|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
54-646 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1104.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRfdDPQTQ 133
Cdd:PRK00290 4 IIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:PRK00290 82 KDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGMN-NKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRSD 292
Cdd:PRK00290 162 EVLRIINEPTAAALAYGLDkKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 293 NIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDAG 372
Cdd:PRK00290 242 GIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALKDAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 373 VTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSLGIETLGAVF 452
Cdd:PRK00290 322 LSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLGGVM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 453 TKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGITTVSA 532
Cdd:PRK00290 402 TKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 533 KDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAEIASEIETA 612
Cdd:PRK00290 482 KDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIEAA 561
|
570 580 590
....*....|....*....|....*....|....
gi 30691626 613 VSDLRTAMAGEDVEDIKAKVEAANKAVSKIGEHM 646
Cdd:PRK00290 562 IKELKEALKGEDKEAIKAKTEELTQASQKLGEAM 595
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
54-648 |
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: 955.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDdpQTQ 133
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVkAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:TIGR02350 80 EEAKRVPYKVV-GDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGMN--NKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRS 291
Cdd:TIGR02350 159 EVLRIINEPTAAALAYGLDksKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 292 DNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDA 371
Cdd:TIGR02350 239 EGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 372 GVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSLGIETLGAV 451
Cdd:TIGR02350 319 GLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 452 FTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGITTVS 531
Cdd:TIGR02350 399 MTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 532 AKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAEIASEIET 611
Cdd:TIGR02350 479 AKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEK 558
|
570 580 590
....*....|....*....|....*....|....*..
gi 30691626 612 AVSDLRTAMAGEDVEDIKAKVEAANKAVSKIGEHMSK 648
Cdd:TIGR02350 559 AVAELKEALKGEDVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
46-648 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 947.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 46 CSRPVGNDVIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGR 125
Cdd:PTZ00400 35 RFAKATGDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 126 RFDDPQTQKEMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATK 205
Cdd:PTZ00400 115 RYDEDATKKEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 206 DAGKIAGLDVQRIINEPTAAALSYGMNNKEG-VIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYL 284
Cdd:PTZ00400 195 DAGKIAGLDVLRIINEPTAAALAFGMDKNDGkTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 285 VNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPC 364
Cdd:PTZ00400 275 IAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPC 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 365 QNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSLG 444
Cdd:PTZ00400 355 EKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 445 IETLGAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDA 524
Cdd:PTZ00400 435 IETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 525 NGITTVSAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAE 604
Cdd:PTZ00400 515 NGIMNISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDA 594
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 30691626 605 IASEIETAVSDLRTAMAGEDVEDIKAKVEAANKAVSKIGEHMSK 648
Cdd:PTZ00400 595 DKDELKQKITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYK 638
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
54-648 |
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: 941.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKgELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPK-ERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEAN--GQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIA 211
Cdd:pfam00012 80 RDIKHLPYKVVKLPNGDAGVEVRylGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 212 GLDVQRIINEPTAAALSYGMN--NKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFK 289
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDktDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 290 RSDNIDLTKDNLALQRLREAAEKAKIELSSTtQTEINLPFITADASGaKHLNITLTRSKFEGLVGKLIERTRSPCQNCLK 369
Cdd:pfam00012 240 KKYGIDLSKDKRALQRLREAAEKAKIELSSN-QTNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 370 DAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRG--DVKDLLLLDVVPLSLGIET 447
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIET 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 448 LGAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGI 527
Cdd:pfam00012 398 LGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 528 TTVSAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAEIAS 607
Cdd:pfam00012 478 LTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKS 557
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 30691626 608 EIETAVSDLRTAMAGEDVEDIKAKVEAANKAVSKIGEHMSK 648
Cdd:pfam00012 558 KVESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
47-643 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 815.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 47 SRPVGNDVIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMnqKG-ELLVGTPAKRQAVTNPTNTIFGSKRLIGR 125
Cdd:PTZ00186 22 SQKVQGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAF--KGsEKLVGLAAKRQAITNPQSTFYAVKRLIGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 126 RFDDPQTQKEMKMVPYKIVKAPNGDAWVE-ANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQAT 204
Cdd:PTZ00186 100 RFEDEHIQKDIKNVPYKIVRAGNGDAWVQdGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 205 KDAGKIAGLDVQRIINEPTAAALSYGMN-NKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEY 283
Cdd:PTZ00186 180 KDAGTIAGLNVIRVVNEPTAAALAYGMDkTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 284 LVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSP 363
Cdd:PTZ00186 260 ILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 364 CQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSL 443
Cdd:PTZ00186 340 CKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 444 GIETLGAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDID 523
Cdd:PTZ00186 420 GIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDID 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 524 ANGITTVSAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPA 603
Cdd:PTZ00186 500 ANGICHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSDA 579
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 30691626 604 EiASEIETAVSDLRTAMAGEDV--EDIKAKVEAANKAVSKIG 643
Cdd:PTZ00186 580 E-KENVKTLVAELRKAMENPNVakDDLAAATDKLQKAVMECG 620
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
52-644 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 815.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 52 NDVIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDdpQ 131
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 132 TQKEMKMVPYKIVKAPNGDAWVE--ANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGK 209
Cdd:CHL00094 80 ISEEAKQVSYKVKTDSNGNIKIEcpALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGMNNKEG-VIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEF 288
Cdd:CHL00094 160 IAGLEVLRIINEPTAASLAYGLDKKNNeTILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 289 KRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCL 368
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 369 KDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSLGIETL 448
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 449 GAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGIT 528
Cdd:CHL00094 400 GGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 529 TVSAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAEIASE 608
Cdd:CHL00094 480 SVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEK 559
|
570 580 590
....*....|....*....|....*....|....*.
gi 30691626 609 IETAVSDLRTAMAGEDVEDIKAKVEAANKAVSKIGE 644
Cdd:CHL00094 560 IENLIKKLRQALQNDNYESIKSLLEELQKALMEIGK 595
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
54-644 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 803.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDpqTQ 133
Cdd:PRK13411 4 VIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD--TE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:PRK13411 82 EERSRVPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGMN--NKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRS 291
Cdd:PRK13411 162 EVLRIINEPTAAALAYGLDkqDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQQQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 292 DNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDA 371
Cdd:PRK13411 242 EGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALKDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 372 GVTIKEVDEVLLVGGMTRVPKVQEIVSEIF-GKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSLGIETLGA 450
Cdd:PRK13411 322 GLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETLGE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 451 VFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGITTV 530
Cdd:PRK13411 402 VFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILKV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 531 SAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAEIASEIE 610
Cdd:PRK13411 482 SAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRAE 561
|
570 580 590
....*....|....*....|....*....|....*.
gi 30691626 611 TAVSDLRTAMAGEDV--EDIKAKVEAANKAVSKIGE 644
Cdd:PRK13411 562 QKVEQLEAALTDPNIslEELKQQLEEFQQALLAIGA 597
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
52-427 |
0e+00 |
|
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: 794.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 52 NDVIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQ 131
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 132 TQKEMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIA 211
Cdd:cd11733 81 VQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 212 GLDVQRIINEPTAAALSYGMNNKEG-VIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKR 290
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKKDDkIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 291 SDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKD 370
Cdd:cd11733 241 EQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLKD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 30691626 371 AGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILR 427
Cdd:cd11733 321 AGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVLA 377
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
54-624 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 749.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDpqTQ 133
Cdd:PRK13410 4 IVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE--LD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVE--ANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIA 211
Cdd:PRK13410 82 PESKRVPYTIRRNEQGNVRIKcpRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 212 GLDVQRIINEPTAAALSYGMNNKEG-VIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKR 290
Cdd:PRK13410 162 GLEVERILNEPTAAALAYGLDRSSSqTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 291 SDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKD 370
Cdd:PRK13410 242 KEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRALKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 371 AGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSLGIETLGA 450
Cdd:PRK13410 322 AGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETIGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 451 VFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGITTV 530
Cdd:PRK13410 402 VMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGILQV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 531 SAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAEIASE-- 608
Cdd:PRK13410 482 SATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAALEFGPYFAERqr 561
|
570
....*....|....*...
gi 30691626 609 --IETAVSDLRTAMAGED 624
Cdd:PRK13410 562 raVESAMRDVQDSLEQDD 579
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
18-646 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 742.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 18 ASVSAFKSVSANGKNSMFGKLGYLARPFcsRPVGNDVIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGE 97
Cdd:PLN03184 7 PFSTPTAAFLKMGKRRGNGARRRAGGPL--RVVAEKVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 98 LLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDdpQTQKEMKMVPYKIVKAPNGDAWVE--ANGQKFSPSQIGANVLTKMKE 175
Cdd:PLN03184 85 RLVGQIAKRQAVVNPENTFFSVKRFIGRKMS--EVDEESKQVSYRVVRDENGNVKLDcpAIGKQFAAEEISAQVLRKLVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 176 TAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGLDVQRIINEPTAAALSYGMNNKEG-VIAVFDLGGGTFDVSILE 254
Cdd:PLN03184 163 DASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLEVLRIINEPTAASLAYGFEKKSNeTILVFDLGGGTFDVSVLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 255 ISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADA 334
Cdd:PLN03184 243 VGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 335 SGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEA 414
Cdd:PLN03184 323 DGPKHIDTTLTRAKFEELCSDLLDRCKTPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 415 VAMGAAIQGGILRGDVKDLLLLDVVPLSLGIETLGAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAAD 494
Cdd:PLN03184 403 VALGAAVQAGVLAGEVSDIVLLDVTPLSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 495 NKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGITTVSAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKK 574
Cdd:PLN03184 483 NKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKR 562
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30691626 575 QLIDLRNSADTTIYSVEKSLSEYREKIPAEIASEIETAVSDLRTAMAGEDVEDIKAKVEAANKAVSKIGEHM 646
Cdd:PLN03184 563 DAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVEAKLKELKDAIASGSTQKMKDAMAALNQEVMQIGQSL 634
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
54-560 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 727.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPqtq 133
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 kemkmvpykivkapngdaWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:COG0443 78 ------------------ATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGMNNK--EGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRS 291
Cdd:COG0443 140 EVLRLLNEPTAAALAYGLDKGkeEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 292 DNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFitadaSGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDA 371
Cdd:COG0443 220 EGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 372 GVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPlslGIETLGAV 451
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKDLDVTPLSL---GIETLGGV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 452 FTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGITTVS 531
Cdd:COG0443 372 FTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVS 451
|
490 500
....*....|....*....|....*....
gi 30691626 532 AKDKATGKEQNITIrssgglsDDEINRMV 560
Cdd:COG0443 452 AKDLGTGKEQSITI-------KEEIERML 473
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
54-426 |
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: 700.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQtq 133
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:cd10234 79 VERKQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGMN-NKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRSD 292
Cdd:cd10234 159 EVLRIINEPTAAALAYGLDkKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 293 NIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDAG 372
Cdd:cd10234 239 GIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 30691626 373 VTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd10234 319 LSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVL 372
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
54-428 |
0e+00 |
|
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: 654.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAEVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:cd11734 83 RDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGMNNKE-GVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRSD 292
Cdd:cd11734 163 NVLRVINEPTAAALAYGLDKSGdKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFKKES 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 293 NIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDAG 372
Cdd:cd11734 243 GIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALKDAG 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 30691626 373 VTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRG 428
Cdd:cd11734 323 VKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
55-615 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 628.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKgELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQK 134
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 135 EMKMVPYKIVKAPNGDAWVEAN--GQK--FSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKI 210
Cdd:PTZ00009 86 DMKHWPFKVTTGGDDKPMIEVTyqGEKktFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 211 AGLDVQRIINEPTAAALSYGMNNK---EGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNE 287
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKgdgEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 288 FKRSDN-IDLTKDNLALQRLREAAEKAKIELSSTTQT--EINLPFITADasgakhLNITLTRSKFEGLVGKLIERTRSPC 364
Cdd:PTZ00009 246 FKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQAtiEIDSLFEGID------YNVTISRARFEELCGDYFRNTLQPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 365 QNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIF-GKSPCKGVNPDEAVAMGAAIQGGILRGD----VKDLLLLDVV 439
Cdd:PTZ00009 320 EKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLDVT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 440 PLSLGIETLGAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVT 519
Cdd:PTZ00009 400 PLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 520 FDIDANGITTVSAKDKATGKEQNITIRSSGG-LSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSE-- 596
Cdd:PTZ00009 480 FDIDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDek 559
|
570
....*....|....*....
gi 30691626 597 YREKIPAEIASEIETAVSD 615
Cdd:PTZ00009 560 VKGKLSDSDKATIEKAIDE 578
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
55-638 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 562.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCV-SVMEGKtARVIENAEGSRTTPSVVAMNQKGeLLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:PRK05183 22 VGIDLGTTNSLVaTVRSGQ-AEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLADIQQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMkmVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:PRK05183 100 YPH--LPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGM-NNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFkrsd 292
Cdd:PRK05183 178 NVLRLLNEPTAAAIAYGLdSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQA---- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 293 NIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLpfitADASGakhlniTLTRSKFEGLVGKLIERTRSPCQNCLKDAG 372
Cdd:PRK05183 254 GLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV----ALWQG------EITREQFNALIAPLVKRTLLACRRALRDAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 373 VTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRG----------DVkdlllldvVPLS 442
Cdd:PRK05183 324 VEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGnkpdsdmlllDV--------IPLS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 443 LGIETLGAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDI 522
Cdd:PRK05183 396 LGLETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 523 DANGITTVSAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIP 602
Cdd:PRK05183 476 DADGLLSVTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLS 555
|
570 580 590
....*....|....*....|....*....|....*.
gi 30691626 603 AEIASEIETAVSDLRTAMAGEDVEDIKAKVEAANKA 638
Cdd:PRK05183 556 AAERAAIDAAMAALREVAQGDDADAIEAAIKALDKA 591
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
54-638 |
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: 548.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMkmvPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:TIGR01991 81 SIL---PYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGM-NNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEfkrsD 292
Cdd:TIGR01991 158 NVLRLLNEPTAAAVAYGLdKASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQ----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 293 NIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGakhlniTLTRSKFEGLVGKLIERTRSPCQNCLKDAG 372
Cdd:TIGR01991 234 GISADLNPEDQRLLLQAARAAKEALTDAESVEVDFTLDGKDFKG------KLTRDEFEALIQPLVQKTLSICRRALRDAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 373 VTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRG----------DVkdlllldvVPLS 442
Cdd:TIGR01991 308 LSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGnrigndllllDV--------TPLS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 443 LGIETLGAVFTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDI 522
Cdd:TIGR01991 380 LGIETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 523 DANGITTVSAKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIP 602
Cdd:TIGR01991 460 DADGLLTVSAQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLS 539
|
570 580 590
....*....|....*....|....*....|....*.
gi 30691626 603 AEIASEIETAVSDLRTAMAGEDVEDIKAKVEAANKA 638
Cdd:TIGR01991 540 EDERAAIDAAMEALQKALQGDDADAIKAAIEALEEA 575
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
54-426 |
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: 537.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQkGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTD-GERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEA--NGQK--FSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGK 209
Cdd:cd24028 80 SDIKHWPFKVVEDEDGKPKIEVtyKGEEktFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGMNNK---EGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVN 286
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDKKssgERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 287 EFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASgakhLNITLTRSKFEGLVGKLIERTRSPCQN 366
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGID----FETTITRAKFEELCEDLFKKCLEPVEK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30691626 367 CLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIF-GKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd24028 316 VLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
54-426 |
2.11e-179 |
|
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: 514.84 E-value: 2.11e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQkGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:cd10241 3 VIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTD-GERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKApNGDAW--VEANGQK--FSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGK 209
Cdd:cd10241 82 KDIKLLPFKIVNK-NGKPYiqVEVKGEKktFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGMNNKEGV--IAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNE 287
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKKGGEknILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 288 FKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINlpfITADASGaKHLNITLTRSKFEGLVGKLIERTRSPCQNC 367
Cdd:cd10241 241 FKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIE---IESLFDG-EDFSETLTRAKFEELNMDLFRKTLKPVQKV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 368 LKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIF-GKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd10241 317 LEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
55-426 |
6.12e-168 |
|
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: 485.60 E-value: 6.12e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKgELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQK 134
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 135 EMKMVPYKIVKAPNGDAW-VEANGQK--FSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIA 211
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIqVEYKGETktFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 212 GLDVQRIINEPTAAALSYGMNNK---EGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEF 288
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKgkgERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 289 KRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQT--EINLPFITADasgakhLNITLTRSKFEGLVGKLIERTRSPCQN 366
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQAsiEIDSLFEGID------FYTSITRARFEELCADLFRSTLEPVEK 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30691626 367 CLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIF-GKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd10233 315 VLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
54-428 |
5.33e-153 |
|
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: 447.05 E-value: 5.33e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDpqTQ 133
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:cd10236 82 EELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYGMNNK-EGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFkrsd 292
Cdd:cd10236 162 NVLRLLNEPTAAALAYGLDQKkEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQI---- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 293 NIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGakhlniTLTRSKFEGLVGKLIERTRSPCQNCLKDAG 372
Cdd:cd10236 238 GIDARLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWER------EITREEFEELIQPLVKRTLEPCRRALKDAG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 30691626 373 VTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRG 428
Cdd:cd10236 312 LEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
55-426 |
3.75e-150 |
|
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: 439.32 E-value: 3.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVI-ENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPqtq 133
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 kemkmvpykivkapngdawVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGL 213
Cdd:cd24029 78 -------------------EEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 214 DVQRIINEPTAAALSYG--MNNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRS 291
Cdd:cd24029 139 NVLRLINEPTAAALAYGldKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 292 -DNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITadasGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKD 370
Cdd:cd24029 219 tGILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDG----KGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 30691626 371 AGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
55-426 |
2.03e-146 |
|
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: 430.94 E-value: 2.03e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGkTARVIENAEGSRTTPSVVAMNQKgELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQK 134
Cdd:cd24093 2 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 135 EMKMVPYKIVKApNGDAWVEAN--GQK--FSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKI 210
Cdd:cd24093 80 DMKTWPFKVIDV-NGNPVIEVQylGETktFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 211 AGLDVQRIINEPTAAALSYGM----NNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVN 286
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLgagkSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 287 EFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFItadaSGAKHLNITLTRSKFEGLVGKLIERTRSPCQN 366
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSL----FDGEDFESSITRARFEDLNAALFKSTLEPVEQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30691626 367 CLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIF-GKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd24093 315 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
55-425 |
5.10e-128 |
|
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: 382.36 E-value: 5.10e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGrrfddpqTQK 134
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMG-------TDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 135 EmkmvpykivkapngdawVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGLD 214
Cdd:cd10235 74 Q-----------------YRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 215 VQRIINEPTAAALSYGMNNK--EGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVnefKRSD 292
Cdd:cd10235 137 VERLINEPTAAALAYGLHKRedETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFL---KKHR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 293 NIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLpfitadASGAKHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDAG 372
Cdd:cd10235 214 LDFTSLSPSELAALRKRAEQAKRQLSSQDSAEIRL------TYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAG 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 30691626 373 VTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGI 425
Cdd:cd10235 288 LKPSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
39-428 |
1.39e-123 |
|
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: 373.60 E-value: 1.39e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 39 GYLARPFCSRPVGNdVIGIDLGTTNSCVSVMEGKTA--RVIENAEGSRTTPSVVAMNQKGELLVGTPAKRQAVTNPTNTI 116
Cdd:cd10237 10 GYLGQQYLPPPKPK-IVGIDLGTTYSCVGVYHAVTGevEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 117 FGSKRLIGRRFDDPQTQKEMKMVPYKIVKAPNGDAW--VEANGQKF--SPSQIGANVLTKMKETAEAYLGKSINKAVVTV 192
Cdd:cd10237 89 YDAKRFIGKTFTKEELEEEAKRYPFKVVNDNIGSAFfeVPLNGSTLvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 193 PAYFNDAQRQATKDAGKIAGLDVQRIINEPTAAALSYGMNNKEGV--IAVFDLGGGTFDVSILEISSGVFEVKATNGDTF 270
Cdd:cd10237 169 PAEFDEKQRNATRKAANLAGLEVLRVINEPTAAAMAYGLHKKSDVnnVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 271 LGGEDFDNTLLEYLVNEFKRSDNIDLTkDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHL-NITLTRSKF 349
Cdd:cd10237 249 LGGQDFNQRLFQYLIDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKfKEEITRDLF 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30691626 350 EGLVGKLIERTRSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRG 428
Cdd:cd10237 328 ETLNEDLFQRVLEPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
54-629 |
1.04e-110 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 346.46 E-value: 1.04e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGeLLVGTpakrqavtnpTNTIFGSKRLIGRRFDDP-QT 132
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN-FTIGN----------NKGLRSIKRLFGKTLKEIlNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 QKEMKMVPYKIVKAPNGDAWVEANgQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAG 212
Cdd:PRK01433 90 PALFSLVKDYLDVNSSELKLNFAN-KQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 213 LDVQRIINEPTAAALSYGMN-NKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLVNEFKRS 291
Cdd:PRK01433 169 FEVLRLIAEPTAAAYAYGLNkNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNKFDLP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 292 DNIDLTkdnlalqrlrEAAEKAKielssttQTEINLPFITADasgakhlNITLTRSKFEGLVGKLIERTRSPCQNCLKDA 371
Cdd:PRK01433 249 NSIDTL----------QLAKKAK-------ETLTYKDSFNND-------NISINKQTLEQLILPLVERTINIAQECLEQA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 372 GVtiKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVVPLSLGIETLGAV 451
Cdd:PRK01433 305 GN--PNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGMELYGGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 452 FTKLIPRNTTIPTKKSQVFSTAADNQMQVGIKVLQGEREMAADNKVLGEFDLVGIPPAPRGMPQIEVTFDIDANGITTVS 531
Cdd:PRK01433 383 VEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 532 AKDKATGKEQNITIRSSGGLSDDEINRMVKEAELNAQKDQEKKQLIDLRNSADTTIYSVEKSLSEYREKIPAEIASEIET 611
Cdd:PRK01433 463 AYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISIINS 542
|
570
....*....|....*...
gi 30691626 612 AVSDLRTAMAGEDVEDIK 629
Cdd:PRK01433 543 LLDNIKEAVHARDIILIN 560
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
55-422 |
2.41e-110 |
|
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: 337.99 E-value: 2.41e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKgELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQK 134
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEK-ERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 135 EMKMVPYKIVKAPNGDAWVEAN----GQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKI 210
Cdd:cd11732 80 EIKLLPFKLVELEDGKVGIEVSyngeEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 211 AGLDVQRIINEPTAAALSYGM-------NNKEGVIAVF-DLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLE 282
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIyksdlleSEEKPRIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 283 YLVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADasgaKHLNITLTRSKFEGLVGKLIERTRS 362
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMED----IDFSGQIKREEFEELIQPLLARLEA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 363 PCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQ 422
Cdd:cd11732 316 PIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQ 375
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
54-426 |
2.05e-106 |
|
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: 328.05 E-value: 2.05e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKgELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDN-EKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKApNGDAW--VEANGQK--FSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGK 209
Cdd:cd10238 81 ELKKESKCKIIEK-DGKPGyeIELEEKKklVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGM----NNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYLV 285
Cdd:cd10238 160 KAGFNVLRVISEPSAAALAYGIgqddPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 286 NEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTtqteinlpfITADAS-----GAKHLNITLTRSKFEGLVGKLIERT 360
Cdd:cd10238 240 SEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTL---------NTATCSveslyDGMDFQCNVSRARFESLCSSLFQQC 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30691626 361 RSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIF-GKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd10238 311 LEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
55-422 |
3.12e-102 |
|
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: 317.29 E-value: 3.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLvGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQK 134
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSM-GVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 135 EMKMVPYKIVKAPNGDAWVEAN----GQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKI 210
Cdd:cd10228 80 ELKHLPYKVVKLPNGSVGIKVQylgeEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 211 AGLDVQRIINEPTAAALSYGMNN--------KEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLE 282
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGIYKqdlpaeeeKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 283 YLVNEFKRSDNIDLTKDNLALQRLREAAEKAKiELSSTTQTEINLP---FIT-ADASGakhlniTLTRSKFEGLVGKLIE 358
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATELPLNiecFMDdKDVSG------KMKRAEFEELCAPLFA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30691626 359 RTRSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQ 422
Cdd:cd10228 313 RVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
54-426 |
8.34e-98 |
|
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: 306.16 E-value: 8.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKgELLVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEK-QRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEA--NGQK--FSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGK 209
Cdd:cd24095 82 RDLKLFPFKVTEGPDGEIGINVnyLGEQkvFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGM------NNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEY 283
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGIyktdlpETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 284 LVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADasgaKHLNITLTRSKFEGLVGKLIERTRSP 363
Cdd:cd24095 242 FAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMED----KDVKGMITREEFEELAAPLLERLLEP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30691626 364 CQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd24095 318 LEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
55-426 |
5.08e-93 |
|
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: 293.51 E-value: 5.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLvGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQK 134
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYL-GEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 135 EMKMVPYKIVKApNGDAWVEAN----GQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKI 210
Cdd:cd24094 80 EEKYFTAKLVDA-NGEVGAEVNylgeKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 211 AGLDVQRIINEPTAAALSYGMN--------NKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLE 282
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITktdlpepeEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 283 YLVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHlnitLTRSKFEGLVGKLIERTRS 362
Cdd:cd24094 239 HFADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSM----LKREEFEELIAPLLERVTA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30691626 363 PCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd24094 315 PLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
54-423 |
1.12e-76 |
|
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: 249.33 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVS-VMEGKTARVIENAEGSRTTPSVVAMnQKGELLVGTPAKRQAVTNPTNTIFGSKRLIGrrfddpqt 132
Cdd:cd10230 2 VLGIDLGSEFIKVAlVKPGVPFEIVLNEESKRKTPSAVAF-RNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 qkemkmvpykivkapngdawveangqkFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAG 212
Cdd:cd10230 73 ---------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 213 LDVQRIINEPTAAALSYGMNNKEGV-----IAVFDLGGGTFDVSILEISS------------GVFEVKATNGDTFLGGED 275
Cdd:cd10230 126 LNVLSLINDNTAAALNYGIDRRFENnepqnVLFYDMGASSTSATVVEFSSvkekdkgknktvPQVEVLGVGWDRTLGGLE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 276 FDNTLLEYLVNEFKRS--DNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADasgaKHLNITLTRSKFEGLV 353
Cdd:cd10230 206 FDLRLADHLADEFNEKhkKDKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDD----IDFRTKITREEFEELC 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30691626 354 GKLIERTRSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPC-KGVNPDEAVAMGAAIQG 423
Cdd:cd10230 282 ADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELgKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
54-422 |
1.51e-75 |
|
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: 247.47 E-value: 1.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELlVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRT-IGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEA----NGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGK 209
Cdd:cd11739 81 KEKENLSYDLVPLKNGGVGVKVmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGM--------NNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLL 281
Cdd:cd11739 161 IVGLNCLRLMNDMTAVALNYGIykqdlpapDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 282 EYLVNEFKRSDNIDLTKDNLALQRLREAAEKAKiELSSTTQTEINLP---FIT-ADASGakhlniTLTRSKFEGLVGKLI 357
Cdd:cd11739 241 EHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLPLNiecFMNdKDVSG------KMNRSQFEELCADLL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30691626 358 ERTRSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQ 422
Cdd:cd11739 314 QRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
54-425 |
1.77e-73 |
|
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: 242.15 E-value: 1.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELlVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRS-IGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEA----NGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGK 209
Cdd:cd11737 81 AEKPSLAYELVQLPTGTTGIKVmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGM--------NNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLL 281
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIykqdlpapEEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 282 EYLVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSS-TTQTEINLP-FIT-ADASGakhlniTLTRSKFEGLVGKLIE 358
Cdd:cd11737 241 NHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIEcFMNdIDVSG------TMNRGQFEEMCADLLA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30691626 359 RTRSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGI 425
Cdd:cd11737 315 RVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
54-426 |
1.09e-72 |
|
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: 240.20 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELlVGTPAKRQAVTNPTNTIFGSKRLIGRRFDDPQTQ 133
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRA-IGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 134 KEMKMVPYKIVKAPNGDAWVEA----NGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGK 209
Cdd:cd11738 81 AEKIKLPYELQKMPNGSTGVKVryldEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGM--------NNKEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLL 281
Cdd:cd11738 161 IAGLNCLRLMNETTAVALAYGIykqdlpalEEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 282 EYLVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSS-TTQTEINLPFITADASGAKHLNitltRSKFEGLVGKLIERT 360
Cdd:cd11738 241 DYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMN----RAQFEELCASLLARV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30691626 361 RSPCQNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd11738 317 EPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
54-426 |
1.83e-69 |
|
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: 230.33 E-value: 1.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVS--VMEGKtARVIENAEGSRTTPSVVAMNqKGELLVGTPAKRQAVTNPTNTIFGSKRLIGRrfddpq 131
Cdd:cd10232 2 VIGISFGNSNSSIAiiNKDGR-AEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLGT------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 132 tqkemkmvpykivkapngdawveangQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIA 211
Cdd:cd10232 74 --------------------------TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 212 GLDVQRIINEPTAAALSYGMNN-------KEGVIAVFDLGGGTFDVSILEISSGVFEVKATNGDTFLGGEDFDNTLLEYL 284
Cdd:cd10232 128 GLEVLQLIPEPAAAALAYDLRAetsgdtiKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 285 VNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEInlpFITADASGAKhLNITLTRSKFEGLVGKLIERTRSPC 364
Cdd:cd10232 208 AKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPC---SVESLADGID-FHSSINRTRYELLASKVFQQFADLV 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30691626 365 QNCLKDAGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKS----PCKGVNPDEAVAMGAAIQGGIL 426
Cdd:cd10232 284 TDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEStiirAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
55-421 |
4.25e-53 |
|
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: 185.77 E-value: 4.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTarvienaegsrttpsvvamnqkgellvgtpakrqavtnptntifGSKRLIGRRFDDPQTQK 134
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGP--------------------------------------------GEPPLVVLQLPWPGGDG 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 135 EMKMVPykivkapngdawveangqkfSPSQIGANVLTKMKETAEAYLGKSIN-------KAVVTVPAYFNDAQRQATKDA 207
Cdd:cd10170 37 GSSKVP--------------------SVLEVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALREA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 208 GKIAGLDVQ----RIINEPTAAALSYGMNNKEG-------VIAVFDLGGGTFDVSILEISSGVFEVK---ATNGDTFLGG 273
Cdd:cd10170 97 ARAAGFGSDsdnvRLVSEPEAAALYALEDKGDLlplkpgdVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALLGG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 274 EDFDNTLLEYLVNEFKRSDNIDLTKDNLALQRLREAAEKAKIELSSTTQTEINLPFITADASGAKHLnITLTRSKFEGLV 353
Cdd:cd10170 177 TDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPELGL-EKGTLLLTEEEI 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30691626 354 GKLIERTRSPCQNCLKDAGVT--IKEVDEVLLVGGMTRVPKVQEIVSEIFGKSPCKGV----NPDEAVAMGAAI 421
Cdd:cd10170 256 RDLFDPVIDKILELIEEQLEAksGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
55-420 |
1.75e-40 |
|
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: 153.20 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVVAMNQKGELLVGTP-----AKRQAVTNPTNT-IFGS-KRLIGRRF 127
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGAESIyfgndAIDAYLNDPEEGrLIKSvKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 128 DDPQTqkemkmvpykivkapngdawveANGQKFSPSQIGANVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQAT--- 204
Cdd:cd10231 81 FDETT----------------------IFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqa 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 205 ----KDAGKIAGLDVQRIINEPTAAALSY-GMNNKEGVIAVFDLGGGTFDVSILEISSGVFE----VKATNGDtFLGGED 275
Cdd:cd10231 139 esrlRDAARRAGFRNVEFQYEPIAAALDYeQRLDREELVLVVDFGGGTSDFSVLRLGPNRTDrradILATSGV-GIGGDD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 276 FDNTLLEYLV-------NEFKRSDNI---------DL----------TKDNLAL-------------------------- 303
Cdd:cd10231 218 FDRELALKKVmphlgrgSTYVSGDKGlpvpawlyaDLsnwhaisllyTKKTLRLlldlrrdaadpekierllslvedqlg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 304 QRLREAAEKAKIELSSTTQTEINLPFITAdasgakHLNITLTRSKFEGLVGKLIERTRSPCQNCLKDAGVTIKEVDEVLL 383
Cdd:cd10231 298 HRLFRAVEQAKIALSSADEATLSFDFIEI------SIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFL 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 30691626 384 VGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMGAA 420
Cdd:cd10231 372 TGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
54-423 |
7.21e-19 |
|
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: 88.87 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 54 VIGIDLGTTNSCVSVM---EGKTARVIENAEG------SRTTPSVVAMNQKGELL-VGTPAKRQAvtnptntifgskrli 123
Cdd:cd10229 2 VVAIDFGTTYSGYAYSfitDPGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHsFGYEAREKY--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 124 gRRFDDPQTQK-----EMKMVPYKIVKAPNGDAWVEANGQKFSPSQIGANVLTKMKETAEAYLGKSINKA--------VV 190
Cdd:cd10229 67 -SDLAEDEEHQwlyffKFKMMLLSEKELTRDTKVKAVNGKSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 191 TVPAYFNDAQ----RQATKDAGKIAGLDVQR--IINEPTAAALSYGMNNKEGVIA---------VFDLGGGTFDVSILEI 255
Cdd:cd10229 146 TVPAIWSDAAkqfmREAAVKAGLISEENSEQliIALEPEAAALYCQKLLAEGEEKelkpgdkylVVDCGGGTVDITVHEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 256 SS--GVFEVKATNGDTFlGGEDFDNTLLEYLVNEFkRSDNIDLTKDN--LALQRLREAAEKAKielssttqteinlpfit 331
Cdd:cd10229 226 LEdgKLEELLKASGGPW-GSTSVDEEFEELLEEIF-GDDFMEAFKQKypSDYLDLLQAFERKK----------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 332 adasgaKHLNITLTRSKFEGLVGKLIERTRspcqNCLKD--AGVTIKEVDEVLLVGGMTRVPKVQEIVSEIFGKS----- 404
Cdd:cd10229 287 ------RSFKLRLSPELMKSLFDPVVKKII----EHIKEllEKPELKGVDYIFLVGGFAESPYLQKAVKEAFSTKvkiii 356
|
410
....*....|....*....
gi 30691626 405 PckgVNPDEAVAMGAAIQG 423
Cdd:cd10229 357 P---PEPGLAVVKGAVLFG 372
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
55-405 |
1.55e-12 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 70.28 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVMEGKTARVIENAEGSRTTPSVV-AMNQK--GELL-----VGTPAK-RQAV--------------TN 111
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLcAPTREavSEWLyrhldVPAYDDeRQALlrrairynreedidVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 112 PTNTIFGsKRLIGRRFDDPQTqkemkmVPYkiVKAPNgdAWVEANGQKfsPSQIG--ANVLTKM----KETAEAYLGKSI 185
Cdd:PRK11678 83 AQSVFFG-LAALAQYLEDPEE------VYF--VKSPK--SFLGASGLK--PQQVAlfEDLVCAMmlhiKQQAEAQLQAAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 186 NKAVVTVPAYFN-----DAQRQAT---KDAGKIAGL-DVqRIINEPTAAALSYGMN-NKEGVIAVFDLGGGTFDVSILEI 255
Cdd:PRK11678 150 TQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFkDV-EFQFEPVAAGLDFEATlTEEKRVLVVDIGGGTTDCSMLLM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 256 SSGvFEVKATNGDTFL-------GGEDFD--------------NTLLE-------------YLVN------EFKRSDNI- 294
Cdd:PRK11678 229 GPS-WRGRADRSASLLghsgqriGGNDLDialafkqlmpllgmGSETEkgialpslpfwnaVAINdvpaqsDFYSLANGr 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 295 ---DLTKDN---------LALQ------RLREAAEKAKIELSSTTQTEINLPFITADasgakhLNITLTRSKFEGLVGKL 356
Cdd:PRK11678 308 llnDLIRDArepekvarlLKVWrqrlsyRLVRSAEEAKIALSDQAETRASLDFISDG------LATEISQQGLEEAISQP 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 30691626 357 IERTRSPCQNCLKDAGVTikeVDEVLLVGGMTRVPKVQEIVSEIFGKSP 405
Cdd:PRK11678 382 LARILELVQLALDQAQVK---PDVIYLTGGSARSPLIRAALAQQLPGIP 427
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
55-319 |
1.59e-10 |
|
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: 62.88 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVmegKTARVIENaEgsrttPSVVAMNQK-GELL-VGTPAKRqavtnptntifgskrLIGRrfddpqT 132
Cdd:cd10225 2 IGIDLGTANTLVYV---KGKGIVLN-E-----PSVVAVDKNtGKVLaVGEEAKK---------------MLGR------T 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 QKEMKMV-PYKivkapngdawveaNGqkfspsqiganVLTKMkETAEAYLGKSINKA-----------VVTVPAYFNDAQ 200
Cdd:cd10225 52 PGNIVAIrPLR-------------DG-----------VIADF-EATEAMLRYFIRKAhrrrgflrprvVIGVPSGITEVE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 201 RQATKDAGKIAGLDVQRIINEPTAAALSYGMN--NKEGVIAVfDLGGGTFDVSIleIS-SGVFEVKATNgdtfLGGEDFD 277
Cdd:cd10225 107 RRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPieEPRGSMVV-DIGGGTTEIAV--ISlGGIVTSRSVR----VAGDEMD 179
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 30691626 278 NTLLEYLvnefKRSDNIDLTkdnlalqrlREAAEKAKIELSS 319
Cdd:cd10225 180 EAIINYV----RRKYNLLIG---------ERTAERIKIEIGS 208
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
165-411 |
5.62e-10 |
|
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: 60.36 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 165 IGA-NVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGLDVQRIINEPTAAALSYGMNNKegviAVFDL 243
Cdd:cd24047 43 IGAiRIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG----AVVDI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 244 GGGTFDVSILEisSGvfEVKATnGDTFLGGEDFDntlleyLVnefkrsdnidltkdnLALQRLREAAEKAKIELSSTTQT 323
Cdd:cd24047 119 GGGTTGIAVLK--DG--KVVYT-ADEPTGGTHLS------LV---------------LAGNYGISFEEAEIIKRDPARHK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 324 EInLPFITAdasgakhlnitltrskfeglvgkLIERTRSPCQNCLKDAgvtikEVDEVLLVGGMTRVPKVQEIVSEIFGK 403
Cdd:cd24047 173 EL-LPVVRP-----------------------VIEKMASIVKRHIKGY-----KVKDLYLVGGTCCLPGIEEVFEKETGL 223
|
....*...
gi 30691626 404 SPCKGVNP 411
Cdd:cd24047 224 PVYKPSNP 231
|
|
| PLN00130 |
PLN00130 |
succinate dehydrogenase (SDH3); Provisional |
1-64 |
1.04e-08 |
|
succinate dehydrogenase (SDH3); Provisional
Pssm-ID: 177741 [Multi-domain] Cd Length: 213 Bit Score: 55.92 E-value: 1.04e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30691626 1 MASVALLRSFRRREVQMASVSAFKSVSANGK---NSMFGKLGY--LARPFCSRPVGNDVIGIDLGTTNS 64
Cdd:PLN00130 1 MAATALFRSIRRRDVVSAPLSVYKSLAGNAQpswGSSYIGQNYasFSRAFGSKPVVNDILGTGLGTNNA 69
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
55-324 |
1.11e-08 |
|
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: 57.40 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVmEGKTARVIEnaegsrttPSVVAMNQK-GELL-VGTPAKRqavtnptntifgskrLIGRrfddpqt 132
Cdd:COG1077 10 IGIDLGTANTLVYV-KGKGIVLNE--------PSVVAIDKKtGKVLaVGEEAKE---------------MLGR------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 qkemkmVPYKIVkapngdawveangqkfspsqiganVLTKMK-------ETAEAYLGKSINKA-----------VVTVPA 194
Cdd:COG1077 59 ------TPGNIV------------------------AIRPLKdgviadfEVTEAMLKYFIKKVhgrrsffrprvVICVPS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 195 YFNDAQRQATKDAGKIAGL-DVqRIINEPTAAALSYGMNNKE--GVIAVfDLGGGTFDVSIleISSG--VFE--VKatng 267
Cdd:COG1077 109 GITEVERRAVRDAAEQAGArEV-YLIEEPMAAAIGAGLPIEEptGNMVV-DIGGGTTEVAV--ISLGgiVVSrsIR---- 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 268 dtfLGGEDFDNTLLEYLvnefKRSDNI---DLTkdnlalqrlreaAEKAKIELSSTTQTE 324
Cdd:COG1077 181 ---VAGDELDEAIIQYV----RKKYNLligERT------------AEEIKIEIGSAYPLE 221
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
55-327 |
1.53e-08 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 56.79 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVmEGKTARVIEnaegsrttPSVVAMNQK-GELL-VGTPAKRqavtnptntifgskrLIGRrfddpqT 132
Cdd:pfam06723 4 IGIDLGTANTLVYV-KGKGIVLNE--------PSVVAINTKtKKVLaVGNEAKK---------------MLGR------T 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 QKEMKMV-PYKivkapngdawveaNGqkfspsqiganVLTKMkETAEAYLGKSINKA-----------VVTVPAYFNDAQ 200
Cdd:pfam06723 54 PGNIVAVrPLK-------------DG-----------VIADF-EVTEAMLKYFIKKVhgrrsfskprvVICVPSGITEVE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 201 RQATKDAGKIAGLDVQRIINEPTAAALSYGMNNKEGV-IAVFDLGGGTFDVSILEISSGVfevkaTNGDTFLGGEDFDNT 279
Cdd:pfam06723 109 RRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTgNMVVDIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFDEA 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 30691626 280 LLEYLVNEFkrsdnidltkdNLAL-QRlreAAEKAKIELSSTTQTEINL 327
Cdd:pfam06723 184 IIKYIRKKY-----------NLLIgER---TAERIKIEIGSAYPTEEEE 218
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
165-254 |
3.91e-08 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 55.22 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 165 IGA-NVLTKMKETAEAYLGKSINKAVVTVPAYFNDAQRQATKDAGKIAGLDVQRIINEPTAAALSYGMNNKegviAVFDL 243
Cdd:PRK15080 67 IGAvTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG----AVVDI 142
|
90
....*....|.
gi 30691626 244 GGGTFDVSILE 254
Cdd:PRK15080 143 GGGTTGISILK 153
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
55-418 |
2.83e-07 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 52.99 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSvmeGKTARVIENAegsrttPSVVAMNQ--KGELLVGTPAKRqavtnptntifgskrLIGRrfddpqt 132
Cdd:PRK13929 7 IGIDLGTANILVY---SKNKGIILNE------PSVVAVDTetKAVLAIGTEAKN---------------MIGK------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 qkemkmVPYKIVKA-PNGDAWVeangqkfSPSQIGANVLTKMKETAEAYLGKSINK--AVVTVPAYFNDAQRQATKDAGK 209
Cdd:PRK13929 56 ------TPGKIVAVrPMKDGVI-------ADYDMTTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAVK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 210 IAGLDVQRIINEPTAAALSYGMNNKEGVI-AVFDLGGGTFDVSILEIsSGVFEVKATNgdtfLGGEDFDNTLLEYLVNEF 288
Cdd:PRK13929 123 NCGAKNVHLIEEPVAAAIGADLPVDEPVAnVVVDIGGGTTEVAIISF-GGVVSCHSIR----IGGDQLDEDIVSFVRKKY 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 289 krsdnidltkdNLALQrlREAAEKAKIELSSTTQTEINLpfiTADASGAKHLN-----ITLTRSKFEG----LVGKLIER 359
Cdd:PRK13929 198 -----------NLLIG--ERTAEQVKMEIGYALIEHEPE---TMEVRGRDLVTglpktITLESKEIQGamreSLLHILEA 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 360 TRSPCQNCLKDAGVTIkeVDE-VLLVGGMTRVPKVQEIVSEIFGKSPCKGVNPDEAVAMG 418
Cdd:PRK13929 262 IRATLEDCPPELSGDI--VDRgVILTGGGALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
55-324 |
4.55e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 52.44 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVmegKTARVIENaEgsrttPSVVAMNQK-GELL-VGTPAKRqavtnptntifgskrLIGRRFDDPQT 132
Cdd:PRK13930 11 IGIDLGTANTLVYV---KGKGIVLN-E-----PSVVAIDTKtGKVLaVGEEAKE---------------MLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 QKEMKmvpykivkapNGdawVEANgqkFspsqiganvltkmkETAEAYLGKSINKA-----------VVTVPAYFNDAQR 201
Cdd:PRK13930 67 IRPLK----------DG---VIAD---F--------------EATEAMLRYFIKKArgrrffrkpriVICVPSGITEVER 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 202 QATKDAGKIAGL-DVqRIINEPTAAALSYGMNNKEGVIA-VFDLGGGTFDVSIleIS-SGVfevkATNGDTFLGGEDFDN 278
Cdd:PRK13930 117 RAVREAAEHAGArEV-YLIEEPMAAAIGAGLPVTEPVGNmVVDIGGGTTEVAV--ISlGGI----VYSESIRVAGDEMDE 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 30691626 279 TLLEYLVNEFkrsdnidltkdNLAL-QRlreAAEKAKIELSSTTQTE 324
Cdd:PRK13930 190 AIVQYVRRKY-----------NLLIgER---TAEEIKIEIGSAYPLD 222
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
328-431 |
6.65e-07 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 52.53 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 328 PFITADASGAkHLNIT-------LTRSKFEGLVGKLIErtrspCQNCLKDAGVtikEVDEVLLVGGMTRVPKVQEIVSEI 400
Cdd:COG1070 348 PHWDPNARGA-FFGLTlshtrahLARAVLEGVAFALRD-----GLEALEEAGV---KIDRIRATGGGARSPLWRQILADV 418
|
90 100 110
....*....|....*....|....*....|.
gi 30691626 401 FGKsPCKGVNPDEAVAMGAAIQGGILRGDVK 431
Cdd:COG1070 419 LGR-PVEVPEAEEGGALGAALLAAVGLGLYD 448
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
55-289 |
1.87e-06 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 50.29 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVmEGKTARVIEnaegsrttPSVVAMN-QKGELL-VGTPAKRqavtnptntifgskrLIGRrfddpqt 132
Cdd:PRK13928 6 IGIDLGTANVLVYV-KGKGIVLNE--------PSVVAIDkNTNKVLaVGEEARR---------------MVGR------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 qkemkmvpykivkapngdawveangqkfSPSQIGAnvLTKMK-------ETAEAYLGKSINKA-----------VVTVPA 194
Cdd:PRK13928 55 ----------------------------TPGNIVA--IRPLRdgviadyDVTEKMLKYFINKAcgkrffskpriMICIPT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 195 YFNDAQRQATKDAGKIAGLDVQRIINEPTAAALSYGMNnkegvIA------VFDLGGGTFDVSILEISSGVfevkaTNGD 268
Cdd:PRK13928 105 GITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLD-----ISqpsgnmVVDIGGGTTDIAVLSLGGIV-----TSSS 174
|
250 260
....*....|....*....|.
gi 30691626 269 TFLGGEDFDNTLLEYLVNEFK 289
Cdd:PRK13928 175 IKVAGDKFDEAIIRYIRKKYK 195
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
55-319 |
1.10e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 44.70 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 55 IGIDLGTTNSCVSVmEGKTARVIEnaegsrttPSVVAMNQ-KGELL-VGTPAKRqavtnptntifgskrLIGRRFDDPQT 132
Cdd:PRK13927 8 LGIDLGTANTLVYV-KGKGIVLNE--------PSVVAIRTdTKKVLaVGEEAKQ---------------MLGRTPGNIVA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 133 QKEMKmvpykivkapNGdawVEANgqkFspsqiganvltkmkETAEAYLGKSINKA----------VVTVPAYFNDAQRQ 202
Cdd:PRK13927 64 IRPMK----------DG---VIAD---F--------------DVTEKMLKYFIKKVhknfrpsprvVICVPSGITEVERR 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691626 203 ATKDAGKIAGL-DVqRIINEPTAAALSYGMNNKE--GVIAVfDLGGGTFDVSIleIS-SGVfevkATNGDTFLGGEDFDN 278
Cdd:PRK13927 114 AVRESALGAGArEV-YLIEEPMAAAIGAGLPVTEptGSMVV-DIGGGTTEVAV--ISlGGI----VYSKSVRVGGDKFDE 185
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 30691626 279 TLLEYLVNEFkrsdnidltkdNLAL-QRlreAAEKAKIELSS 319
Cdd:PRK13927 186 AIINYVRRNY-----------NLLIgER---TAERIKIEIGS 213
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
368-428 |
1.33e-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: 44.85 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30691626 368 LKDAGVTIkevDEVLLVGGMTRVPKVQEIVSEIFGkSPCKGVNPDEAVAMGAAIQGGILRG 428
Cdd:cd07809 387 LRELGVEI---DEIRLIGGGSKSPVWRQILADVFG-VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| |
