SSDTLPGGEEA 199
|
250 260
....*....|....*....|..
gi 266308 234 DNRLVNHFVQEFQRKHKKDLGQ 255
Cdd:cd10227 200 LEKYADDILNELLKKLGDELDS 221
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
7-239 |
2.75e-05 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 46.44 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 7 VGIDLGTTYSCvgvfqhgkveiIANDQGNR-TTPSYVAFT---------ESERLIGDAA-KNQVAMNpnntifdakrlig 75
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGYPkdiiarkllGKEVLFGDEAlENRLALD------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 76 rrfddatvqsdmKHWPFEvfaeNGkprirVEYKGERKSFypeEVSSMVLTKMRETAEAYLGGTVTdAVVTVPAYFNDSQR 155
Cdd:cd24009 60 ------------LRRPLE----DG-----VIKEGDDRDL---EAARELLQHLIELALPGPDDEIY-AVIGVPARASAENK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 156 QATKDAGAIAGLNVLrIINEPTAaaIAYGLDKQgtseRNVLIFDLGGGTFDV-----SVLTIEDGIFEVKAtagdthlgG 230
Cdd:cd24009 115 QALLEIARELVDGVM-VVSEPFA--VAYGLDRL----DNSLIVDIGAGTTDLcrmkgTIPTEEDQITLPKA--------G 179
|
....*....
gi 266308 231 EDFDNRLVN 239
Cdd:cd24009 180 DYIDEELVD 188
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
307-379 |
5.05e-05 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 46.38 E-value: 5.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 266308 307 GDLFRGTMEPVAKALRDA----KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPDEAvAYGAAVQAAI 379
Cdd:cd07808 365 AHLARAVLEGVAFSLRDSlevlKELGIKVKEIRLIGGGAKSPLWRQILADVL-GVPVVVPAEEEGS-AYGAALLAAV 439
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
296-382 |
8.29e-05 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 45.62 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 296 SVTRARFEELN-GDLFRGTMEPVAKALRDAkMDK-----GQIHDIVLVGGSTRIPKVQRLLQDFFNgkelnKSI---NPD 366
Cdd:cd07809 354 SLVGLTLSNFTrANLARAALEGATFGLRYG-LDIlrelgVEIDEIRLIGGGSKSPVWRQILADVFG-----VPVvvpETG 427
|
90
....*....|....*.
gi 266308 367 EAVAYGAAVQAAILHG 382
Cdd:cd07809 428 EGGALGAALQAAWGAG 443
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
143-339 |
4.15e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 42.77 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 143 VVTVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDkqgTSE-RNVLIFDLGGGTFDVSVLTIeDGIfevkA 221
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLP---VTEpTGSMVVDIGGGTTEVAVISL-GGI----V 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 222 TAGDTHLGGEDFDNRLVNHfvqeFQRKHKKDLGQnkralrrlRTAcERAKrtlssstqasIEIDSLFEGVDFYTSVTRAR 301
Cdd:PRK13927 172 YSKSVRVGGDKFDEAIINY----VRRNYNLLIGE--------RTA-ERIK----------IEIGSAYPGDEVLEMEVRGR 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 266308 302 feelngDLFRG-------TMEPVAKALRDA--------K--------------MDKGqihdIVLVGG 339
Cdd:PRK13927 229 ------DLVTGlpktitiSSNEIREALQEPlsaiveavKvaleqtppelaadiVDRG----IVLTGG 285
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
165-381 |
5.81e-04 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 42.52 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 165 AGLNVLRIINEPTAAAIAYgLDkqgTSERN--VLIFDLGGGTFDVSVLtiEDGIFEvkatagDTH---LGGEDFDNRLVn 239
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LT---EDEKElgVALIDIGGGTTDIAVF--KNGSLR------YTAvipVGGNHITNDIA- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 240 hfvqefqrkhkkdlgqnkRALRRLRTACERAKRTLSSSTQASIEIDSLFE----GVDFYTSVTR--------ARFEELng 307
Cdd:cd24048 239 ------------------IGLNTPFEEAERLKIKYGSALSEEADEDEIIEipgvGGREPREVSRrelaeiieARVEEI-- 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 266308 308 dlfrgtMEPVAKALRDAKMDKGQIHDIVLVGGSTRIPKVQRLLQDFFN-----GKELNKSINPDEAVAYGAAVQAAILH 381
Cdd:cd24048 299 ------LELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvriGRPKNIGGLPEEVNDPAYATAVGLLL 371
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
135-204 |
1.24e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 39.37 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 135 LGGTVTDAVV----TVPAYFNDSQRQAT-----------KDAGAIAGLNVLRIINEPTAAAIAYGLDkqgTSERNVLIFD 199
Cdd:cd00012 5 LGSTSTKVAVpiviTVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLT---LGPEGLLVVD 81
|
....*
gi 266308 200 LGGGT 204
Cdd:cd00012 82 LGGGT 86
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
307-379 |
1.93e-03 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 41.03 E-value: 1.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 266308 307 GDLFRGTMEPVAKALRD--AKMDK--GQIHDIVLVGGSTRIPKVQRLLQDFFnGKELNKSINPdEAVAYGAAVQAAI 379
Cdd:cd07773 366 ADLLRAILEGLAFELRLnlEALEKagIPIDEIRAVGGGARSPLWLQLKADIL-GRPIEVPEVP-EATALGAALLAGV 440
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
118-245 |
2.03e-03 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 40.66 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 118 EVSSMVLTKMRETAEAYLGGTV--TDAVVTVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIayGLDKQGTSERNV 195
Cdd:PRK13929 75 DMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAI--GADLPVDEPVAN 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 266308 196 LIFDLGGGTFDVSVLTiedgiFEVKATAGDTHLGGEDFDNRLVNHFVQEF 245
Cdd:PRK13929 153 VVVDIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSFVRKKY 197
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
299-379 |
2.58e-03 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 40.67 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266308 299 RARFEELN---GDLFRGTMEPVAKALRDA-----KMDKGQIHDIVLVGGSTRIPKVQRLLQDFFnGKELnkSINPDEAVA 370
Cdd:cd07783 342 RGFLLPRPhdrAEFLRALLEGIAFIERLGyerleELGAPPVEEVRTAGGGARNDLWNQIRADVL-GVPV--VIAEEEEAA 418
|
....*....
gi 266308 371 YGAAVQAAI 379
Cdd:cd07783 419 LGAALLAAA 427
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
331-374 |
6.22e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.45 E-value: 6.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 266308 331 IHDIVLVGGSTRIPKVQRLLQDFF---NGKELNKSINPDEAVAYGAA 374
Cdd:cd00012 89 SANVVLVGGGARNNGLAKRLKELLlfrGGLKVVKAVDPDEAVALGAA 135
|
|
| |
