|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
2-615 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1146.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 2 SARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFED 81
Cdd:PTZ00009 1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 82 ATVQSDMKHWPFRVVSEG-GKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATK 160
Cdd:PTZ00009 81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 161 DAGTITGLNVLRIINEPTAAAIAYGLDKKGCagGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRM 240
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGD--GEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 241 VSHLAEEFKRKHK-KDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEP 319
Cdd:PTZ00009 239 VEFCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 320 VEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILIGDKSENVQDLLLLDV 399
Cdd:PTZ00009 319 VEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 400 TPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEV 479
Cdd:PTZ00009 399 TPLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 480 TFDIDANGILNVTAADKSTGKENKITITNDKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVEDE 559
Cdd:PTZ00009 479 TFDIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 13676857 560 KLRGKISEQDKNKILDKCQEVINWLDRNQMAEKDEYEHKQKELERVCNPIISKLYQ 615
Cdd:PTZ00009 559 KVKGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQ 614
|
|
| 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: 932.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQS 86
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DMKHWPFRVV-SEGGKPKVQVEYKGETktFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:pfam00012 81 DIKHLPYKVVkLPNGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKKGcagGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLA 245
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKTD---KERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSS-STQASIEIDSLYE-GVDFYTSITRARFEELNADLFRGTLEPVEKA 323
Cdd:pfam00012 236 EEFKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 324 LRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDksENVQDLLLLDVTPLS 403
Cdd:pfam00012 316 LKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 404 LGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDI 483
Cdd:pfam00012 393 LGIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 484 DANGILNVTAADKSTGKENKITITNDKGrLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVEDEKlrG 563
Cdd:pfam00012 473 DANGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEG--D 549
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 13676857 564 KISEQDKNKIldkcQEVINWLDRN-QMAEKDEYEHKQKELERVCNPIISKLYQ 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: 898.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQS 86
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DMKHWPFRVVSEGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKGcaGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAE 246
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKG--KGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 247 EFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALRD 326
Cdd:cd10233 239 EFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 13676857 327 AKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd10233 319 AKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
5-615 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 869.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 5 GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDat 83
Cdd:PRK00290 2 GKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRRDEE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 84 VQSDMKHWPFRVVS-EGGKPKVQVEykgeTKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDA 162
Cdd:PRK00290 80 VQKDIKLVPYKIVKaDNGDAWVEID----GKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 163 GTITGLNVLRIINEPTAAAIAYGLDKKGcaggEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVS 242
Cdd:PRK00290 156 GKIAGLEVLRIINEPTAAALAYGLDKKG----DEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIID 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 243 HLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIeidSL-YEGVD------FYTSITRARFEELNADLFRG 315
Cdd:PRK00290 232 YLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEI---NLpFITADasgpkhLEIKLTRAKFEELTEDLVER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 316 TLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDksenVQDLL 395
Cdd:PRK00290 309 TIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 396 LLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVP 475
Cdd:PRK00290 384 LLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 476 QIEVTFDIDANGILNVTAADKSTGKENKITITNDKGrLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQT 555
Cdd:PRK00290 464 QIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKT 542
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 556 VEDekLRGKISEQDKNKILDKCQEVINWLDRNqmaEKDEYEHKQKELERVCNPIISKLYQ 615
Cdd:PRK00290 543 LKE--LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQ 597
|
|
| 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: 799.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDatVQ 85
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 86 SDMKHWPFRVVSEGGKPKVQVEykgeTKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKVD----GKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKkgcAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLA 245
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDK---SKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVD----FYTSITRARFEELNADLFRGTLEPVE 321
Cdd:TIGR02350 233 DEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 322 KALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDksenVQDLLLLDVTP 401
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 402 LSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTF 481
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 482 DIDANGILNVTAADKSTGKENKITITNDKGrLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVEDEKl 561
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAG- 545
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 13676857 562 rGKISEQDKNKILDKCQEVINWLDRNqmaEKDEYEHKQKELERVCNPIISKLYQ 615
Cdd:TIGR02350 546 -DKLPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
5-383 |
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: 752.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 5 GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATV 84
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 QSDMKHWPFRVVSEGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGT 164
Cdd:cd10241 81 QKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 165 ITGLNVLRIINEPTAAAIAYGLDKKgcaGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHL 244
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKK---GGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 245 AEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKAL 324
Cdd:cd10241 238 IKLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 325 RDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd10241 318 EDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| 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: 745.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQS 86
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DMKHWPFRVVS-EGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:cd24028 81 DIKHWPFKVVEdEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKKgcAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLA 245
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKK--SSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALR 325
Cdd:cd24028 239 EEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 13676857 326 DAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd24028 319 DAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
5-615 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 688.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 5 GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDAt 83
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 84 vQSDMKHWPFRVVsEGGKPKVQVEYKGetKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAG 163
Cdd:PRK13411 81 -EEERSRVPYTCV-KGRDDTVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 164 TITGLNVLRIINEPTAAAIAYGLDKKGcagGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:PRK13411 157 TIAGLEVLRIINEPTAAALAYGLDKQD---QEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDslyegvdFYTS-----------ITRARFEELNADL 312
Cdd:PRK13411 234 LVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLP-------FITAdetgpkhlemeLTRAKFEELTKDL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 313 FRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILIGDksenVQ 392
Cdd:PRK13411 307 VEATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 393 DLLLLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPR 472
Cdd:PRK13411 383 DLLLLDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 473 GVPQIEVTFDIDANGILNVTAADKSTGKENKITITNdKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNI 552
Cdd:PRK13411 463 GVPQIEVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSY 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13676857 553 KQTVEDEklRGKISEQDKNKILDKCQEVINWLdRNQMAEKDEYEHKQKELERVCNPIISKLYQ 615
Cdd:PRK13411 542 ESTLKEN--GELISEELKQRAEQKVEQLEAAL-TDPNISLEELKQQLEEFQQALLAIGAEVYQ 601
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
5-615 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 685.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 5 GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDat 83
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 84 VQSDMKHWPFRVVSEGgKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAG 163
Cdd:CHL00094 80 ISEEAKQVSYKVKTDS-NGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 164 TITGLNVLRIINEPTAAAIAYGLDKKGcaggEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:CHL00094 159 KIAGLEVLRIINEPTAASLAYGLDKKN----NETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIE---IDSLYEG-VDFYTSITRARFEELNADLFRGTLEP 319
Cdd:CHL00094 235 LIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 320 VEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDksenVQDLLLLDV 399
Cdd:CHL00094 315 VENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 400 TPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEV 479
Cdd:CHL00094 390 TPLSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 480 TFDIDANGILNVTAADKSTGKENKITITNdKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVEDe 559
Cdd:CHL00094 470 TFDIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE- 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 560 kLRGKISEQDKNKILDKCQEVinwldrNQMAEKDEYEH---KQKELERVCNPIISKLYQ 615
Cdd:CHL00094 548 -LKDKISEEKKEKIENLIKKL------RQALQNDNYESiksLLEELQKALMEIGKEVYS 599
|
|
| 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: 684.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDatvq 85
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 86 sdmkhwpfrvvseggkpkVQVEYKGETKTffPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:COG0443 77 ------------------EATEVGGKRYS--PEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKKGcagGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLA 245
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKGK---EEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDsLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALR 325
Cdd:COG0443 214 PEFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 326 DAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDKSEnvqdlllLDVTPLSLG 405
Cdd:COG0443 293 DAGLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 406 IETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDA 485
Cdd:COG0443 365 IETLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDA 444
|
490 500 510
....*....|....*....|....*....|....*..
gi 13676857 486 NGILNVTAADKSTGKENKITItndkgrlsKDDIDRMV 522
Cdd:COG0443 445 NGILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
3-615 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 667.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 3 ARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFED 81
Cdd:PTZ00400 39 ATGDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 82 ATVQSDMKHWPFRVV--SEGgkpKVQVEYKGetKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQAT 159
Cdd:PTZ00400 119 DATKKEQKILPYKIVraSNG---DAWIEAQG--KKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQAT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 160 KDAGTITGLNVLRIINEPTAAAIAYGLDKkgcAGGeKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNR 239
Cdd:PTZ00400 194 KDAGKIAGLDVLRIINEPTAAALAFGMDK---NDG-KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 240 MVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQasIEIDSLYEGVD------FYTSITRARFEELNADLF 313
Cdd:PTZ00400 270 ILNYLIAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQ--TEINLPFITADqsgpkhLQIKLSRAKLEELTHDLL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 314 RGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDksenVQD 393
Cdd:PTZ00400 348 KKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 394 LLLLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRG 473
Cdd:PTZ00400 423 LLLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRG 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 474 VPQIEVTFDIDANGILNVTAADKSTGKENKITITNDKGrLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIK 553
Cdd:PTZ00400 503 VPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVE 581
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13676857 554 QTVEDekLRGKISEQDKNKILDKCQEVinwldRNQMAEKD--EYEHKQKELERVCNPIISKLYQ 615
Cdd:PTZ00400 582 KQLSD--LKDKISDADKDELKQKITKL-----RSTLSSEDvdSIKDKTKQLQEASWKISQQAYK 638
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
5-593 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 654.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 5 GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDAT 83
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDELD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 84 VQSdmKHWPFRVVS-EGGKPKV---QVEykgetKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQAT 159
Cdd:PRK13410 82 PES--KRVPYTIRRnEQGNVRIkcpRLE-----REFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 160 KDAGTITGLNVLRIINEPTAAAIAYGLDKkgcaGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNR 239
Cdd:PRK13410 155 RDAGRIAGLEVERILNEPTAAALAYGLDR----SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 240 MVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLS--SSTQASIE-IDSLYEG-VDFYTSITRARFEELNADLFRG 315
Cdd:PRK13410 231 IVDWLAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpKHIETRLDRKQFESLCGDLLDR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 316 TLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDksenVQDLL 395
Cdd:PRK13410 311 LLRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 396 LLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVP 475
Cdd:PRK13410 386 LLDVTPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 476 QIEVTFDIDANGILNVTAADKSTGKENKITITNdKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQT 555
Cdd:PRK13410 466 QVQVAFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERR 544
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 13676857 556 VEDEKLR--GKISEQDKNKILDKCQEVINWLDRNQMAEKD 593
Cdd:PRK13410 545 LRDAALEfgPYFAERQRRAVESAMRDVQDSLEQDDDRELD 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: 635.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQhGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQS 86
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DMKHWPFRVVSEGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKkGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAE 246
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGA-GKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 247 EFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALRD 326
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 13676857 327 AKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd24093 319 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
8-580 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 632.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDatVQS 86
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DMKHWPFRVVS-EGGKPKVQVEYKGetKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:PLN03184 120 ESKQVSYRVVRdENGNVKLDCPAIG--KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKKGcaggEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLA 245
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKKS----NETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVD----FYTSITRARFEELNADLFRGTLEPVE 321
Cdd:PLN03184 274 SNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADgpkhIDTTLTRAKFEELCSDLLDRCKTPVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 322 KALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFfNGKELNKSINPDEAVAYGAAVQAAILIGDksenVQDLLLLDVTP 401
Cdd:PLN03184 354 NALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTP 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 402 LSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTF 481
Cdd:PLN03184 429 LSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKF 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 482 DIDANGILNVTAADKSTGKENKITITNdKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVEDekL 561
Cdd:PLN03184 509 DIDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--L 585
|
570
....*....|....*....
gi 13676857 562 RGKISEQDKNKILDKCQEV 580
Cdd:PLN03184 586 GDKVPADVKEKVEAKLKEL 604
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
5-547 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 597.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 5 GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATV 84
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 QSDMKHWPFRVVSEG-GKPKVQveyKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAG 163
Cdd:PTZ00186 107 QKDIKNVPYKIVRAGnGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 164 TITGLNVLRIINEPTAAAIAYGLDKKGcaggEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:PTZ00186 184 TIAGLNVIRVVNEPTAAALAYGMDKTK----DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVD----FYTSITRARFEELNADLFRGTLEP 319
Cdd:PTZ00186 260 ILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 320 VEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDksenVQDLLLLDV 399
Cdd:PTZ00186 340 CKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 400 TPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEV 479
Cdd:PTZ00186 415 TPLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEV 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13676857 480 TFDIDANGILNVTAADKSTGKENKITITNDKGrLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALES 547
Cdd:PTZ00186 495 TFDIDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAET 561
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
7-547 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 563.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDatVQS 86
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DMKHWPFR-VVSEGGKPKVQVeyKGETKTffPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:PRK05183 99 RYPHLPYQfVASENGMPLIRT--AQGLKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKkgcaGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLA 245
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDS----GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWIL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKHKkdigPNKRAVRRLRTACERAKRTLSSSTQASIEIdSLYEGvdfytSITRARFEELNADLFRGTLEPVEKALR 325
Cdd:PRK05183 251 EQAGLSPR----LDPEDQRLLLDAARAAKEALSDADSVEVSV-ALWQG-----EITREQFNALIAPLVKRTLLACRRALR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 326 DAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDKSENvqDLLLLDVTPLSLG 405
Cdd:PRK05183 321 DAGVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 406 IETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDA 485
Cdd:PRK05183 398 LETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDA 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13676857 486 NGILNVTAADKSTGKENKITITNDKGrLSKDDIDRMVQEAERYKSEDEANR----DRVAAKNALES 547
Cdd:PRK05183 478 DGLLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEA 542
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
8-383 |
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: 546.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQS 86
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DMKHWPFrVVSEGGKPKVQVEykgeTKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd10234 82 KQVPYPV-VSAGNGDAWVEIG----GKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKgcagGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAE 246
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDKK----KDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 247 EFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIE---IDSLYEG-VDFYTSITRARFEELNADLFRGTLEPVEK 322
Cdd:cd10234 233 EFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpKHLEMKLTRAKFEELTEDLVERTIEPVEQ 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13676857 323 ALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd10234 313 ALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVL 372
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
7-580 |
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: 545.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQ 85
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 86 SDMkhwPFRVVsEGGKPKVQVEYKGETKTffPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:TIGR01991 81 SIL---PYRFV-DGPGEMVRLRTVQGTVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKkgcaGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRmvshLA 245
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDK----ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHA----LA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSssTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALR 325
Cdd:TIGR01991 227 KWILKQLGISADLNPEDQRLLLQAARAAKEALT--DAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 326 DAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIGDKSENvqDLLLLDVTPLSLG 405
Cdd:TIGR01991 305 DAGLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 406 IETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDA 485
Cdd:TIGR01991 382 IETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 486 NGILNVTAADKSTGKENKITITNDKGrLSKDDIDRMVQEAERYKSED-----------EANRDRVAAKNAL--------E 546
Cdd:TIGR01991 462 DGLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDmyaralaeqkvEAERILEALQAALaadgdllsE 540
|
570 580 590
....*....|....*....|....*....|....
gi 13676857 547 SYTYNIKQTVEDekLRGKISEQDKNKILDKCQEV 580
Cdd:TIGR01991 541 DERAAIDAAMEA--LQKALQGDDADAIKAAIEAL 572
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
5-383 |
5.61e-172 |
|
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: 494.48 E-value: 5.61e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 5 GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDAT 83
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 84 VQSDMKHWPFRVVsEGGKPKVQVEYKGetKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAG 163
Cdd:cd11733 81 VQKDIKMVPYKIV-KASNGDAWVEAHG--KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 164 TITGLNVLRIINEPTAAAIAYGLDKKgcagGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:cd11733 158 QIAGLNVLRIINEPTAAALAYGLDKK----DDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQAsiEIDSLYEGVD------FYTSITRARFEELNADLFRGTL 317
Cdd:cd11733 234 LVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13676857 318 EPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd11733 312 EPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
5-385 |
7.78e-157 |
|
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: 456.14 E-value: 7.78e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 5 GPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDAT 83
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 84 VQSDMKHWPFRVVSEGGKpKVQVEYKGetKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAG 163
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNG-DAWVEARG--QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 164 TITGLNVLRIINEPTAAAIAYGLDKKgcagGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:cd11734 158 QIAGLNVLRVINEPTAAALAYGLDKS----GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVD----FYTSITRARFEELNADLFRGTLEP 319
Cdd:cd11734 234 IVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKLTRAQFESLVKPLVDRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13676857 320 VEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIG 385
Cdd:cd11734 314 CKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
8-385 |
2.83e-149 |
|
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: 437.93 E-value: 2.83e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQH--GKVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATV 84
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 QSDMKHWPFRVVSEG-GKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAG 163
Cdd:cd10237 105 EEEAKRYPFKVVNDNiGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 164 TITGLNVLRIINEPTAAAIAYGLDKKgcaGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKK---SDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGpNKRAVRRLRTACERAKRTLSSSTQASIEID-----SLYEGVDFYTSITRARFEELNADLFRGTLE 318
Cdd:cd10237 262 LIDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqislPSAFKVKFKEEITRDLFETLNEDLFQRVLE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13676857 319 PVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIG 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 |
1.34e-147 |
|
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: 432.44 E-value: 1.34e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 6 PAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQ 85
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 86 SDMKHWPFRVVSEGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKKGCAGGeKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLA 245
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPTEN-SNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALR 325
Cdd:cd10238 240 SEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 13676857 326 DAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 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 |
3.20e-147 |
|
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: 430.87 E-value: 3.20e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLI-GDAAKNQVAMNPTNTIFDAKRLIGRKFEDatVQ 85
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 86 SDMKHWPFRVV-SEGGKPKVQVEykgeTKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGT 164
Cdd:cd10236 82 EELPLLPYRLVgDENELPRFRTG----AGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 165 ITGLNVLRIINEPTAAAIAYGLDKKgcagGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHL 244
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQK----KEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 245 AEEFkrkhKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSlyEGVDFYTSITRARFEELNADLFRGTLEPVEKAL 324
Cdd:cd10236 234 LKQI----GIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRAL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13676857 325 RDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAILIG 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 ... |
8-383 |
1.30e-140 |
|
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: 413.51 E-value: 1.30e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVF-QHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDatvq 85
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 86 sdmkhwpfrvvseggkpkvqvEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:cd24029 77 ---------------------KEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKKgcaGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLA 245
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKE---GKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELIL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 246 EEFKRKH-KKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKAL 324
Cdd:cd24029 213 EKIGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKAL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 325 RDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd24029 293 KDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASL 350
|
|
| 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 |
3.31e-140 |
|
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: 413.49 E-value: 3.31e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSD 87
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 88 MKHWPFRVVS-EGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKGCAGGE---KNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLESEekpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKA 323
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 13676857 324 LRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAA 381
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
7-383 |
3.01e-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: 406.31 E-value: 3.01e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQS 86
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DMKHWPFRVV-SEGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTI 165
Cdd:cd24095 83 DLKLFPFKVTeGPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TGLNVLRIINEPTAAAIAYGLDKKGCAGGE-KNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHL 244
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIYKTDLPETDpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 245 AEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKAL 324
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKAL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 325 RDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd24095 323 ADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
8-381 |
4.65e-129 |
|
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: 384.70 E-value: 4.65e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSD 87
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 88 MKHWPFRVVS-EGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKGC-AGGEK--NVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDLpAEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEK 322
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 323 ALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAA 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 |
1.19e-125 |
|
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: 374.66 E-value: 1.19e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPTNTIFDAKRLIGrkfedatvqS 86
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMG---------T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 DmkhwpfRVVSEGGKpkvqveykgetkTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd10235 72 D------KQYRLGNH------------TFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKgcaGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRmvshLAE 246
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKR---EDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHA----LAD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 247 EFKRKHKKDIGPNKRAVR-RLRTACERAKRTLSSstQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALR 325
Cdd:cd10235 207 YFLKKHRLDFTSLSPSELaALRKRAEQAKRQLSS--QDSAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALR 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 13676857 326 DAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAI 382
Cdd:cd10235 285 DAGLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
8-383 |
3.10e-119 |
|
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: 359.77 E-value: 3.10e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSD 87
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 88 MKHWPFRVVSEGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTITG 167
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 168 LNVLRIINEPTAAAIAYGLDKKGCAGGE---KNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHL 244
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTDLPEPEekpRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 245 AEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKAL 324
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 325 RDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
8-381 |
3.81e-117 |
|
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: 353.34 E-value: 3.81e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGK-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGrkfedatvqs 86
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 dmkhwpfrvvseggkpkvqveykgetktFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTI------EDGI------FEVKSTAGDTHLGGE 234
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRRFENNEPQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 235 DFDNRMVSHLAEEFKRKHKKDIGP--NKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADL 312
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKDKDVrtNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 313 FRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAA 381
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
7-615 |
4.84e-107 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 335.67 E-value: 4.84e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 7 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDaaknqvamnpTNTIFDAKRLIGRKFED----A 82
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTLKEilntP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 83 TVQSDMKHWpfrVVSEGGKPKVQVEykgeTKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDA 162
Cdd:PRK01433 91 ALFSLVKDY---LDVNSSELKLNFA----NKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 163 GTITGLNVLRIINEPTAAAIAYGLDK--KGCaggeknVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRM 240
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNKnqKGC------YLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 241 VSHLAEEFKRkhkkdigPNKRAVRRLrtaCERAKRTLSSstQASIEIDSLyegvdfytSITRARFEELNADLFRGTLEPV 320
Cdd:PRK01433 238 TQYLCNKFDL-------PNSIDTLQL---AKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 321 EKALRDAKldKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNkSINPDEAVAYGAAVQAAILIGDKsenvQDLLLLDVT 400
Cdd:PRK01433 298 QECLEQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLIAPH----TNSLLIDVV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 401 PLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVT 480
Cdd:PRK01433 371 PLSLGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 481 FDIDANGILNVTAADKSTGKENKITITNDKGrLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVedEK 560
Cdd:PRK01433 451 FAIDADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAI--AE 527
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 561 LRGKISEQDKNKI---LDKCQEVINWLDRNQMAE--KDEYEHKQKELERVCNPIISKLYQ 615
Cdd:PRK01433 528 LTTLLSESEISIInslLDNIKEAVHARDIILINNsiKEFKSKIKKSMDTKLNIIINDLLK 587
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
6-383 |
2.54e-102 |
|
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: 315.07 E-value: 2.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 6 PAIGIDLGTTYSCVG-VFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGrkfedatv 84
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 qsdmkhwpfrvvseggkpkvqveykgeTKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGT 164
Cdd:cd10232 73 ---------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 165 ITGLNVLRIINEPTAAAIAYGL--DKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVS 242
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLraETSGDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 243 HLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEK 322
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13676857 323 ALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNG---KELNKSINPDEAVAYGAAVQAAIL 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 |
1.23e-92 |
|
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: 291.07 E-value: 1.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSD 87
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 88 MKHWPFRVVS-EGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd11737 83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKGCAGGE---KNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQDLPAPEekpRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEK 322
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 323 ALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAI 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 |
7.55e-91 |
|
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: 286.37 E-value: 7.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSD 87
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 88 MKHWPFRVVS-EGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd11739 83 KENLSYDLVPlKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKGCAGGEKN---VLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQDLPAPDEKpriVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEK 322
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 323 ALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAA 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; ... |
8-383 |
2.43e-88 |
|
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: 279.88 E-value: 2.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSD 87
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 88 MKHWPFRVVS-EGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTIT 166
Cdd:cd11738 83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYGLDKKGCAGGE---KNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSH 243
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQDLPALEekpRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 244 LAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEK 322
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13676857 323 ALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 383
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
8-378 |
7.23e-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: 203.49 E-value: 7.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDqgnrttpsyvaftdterligdaaknqvamnptntifdakrligrkfedatvqsd 87
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVV------------------------------------------------------ 26
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 88 mkHWPFRVVSEGGKPKVQVEYkgetktffpeEISSMVLTKMKEIAEAYLGGKVHSA-------VITVPAYFNDSQRQATK 160
Cdd:cd10170 27 --LQLPWPGGDGGSSKVPSVL----------EVVADFLRALLEHAKAELGDRIWELekapievVITVPAGWSDAAREALR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 161 DAGTITGL----NVLRIINEPTAAAIAYGLDKKGCAGGEKN--VLIFDLGGGTFDVSILTIEDGIFEVK---STAGDTHL 231
Cdd:cd10170 95 EAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDLLPLKPGdvVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 232 GGEDFDNRMVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVD---FYTSITRARFEEL 308
Cdd:cd10170 175 GGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEEE 254
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13676857 309 NADLFRGTLEPVEKALRDA--KLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELN---KSINPDEAVAYGAAV 378
Cdd:cd10170 255 IRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
8-357 |
1.20e-31 |
|
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: 127.39 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAknqvamnptntifdakrLIGRKFEDATVQSD 87
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGAESI-----------------YFGNDAIDAYLNDP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 88 MKHWPFRVV-----SEGGKPKVQVEYKgetktFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQAT--- 159
Cdd:cd10231 64 EEGRLIKSVksflgSSLFDETTIFGRR-----YPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqa 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 160 ----KDAGTITGLNVLRIINEPTAAAIAY--GLDKkgcaggEKNVLIFDLGGGTFDVSIL----TIEDGIFEVKSTAGDt 229
Cdd:cd10231 139 esrlRDAARRAGFRNVEFQYEPIAAALDYeqRLDR------EELVLVVDFGGGTSDFSVLrlgpNRTDRRADILATSGV- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 230 HLGGEDFDNRMVSH-LAEEFKRKHKKDIGPN---------------------------------------KRAVRRLRT- 268
Cdd:cd10231 212 GIGGDDFDRELALKkVMPHLGRGSTYVSGDKglpvpawlyadlsnwhaisllytkktlrllldlrrdaadPEKIERLLSl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 269 -----------ACERAKRTLSSSTQASIEIDSLYEGVDfyTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEI 337
Cdd:cd10231 292 vedqlghrlfrAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420
....*....|....*....|
gi 13676857 338 VLVGGSTRIPKIQKLLQDFF 357
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLF 389
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
8-377 |
8.49e-20 |
|
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: 91.57 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVG-VFQH--GKVEIIANDQG------NRTTPSYVAFTDTERLIG---DAAKNQVAMNPTNtifDAKRLI 75
Cdd:cd10229 3 VAIDFGTTYSGYAySFITdpGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDE---EHQWLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 76 GRKFEDATVQSDMKHWPFRVVSEGGKP----KVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYlggkvhsaVITVPAYF 151
Cdd:cd10229 80 FFKFKMMLLSEKELTRDTKVKAVNGKSmpalEVFAEALRYLKDHALKELRDRSGSSLDEDDIRW--------VLTVPAIW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 152 NDSQ----RQATKDAGTITGLN--VLRIINEPTAAAIAYGLDKKGCAGGE----KNVLIFDLGGGTFDVSILTI-EDGIF 220
Cdd:cd10229 152 SDAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCQKLLAEGEEKElkpgDKYLVVDCGGGTVDITVHEVlEDGKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 221 EVKSTAGDTHLGGEDFDNRMVSHLAE--------EFKRKHkkdigpnKRAVRRLRTACERAKRTlssstqasieiDSLYe 292
Cdd:cd10229 232 EELLKASGGPWGSTSVDEEFEELLEEifgddfmeAFKQKY-------PSDYLDLLQAFERKKRS-----------FKLR- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 293 gvdfytsITRARFEELNADLFRGTLEPVEKALRDAKLDKgqIQEIVLVGGSTRIPKIQKLLQDFFNGKelNKSI---NPD 369
Cdd:cd10229 293 -------LSPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAFSTK--VKIIippEPG 361
|
....*...
gi 13676857 370 EAVAYGAA 377
Cdd:cd10229 362 LAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
8-378 |
5.55e-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: 79.44 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnptntifDAKRLIGRKFEDATV 84
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 qsdmkHWPFRvvsEGgkpkvqVeykgetktffpeeISSMvltkmkEIAEAYLGG---KVHS--------AVITVPAYFND 153
Cdd:cd10225 58 -----IRPLR---DG------V-------------IADF------EATEAMLRYfirKAHRrrgflrprVVIGVPSGITE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 154 SQRQATKDAGTITGLNVLRIINEPTAAAIAYGLD---KKGcaggeknVLIFDLGGGTFDVSILTIeDGIFEVKStagdTH 230
Cdd:cd10225 105 VERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPieePRG-------SMVVDIGGGTTEIAVISL-GGIVTSRS----VR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 231 LGGEDFDNRMVSHLaeefKRKHKKDIGPnkravrrlRTAcERAKRTLSSstqASIEIDSL---YEGVDFYTSITRARfeE 307
Cdd:cd10225 173 VAGDEMDEAIINYV----RRKYNLLIGE--------RTA-ERIKIEIGS---AYPLDEELsmeVRGRDLVTGLPRTI--E 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 308 LNADLFRGTLEP--------VEKALRDAK-------LDKGqiqeIVLVGGSTRIPKIQKLLQdffngKELNKSI----NP 368
Cdd:cd10225 235 ITSEEVREALEEpvnaiveaVRSTLERTPpelaadiVDRG----IVLTGGGALLRGLDELLR-----EETGLPVhvadDP 305
|
410
....*....|
gi 13676857 369 DEAVAYGAAV 378
Cdd:cd10225 306 LTCVAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
8-377 |
9.80e-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: 66.64 E-value: 9.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnptntifDAKRLIGRkfedatv 84
Cdd:COG1077 10 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIdKKTGKVLavGE---------------EAKEMLGR------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 qsdmkhwpfrvvseggkpkvqveykgetkTffPEEISsmVLTKMK-------EIAEAYLG---GKVHS--------AVIT 146
Cdd:COG1077 59 -----------------------------T--PGNIV--AIRPLKdgviadfEVTEAMLKyfiKKVHGrrsffrprVVIC 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 147 VPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGgeknVLIFDLGGGTFDVSILTIeDGIfeVKSTA 226
Cdd:COG1077 106 VPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTG----NMVVDIGGGTTEVAVISL-GGI--VVSRS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 227 gdTHLGGEDFDNRMVSHLaeefKRKHKKDIGPnkravrrlRTAcERAKRTLSS----STQASIEIdslyEGVDFYTSITR 302
Cdd:COG1077 179 --IRVAGDELDEAIIQYV----RKKYNLLIGE--------RTA-EEIKIEIGSayplEEELTMEV----RGRDLVTGLPK 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 303 ARfeELNADLFRGTLEP--------VEKALRDAK-------LDKGqiqeIVLVGGSTRIPKIQKLLQDFFNgkeLNKSI- 366
Cdd:COG1077 240 TI--TITSEEIREALEEplnaiveaIKSVLEKTPpelaadiVDRG----IVLTGGGALLRGLDKLLSEETG---LPVHVa 310
|
410
....*....|..
gi 13676857 367 -NPDEAVAYGAA 377
Cdd:COG1077 311 eDPLTCVARGTG 322
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
8-377 |
1.35e-11 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 66.31 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYscVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERL--IGDaaknqvamnptntifDAKRLIGRKFEDATV 84
Cdd:PRK13930 11 IGIDLGTAN--TLVYVKGK-GIVLNE------PSVVAIdTKTGKVlaVGE---------------EAKEMLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 QSDMKHwpfrvvsegGkpkVQVEYkgetktffpeeissmvltkmkEIAEA---YLGGKVHS--------AVITVPAYFND 153
Cdd:PRK13930 67 IRPLKD---------G---VIADF---------------------EATEAmlrYFIKKARGrrffrkprIVICVPSGITE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 154 SQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGeknvLIFDLGGGTFDVSILTIeDGIFEVKSTAgdthLGG 233
Cdd:PRK13930 114 VERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPVTEPVGN----MVVDIGGGTTEVAVISL-GGIVYSESIR----VAG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 234 EDFDNRMVSHLaeefKRKHKKDIGPnkravrrlRTAcERAKRTLSSSTQA----SIEIdslyEGVDFYTSITRARfeELN 309
Cdd:PRK13930 185 DEMDEAIVQYV----RRKYNLLIGE--------RTA-EEIKIEIGSAYPLdeeeSMEV----RGRDLVTGLPKTI--EIS 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 310 ADLFRGTLEP--------VEKALRDAK-------LDKGqiqeIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAVAY 374
Cdd:PRK13930 246 SEEVREALAEplqqiveaVKSVLEKTPpelaadiIDRG----IVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVAR 320
|
...
gi 13676857 375 GAA 377
Cdd:PRK13930 321 GTG 323
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
8-376 |
1.60e-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: 62.96 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnptntifDAKRLIGRKFEDATV 84
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGN---------------EAKKMLGRTPGNIVA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 QSDMKHwpfrvvsegGKpkvqveykgetktffpeeISSMvltkmkEIAEA---YLGGKVHSA--------VITVPAYFND 153
Cdd:pfam06723 60 VRPLKD---------GV------------------IADF------EVTEAmlkYFIKKVHGRrsfskprvVICVPSGITE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 154 SQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGeknvLIFDLGGGTFDVSILTIeDGIFEVKStagdTHLGG 233
Cdd:pfam06723 107 VERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGN----MVVDIGGGTTEVAVISL-GGIVTSKS----VRVAG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 234 EDFDNRMVSHLaeefKRKHKKDIGPnkravrrlRTAcERAKrtlssstqasIEIDSLYEGVDFYTSITRAR--------- 304
Cdd:pfam06723 178 DEFDEAIIKYI----RKKYNLLIGE--------RTA-ERIK----------IEIGSAYPTEEEEKMEIRGRdlvtglpkt 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 305 -------FEELNADLFRGTLEPVEKALRDAK-------LDKGqiqeIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDE 370
Cdd:pfam06723 235 ieisseeVREALKEPVSAIVEAVKEVLEKTPpelaadiVDRG----IVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLT 309
|
....*.
gi 13676857 371 AVAYGA 376
Cdd:pfam06723 310 CVALGT 315
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
8-354 |
3.55e-07 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 52.94 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTErLIGDAAKNQVAMNPTNTIFDA--KRLI-GRKFEDATV 84
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTRE-AVSEWLYRHLDVPAYDDERQAllRRAIrYNREEDIDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 85 QSD--------MKH---WP---FRVVSeggkPK----------VQVeykgetkTFFpEEISSMVLTKMKEIAEAYLGGKV 140
Cdd:PRK11678 82 TAQsvffglaaLAQyleDPeevYFVKS----PKsflgasglkpQQV-------ALF-EDLVCAMMLHIKQQAEAQLQAAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 141 HSAVITVPAYFN-----DSQRQAT---KDAGTITGLNVLRIINEPTAAAIAY--GLDKkgcaggEKNVLIFDLGGGTFDV 210
Cdd:PRK11678 150 TQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTE------EKRVLVVDIGGGTTDC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 211 SILTIedGIFEVKSTAGDTHL--------GGEDFD-----NRMVSHL-----------------------------AEEF 248
Cdd:PRK11678 224 SMLLM--GPSWRGRADRSASLlghsgqriGGNDLDialafKQLMPLLgmgsetekgialpslpfwnavaindvpaqSDFY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 249 KRKHKKDIG--------PNKraVRRL-------------RTAcERAKRTLSSSTQASIEIDSLYEGVDfyTSITRARFEE 307
Cdd:PRK11678 302 SLANGRLLNdlirdarePEK--VARLlkvwrqrlsyrlvRSA-EEAKIALSDQAETRASLDFISDGLA--TEISQQGLEE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 13676857 308 LNADLfrgtLEPVEKALRDAkLDKGQIQE--IVLVGGSTRIPKIQKLLQ 354
Cdd:PRK11678 377 AISQP----LARILELVQLA-LDQAQVKPdvIYLTGGSARSPLIRAALA 420
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
124-254 |
4.52e-07 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 51.50 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 124 VLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLdkkgcaggeKNVLIFDL 203
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI---------RDGAVVDI 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13676857 204 GGGTFDVSIltIEDGifEVKSTA----GDTHLG-------GEDFDNrmvshlAEEFKRKHKK 254
Cdd:cd24047 119 GGGTTGIAV--LKDG--KVVYTAdeptGGTHLSlvlagnyGISFEE------AEIIKRDPAR 170
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
144-355 |
1.16e-06 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 51.06 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 144 VITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGeknvLIFDLGGGTFDVSILTIEdGIFEVK 223
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGN----MVVDIGGGTTDIAVLSLG-GIVTSS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 224 StagdTHLGGEDFDNRMVSHLaeefKRKHKKDIGpnKRAVRRLR----TACERAK--------RTLSSSTQASIEIDS-- 289
Cdd:PRK13928 174 S----IKVAGDKFDEAIIRYI----RKKYKLLIG--ERTAEEIKikigTAFPGAReeemeirgRDLVTGLPKTITVTSee 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13676857 290 ----LYEGVDFYTSITRARFE----ELNADLfrgtlepvekalrdakLDKGqiqeIVLVGGSTRIPKIQKLLQD 355
Cdd:PRK13928 244 ireaLKEPVSAIVQAVKSVLErtppELSADI----------------IDRG----IIMTGGGALLHGLDKLLAE 297
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
8-376 |
4.72e-06 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 49.13 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCvgvfqhgkveiIANDQGNR-TTPSYVAFTD---------TERLIGDAA-KNQVAMNptntifdakrlig 76
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGYPKdiiarkllgKEVLFGDEAlENRLALD------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 77 rkfedatvqsdmKHWPFR--VVSEGGKPKvqveykgetktffpEEISSMVLTKMKEIAEAYLGGKVHsAVITVPAYFNDS 154
Cdd:cd24009 60 ------------LRRPLEdgVIKEGDDRD--------------LEAARELLQHLIELALPGPDDEIY-AVIGVPARASAE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 155 QRQATKDAgTITGLNVLRIINEPTAaaIAYGLDKKgcaggeKNVLIFDLGGGTFDV-----SILTIEDGIfeVKSTAGDt 229
Cdd:cd24009 113 NKQALLEI-ARELVDGVMVVSEPFA--VAYGLDRL------DNSLIVDIGAGTTDLcrmkgTIPTEEDQI--TLPKAGD- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 230 hlggeDFDNRmvshLAEEFKRKHkKDIGPNKRAVRRLRtacERAKRTLSSSTQASIE--IDSLYEGVDFyTSITRARFEE 307
Cdd:cd24009 181 -----YIDEE----LVDLIKERY-PEVQLTLNMARRWK---EKYGFVGDASEPVKVElpVDGKPVTYDI-TEELRIACES 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13676857 308 LNADLFRGtlepVEKALRDAKLDKGQ--IQEIVLVGGSTRI----PKIQKLLQDFFNGKeLNKSINPDEAVAYGA 376
Cdd:cd24009 247 LVPDIVEG----IKKLIASFDPEFQEelRNNIVLAGGGSRIrgldTYIEKALKEYGGGK-VTCVDDPVFAGAEGA 316
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
122-358 |
1.06e-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: 47.67 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 122 SMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKdagtiTGLNVLRIINEPTAAAIAYGLDkkgcAGGEKNVLIF 201
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPY----DMRDLNIALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 202 DLGGGTFDVSIltIEDGifEVKSTaGDTHLGGEDFDNRmvshLAEEFkrkhkkDIGPNKravrrlrtaCERAKRTLSSST 281
Cdd:cd24004 120 DIGAGTTDIAL--IRNG--GIEAY-RMVPLGGDDFTKA----IAEGF------LISFEE---------AEKIKRTYGIFL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13676857 282 --QASIEIDSLYEGVDFYTSITRArFEELnadlfrgtLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFN 358
Cdd:cd24004 176 liEAKDQLGFTINKKEVYDIIKPV-LEEL--------ASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
124-258 |
1.18e-05 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 47.52 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 124 VLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLdkkgcaggeKNVLIFDL 203
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGI---------DNGAVVDI 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13676857 204 GGGTFDVSILtiEDGifEVKSTA----GDTHLG-------GEDFDNrmvshlAEEFKR--KHKKDIGP 258
Cdd:PRK15080 143 GGGTTGISIL--KDG--KVVYSAdeptGGTHMSlvlagayGISFEE------AEQYKRdpKHHKEIFP 200
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
136-378 |
1.20e-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: 47.91 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 136 LGGKVHsaVITVPAYFNDSQRQATKDAGtitgLNVLRIINEPTAAAIAYgLDKKgcaggEKN--VLIFDLGGGTFDVSIL 213
Cdd:cd24048 148 LEVDVH--VITGSSSAIQNLIKCVERAG----LEVDDIVLSPLASAEAV-LTED-----EKElgVALIDIGGGTTDIAVF 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 214 tiEDGIFEvkstagDTH---LGGEDFDNRMVSHL------AEEFKRKHKKDIGPN--KRAVRRLRTACERAKRTLSSSTq 282
Cdd:cd24048 216 --KNGSLR------YTAvipVGGNHITNDIAIGLntpfeeAERLKIKYGSALSEEadEDEIIEIPGVGGREPREVSRRE- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 283 asieidsLYEgvdfytsITRARFEELnadlfrgtLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFN---- 358
Cdd:cd24048 287 -------LAE-------IIEARVEEI--------LELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvr 344
|
250 260
....*....|....*....|.
gi 13676857 359 -GKELNKSINPDEAVAYGAAV 378
Cdd:cd24048 345 iGRPKNIGGLPEEVNDPAYAT 365
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
310-385 |
1.21e-05 |
|
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: 48.29 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 310 ADLFRGTLEPVEKALRDAkLD-----KGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSiNPDEAVAYGAAVQAAILI 384
Cdd:COG1070 368 AHLARAVLEGVAFALRDG-LEaleeaGVKIDRIRATGGGARSPLWRQILADVL-GRPVEVP-EAEEGGALGAALLAAVGL 444
|
.
gi 13676857 385 G 385
Cdd:COG1070 445 G 445
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
142-375 |
1.67e-04 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 44.13 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 142 SAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGgekNVLIfDLGGGTFDVSILTIeDGIFE 221
Cdd:PRK13929 100 NVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVA---NVVV-DIGGGTTEVAIISF-GGVVS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 222 VKStagdTHLGGEDFDNRMVSH--------LAEEFKRKHKKDIGpnKRAVRRLRTACERAKRTLSSSTQASIEIDSlyeg 293
Cdd:PRK13929 175 CHS----IRIGGDQLDEDIVSFvrkkynllIGERTAEQVKMEIG--YALIEHEPETMEVRGRDLVTGLPKTITLES---- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 294 vdfyTSITRARFEELNADL--FRGTLEPVEKALRDAKLDKGqiqeIVLVGGSTRIPKIQKLLQDFFNgKELNKSINPDEA 371
Cdd:PRK13929 245 ----KEIQGAMRESLLHILeaIRATLEDCPPELSGDIVDRG----VILTGGGALLNGIKEWLSEEIV-VPVHVAANPLES 315
|
....
gi 13676857 372 VAYG 375
Cdd:PRK13929 316 VAIG 319
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
299-385 |
2.53e-04 |
|
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: 44.08 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 299 SITRARFEELN-ADLFRGTLEPVEKALR---DAKLDKG-QIQEIVLVGGSTRIPKIQKLLQDFFNgkelnKSI---NPDE 370
Cdd:cd07809 354 SLVGLTLSNFTrANLARAALEGATFGLRyglDILRELGvEIDEIRLIGGGSKSPVWRQILADVFG-----VPVvvpETGE 428
|
90
....*....|....*
gi 13676857 371 AVAYGAAVQAAILIG 385
Cdd:cd07809 429 GGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
310-385 |
2.94e-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: 43.68 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 310 ADLFRGTLEPVEKALRDA----KLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELNKSINPDEAvAYGAAVQAAILIG 385
Cdd:cd07808 365 AHLARAVLEGVAFSLRDSlevlKELGIKVKEIRLIGGGAKSPLWRQILADVL-GVPVVVPAEEEGS-AYGAALLAAVGAG 442
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
111-358 |
3.27e-04 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; 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. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 43.42 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 111 ETKTFFPEEISSMVL--TKMKEIAEAylGGKVHSAVITVPAYFNDSQRQATKDAGtitgLNVLRIinEPTAAAIAYGLDK 188
Cdd:cd24049 97 EAEQYLPFPLEEVVLdyQILGEVEEG--GEKLEVLVVAAPKEIVESYLELLKEAG----LKPVAI--DVESFALARALEY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 189 KGCAGGEKNVLIFDLGGGTFDVSIltIEDGIFEVKSTAGdthLGGEDFDNRMVSHL------AEEFKRKHKKDIGPNKRA 262
Cdd:cd24049 169 LLPDEEEETVALLDIGASSTTLVI--VKNGKLLFTRSIP---VGGNDITEAIAKALglsfeeAEELKREYGLLLEGEEGE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 263 VRRLRTACERAKRTLSSSTQASIeidslyegvDFYTSITRarfeelnadlfrgtlepvekalrdakldKGQIQEIVLVGG 342
Cdd:cd24049 244 LKKVAEALRPVLERLVSEIRRSL---------DYYRSQNG----------------------------GEPIDKIYLTGG 286
|
250
....*....|....*.
gi 13676857 343 STRIPKIQKLLQDFFN 358
Cdd:cd24049 287 GSLLPGLDEYLSERLG 302
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
130-293 |
7.85e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 42.00 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 130 EIAEA---YLGGKVHSA-------VITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGgeknVL 199
Cdd:PRK13927 76 DVTEKmlkYFIKKVHKNfrpsprvVICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTG----SM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 200 IFDLGGGTFDVSILTIeDGIFEVKStagdTHLGGEDFDNRMVSHLaeefKRKHKKDIGPnkravrrlRTAcERAKrtlss 279
Cdd:PRK13927 152 VVDIGGGTTEVAVISL-GGIVYSKS----VRVGGDKFDEAIINYV----RRNYNLLIGE--------RTA-ERIK----- 208
|
170
....*....|....
gi 13676857 280 stqasIEIDSLYEG 293
Cdd:PRK13927 209 -----IEIGSAYPG 217
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
167-358 |
1.09e-03 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 41.66 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 167 GLNVLRIINEPTAAAIAYgLDKkgcagGEK--NVLIFDLGGGTFDVSIltIEDGIfeVKSTAGDThLGGEDFDNrmvshl 244
Cdd:COG0849 175 GLEVEDLVLSPLASAEAV-LTE-----DEKelGVALVDIGGGTTDIAV--FKDGA--LRHTAVIP-VGGDHITN------ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 245 aeefkrkhkkDIgpnkraVRRLRT---ACERAKRTLSS------STQASIEIDSLyeGVDFYTSITR--------ARFEE 307
Cdd:COG0849 238 ----------DI------AIGLRTpleEAERLKIKYGSalaslaDEDETIEVPGI--GGRPPREISRkelaeiieARVEE 299
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13676857 308 LnadlfrgtLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFN 358
Cdd:COG0849 300 I--------FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
8-257 |
2.19e-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: 40.20 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 8 IGIDLGTTYSCVgVFQHGKVEIIandqgnrttPSYVAFTDTERLIGDAAKNqvamnPTNTIFDAKR-LIGrkfEDAtvqs 86
Cdd:cd10227 1 IGIDIGNGNTKV-VTGGGKEFKF---------PSAVAEARESSLDDGLLED-----DIIVEYNGKRyLVG---ELA---- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 87 dmkhwpfrvVSEGGKPKVQVEYKGETKTFFPeeissMVLTKMKEIAEAYlGGKVHsAVITVP-AYFNDSQRQATKDAGTI 165
Cdd:cd10227 59 ---------LREGGGGRSTGDDKKKSEDALL-----LLLAALALLGDDE-EVDVN-LVVGLPiSEYKEEKKELKKKLLKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 166 TG------------LNVLRIINEPTAAAIAYGLDKKGCAggEKNVLIFDLGGGTfdVSILTIEDGIFEVKStaGDTHLGG 233
Cdd:cd10227 123 LHeftfngkerritINDVKVLPEGAGAYLDYLLDDDELE--DGNVLVIDIGGGT--TDILTFENGKPIEES--SDTLPGG 196
|
250 260
....*....|....*....|....
gi 13676857 234 EDFDNRMVSHLAEEFKRKHKKDIG 257
Cdd:cd10227 197 EEALEKYADDILNELLKKLGDELD 220
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
302-382 |
4.63e-03 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 39.90 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 302 RARFEELN---ADLFRGTLEPVEKALRDA-----KLDKGQIQEIVLVGGSTRIPKIQKLLQDFFnGKELnkSINPDEAVA 373
Cdd:cd07783 342 RGFLLPRPhdrAEFLRALLEGIAFIERLGyerleELGAPPVEEVRTAGGGARNDLWNQIRADVL-GVPV--VIAEEEEAA 418
|
....*....
gi 13676857 374 YGAAVQAAI 382
Cdd:cd07783 419 LGAALLAAA 427
|
|
| ASKHA_NBD_PPX_GppA |
cd24006 |
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
124-318 |
5.74e-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: 39.05 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 124 VLTKMKEIAEAYLGGKVH----SAVitvpayfndsqRQAtKDAGTI-------TGLNVlRIINEP-----TAAAIAYGLD 187
Cdd:cd24006 56 ALRRFKKLADEYGVKRIRavatSAV-----------REA-SNGDEFlerikreTGIDV-EIISGEeearlIYLAVRSGLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676857 188 KkgcagGEKNVLIFDLGGGTFDVSILTiEDGIFEVKStagdTHLGGedfdNRmvshLAEEFkrkhKKDIGPNKRAVRRLR 267
Cdd:cd24006 123 L-----GDGNALIVDIGGGSTELTLGD-NGEILFSES----LPLGA----VR----LTERF----LKDDPPSELLEEYLR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13676857 268 TACERAKRTL--------------SSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLE 318
Cdd:cd24006 181 SFVRSVLRPLpkrrkikfdvaigsGGTILALAAMALARKGKPHGYEISREELKALYDELLRLSLE 245
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
334-377 |
7.80e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.06 E-value: 7.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 13676857 334 IQEIVLVGGSTRIPKIQKLLQDFF---NGKELNKSINPDEAVAYGAA 377
Cdd:cd00012 89 SANVVLVGGGARNNGLAKRLKELLlfrGGLKVVKAVDPDEAVALGAA 135
|
|
| |
