|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
2-634 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1156.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 2 SAKAPAVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDD 81
Cdd:PTZ00009 1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 82 PTVQSDMKHWPFTVVSDG-GKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATK 160
Cdd:PTZ00009 81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 161 DAGIIAGINVLRIINEPTAAAIAYGLDKKsaGLGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRM 240
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKK--GDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 241 VAHFLDEFKRKNK-KDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEP 319
Cdd:PTZ00009 239 VEFCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 320 VEKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAILSGDKSHNVQDLLLLDV 399
Cdd:PTZ00009 319 VEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 400 APLSLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEV 479
Cdd:PTZ00009 399 TPLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 480 TFDIDANGILNVTAADKSTGKENKITITNDKGRLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHVKQTAEDE 559
Cdd:PTZ00009 479 TFDIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 560 KLKGKLSEKEKSQILDKCKEVIDWLDKNQMAEKDEFEHKQKELEKVCNPIITKLYQ--------------------GGAP 619
Cdd:PTZ00009 559 KVKGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQaagggmpggmpggmpggmpgGAGP 638
|
650
....*....|....*
gi 148229965 620 NPGTAAGGPTIEEVD 634
Cdd:PTZ00009 639 AGAGASSGPTVEEVD 653
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
7-615 |
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: 921.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVV-SDGGKPKVKVEYKGEakTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:pfam00012 81 DIKHLPYKVVkLPNGDAGVEVRYLGE--TFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSaglGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKTD---KERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISGNKRAVRRLRTACERAKRTLSS-STQASLEIDSLYE-GTDFYTSITRARFEELCADLFRGTLEPVEKA 323
Cdd:pfam00012 236 EEFKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 324 LRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDKshNVQDLLLLDVAPLS 403
Cdd:pfam00012 316 LKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGTF--DVKDFLLLDVTPLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 404 LGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFDI 483
Cdd:pfam00012 393 LGIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 484 DANGILNVTAADKSTGKENKITITNDKGrLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHVKQTAEDEklKG 563
Cdd:pfam00012 473 DANGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE--GD 549
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 148229965 564 KLSEKEKSQIldkcKEVIDWLDKN-QMAEKDEFEHKQKELEKVCNPIITKLYQ 615
Cdd:pfam00012 550 KVPEAEKSKV----ESAIEWLKDElEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
7-383 |
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: 876.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVVSDGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKsaGLGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKK--GKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKALRD 326
Cdd:cd10233 239 EFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 148229965 327 AKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd10233 319 AKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
7-633 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 864.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDT-ERLIGDAARNQVALNPTNTIFDAKRLIGRRfdDPTVQ 85
Cdd:PRK00290 4 IIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 86 SDMKHWPFTVVS-DGGKPKVKVEykgeAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGI 164
Cdd:PRK00290 82 KDIKLVPYKIVKaDNGDAWVEID----GKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 165 IAGINVLRIINEPTAAAIAYGLDKKsaglGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHF 244
Cdd:PRK00290 158 IAGLEVLRIINEPTAAALAYGLDKK----GDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 245 LDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQAslEIDSLYEGTD------FYTSITRARFEELCADLFRGTLE 318
Cdd:PRK00290 234 ADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EINLPFITADasgpkhLEIKLTRAKFEELTEDLVERTIE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 319 PVEKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLLLLD 398
Cdd:PRK00290 312 PCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVLLLD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 399 VAPLSLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIE 478
Cdd:PRK00290 387 VTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 479 VTFDIDANGILNVTAADKSTGKENKITITNDKGrLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHVKQTAED 558
Cdd:PRK00290 467 VTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKE 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148229965 559 ekLKGKLSEKEKSQILDKCKEVIDWLDKNqmaEKDEFEHKQKELEKVCNPIITKLYQGGAPNPGTAAGGPTIEEV 633
Cdd:PRK00290 546 --LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDDV 615
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
7-615 |
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: 792.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDT-ERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDptVQ 85
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 86 SDMKHWPFTVVSDGGKPKVKVEykgeAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKVD----GKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSaglGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSK---KDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTD----FYTSITRARFEELCADLFRGTLEPVE 321
Cdd:TIGR02350 233 DEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 322 KALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLLLLDVAP 401
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 402 LSLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTF 481
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 482 DIDANGILNVTAADKSTGKENKITITNDKGrLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHVKQTAEDekL 561
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--A 544
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 148229965 562 KGKLSEKEKSQILDKCKEVidwldKNQMAEKD--EFEHKQKELEKVCNPIITKLYQ 615
Cdd:TIGR02350 545 GDKLPAEEKEKIEKAVAEL-----KEALKGEDveEIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
7-383 |
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: 729.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVVSDG-GKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:cd24028 81 DIKHWPFKVVEDEdGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSAGlgETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSG--ERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKALR 325
Cdd:cd24028 239 EEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 148229965 326 DAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd24028 319 DAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
6-383 |
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: 729.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 6 PAVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQ 85
Cdd:cd10241 2 TVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 86 SDMKHWPFTVVSDGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:cd10241 82 KDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSaglGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:cd10241 162 AGLNVLRIINEPTAAAIAYGLDKKG---GEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKALR 325
Cdd:cd10241 239 KLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 148229965 326 DAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd10241 319 DAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
8-631 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 681.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDT-ERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDptVQS 86
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE--ISE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVVSDGgKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:CHL00094 83 EAKQVSYKVKTDS-NGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSaglGETnVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:CHL00094 162 GLEVLRIINEPTAASLAYGLDKKN---NET-ILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLE---IDSLYEG-TDFYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:CHL00094 238 EFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVEN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLLLLDVAPL 402
Cdd:CHL00094 318 ALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 403 SLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFD 482
Cdd:CHL00094 393 SLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 483 IDANGILNVTAADKSTGKENKITITNdKGRLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHV-KQTAEdekL 561
Cdd:CHL00094 473 IDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAeKQLKE---L 548
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 562 KGKLSEKEKSQILDKCKEVIDWLDKNQMaekDEFEHKQKELEKVCNPIITKLYQGGAPNPGTAAGGPTIE 631
Cdd:CHL00094 549 KDKISEEKKEKIENLIKKLRQALQNDNY---ESIKSLLEELQKALMEIGKEVYSSTSTTDPASNDDDVID 615
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
8-622 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 675.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDT-ERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDptVQS 86
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD--TEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVVSdGGKPKVKVEYKGeaKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:PRK13411 83 ERSRVPYTCVK-GRDDTVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAglgETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:PRK13411 160 GLEVLRIINEPTAAALAYGLDKQDQ---EQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASleIDSLYEGTD------FYTSITRARFEELCADLFRGTLEPV 320
Cdd:PRK13411 237 NFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTS--INLPFITADetgpkhLEMELTRAKFEELTKDLVEATIEPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 321 EKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLLLLDVA 400
Cdd:PRK13411 315 QQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDLLLLDVT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 401 PLSLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVT 480
Cdd:PRK13411 391 PLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 481 FDIDANGILNVTAADKSTGKENKITITNdKGRLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHVKQTAEDEk 560
Cdd:PRK13411 471 FEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKEN- 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148229965 561 lkGKLSEKEKSQILDKCKEVIDWLDKNQMAEKDEFEHKQKELEKVCNPIITKLYQGGAPNPG 622
Cdd:PRK13411 549 --GELISEELKQRAEQKVEQLEAALTDPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTT 608
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
8-632 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 671.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDT-ERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVV-SDGGKPKVKveykGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:PTZ00400 124 EQKILPYKIVrASNGDAWIE----AQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSaglGETnVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:PTZ00400 200 AGLDVLRIINEPTAAALAFGMDKND---GKT-IAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQAslEIDSLYEGTD------FYTSITRARFEELCADLFRGTLEP 319
Cdd:PTZ00400 276 AEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADqsgpkhLQIKLSRAKLEELTHDLLKKTIEP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 320 VEKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLLLLDV 399
Cdd:PTZ00400 354 CEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDLLLLDV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 400 APLSLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEV 479
Cdd:PTZ00400 429 TPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 480 TFDIDANGILNVTAADKSTGKENKITITNDKGrLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHVKQTAEDe 559
Cdd:PTZ00400 509 TFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD- 586
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148229965 560 kLKGKLSEKEKSQILDKCKEVidwldKNQMAEKD--EFEHKQKELEKVCNPIITKLYQGGAPNpGTAAGGPTIEE 632
Cdd:PTZ00400 587 -LKDKISDADKDELKQKITKL-----RSTLSSEDvdSIKDKTKQLQEASWKISQQAYKQGNSD-NQQSEQSTNSE 654
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
7-522 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 669.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFT-DTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPtvq 85
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 86 sdmkhwpftvvsdggkpkvKVEYKGEAKTffPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:COG0443 78 -------------------ATEVGGKRYS--PEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSAglgETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKGKE---EETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDsLYEGTDFYTSITRARFEELCADLFRGTLEPVEKALR 325
Cdd:COG0443 214 PEFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 326 DAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLlllDVAPLSLG 405
Cdd:COG0443 293 DAGLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGD----VKDL---DVTPLSLG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 406 IETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDA 485
Cdd:COG0443 365 IETLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDA 444
|
490 500 510
....*....|....*....|....*....|....*..
gi 148229965 486 NGILNVTAADKSTGKENKITItndkgrlsKEDIERMV 522
Cdd:COG0443 445 NGILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
8-593 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 659.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFT-DTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDELDPES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 dmKHWPFTVVSDGgKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:PRK13410 85 --KRVPYTIRRNE-QGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSaglgETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:PRK13410 162 GLEVERILNEPTAAALAYGLDRSS----SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFKRKNKKDISGNKRAVRRLRTACERAKRTLS--SSTQASLE-IDSLYEG-TDFYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:PRK13410 238 QFLEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpKHIETRLDRKQFESLCGDLLDRLLRPVKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLLLLDVAPL 402
Cdd:PRK13410 318 ALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 403 SLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFD 482
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 483 IDANGILNVTAADKSTGKENKITITNdKGRLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHVKQTAEDEKLK 562
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAALE 551
|
570 580 590
....*....|....*....|....*....|...
gi 148229965 563 --GKLSEKEKSQILDKCKEVIDWLDKNQMAEKD 593
Cdd:PRK13410 552 fgPYFAERQRRAVESAMRDVQDSLEQDDDRELD 584
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
7-383 |
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: 628.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQhGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVVSDGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAGlGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGAGKSE-KERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKALRD 326
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 148229965 327 AKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd24093 319 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
8-627 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 623.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDT-ERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDptVQS 86
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVVSDGGKpKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:PLN03184 120 ESKQVSYRVVRDENG-NVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSaglGETnVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:PLN03184 199 GLEVLRIINEPTAASLAYGFEKKS---NET-ILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLAS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTD----FYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:PLN03184 275 NFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADgpkhIDTTLTRAKFEELCSDLLDRCKTPVEN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFfNGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLLLLDVAPL 402
Cdd:PLN03184 355 ALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTPL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 403 SLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFD 482
Cdd:PLN03184 430 SLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFD 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 483 IDANGILNVTAADKSTGKENKITITNdKGRLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHV-KQTAEdekL 561
Cdd:PLN03184 510 IDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTeKQLKE---L 585
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148229965 562 KGKLSEKEKSQILDKCKEVIDWLDKNQMAE-KDEFEHKQKELEKvcnpIITKLY-QGGAPNPGTAAGG 627
Cdd:PLN03184 586 GDKVPADVKEKVEAKLKELKDAIASGSTQKmKDAMAALNQEVMQ----IGQSLYnQPGAGGAGPAPGG 649
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
8-629 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 608.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQSD 87
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 88 MKHWPFTVV-SDGGKPKVKveyKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:PTZ00186 110 IKNVPYKIVrAGNGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAGLgetnVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:PTZ00186 187 GLNVIRVVNEPTAAALAYGMDKTKDSL----IAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTD----FYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:PTZ00186 263 EFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAPCKQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDkshnVQDLLLLDVAPL 402
Cdd:PTZ00186 343 CMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVTPL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 403 SLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFD 482
Cdd:PTZ00186 418 SLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFD 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 483 IDANGILNVTAADKSTGKENKITITNDKGrLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTyhvkQTAEDEKLK 562
Cdd:PTZ00186 498 IDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQL----TTAERQLGE 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148229965 563 GK-LSEKEKSQILDKCKEVIDWLDkNQMAEKDEFEHKQKELEKV---CNPiiTKLYQGGAPNPGTAAGGPT 629
Cdd:PTZ00186 573 WKyVSDAEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQKAvmeCGR--TEYQQAAAANSGSSSNSGE 640
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
7-573 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 546.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDptVQS 86
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFT-VVSDGGKPKVKVeyKGEAKTffPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:PRK05183 99 RYPHLPYQfVASENGMPLIRT--AQGLKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSAGLgetnVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDSGQEGV----IAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWIL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISgnkrAVRRLRTACERAKRTLSSSTQASLEIdslyegTDFYTSITRARFEELCADLFRGTLEPVEKALR 325
Cdd:PRK05183 251 EQAGLSPRLDPE----DQRLLLDAARAAKEALSDADSVEVSV------ALWQGEITREQFNALIAPLVKRTLLACRRALR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 326 DAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDKSHNvqDLLLLDVAPLSLG 405
Cdd:PRK05183 321 DAGVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 406 IETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDA 485
Cdd:PRK05183 398 LETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 486 NGILNVTAADKSTGKENKITITNDKGrLSKEDIERMVNDADKYKAEDEVNR----ERVAAKNGLESYTyhvKQTAEDEKL 561
Cdd:PRK05183 478 DGLLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEALQ---AALAADGDL 553
|
570
....*....|..
gi 148229965 562 kgkLSEKEKSQI 573
Cdd:PRK05183 554 ---LSAAERAAI 562
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
8-384 |
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: 536.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDT-ERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFtVVSDGGKPKVKVEykgeAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd10234 82 KQVPYPV-VSAGNGDAWVEIG----GKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKsaglGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDKK----KDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQAslEIDSLYEGTD------FYTSITRARFEELCADLFRGTLEPV 320
Cdd:cd10234 233 EFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLET--EINLPFITADasgpkhLEMKLTRAKFEELTEDLVERTIEPV 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148229965 321 EKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 384
Cdd:cd10234 311 EQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
7-573 |
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: 526.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAF-TDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQ 85
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 86 SDMkhwPFTVVsDGGKPKVKVEYKGEAKTffPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:TIGR01991 81 SIL---PYRFV-DGPGEMVRLRTVQGTVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSaglgETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDKAS----EGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 defkRKNKKDISGNKRAVRRLRTACERAKRTLSssTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKALR 325
Cdd:TIGR01991 231 ----KQLGISADLNPEDQRLLLQAARAAKEALT--DAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 326 DAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDKSHNvqDLLLLDVAPLSLG 405
Cdd:TIGR01991 305 DAGLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 406 IETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDA 485
Cdd:TIGR01991 382 IETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 486 NGILNVTAADKSTGKENKITITNDKGrLSKEDIERMVNDADKYKAEDEVNR----ERVAAKNGLESYTyhvKQTAEDEKL 561
Cdd:TIGR01991 462 DGLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARalaeQKVEAERILEALQ---AALAADGDL 537
|
570
....*....|..
gi 148229965 562 kgkLSEKEKSQI 573
Cdd:TIGR01991 538 ---LSEDERAAI 546
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
8-383 |
5.25e-169 |
|
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: 486.77 E-value: 5.25e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFT-DTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVV-SDGGKPKVKVEykgeAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:cd11733 84 DIKMVPYKIVkASNGDAWVEAH----GKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSAGLgetnVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:cd11733 160 AGLNVLRIINEPTAAALAYGLDKKDDKI----IAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQAslEIDSLYEGTD------FYTSITRARFEELCADLFRGTLEP 319
Cdd:cd11733 236 AEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148229965 320 VEKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd11733 314 CKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
5-385 |
1.41e-152 |
|
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: 444.97 E-value: 1.41e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 5 APAVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFT-DTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPT 83
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 84 VQSDMKHWPFTVV--SDGgkpKVKVEYKGeaKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKD 161
Cdd:cd11734 81 VQRDIKEVPYKIVkhSNG---DAWVEARG--QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 162 AGIIAGINVLRIINEPTAAAIAYGLDKKsaglGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMV 241
Cdd:cd11734 156 AGQIAGLNVLRVINEPTAAALAYGLDKS----GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 242 AHFLDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTD----FYTSITRARFEELCADLFRGTL 317
Cdd:cd11734 232 RHIVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKLTRAQFESLVKPLVDRTV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148229965 318 EPVEKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSG 385
Cdd:cd11734 312 EPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
8-385 |
1.43e-146 |
|
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: 430.61 E-value: 1.43e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQH--GKVEIIANEQGNRTTPSYVAFTDTER-LIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTV 84
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 85 QSDMKHWPFTVVSDG-GKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAG 163
Cdd:cd10237 105 EEEAKRYPFKVVNDNiGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 164 IIAGINVLRIINEPTAAAIAYGLDKKSaglGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAH 243
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKKS---DVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 244 FLDEFKRKNKKDISgNKRAVRRLRTACERAKRTLSS--STQASLEIDSLYEGTD---FYTSITRARFEELCADLFRGTLE 318
Cdd:cd10237 262 LIDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNhnSASLSLPLQISLPSAFkvkFKEEITRDLFETLNEDLFQRVLE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148229965 319 PVEKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSG 385
Cdd:cd10237 341 PIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
6-383 |
2.10e-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: 423.96 E-value: 2.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 6 PAVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQ 85
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 86 SDMKHWPFTVVSDGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSAgLGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDP-TENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKALR 325
Cdd:cd10238 240 SEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 148229965 326 DAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd10238 320 SAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
7-385 |
1.54e-143 |
|
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: 421.24 E-value: 1.54e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLI-GDAARNQVALNPTNTIFDAKRLIGRRFDDptVQ 85
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 86 SDMKHWPFTVV-SDGGKPKVKVEykgeAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGI 164
Cdd:cd10236 82 EELPLLPYRLVgDENELPRFRTG----AGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 165 IAGINVLRIINEPTAAAIAYGLDKKSAGlgetNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHF 244
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQKKEG----TIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 245 LDEfkrkNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSlyEGTDFYTSITRARFEELCADLFRGTLEPVEKAL 324
Cdd:cd10236 234 LKQ----IGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRAL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148229965 325 RDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSG 385
Cdd:cd10236 308 KDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
8-384 |
1.34e-138 |
|
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: 408.12 E-value: 1.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVF-QHGKVEIIANEQGNRTTPSYVAFT-DTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPtvq 85
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 86 sdmkhwpftvvsdggkpkvkveYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:cd24029 78 ----------------------EEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSaglGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFL 245
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEG---KDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELIL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 DEFKRK-NKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKAL 324
Cdd:cd24029 213 EKIGIEtGILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKAL 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 325 RDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 384
Cdd:cd24029 293 KDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
7-384 |
5.81e-137 |
|
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: 405.54 E-value: 5.81e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQS 86
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DMKHWPFTVV-SDGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGII 165
Cdd:cd24095 83 DLKLFPFKVTeGPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYGLDKKSAGLGE-TNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHF 244
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIYKTDLPETDpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 245 LDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKAL 324
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKAL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 325 RDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 384
Cdd:cd24095 323 ADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
8-381 |
7.29e-137 |
|
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: 404.63 E-value: 7.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQSD 87
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 88 MKHWPFTVVS-DGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAGLGET---NVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAH 243
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLESEEkprIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 244 FLDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKA 323
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 148229965 324 LRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAA 381
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
8-381 |
1.58e-128 |
|
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: 383.55 E-value: 1.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQSD 87
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 88 MKHWPFTVVS-DGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKS-AGLGET--NVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAH 243
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDlPAEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 244 FLDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSS-STQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAA 381
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
8-382 |
5.65e-126 |
|
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: 375.43 E-value: 5.65e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAF-TDTERLIGDAARNQVALNPTNTIFDAKRLIGrrfddptvqS 86
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMG---------T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 DmkhwpfTVVSDGGKpkvkveykgeakTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd10235 72 D------KQYRLGNH------------TFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAglgETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHFLD 246
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKRED---ETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 247 EFkRKNKKDISGNKRAvrRLRTACERAKRTLSSSTQAslEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKALRD 326
Cdd:cd10235 211 KH-RLDFTSLSPSELA--ALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRD 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 148229965 327 AKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAI 382
Cdd:cd10235 286 AGLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
8-384 |
4.52e-118 |
|
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: 356.68 E-value: 4.52e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQSD 87
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 88 MKHWPFTVVSDGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIAG 167
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 168 INVLRIINEPTAAAIAYGLDKKSAGLGET---NVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAHF 244
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTDLPEPEEkprIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 245 LDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEKAL 324
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 325 RDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 384
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
8-381 |
1.13e-113 |
|
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: 344.09 E-value: 1.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGK-VEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGrrfddptvqs 86
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 87 dmkhwpftvvsdggkpkvkveykgeaktFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAGLGETNVLIFDLGGGTFDVSVLTIDG------------GIFEVKSTAGDTHLGGE 234
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRRFENNEPQNVLFYDMGASSTSATVVEFSSvkekdkgknktvPQVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 235 DFDNRMVAHFLDEFKRKNKK--DISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADL 312
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148229965 313 FRGTLEPVEKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAA 381
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
7-616 |
6.71e-109 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 340.29 E-value: 6.71e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 7 AVGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDaarnqvalnpTNTIFDAKRLIGRRFDD----P 82
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTLKEilntP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 83 TVQSDMKHWpftVVSDGGKPKVKVEykgeAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDA 162
Cdd:PRK01433 91 ALFSLVKDY---LDVNSSELKLNFA----NKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 163 GIIAGINVLRIINEPTAAAIAYGLDKKSAGLgetnVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVA 242
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNKNQKGC----YLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 243 HFLDEFKRKNKKDISgnkravrrlrTACERAKRTLSSstQASLEIDSLyegtdfytSITRARFEELCADLFRGTLEPVEK 322
Cdd:PRK01433 240 YLCNKFDLPNSIDTL----------QLAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 323 ALRDAKLDKghIREIVLVGGSIRIPKIQKLLQDFFNGRELNkSINPDEAVAYGAAVQAAILSGDKSHNvqdlLLLDVAPL 402
Cdd:PRK01433 300 CLEQAGNPN--IDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLIAPHTNS----LLIDVVPL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 403 SLGIETAGGVMTPLIKRNTTIPSKQTQTFTTYSDNQSSVLVQVYEGERAMTRDNNLLGKFDLTGIPPAPRGVPQIEVTFD 482
Cdd:PRK01433 373 SLGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 483 IDANGILNVTAADKSTGKENKITITNDKGrLSKEDIERMVNDADKYKAEDEVNRERVAAKNGLESYTYHVKQTAedEKLK 562
Cdd:PRK01433 453 IDADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAI--AELT 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 148229965 563 GKLSEKEKSQI---LDKCKEVIDWLDKNQMAEK-DEFEHK-QKELEKVCNPIITKLYQG 616
Cdd:PRK01433 530 TLLSESEISIInslLDNIKEAVHARDIILINNSiKEFKSKiKKSMDTKLNIIINDLLKG 588
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
6-383 |
3.67e-98 |
|
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: 304.28 E-value: 3.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 6 PAVGIDLGTTYSCVG-VFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGrrfddptv 84
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 85 qsdmkhwpftvvsdggkpkvkveykgeAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGI 164
Cdd:cd10232 73 ---------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 165 IAGINVLRIINEPTAAAIAYGL--DKKSAGLGETNVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVA 242
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLraETSGDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 243 HFLDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGR---ELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd10232 286 AIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEStiiRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
8-382 |
2.46e-94 |
|
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: 295.31 E-value: 2.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQSD 87
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 88 MKHWPFTVVS-DGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd11737 83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAGLGET---NVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAH 243
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQDLPAPEEkprNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 244 FLDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSS-STQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAI 382
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
8-381 |
1.55e-92 |
|
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: 290.61 E-value: 1.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQSD 87
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 88 MKHWPFTVVS-DGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd11739 83 KENLSYDLVPlKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAGLGETN---VLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAH 243
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQDLPAPDEKpriVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 244 FLDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSS-STQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAA 381
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
8-384 |
1.53e-91 |
|
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: 288.35 E-value: 1.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTERLIGDAARNQVALNPTNTIFDAKRLIGRRFDDPTVQSD 87
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 88 MKHWPFTVVS-DGGKPKVKVEYKGEAKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIA 166
Cdd:cd11738 83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 167 GINVLRIINEPTAAAIAYGLDKKSAGLGET---NVLIFDLGGGTFDVSVLTIDGGIFEVKSTAGDTHLGGEDFDNRMVAH 243
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQDLPALEEkprNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 244 FLDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSS-STQASLEIDSLYEGTDFYTSITRARFEELCADLFRGTLEPVEK 322
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148229965 323 ALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 384
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
8-378 |
1.92e-60 |
|
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: 204.65 E-value: 1.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVgvfqhgkveiianeqgnrttpsyvAFTDTERligdaarnqvalnptntifdakrligrrfDDPTVQSD 87
Cdd:cd10170 1 VGIDFGTTYSGV------------------------AYALLGP-----------------------------GEPPLVVL 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 88 MKHWPFtvvSDGGKPKV--KVEykgeaktffpeeISSMVLIKMKEVAEAYLGAKVP-------DAVITVPAYFNDSQRQA 158
Cdd:cd10170 28 QLPWPG---GDGGSSKVpsVLE------------VVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 159 TKDAGIIAGI----NVLRIINEPTAAAIAYGLDKKSAGLGETN--VLIFDLGGGTFDVSVLTIDGGIFEVK---STAGDT 229
Cdd:cd10170 93 LREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDLLPLKPGdvVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 230 HLGGEDFDNRMVAHFLDEFKRKNKKDISGNKRAVRRLRTACERAKRTLSSSTQASLEIDSLYEGTD---FYTSITRARFE 306
Cdd:cd10170 173 LLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTE 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148229965 307 ELCADLFRGTLEPVEKALRDA--KLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGRELN---KSINPDEAVAYGAAV 378
Cdd:cd10170 253 EEIRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
8-357 |
7.93e-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: 130.86 E-value: 7.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTE------RLIGDAARNQVALNPTNTIF--DAKRLIGRRF 79
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 80 DDPTVQSDmkhwpftvvsdggkpkvkveykgeaKTFFPEEISSMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQAT 159
Cdd:cd10231 81 FDETTIFG-------------------------RRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 160 -------KDAGIIAGINVLRIINEPTAAAIAYGLDKKSAGLgetnVLIFDLGGGTFDVSVLTIDGGIFE----VKSTAGD 228
Cdd:cd10231 136 aqaesrlRDAARRAGFRNVEFQYEPIAAALDYEQRLDREEL----VLVVDFGGGTSDFSVLRLGPNRTDrradILATSGV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 229 tHLGGEDFDNRMVAH-FLDEFKRKN------------------------------------KKDI---SGNKRAVRRLRT 268
Cdd:cd10231 212 -GIGGDDFDRELALKkVMPHLGRGStyvsgdkglpvpawlyadlsnwhaisllytkktlrlLLDLrrdAADPEKIERLLS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 269 ------------ACERAKRTLSSSTQASLEIDSLYEGTDfyTSITRARFEELCADLFRGTLEPVEKALRDAKLDKGHIRE 336
Cdd:cd10231 291 lvedqlghrlfrAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDR 368
|
410 420
....*....|....*....|.
gi 148229965 337 IVLVGGSIRIPKIQKLLQDFF 357
Cdd:cd10231 369 VFLTGGSSQSPAVRQALASLF 389
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
8-377 |
5.09e-23 |
|
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: 101.20 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVG-VFQH--GKVEIIANEQG------NRTTPSYVAFTDTERL--IGDAARNQVA-LNPTNtifDAKRLI 75
Cdd:cd10229 3 VAIDFGTTYSGYAySFITdpGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFhsFGYEAREKYSdLAEDE---EHQWLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 76 GRRFDDPTVQSDMKHWPFTVVSDGGKpkvkveykgeakTFFPEEISSMVLIKMKEVAEAYLGAKVPDA--------VITV 147
Cdd:cd10229 80 FFKFKMMLLSEKELTRDTKVKAVNGK------------SMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 148 PAYFNDSQ----RQATKDAGIIAGIN--VLRIINEPTAAAIAYGLDKKSAGLGETNV----LIFDLGGGTFDVSVLTI-- 215
Cdd:cd10229 148 PAIWSDAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCQKLLAEGEEKELKPgdkyLVVDCGGGTVDITVHEVle 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 216 DGGIFEV-KSTAGdtHLGGEDFDNRMV--------AHFLDEFKRKnkkdisgNKRAVRRLRTACERAKRTlssstqASLE 286
Cdd:cd10229 228 DGKLEELlKASGG--PWGSTSVDEEFEelleeifgDDFMEAFKQK-------YPSDYLDLLQAFERKKRS------FKLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 287 idslyegtdfytsITRARFEELCADLFRGTLEPVEKALRDAKLDKghIREIVLVGGSIRIPKIQKLLQDFFNGRelNKSI 366
Cdd:cd10229 293 -------------LSPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAFSTK--VKII 355
|
410
....*....|....
gi 148229965 367 ---NPDEAVAYGAA 377
Cdd:cd10229 356 ippEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
8-378 |
1.00e-16 |
|
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: 81.37 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVgvFQHGKvEIIANEqgnrttPSYVAF-TDTERLI--GDaarnqvalnptntifDAKRLIGRRFDDPTV 84
Cdd:cd10225 2 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 85 qsdmkHWPFtvvSDGgkpkvkVeykgeaktffpeeISSMvlikmkEVAEAYLGA---KV--------PDAVITVPAYFND 153
Cdd:cd10225 58 -----IRPL---RDG------V-------------IADF------EATEAMLRYfirKAhrrrgflrPRVVIGVPSGITE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 154 SQRQATKDAGIIAGINVLRIINEPTAAAIAYGLDKKSAglgeTNVLIFDLGGGTFDVSVLTIdGGIFEVKStagdTHLGG 233
Cdd:cd10225 105 VERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPIEEP----RGSMVVDIGGGTTEIAVISL-GGIVTSRS----VRVAG 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 234 EDFDNRMVAHfldeFKRKNKKDISgnkravrrLRTAcERAKRTLSSstqASLEIDSL---YEGTDFYTSITRARfeELCA 310
Cdd:cd10225 176 DEMDEAIINY----VRRKYNLLIG--------ERTA-ERIKIEIGS---AYPLDEELsmeVRGRDLVTGLPRTI--EITS 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 311 DLFRGTLEP--------VEKALRDAK-------LDKGhireIVLVGGSIRIPKIQKLLQDffngrELNKSI----NPDEA 371
Cdd:cd10225 238 EEVREALEEpvnaiveaVRSTLERTPpelaadiVDRG----IVLTGGGALLRGLDELLRE-----ETGLPVhvadDPLTC 308
|
....*..
gi 148229965 372 VAYGAAV 378
Cdd:cd10225 309 VAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
8-377 |
1.34e-12 |
|
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: 69.34 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTtySCVGVFQHGKvEIIANEqgnrttPSYVAF-TDTERLI--GDaarnqvalnptntifDAKRLIGRrfddptv 84
Cdd:COG1077 10 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIdKKTGKVLavGE---------------EAKEMLGR------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 85 qsdmkhwpftvvsdggkpkvkveykgeakTffPEEIssmVLIK-MK-------EVAEAYLGA---KV--------PDAVI 145
Cdd:COG1077 59 -----------------------------T--PGNI---VAIRpLKdgviadfEVTEAMLKYfikKVhgrrsffrPRVVI 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 146 TVPAYFNDSQRQATKDAGIIAGINVLRIINEPTAAAIAYGLDKKSAglgeTNVLIFDLGGGTFDVSVLTIdGGIfeVKST 225
Cdd:COG1077 105 CVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEP----TGNMVVDIGGGTTEVAVISL-GGI--VVSR 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 226 AgdTHLGGEDFDNRMVAHfldeFKRKNKKDISgnkravrrLRTAcERAKRTLSSSTQASLEIDSLYEGTDFYTSITRARF 305
Cdd:COG1077 178 S--IRVAGDELDEAIIQY----VRKKYNLLIG--------ERTA-EEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTIT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 306 ---EELcADLFRGTLEPVEKALRDA--K---------LDKGhireIVLVGGSIRIPKIQKLLQDFFNgreLNKSI--NPD 369
Cdd:COG1077 243 itsEEI-REALEEPLNAIVEAIKSVleKtppelaadiVDRG----IVLTGGGALLRGLDKLLSEETG---LPVHVaeDPL 314
|
....*...
gi 148229965 370 EAVAYGAA 377
Cdd:COG1077 315 TCVARGTG 322
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
8-377 |
9.13e-11 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 63.61 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYscVGVFQHGKvEIIANEqgnrttPSYVAF-TDTERL--IGDaarnqvalnptntifDAKRLIGRRFDDPTV 84
Cdd:PRK13930 11 IGIDLGTAN--TLVYVKGK-GIVLNE------PSVVAIdTKTGKVlaVGE---------------EAKEMLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 85 QSDMKHwpfTVVSDggkpkvkveykgeaktffPEEISSMV--LIKMkeVAEAYLGAKvPDAVITVPAYFNDSQRQATKDA 162
Cdd:PRK13930 67 IRPLKD---GVIAD------------------FEATEAMLryFIKK--ARGRRFFRK-PRIVICVPSGITEVERRAVREA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 163 GIIAGINVLRIINEPTAAAIAYGLD-KKSAGlgetNvLIFDLGGGTFDVSVLTIdGGIFEVKSTAgdthLGGEDFDNRMV 241
Cdd:PRK13930 123 AEHAGAREVYLIEEPMAAAIGAGLPvTEPVG----N-MVVDIGGGTTEVAVISL-GGIVYSESIR----VAGDEMDEAIV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 242 AHfldeFKRKNKKDISGnkravrrlRTAcERAKRTLSSSTQA----SLEIdslyEGTDFYTSITRARfeELCADLFRGTL 317
Cdd:PRK13930 193 QY----VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLdeeeSMEV----RGRDLVTGLPKTI--EISSEEVREAL 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148229965 318 EP--------VEKALRDAK-------LDKGhireIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAA 377
Cdd:PRK13930 254 AEplqqiveaVKSVLEKTPpelaadiIDRG----IVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVARGTG 323
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
8-376 |
3.83e-10 |
|
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: 61.80 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGkveIIANEqgnrttPSYVAF-TDTERLI--GDaarnqvalnptntifDAKRLIGRRFDDPTV 84
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGN---------------EAKKMLGRTPGNIVA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 85 QSDMKHwpfTVVSDggkpkvkveykgeaktfFpEEISSMVLIKMKEVAEAYLGAKvPDAVITVPAYFNDSQRQATKDAGI 164
Cdd:pfam06723 60 VRPLKD---GVIAD-----------------F-EVTEAMLKYFIKKVHGRRSFSK-PRVVICVPSGITEVERRAVKEAAK 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 165 IAGINVLRIINEPTAAAIAYGLDKKSAglgeTNVLIFDLGGGTFDVSVLTIdGGIFEVKStagdTHLGGEDFDNRMVahf 244
Cdd:pfam06723 118 NAGAREVFLIEEPMAAAIGAGLPVEEP----TGNMVVDIGGGTTEVAVISL-GGIVTSKS----VRVAGDEFDEAII--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 245 ldEFKRKNKKDISGNkravrrlRTAcERAKRTLSSSTQA----SLEIdslyEGTDFYT------SITRARFEELCADLFR 314
Cdd:pfam06723 186 --KYIRKKYNLLIGE-------RTA-ERIKIEIGSAYPTeeeeKMEI----RGRDLVTglpktiEISSEEVREALKEPVS 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148229965 315 GTLEPVEKALRDAK-------LDKGhireIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAVAYGA 376
Cdd:pfam06723 252 AIVEAVKEVLEKTPpelaadiVDRG----IVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
8-354 |
5.53e-08 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 55.64 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYSCVGVFQHGKVEIIANEQGNRTTPSYVAFTDTErLIGDAARNQVALNPTNTIFDA--KRLIGRRFD---DP 82
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTRE-AVSEWLYRHLDVPAYDDERQAllRRAIRYNREediDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 83 TVQS------------DMKHWPFTVVSdggkPK----------VKVeykgeakTFFpEEISSMVLIKMKEVAEAYLGAKV 140
Cdd:PRK11678 82 TAQSvffglaalaqylEDPEEVYFVKS----PKsflgasglkpQQV-------ALF-EDLVCAMMLHIKQQAEAQLQAAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 141 PDAVITVPAYFN-----DSQRQATkdaGII------AGINVLRIINEPTAAaiayGLDKKSAGLGETNVLIFDLGGGTFD 209
Cdd:PRK11678 150 TQAVIGRPVNFQglggeEANRQAE---GILeraakrAGFKDVEFQFEPVAA----GLDFEATLTEEKRVLVVDIGGGTTD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 210 VSVLTIdGGIFEVKSTAGDTHL-------GGEDFD-----NRMVAHF-----------------------------LDEF 248
Cdd:PRK11678 223 CSMLLM-GPSWRGRADRSASLLghsgqriGGNDLDialafKQLMPLLgmgsetekgialpslpfwnavaindvpaqSDFY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 249 KRKNKKDISGNKR------AVRRL-------------RTAcERAKRTLSS--STQASLE-IDSLYEgtdfyTSITRARFE 306
Cdd:PRK11678 302 SLANGRLLNDLIRdarepeKVARLlkvwrqrlsyrlvRSA-EEAKIALSDqaETRASLDfISDGLA-----TEISQQGLE 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 148229965 307 ELCADLfrgtLEPVEKALRDAkLDKGHIRE--IVLVGGSIRIPKIQKLLQ 354
Cdd:PRK11678 376 EAISQP----LARILELVQLA-LDQAQVKPdvIYLTGGSARSPLIRAALA 420
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
141-249 |
1.18e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 54.14 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 141 PDAVITVPAYFNDSQRQATKDAGIIAGINVLRIINEPTAAAIAYGLDKKSAglgeTNVLIFDLGGGTFDVSVLTIdGGIF 220
Cdd:PRK13928 96 PRIMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQP----SGNMVVDIGGGTTDIAVLSL-GGIV 170
|
90 100
....*....|....*....|....*....
gi 148229965 221 EVKStagdTHLGGEDFDNRMVAHFLDEFK 249
Cdd:PRK13928 171 TSSS----IKVAGDKFDEAIIRYIRKKYK 195
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
141-243 |
1.75e-05 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 47.39 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 141 PDAVITVPAYFNDSQRQATKDAGIIAGINVLRIINEPTAAAIAYGLDKKSAglgeTNVLIFDLGGGTFDVSVLTIdGGIF 220
Cdd:PRK13927 97 PRVVICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEP----TGSMVVDIGGGTTEVAVISL-GGIV 171
|
90 100
....*....|....*....|...
gi 148229965 221 EVKStagdTHLGGEDFDNRMVAH 243
Cdd:PRK13927 172 YSKS----VRVGGDKFDEAIINY 190
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
100-360 |
1.81e-05 |
|
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: 47.27 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 100 GKPKVKVEYKGEAKTFFPEEissmVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIAGI------NVLRI 173
Cdd:cd11736 104 GKKVQALEVFAHALRFFKEH----ALQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 174 INEPTAAAI-AYGLDKksaglgetnVLIFDLGGGTFDVSVLTID---GGIFEV-KSTAGDTHLGGEDFD-NRMVAH---- 243
Cdd:cd11736 180 ALEPEAASIyCRKLDR---------YIVADCGGGTVDLTVHQIEqpqGTLKELyKASGGPYGAVGVDLAfEKLLCQifge 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 244 -FLDEFKRKNKKdisgnkrAVRRLRTACERAKRTlssstqASLEIDSlyegtdfytsitrarfeELCADLFRGTLEPVEK 322
Cdd:cd11736 251 dFIATFKAKRPA-------AWVDLTIAFEARKRT------AALRMSS-----------------EAMNELFQPTISQIIQ 300
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148229965 323 ALRD--AKLDKGHIREIVLVGGSIRIPKIQKLLQDFFNGR 360
Cdd:cd11736 301 HIDDlmKKPEVKGIKFLFLVGGFAESPMLQRAVQAAFGNI 340
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
8-360 |
6.76e-05 |
|
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: 45.77 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 8 VGIDLGTTYS-----------CVGVFQHGKveiiANEQG--NRTTPSYVAFTDTERL--IGDAARNQVA-LNPTNT---- 67
Cdd:cd11735 3 VAIDFGTTSSgyaysftkepeCIHVMRRWE----GGDPGvsNQKTPTTILLTPERKFhsFGYAARDFYHdLDPNESkqwl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 68 IFDAKRLIGRRFDDPTVQSDMKhwpftvVSDGGKPKVkVEYKGEAKTFFPEEissmvliKMKEVAEAyLGAKVPDA---- 143
Cdd:cd11735 79 YFEKFKMKLHTTGNLTMETDLT------AANGKKVKA-LEIFAYALQFFKEQ-------ALKELSDQ-AGSEFDNSdvrw 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 144 VITVPAYFNDSQRQATKDAGIIAGINV------LRIINEPTAAAI------AYGLDKksaglgetnVLIFDLGGGTFDVS 211
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIycrklrLHQMDR---------YVVVDCGGGTVDLT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 212 VLTI---DGGIFEV-KSTAGDTHLGGEDFDNRMV------AHFLDEFKRKNKKdisgnkrAVRRLRTACERAKRTLSSST 281
Cdd:cd11735 215 VHQIrlpEGHLKELyKASGGPYGSLGVDYEFEKLlckifgEDFIDQFKIKRPA-------AWVDLMIAFESRKRAAAPDR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 282 QASLEIDSLYEGTDFYTSITRARFE-------------------ELCAD----LFRGTLEPVEKALRD--AKLDKGHIRE 336
Cdd:cd11735 288 TNPLNITLPFSFIDYYKKFRGHSVEhalrksnvdfvkwssqgmlRMSPDamnaLFKPTIDHIIQHLTDlfQKPEVSGVKF 367
|
410 420
....*....|....*....|....
gi 148229965 337 IVLVGGSIRIPKIQKLLQDFFNGR 360
Cdd:cd11735 368 LFLVGGFAESPLLQQAVQNAFGDQ 391
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
166-378 |
7.48e-05 |
|
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: 45.21 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAIAYgLDKKSAGLGetnVLIFDLGGGTFDVSVLTiDGGIFEVKSTAgdthLGGEDFDNrmvahfl 245
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEKELG---VALIDIGGGTTDIAVFK-NGSLRYTAVIP----VGGNHITN------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 246 defkrknkkDISgnkRAVRRLRTACERAKRTLSSSTQASLEIDSLYE----GTDFYTSITR--------ARFEELcadlf 313
Cdd:cd24048 236 ---------DIA---IGLNTPFEEAERLKIKYGSALSEEADEDEIIEipgvGGREPREVSRrelaeiieARVEEI----- 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 314 rgtLEPVEKALRDAKLDKGHIREIVLVGGSIRIPKIQKLLQDFFN-----GRELNKSINPDEAVAYGAAV 378
Cdd:cd24048 299 ---LELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvriGRPKNIGGLPEEVNDPAYAT 365
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
122-358 |
7.75e-05 |
|
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: 44.98 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 122 SMVLIKMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKdagiiAGINVLRIINEPTAAAIAYGLDKKSAGlgetNVLIF 201
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPYDMRDL----NIALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 202 DLGGGTFDVSvLTIDGGIFevksTAGDTHLGGEDFDNRMVAHFLDEFKrknkkdisgnkravrrlrtACERAKRTLSSST 281
Cdd:cd24004 120 DIGAGTTDIA-LIRNGGIE----AYRMVPLGGDDFTKAIAEGFLISFE-------------------EAEKIKRTYGIFL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148229965 282 --QASLEIDSLYEGTDFYTSITRArFEELCADLFRGTLEPVEKALRdakldkghIREIVLVGGSIRIPKIQKLLQDFFN 358
Cdd:cd24004 176 liEAKDQLGFTINKKEVYDIIKPV-LEELASGIANAIEEYNGKFKL--------PDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
141-375 |
8.70e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 44.90 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 141 PDAVITVPAYFNDSQRQATKDAGIIAGINVLRIINEPTAAAIAYGL--DKKSAglgetNVLIfDLGGGTFDVSVLTIdGG 218
Cdd:PRK13929 99 PNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLpvDEPVA-----NVVV-DIGGGTTEVAIISF-GG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 219 IFEVKStagdTHLGGEDFDNRMVAHFldefkRKNKKDISGNKRA-----------VRRLRTACERAKRTLSSSTQASLEI 287
Cdd:PRK13929 172 VVSCHS----IRIGGDQLDEDIVSFV-----RKKYNLLIGERTAeqvkmeigyalIEHEPETMEVRGRDLVTGLPKTITL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 288 DSlyegtdfyTSITRARFEELCADL--FRGTLEPVEKALRDAKLDKGhireIVLVGGSIRIPKIQKLLQDFFNgRELNKS 365
Cdd:PRK13929 243 ES--------KEIQGAMRESLLHILeaIRATLEDCPPELSGDIVDRG----VILTGGGALLNGIKEWLSEEIV-VPVHVA 309
|
250
....*....|
gi 148229965 366 INPDEAVAYG 375
Cdd:PRK13929 310 ANPLESVAIG 319
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
310-385 |
1.51e-04 |
|
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: 44.82 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 310 ADLFRGTLEPVEKALRDAkLD-----KGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSiNPDEAVAYGAAVQAAILS 384
Cdd:COG1070 368 AHLARAVLEGVAFALRDG-LEaleeaGVKIDRIRATGGGARSPLWRQILADVL-GRPVEVP-EAEEGGALGAALLAAVGL 444
|
.
gi 148229965 385 G 385
Cdd:COG1070 445 G 445
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
94-231 |
1.52e-04 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 44.05 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 94 TVVSDGgkpkVKVEYKGeaktffpeeiSSMVLIKMKEVAEAYLGAKVPDAVITVPAyfndsqrqAT--KDAGII------ 165
Cdd:PRK15080 56 DVVRDG----IVVDFIG----------AVTIVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvves 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVLRIINEPTAAAiaygldkksAGLGETNVLIFDLGGGTFDVSVLTiDGgifEVKSTA----GDTHL 231
Cdd:PRK15080 114 AGLEVTHVLDEPTAAA---------AVLGIDNGAVVDIGGGTTGISILK-DG---KVVYSAdeptGGTHM 170
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
310-385 |
2.49e-04 |
|
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: 44.07 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 310 ADLFRGTLEPVEKALRDA----KLDKGHIREIVLVGGSIRIPKIQKLLQDFFnGRELNKSINPDEAvAYGAAVQAAILSG 385
Cdd:cd07808 365 AHLARAVLEGVAFSLRDSlevlKELGIKVKEIRLIGGGAKSPLWRQILADVL-GVPVVVPAEEEGS-AYGAALLAAVGAG 442
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
127-231 |
2.67e-04 |
|
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: 43.02 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 127 KMKEVAEAYLGAKVPDAVITVPAYFNDSQRQATKDAGIIAGINVLRIINEPTAAAiaygldkksAGLGETNVLIFDLGGG 206
Cdd:cd24047 51 KLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAAN---------AVLGIRDGAVVDIGGG 121
|
90 100
....*....|....*....|....*....
gi 148229965 207 TFDVSVLTiDGgifEVKSTA----GDTHL 231
Cdd:cd24047 122 TTGIAVLK-DG---KVVYTAdeptGGTHL 146
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
142-221 |
3.08e-04 |
|
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: 41.30 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 142 DAVITVPAYFNDSQRQAT-----------KDAGIIAGINVLRIINEPTAAAIAYGLDkksagLGETNVLIFDLGGGTfDV 210
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLT-----LGPEGLLVVDLGGGT-DI 88
|
90
....*....|..
gi 148229965 211 SVLTI-DGGIFE 221
Cdd:cd00012 89 SANVVlVGGGAR 100
|
|
| ASKHA_NBD_PPX_GppA |
cd24006 |
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
166-318 |
1.05e-03 |
|
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs 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: 466856 [Multi-domain] Cd Length: 294 Bit Score: 41.37 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 166 AGINVlRIINEP-----TAAAIAYGLDkksagLGETNVLIFDLGGGTFDVSVLTiDGGIFEVKStagdTHLGGedfdNRM 240
Cdd:cd24006 97 TGIDV-EIISGEeearlIYLAVRSGLP-----LGDGNALIVDIGGGSTELTLGD-NGEILFSES----LPLGA----VRL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 241 VAHFLdefkrknkKDISGNKRAVRRLRTACERAKRTL--------------SSSTQASLEIDSLYEGTDFYTSITRARFE 306
Cdd:cd24006 162 TERFL--------KDDPPSELLEEYLRSFVRSVLRPLpkrrkikfdvaigsGGTILALAAMALARKGKPHGYEISREELK 233
|
170
....*....|..
gi 148229965 307 ELCADLFRGTLE 318
Cdd:cd24006 234 ALYDELLRLSLE 245
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
168-256 |
1.14e-03 |
|
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: 41.35 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 168 INVLRIINEPTAAAIAYGLDKKsaGLGETNVLIFDLGGGTfdVSVLTIDGGIFEVKStaGDTHLGGEDFDNRMVAHFLDE 247
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDD--ELEDGNVLVIDIGGGT--TDILTFENGKPIEES--SDTLPGGEEALEKYADDILNE 210
|
....*....
gi 148229965 248 FKRKNKKDI 256
Cdd:cd10227 211 LLKKLGDEL 219
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
299-385 |
7.15e-03 |
|
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: 39.07 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148229965 299 SITRARFEELC-ADLFRGTLEPVEKALR---DAKLDKGH-IREIVLVGGSIRIPKIQKLLQDFFNgrelnKSI---NPDE 370
Cdd:cd07809 354 SLVGLTLSNFTrANLARAALEGATFGLRyglDILRELGVeIDEIRLIGGGSKSPVWRQILADVFG-----VPVvvpETGE 428
|
90
....*....|....*
gi 148229965 371 AVAYGAAVQAAILSG 385
Cdd:cd07809 429 GGALGAALQAAWGAG 443
|
|
| |
