|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
52-673 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1166.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 52 KGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRydDP 131
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 132 EVQKDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQI 211
Cdd:PRK00290 79 EVQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 212 SGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFK 291
Cdd:PRK00290 159 AGLEVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 292 RETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQ 371
Cdd:PRK00290 239 KENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 372 DAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLG 451
Cdd:PRK00290 319 DAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 452 GVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVH 531
Cdd:PRK00290 399 GVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 532 VSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKL 611
Cdd:PRK00290 479 VSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKI 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408360268 612 KEEISKMRALLAGKDSETgenIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTGEQKED 673
Cdd:PRK00290 559 EAAIKELKEALKGEDKEA---IKAKTEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDDVVD 617
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
51-676 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 1001.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 51 IKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDD 130
Cdd:PTZ00400 39 ATGDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 131 PEVQKDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQ 210
Cdd:PTZ00400 119 DATKKEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 211 ISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEF 290
Cdd:PTZ00400 199 IAGLDVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 291 KRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAM 370
Cdd:PTZ00400 279 KKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCEKCI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 371 QDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETL 450
Cdd:PTZ00400 359 KDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGIETL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 451 GGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIV 530
Cdd:PTZ00400 439 GGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIM 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 531 HVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNK 610
Cdd:PTZ00400 519 NISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDE 598
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 408360268 611 LKEEISKMRALLAgkdSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTGEQKEDQKE 676
Cdd:PTZ00400 599 LKQKITKLRSTLS---SEDVDSIKDKTKQLQEASWKISQQAYKQGNSDNQQSEQSTNSEESEEKND 661
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
55-653 |
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: 1000.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDdpEVQ 134
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 KDTKNVPFKiVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGL 214
Cdd:TIGR02350 80 EEAKRVPYK-VVGDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 215 NVLRVINEPTAAALAYGLDKS-EDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRE 293
Cdd:TIGR02350 159 EVLRIINEPTAAALAYGLDKSkKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 294 TGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQDA 373
Cdd:TIGR02350 239 EGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 374 EVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGV 453
Cdd:TIGR02350 319 GLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 454 FTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVS 533
Cdd:TIGR02350 399 MTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 534 AKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKE 613
Cdd:TIGR02350 479 AKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEK 558
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 408360268 614 EISKMRALLAGKDsetGENIRQAASSLQQASLKLFEMAYK 653
Cdd:TIGR02350 559 AVAELKEALKGED---VEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
55-653 |
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: 976.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQ 134
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFT-PKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 KDTKNVPFKIVRASNGDAWVEAH--GKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQIS 212
Cdd:pfam00012 80 RDIKHLPYKVVKLPNGDAGVEVRylGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 213 GLNVLRVINEPTAAALAYGLDKSE-DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFK 291
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDkERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 292 RETGVDLTKDNMALQRVREAAEKAKCELSSSvQTDINLPYLTMDASGpKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQ 371
Cdd:pfam00012 240 KKYGIDLSKDKRALQRLREAAEKAKIELSSN-QTNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 372 DAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG--DVTDVLLLDVTPLSLGIET 449
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIET 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 450 LGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGI 529
Cdd:pfam00012 398 LGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 530 VHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECN 609
Cdd:pfam00012 478 LTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKS 557
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 408360268 610 KLKEEISKMRALLAGKDSETgenIRQAASSLQQASLKLFEMAYK 653
Cdd:pfam00012 558 KVESAIEWLKDELEGDDKEE---IEAKTEELAQVSQKIGERMYQ 598
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
46-679 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 862.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 46 YASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADgERLVGMPAKRQAVTNPNNTFYATKRLIG 125
Cdd:PTZ00186 20 HESQKVQGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGS-EKLVGLAAKRQAITNPQSTFYAVKRLIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 126 RRYDDPEVQKDTKNVPFKIVRASNGDAWVE-AHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQA 204
Cdd:PTZ00186 99 RRFEDEHIQKDIKNVPYKIVRAGNGDAWVQdGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 205 TKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLR 284
Cdd:PTZ00186 179 TKDAGTIAGLNVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 285 HIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIA 364
Cdd:PTZ00186 259 YILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 365 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLS 444
Cdd:PTZ00186 339 PCKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 445 LGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDI 524
Cdd:PTZ00186 419 LGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDI 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 525 DANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLP 604
Cdd:PTZ00186 499 DANGICHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSD 578
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 408360268 605 ADECNkLKEEISKMRALLAGKDSeTGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTGEQKEDQKEEKQ 679
Cdd:PTZ00186 579 AEKEN-VKTLVAELRKAMENPNV-AKDDLAAATDKLQKAVMECGRTEYQQAAAANSGSSSNSGEQQQQQQQQQQQ 651
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
53-429 |
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: 860.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 53 GAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPE 132
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 VQKDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQIS 212
Cdd:cd11733 81 VQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 213 GLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKR 292
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 293 ETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQD 372
Cdd:cd11733 241 EQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLKD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 408360268 373 AEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 429
Cdd:cd11733 321 AGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVLA 377
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
53-662 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 838.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 53 GAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDdpE 132
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 VQKDTKNVPFKIVRASNGDAWVE--AHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQ 210
Cdd:CHL00094 80 ISEEAKQVSYKVKTDSNGNIKIEcpALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 211 ISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEF 290
Cdd:CHL00094 160 IAGLEVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 291 KRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAM 370
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 371 QDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETL 450
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 451 GGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIV 530
Cdd:CHL00094 400 GGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 531 HVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNK 610
Cdd:CHL00094 480 SVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEK 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 408360268 611 LKEEISKMRALLagkDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGS 662
Cdd:CHL00094 560 IENLIKKLRQAL---QNDNYESIKSLLEELQKALMEIGKEVYSSTSTTDPAS 608
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
53-662 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 826.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 53 GAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPE 132
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 VQKdtKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQIS 212
Cdd:PRK13411 82 EER--SRVPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 213 GLNVLRVINEPTAAALAYGLDK-SEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFK 291
Cdd:PRK13411 160 GLEVLRIINEPTAAALAYGLDKqDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 292 RETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQ 371
Cdd:PRK13411 240 QQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 372 DAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETL 450
Cdd:PRK13411 320 DAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 451 GGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIV 530
Cdd:PRK13411 400 GEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 531 HVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNK 610
Cdd:PRK13411 480 KVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQR 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 408360268 611 LKEEISKMRALLAGKDSETgENIRQAASSLQQASLKLFEMAYKKMASEREGS 662
Cdd:PRK13411 560 AEQKVEQLEAALTDPNISL-EELKQQLEEFQQALLAIGAEVYQQGGSQTTDT 610
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
53-660 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 799.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 53 GAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDdpE 132
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYD--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 VQKDTKNVPFKIVRASNGDAWVE--AHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQ 210
Cdd:PRK13410 80 LDPESKRVPYTIRRNEQGNVRIKcpRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 211 ISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEF 290
Cdd:PRK13410 160 IAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 291 KRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAM 370
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 371 QDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETL 450
Cdd:PRK13410 320 KDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 451 GGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIV 530
Cdd:PRK13410 400 GGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 531 HVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNK 610
Cdd:PRK13410 480 QVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAALEFGPYFAER 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 408360268 611 LKEEI-SKMRALLAGKDSETGENIRQAASSLQQAslkLFEMAyKKMASERE 660
Cdd:PRK13410 560 QRRAVeSAMRDVQDSLEQDDDRELDLAVADLQEA---LYGLN-REVRAEYK 606
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
55-562 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 768.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPevq 134
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 kdtknvpfkivrasngdaWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGL 214
Cdd:COG0443 78 ------------------ATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 215 NVLRVINEPTAAALAYGLDK-SEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRE 293
Cdd:COG0443 140 EVLRLLNEPTAAALAYGLDKgKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 294 TGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYltmdaSGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQDA 373
Cdd:COG0443 220 EGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 374 EVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDvllLDVTPLSLGIETLGGV 453
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIETLGGV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 454 FTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVS 533
Cdd:COG0443 372 FTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVS 451
|
490 500
....*....|....*....|....*....
gi 408360268 534 AKDKGTGREQQIVIqssgglsKDDIENMV 562
Cdd:COG0443 452 AKDLGTGKEQSITI-------KEEIERML 473
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
55-668 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 754.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDdpEVQ 134
Cdd:PLN03184 41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMS--EVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 KDTKNVPFKIVRASNGDAWVE--AHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQIS 212
Cdd:PLN03184 119 EESKQVSYRVVRDENGNVKLDcpAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 213 GLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKR 292
Cdd:PLN03184 199 GLEVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 293 ETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQD 372
Cdd:PLN03184 279 DEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVENALRD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 373 AEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGG 452
Cdd:PLN03184 359 AKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLGLETLGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 453 VFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHV 532
Cdd:PLN03184 439 VMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSV 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 533 SAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLK 612
Cdd:PLN03184 519 SATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVE 598
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 408360268 613 EEISKMRALLAGKDSETgenIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTG 668
Cdd:PLN03184 599 AKLKELKDAIASGSTQK---MKDAMAALNQEVMQIGQSLYNQPGAGGAGPAPGGEA 651
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
55-429 |
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: 732.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQ 134
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 KdtKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGL 214
Cdd:cd10234 81 R--KQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 215 NVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRET 294
Cdd:cd10234 159 EVLRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 295 GVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQDAE 374
Cdd:cd10234 239 GIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 408360268 375 VSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 429
Cdd:cd10234 319 LSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
53-430 |
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: 728.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 53 GAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPE 132
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 VQKDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQIS 212
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 213 GLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKR 292
Cdd:cd11734 161 GLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 293 ETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQD 372
Cdd:cd11734 241 ESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALKD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 408360268 373 AEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG 430
Cdd:cd11734 321 AGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
52-616 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 665.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 52 KGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDP 131
Cdd:PTZ00009 3 KGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 132 EVQKDTKNVPFKIVRASNGDAWVEAH----GKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKD 207
Cdd:PTZ00009 82 VVQSDMKHWPFKVTTGGDDKPMIEVTyqgeKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 208 AGQISGLNVLRVINEPTAAALAYGLDKSED--KVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRH 285
Cdd:PTZ00009 162 AGTIAGLNVLRIINEPTAAAIAYGLDKKGDgeKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 286 IVKEFKRET-GVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGpkhlNMKLTRAQFEGIVTDLIKRTIA 364
Cdd:PTZ00009 242 CVQDFKRKNrGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDY----NVTISRARFEELCGDYFRNTLQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 365 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVLAGD----VTDVLLLD 439
Cdd:PTZ00009 318 PVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 440 VTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIE 519
Cdd:PTZ00009 398 VTPLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 520 VTFDIDANGIVHVSAKDKGTGREQQIVIQSSGG-LSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEE 598
Cdd:PTZ00009 478 VTFDIDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD 557
|
570 580
....*....|....*....|
gi 408360268 599 --FKDQLPADECNKLKEEIS 616
Cdd:PTZ00009 558 ekVKGKLSDSDKATIEKAID 577
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
56-644 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 609.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGeRLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDpeVQK 135
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 136 DTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLN 215
Cdd:PRK05183 99 RYPHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 216 VLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEfkreTG 295
Cdd:PRK05183 179 VLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQ----AG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 296 VDLTKDNMALQRVREAAEKAKCELSSSVQTDINLpyltMDASGpkhlnmKLTRAQFEGIVTDLIKRTIAPCQKAMQDAEV 375
Cdd:PRK05183 255 LSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV----ALWQG------EITREQFNALIAPLVKRTLLACRRALRDAGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 376 SKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVT--DVLLLDVTPLSLGIETLGGV 453
Cdd:PRK05183 325 EADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKPdsDMLLLDVIPLSLGLETMGGL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 454 FTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVS 533
Cdd:PRK05183 405 VEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 534 AKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEED---RRKKE-RVEAVNMAEGiihdTETKMEEFKDQLPADECN 609
Cdd:PRK05183 485 AMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDmqaRALAEqKVEAERVLEA----LQAALAADGDLLSAAERA 560
|
570 580 590
....*....|....*....|....*....|....*
gi 408360268 610 KLKEEISKMRALLAGKDSETgenIRQAASSLQQAS 644
Cdd:PRK05183 561 AIDAAMAALREVAQGDDADA---IEAAIKALDKAT 592
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
55-644 |
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: 600.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPevq 134
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 KDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGL 214
Cdd:TIGR01991 78 KTFSILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 215 NVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKefkrET 294
Cdd:TIGR01991 158 NVLRLLNEPTAAAVAYGLDKASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILK----QL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 295 GVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGpkhlnmKLTRAQFEGIVTDLIKRTIAPCQKAMQDAE 374
Cdd:TIGR01991 234 GISADLNPEDQRLLLQAARAAKEALTDAESVEVDFTLDGKDFKG------KLTRDEFEALIQPLVQKTLSICRRALRDAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 375 VSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVT--DVLLLDVTPLSLGIETLGG 452
Cdd:TIGR01991 308 LSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIgnDLLLLDVTPLSLGIETMGG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 453 VFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHV 532
Cdd:TIGR01991 388 LVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 533 SAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLK 612
Cdd:TIGR01991 468 SAQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAID 547
|
570 580 590
....*....|....*....|....*....|..
gi 408360268 613 EEISKMRALLAGKDSETgenIRQAASSLQQAS 644
Cdd:TIGR01991 548 AAMEALQKALQGDDADA---IKAAIEALEEAT 576
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
55-428 |
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: 539.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQ 134
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFT-DGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 KDTKNVPFKIVRASNGDAWVEAHG----KLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQ 210
Cdd:cd24028 80 SDIKHWPFKVVEDEDGKPKIEVTYkgeeKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 211 ISGLNVLRVINEPTAAALAYGLDK--SEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVK 288
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDKksSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 289 EFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASgpkhLNMKLTRAQFEGIVTDLIKRTIAPCQK 368
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGID----FETTITRAKFEELCEDLFKKCLEPVEK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408360268 369 AMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVL 428
Cdd:cd24028 316 VLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
53-428 |
0e+00 |
|
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 534.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 53 GAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPE 132
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFT-DGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 VQKDTKNVPFKIVRaSNGDAWVEAHG----KLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDA 208
Cdd:cd10241 80 VQKDIKLLPFKIVN-KNGKPYIQVEVkgekKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 209 GQISGLNVLRVINEPTAAALAYGLDKSED-KVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIV 287
Cdd:cd10241 159 GTIAGLNVLRIINEPTAAAIAYGLDKKGGeKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 288 KEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLT--MDASGPkhlnmkLTRAQFEGIVTDLIKRTIAP 365
Cdd:cd10241 239 KLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFdgEDFSET------LTRAKFEELNMDLFRKTLKP 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 408360268 366 CQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVL 428
Cdd:cd10241 313 VQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
56-428 |
2.63e-173 |
|
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: 499.08 E-value: 2.63e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQK 135
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 136 DTKNVPFKIVraSNGDA---WVEAHG--KLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQ 210
Cdd:cd10233 81 DMKHWPFKVV--SGGDKpkiQVEYKGetKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 211 ISGLNVLRVINEPTAAALAYGLDK--SEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVK 288
Cdd:cd10233 159 IAGLNVLRIINEPTAAAIAYGLDKkgKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 289 EFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYL--TMDasgpkhLNMKLTRAQFEGIVTDLIKRTIAPC 366
Cdd:cd10233 239 EFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLfeGID------FYTSITRARFEELCADLFRSTLEPV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 408360268 367 QKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVL 428
Cdd:cd10233 313 EKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
56-429 |
3.77e-162 |
|
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: 469.75 E-value: 3.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVL-ENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEvq 134
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 kdtknvpfkivrasngdawvEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGL 214
Cdd:cd24029 79 --------------------EIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 215 NVLRVINEPTAAALAYGLDK-SEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRE 293
Cdd:cd24029 139 NVLRLINEPTAAALAYGLDKeGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 294 TGV-DLTKDNMALQRVREAAEKAKCELSSSVQTDINLPyltmDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQD 372
Cdd:cd24029 219 TGIlDDKEDERARARLREAAEEAKIELSSSDSTDILIL----DDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 408360268 373 AEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 429
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
55-430 |
1.43e-161 |
|
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: 469.00 E-value: 1.43e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDpeVQ 134
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 KDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGL 214
Cdd:cd10236 82 EELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 215 NVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKefkrET 294
Cdd:cd10236 162 NVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILK----QI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 295 GVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPkhlnmkLTRAQFEGIVTDLIKRTIAPCQKAMQDAE 374
Cdd:cd10236 238 GIDARLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWERE------ITREEFEELIQPLVKRTLEPCRRALKDAG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 408360268 375 VSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG 430
Cdd:cd10236 312 LEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
56-428 |
6.41e-149 |
|
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: 437.11 E-value: 6.41e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGkQAKVLENAEGARTTPSVVAFTADgERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQK 135
Cdd:cd24093 2 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 136 DTKNVPFKIVRaSNGDAWVEAH----GKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQI 211
Cdd:cd24093 80 DMKTWPFKVID-VNGNPVIEVQylgeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 212 SGLNVLRVINEPTAAALAYGLD--KSE-DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVK 288
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGagKSEkERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 289 EFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLtmdaSGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQK 368
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSL----FDGEDFESSITRARFEDLNAALFKSTLEPVEQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408360268 369 AMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVL 428
Cdd:cd24093 315 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
55-430 |
2.12e-130 |
|
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: 390.93 E-value: 2.12e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGK--QAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPE 132
Cdd:cd10237 24 IVGIDLGTTYSCVGVYHAVtgEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 VQKDTKNVPFKIVRASNGDAWVEAHG----KLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDA 208
Cdd:cd10237 104 LEEEAKRYPFKVVNDNIGSAFFEVPLngstLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 209 GQISGLNVLRVINEPTAAALAYGLDKSED-KVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIV 287
Cdd:cd10237 184 ANLAGLEVLRVINEPTAAAMAYGLHKKSDvNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 288 KEFKRETGVDLTkDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHL-NMKLTRAQFEGIVTDLIKRTIAPC 366
Cdd:cd10237 264 DRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKfKEEITRDLFETLNEDLFQRVLEPI 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 408360268 367 QKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG 430
Cdd:cd10237 343 RQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
56-430 |
3.22e-126 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar proteins; Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. Members in this subfamily belong to the heat shock protein 70 (Hsp70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, Hsp70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Two genes in the vicinity of the HscC gene code for potential cochaperones: J-domain containing proteins, DjlB/YbeS and DjlC/YbeV. HscC and its co-chaperone partners may play a role in the SOS DNA damage response. HscC does not appear to require a NEF.
Pssm-ID: 466833 [Multi-domain] Cd Length: 343 Bit Score: 377.74 E-value: 3.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRryddpevqk 135
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMGT--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 136 dtknvpfkivrasngDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLN 215
Cdd:cd10235 72 ---------------DKQYRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 216 VLRVINEPTAAALAYGLDK-SEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRET 294
Cdd:cd10235 137 VERLINEPTAAALAYGLHKrEDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 295 GVDLTKDNMALqrvREAAEKAKCELSSSVQTDINLPYltmdasGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQDAE 374
Cdd:cd10235 217 TSLSPSELAAL---RKRAEQAKRQLSSQDSAEIRLTY------RGEELEIELTREEFEELCAPLLERLRQPIERALRDAG 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 408360268 375 VSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG 430
Cdd:cd10235 288 LKPSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
55-654 |
5.82e-116 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 359.94 E-value: 5.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 55 VVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGerlvgmpakrqAVTNPNNTFYATKRLIGRryddpeVQ 134
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN-----------FTIGNNKGLRSIKRLFGK------TL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 135 KDTKNVP--FKIVR----ASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDA 208
Cdd:PRK01433 84 KEILNTPalFSLVKdyldVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 209 GQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVK 288
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 289 EFkretgvDLTKDNMALQrvreAAEKAKcelsssvQTDINLPYLTMDasgpkhlNMKLTRAQFEGIVTDLIKRTIAPCQK 368
Cdd:PRK01433 244 KF------DLPNSIDTLQ----LAKKAK-------ETLTYKDSFNND-------NISINKQTLEQLILPLVERTINIAQE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 369 AMQDAevSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIE 448
Cdd:PRK01433 300 CLEQA--GNPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGME 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 449 TLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANG 528
Cdd:PRK01433 378 LYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 529 IVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADec 608
Cdd:PRK01433 458 ILSVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSES-- 535
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 408360268 609 nklkeEISKMRALLagkdsetgENIRQAASS----LQQASLKLFEMAYKK 654
Cdd:PRK01433 536 -----EISIINSLL--------DNIKEAVHArdiiLINNSIKEFKSKIKK 572
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
56-424 |
8.56e-111 |
|
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: 339.15 E-value: 8.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQK 135
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFT-EKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 136 DTKNVPFKIVRASNGDAWVEAHGK----LYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQI 211
Cdd:cd11732 80 EIKLLPFKLVELEDGKVGIEVSYNgeevVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 212 SGLNVLRVINEPTAAALAYGLDKS-----EDK--VIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLR 284
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSdllesEEKprIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 285 HIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDasgpKHLNMKLTRAQFEGIVTDLIKRTIA 364
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMED----IDFSGQIKREEFEELIQPLLARLEA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 365 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQ 424
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; ... |
54-428 |
3.33e-107 |
|
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: 329.97 E-value: 3.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 54 AVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEV 133
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFT-DNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 134 QKDTKNVPFKIVRaSNGDAW--VEAHGK--LYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAG 209
Cdd:cd10238 80 QELKKESKCKIIE-KDGKPGyeIELEEKkkLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 210 QISGLNVLRVINEPTAAALAYGL---DKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHI 286
Cdd:cd10238 159 EKAGFNVLRVISEPSAAALAYGIgqdDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 287 VKEFKRETGVDLTKDNMALQRVREAAEKAKCELSS--SVQTDINLPYLTMDasgpkhLNMKLTRAQFEGIVTDLIKRTIA 364
Cdd:cd10238 239 ASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTlnTATCSVESLYDGMD------FQCNVSRARFESLCSSLFQQCLE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408360268 365 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFgraPSKAV----NPDEAVAIGAAIQGGVL 428
Cdd:cd10238 313 PIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLF---PSAEVlssiPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
53-428 |
7.02e-104 |
|
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: 321.57 E-value: 7.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 53 GAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPE 132
Cdd:cd24095 1 MSVVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFG-EKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 VQKDTKNVPFKIVRASNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDA 208
Cdd:cd24095 80 VQRDLKLFPFKVTEGPDGEIGINVnylgEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 209 GQISGLNVLRVINEPTAAALAYG-----LDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALL 283
Cdd:cd24095 160 AQIAGLNCLRLMNETTATALAYGiyktdLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 284 RHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDasgpKHLNMKLTRAQFEGIVTDLIKRTI 363
Cdd:cd24095 240 DHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMED----KDVKGMITREEFEELAAPLLERLL 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 408360268 364 APCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVL 428
Cdd:cd24095 316 EPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
56-424 |
9.28e-103 |
|
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: 318.45 E-value: 9.28e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQK 135
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFG-EKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 136 DTKNVPFKIVRASNGDAWVEAH----GKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQI 211
Cdd:cd10228 80 ELKHLPYKVVKLPNGSVGIKVQylgeEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 212 SGLNVLRVINEPTAAALAYG-----LDKSEDK--VIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLR 284
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGiykqdLPAEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 285 HIVKEFKRETGVDLTKDNMALQRVREAAEKAKcELSSSVQTDI--NLPYLTMDasgpKHLNMKLTRAQFEGIVTDLIKRT 362
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATELplNIECFMDD----KDVSGKMKRAEFEELCAPLFARV 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408360268 363 IAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQ 424
Cdd:cd10228 315 EVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
56-429 |
1.04e-92 |
|
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: 292.74 E-value: 1.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFtADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQK 135
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGF-GPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 136 DTKNVPFKIVRAsNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQI 211
Cdd:cd24094 80 EEKYFTAKLVDA-NGEVGAEVnylgEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 212 SGLNVLRVINEPTAAALAYGLDKS-----EDK--VIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLR 284
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKTdlpepEEKprIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 285 HIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLT--MDASGpkhlnmKLTRAQFEGIVTDLIKRT 362
Cdd:cd24094 239 HFADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMndIDVSS------MLKREEFEELIAPLLERV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 408360268 363 IAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 429
Cdd:cd24094 313 TAPLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
54-425 |
8.15e-84 |
|
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: 268.21 E-value: 8.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 54 AVVGIDLGTTNSCVA-VMEGKQAKVLENAEGARTTPSVVAFtADGERLVGMPAKRQAVTNPNNTFYATKRLIGrryddpe 132
Cdd:cd10230 1 AVLGIDLGSEFIKVAlVKPGVPFEIVLNEESKRKTPSAVAF-RNGERLFGDDALALATRFPENTFSYLKDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 vqkdtknvpfkivrasngdawveahgklYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQIS 212
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 213 GLNVLRVINEPTAAALAYGLDK----SEDKVIAVYDLGGGTFDISILEIQ------------KGVFEVKSTNGDTFLGGE 276
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRrfenNEPQNVLFYDMGASSTSATVVEFSsvkekdkgknktVPQVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 277 DFDQALLRHIVKEFKRETG--VDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDasgpKHLNMKLTRAQFEGI 354
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKkdKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDD----IDFRTKITREEFEEL 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408360268 355 VTDLIKRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAP-SKAVNPDEAVAIGAAIQG 425
Cdd:cd10230 281 CADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
54-424 |
2.07e-80 |
|
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: 260.18 E-value: 2.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 54 AVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADgERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEV 133
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSK-NRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 134 QKDTKNVPFKIVRASNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAG 209
Cdd:cd11739 80 QKEKENLSYDLVPLKNGGVGVKVmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 210 QISGLNVLRVINEPTAAALAYGLDKSE-------DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQAL 282
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIYKQDlpapdekPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 283 LRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKcELSSSVQTDI--NLPYLTMDasgpKHLNMKLTRAQFEGIVTDLIK 360
Cdd:cd11739 240 VEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLplNIECFMND----KDVSGKMNRSQFEELCADLLQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 408360268 361 RTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQ 424
Cdd:cd11739 315 RIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
54-424 |
1.51e-76 |
|
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: 250.24 E-value: 1.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 54 AVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADgERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEV 133
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPK-NRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 134 QKDTKNVPFKIVRASNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAG 209
Cdd:cd11737 80 QAEKPSLAYELVQLPTGTTGIKVmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 210 QISGLNVLRVINEPTAAALAYGLDKS-----EDK--VIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQAL 282
Cdd:cd11737 160 QIAGLNCLRLMNETTAVALAYGIYKQdlpapEEKprNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 283 LRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELS---SSVQTDINLPYLTMDASGpkhlnmKLTRAQFEGIVTDLI 359
Cdd:cd11737 240 VNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSanaSDLPLNIECFMNDIDVSG------TMNRGQFEEMCADLL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 408360268 360 KRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQ 424
Cdd:cd11737 314 ARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
54-429 |
2.19e-74 |
|
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: 244.44 E-value: 2.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 54 AVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADgERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEV 133
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSR-NRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 134 QKDTKNVPFKIVRASNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAG 209
Cdd:cd11738 80 QAEKIKLPYELQKMPNGSTGVKVryldEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 210 QISGLNVLRVINEPTAAALAYGLDK-----SEDK---VIAVyDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQA 281
Cdd:cd11738 160 QIAGLNCLRLMNETTAVALAYGIYKqdlpaLEEKprnVVFV-DMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 282 LLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELS---SSVQTDINLPYLTMDASGpkhlnmKLTRAQFEGIVTDL 358
Cdd:cd11738 239 LVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSanaSDLPLNIECFMNDIDVSS------KMNRAQFEELCASL 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408360268 359 IKRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 429
Cdd:cd11738 313 LARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
54-428 |
1.03e-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: 231.10 E-value: 1.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 54 AVVGIDLGTTNSCVAVMEGKQ-AKVLENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPNNTFYATKRLIGRryddpe 132
Cdd:cd10232 1 VVIGISFGNSNSSIAIINKDGrAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLGT------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 133 vqkdtknvpfkivrasngdawveahgKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQIS 212
Cdd:cd10232 74 --------------------------TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 213 GLNVLRVINEPTAAALAYGL------DKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHI 286
Cdd:cd10232 128 GLEVLQLIPEPAAAALAYDLraetsgDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 287 VKEFKRETGVDLTKDNMALQRVREAAEKAKCELS--SSVQTDINLPYLTMDASGpkhlnmKLTRAQFEGIVTDLIKRTIA 364
Cdd:cd10232 208 AKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSqgTSAPCSVESLADGIDFHS------SINRTRYELLASKVFQQFAD 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408360268 365 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSK----AVNPDEAVAIGAAIQGGVL 428
Cdd:cd10232 282 LVTDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
56-423 |
4.88e-54 |
|
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: 188.47 E-value: 4.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLE---------NAEGARTTPSVVAFTADgerlvgmpakrqavtnpnntfyatkrligr 126
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLvvlqlpwpgGDGGSSKVPSVLEVVAD------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 127 ryddpevqkdtknvpfkivrasngdawveahgklyspsqigafVLMKMKETAENYLGHTAKNA-------VITVPAYFND 199
Cdd:cd10170 51 -------------------------------------------FLRALLEHAKAELGDRIWELekapievVITVPAGWSD 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 200 SQRQATKDAGQISGL----NVLRVINEPTAAALAYGLDKS------EDKVIAVYDLGGGTFDISILEIQKGVFEVK---S 266
Cdd:cd10170 88 AAREALREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGdllplkPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevA 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 267 TNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNmKL 346
Cdd:cd10170 168 PGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPELGLE-KG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 347 TRAQFEGIVTDLIKRTIAPCQKAMQDA--EVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAV----NPDEAVAIG 420
Cdd:cd10170 247 TLLLTEEEIRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARG 326
|
...
gi 408360268 421 AAI 423
Cdd:cd10170 327 AAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
56-422 |
1.14e-35 |
|
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: 139.33 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERL-----VGMPAKRQAVTNPnntfyATKRLIgrrydd 130
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGaesiyFGNDAIDAYLNDP-----EEGRLI------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 131 pevqkdtKNVpfKIVRASNG--DAWVeaHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQAT--- 205
Cdd:cd10231 70 -------KSV--KSFLGSSLfdETTI--FGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqa 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 206 ----KDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEI----QKGVFEVKSTNGDtFLGGED 277
Cdd:cd10231 139 esrlRDAARRAGFRNVEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLgpnrTDRRADILATSGV-GIGGDD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 278 FDQALLRHIV-KEFKRETG---------------VDL----------TKDNMAL-------------------------- 305
Cdd:cd10231 218 FDRELALKKVmPHLGRGSTyvsgdkglpvpawlyADLsnwhaisllyTKKTLRLlldlrrdaadpekierllslvedqlg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 306 QRVREAAEKAKCELSSSVQTDINLPYLtmdasgPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQDAEVSKSDIGEVIL 385
Cdd:cd10231 298 HRLFRAVEQAKIALSSADEATLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFL 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 408360268 386 VGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAA 422
Cdd:cd10231 372 TGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
54-425 |
4.28e-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: 89.64 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 54 AVVGIDLGTTNSCVAVM---EGKQAKVLENAEGA------RTTPSVVAFTADGErLV--GMPAKRQAVTNPNN---TFYA 119
Cdd:cd10229 1 VVVAIDFGTTYSGYAYSfitDPGDIHTMYNWWGAptgvssPKTPTCLLLNPDGE-FHsfGYEAREKYSDLAEDeehQWLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 120 TKRLIGRRYDDPEVQKDTKnvpfkiVRASNGDaWVEAHGKL-YSPSQIGAFVLMKMKETAENYLghTAKNA--VITVPAY 196
Cdd:cd10229 80 FFKFKMMLLSEKELTRDTK------VKAVNGK-SMPALEVFaEALRYLKDHALKELRDRSGSSL--DEDDIrwVLTVPAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 197 FNDSQ----RQATKDAGQISGLN--VLRVINEPTAAALAYGLDKSE---------DKVIaVYDLGGGTFDISILEIQK-- 259
Cdd:cd10229 151 WSDAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCQKLLAEgeekelkpgDKYL-VVDCGGGTVDITVHEVLEdg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 260 GVFEVKSTNGDTFlGGEDFDQA---LLR-----HIVKEFKRETGVDLTKdnmaLQRvreAAEKAKCelsssvqtdinlpy 331
Cdd:cd10229 230 KLEELLKASGGPW-GSTSVDEEfeeLLEeifgdDFMEAFKQKYPSDYLD----LLQ---AFERKKR-------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 332 lTMDasgpkhlnMKLTRAQFEGIVTDLIKRTIAPCQKAMQDAEVSKSDIgeVILVGGMTRMPKVQQTVQDLFGR-----A 406
Cdd:cd10229 288 -SFK--------LRLSPELMKSLFDPVVKKIIEHIKELLEKPELKGVDY--IFLVGGFAESPYLQKAVKEAFSTkvkiiI 356
|
410
....*....|....*....
gi 408360268 407 PskaVNPDEAVAIGAAIQG 425
Cdd:cd10229 357 P---PEPGLAVVKGAVLFG 372
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
56-423 |
3.25e-12 |
|
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: 67.88 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVmeGKQAKVLEnaEgarttPSVVAF-TADGERL-VGMPAKRqavtnpnntfyatkrLIGRRYDDPEV 133
Cdd:cd10225 2 IGIDLGTANTLVYV--KGKGIVLN--E-----PSVVAVdKNTGKVLaVGEEAKK---------------MLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 134 QKdtknvPFKivrasNG---DawVEAHGKLyspsqIGAFVlmkmkETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQ 210
Cdd:cd10225 58 IR-----PLR-----DGviaD--FEATEAM-----LRYFI-----RKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 211 ISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGGEDFDQALLRHIVKEF 290
Cdd:cd10225 116 HAGAREVYLIEEPMAAAIGAGLPIEEPRGSMVVDIGGGTTEIAVISLG-GIVTSRSVR----VAGDEMDEAIINYVRRKY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 291 KRETGvdltkdnmalqrvREAAEKAKCELSSSVQTDINlpyLTMDASG-------PKhlNMKLTRAQFEGIVTDLIKRTI 363
Cdd:cd10225 191 NLLIG-------------ERTAERIKIEIGSAYPLDEE---LSMEVRGrdlvtglPR--TIEITSEEVREALEEPVNAIV 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408360268 364 APCQKAMQDA--EVSkSDIGE--VILVGGMTRMPKVQQTVQDLFG----RAPskavNPDEAVAIGAAI 423
Cdd:cd10225 253 EAVRSTLERTppELA-ADIVDrgIVLTGGGALLRGLDELLREETGlpvhVAD----DPLTCVAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
56-423 |
1.86e-11 |
|
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: 65.87 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVmEGKQaKVLEnaEgarttPSVVAFTADGERL--VGMPAKRqavtnpnntfyatkrLIGRryddpev 133
Cdd:COG1077 10 IGIDLGTANTLVYV-KGKG-IVLN--E-----PSVVAIDKKTGKVlaVGEEAKE---------------MLGR------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 134 qkdtknVPFKIVrasngdawveahgklyspsqigafVLMKMK-------ETAENYLGHTAKNA-----------VITVPA 195
Cdd:COG1077 59 ------TPGNIV------------------------AIRPLKdgviadfEVTEAMLKYFIKKVhgrrsffrprvVICVPS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 196 YFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGG 275
Cdd:COG1077 109 GITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTGNMVVDIGGGTTEVAVISLG-GIVVSRSIR----VAG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 276 EDFDQALLRHIVKEFKRETGvDLTkdnmalqrvreaAEKAKCELSSSVQTDINlpyLTMDASG-------PKH--LNMKL 346
Cdd:COG1077 184 DELDEAIIQYVRKKYNLLIG-ERT------------AEEIKIEIGSAYPLEEE---LTMEVRGrdlvtglPKTitITSEE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 347 TRAQFEGIVT---DLIKRTIAPCQkamqdAEVSkSDIGE--VILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGA 421
Cdd:COG1077 248 IREALEEPLNaivEAIKSVLEKTP-----PELA-ADIVDrgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGT 321
|
..
gi 408360268 422 AI 423
Cdd:COG1077 322 GK 323
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
56-407 |
1.34e-10 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 64.11 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVV-AFTAD------GERLVGMP--AKRQAVTNpnntfyatkRLI-G 125
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLcAPTREavsewlYRHLDVPAydDERQALLR---------RAIrY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 126 RRYDDPEVQKDTknVPFKivRASNgDAWVEAHGKLY--------------SPSQIGAF------VLMKMKETAENYLGHT 185
Cdd:PRK11678 74 NREEDIDVTAQS--VFFG--LAAL-AQYLEDPEEVYfvkspksflgasglKPQQVALFedlvcaMMLHIKQQAEAQLQAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 186 AKNAVITVPAYFN-----DSQRQAT---KDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEI 257
Cdd:PRK11678 149 ITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSMLLM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 258 QKGvFEVKSTNGDTFL-------GGEDFDQAL-LRHIVKEF----KRETGV----------------------------- 296
Cdd:PRK11678 229 GPS-WRGRADRSASLLghsgqriGGNDLDIALaFKQLMPLLgmgsETEKGIalpslpfwnavaindvpaqsdfyslangr 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 297 ---DLTKDNMA------LQRVRE---------AAEKAKCELSSSVQTDINLPYLTmdasgpKHLNMKLTRAQFEGIVTDL 358
Cdd:PRK11678 308 llnDLIRDAREpekvarLLKVWRqrlsyrlvrSAEEAKIALSDQAETRASLDFIS------DGLATEISQQGLEEAISQP 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 408360268 359 IKRTIAPCQKAMQDAEVsKSDIgeVILVGGMTRMPKVQQTVQDLFGRAP 407
Cdd:PRK11678 382 LARILELVQLALDQAQV-KPDV--IYLTGGSARSPLIRAALAQQLPGIP 427
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
56-423 |
1.70e-10 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 62.96 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVmEGKQAKVLEnaegarttPSVVAFTADGERLVgmpakrqAVTNpnntfyATKRLIGRryddpevqk 135
Cdd:pfam06723 4 IGIDLGTANTLVYV-KGKGIVLNE--------PSVVAINTKTKKVL-------AVGN------EAKKMLGR--------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 136 dtknVPFKIVrasngdawveahgkLYSPSQIGAFVLMKMKETAENYLGHTAKNA--------VITVPAYFNDSQRQATKD 207
Cdd:pfam06723 53 ----TPGNIV--------------AVRPLKDGVIADFEVTEAMLKYFIKKVHGRrsfskprvVICVPSGITEVERRAVKE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 208 AGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGGEDFDQALLRHIV 287
Cdd:pfam06723 115 AAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGNMVVDIGGGTTEVAVISLG-GIVTSKSVR----VAGDEFDEAIIKYIR 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 288 KEFKRETGVdltkdnmalqrvrEAAEKAKCELSSSVQTDINlpyLTMDASG-------PKhlNMKLTRAQ--------FE 352
Cdd:pfam06723 190 KKYNLLIGE-------------RTAERIKIEIGSAYPTEEE---EKMEIRGrdlvtglPK--TIEISSEEvrealkepVS 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 408360268 353 GIVtDLIKRTIAPCQkamqdAEVSkSDIGE--VILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAI 423
Cdd:pfam06723 252 AIV-EAVKEVLEKTP-----PELA-ADIVDrgIVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
190-291 |
4.19e-09 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 58.76 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 190 VITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIqKGVFEVKSTNg 269
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVVDIGGGTTDIAVLSL-GGIVTSSSIK- 176
|
90 100
....*....|....*....|..
gi 408360268 270 dtfLGGEDFDQALLRHIVKEFK 291
Cdd:PRK13928 177 ---VAGDKFDEAIIRYIRKKYK 195
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
56-423 |
3.49e-08 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 55.91 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 56 VGIDLGTTNSCVAVmegKQAKVLENaEgarttPSVVAFTADGERL--VGMPAKRqavtnpnntfyatkrLIGRRYDDPEV 133
Cdd:PRK13930 11 IGIDLGTANTLVYV---KGKGIVLN-E-----PSVVAIDTKTGKVlaVGEEAKE---------------MLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 134 QKDTKN---VPFKIVRAsngdawveahgklyspsQIGAFVlmkmkETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQ 210
Cdd:PRK13930 67 IRPLKDgviADFEATEA-----------------MLRYFI-----KKARGRRFFRKPRIVICVPSGITEVERRAVREAAE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 211 ISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGGEDFDQALLRHIVKEF 290
Cdd:PRK13930 125 HAGAREVYLIEEPMAAAIGAGLPVTEPVGNMVVDIGGGTTEVAVISLG-GIVYSESIR----VAGDEMDEAIVQYVRRKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 291 KRETGvDLTkdnmalqrvreaAEKAKCELSSSVQTDinlPYLTMDASG-------PKhlNMKLTRAQFEGIVTDLIKRTI 363
Cdd:PRK13930 200 NLLIG-ERT------------AEEIKIEIGSAYPLD---EEESMEVRGrdlvtglPK--TIEISSEEVREALAEPLQQIV 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 408360268 364 APCQKAMQD--AEVSkSDIGE--VILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAI 423
Cdd:PRK13930 262 EAVKSVLEKtpPELA-ADIIDrgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGTGK 324
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
346-435 |
5.12e-08 |
|
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: 55.99 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 346 LTRAQFEGIVtdlikRTIAPCQKAMQDAEVsksDIGEVILVGGMTRMPKVQQTVQDLFGRaPSKAVNPDEAVAIGAAIQG 425
Cdd:COG1070 370 LARAVLEGVA-----FALRDGLEALEEAGV---KIDRIRATGGGARSPLWRQILADVLGR-PVEVPEAEEGGALGAALLA 440
|
90
....*....|
gi 408360268 426 GVLAGDVTDV 435
Cdd:COG1070 441 AVGLGLYDDL 450
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
174-420 |
7.10e-08 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 54.91 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 174 MKETAENyLGHTAK--NAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFD 251
Cdd:PRK13929 85 MKKAGKN-IGMTFRkpNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 252 ISILEIqKGVFEVKSTNgdtfLGGEDFDQALLRHIVKEFKRETGvdltkdnmalqrvREAAEKAKCELSSSVqtdINLPY 331
Cdd:PRK13929 164 VAIISF-GGVVSCHSIR----IGGDQLDEDIVSFVRKKYNLLIG-------------ERTAEQVKMEIGYAL---IEHEP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 332 LTMDASGPKHLN-----MKLTRAQFEGIVTDLIKRTIAPCQKAMQDAEVSKS-DIGE--VILVGGMTRMPKVQQTVQDLF 403
Cdd:PRK13929 223 ETMEVRGRDLVTglpktITLESKEIQGAMRESLLHILEAIRATLEDCPPELSgDIVDrgVILTGGGALLNGIKEWLSEEI 302
|
250
....*....|....*..
gi 408360268 404 GRAPSKAVNPDEAVAIG 420
Cdd:PRK13929 303 VVPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
346-430 |
2.25e-07 |
|
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: 53.71 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 346 LTRAQFEGIVTdlikrTIAPCQKAMQDAEVsksDIGEVILVGGMTRMPKVQQTVQDLFGrAPSKAVNPDEAVAIGAAIQG 425
Cdd:cd07809 368 LARAALEGATF-----GLRYGLDILRELGV---EIDEIRLIGGGSKSPVWRQILADVFG-VPVVVPETGEGGALGAALQA 438
|
....*
gi 408360268 426 GVLAG 430
Cdd:cd07809 439 AWGAG 443
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
166-256 |
3.05e-07 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 51.88 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 166 IGAF-VLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSedkviAVYD 244
Cdd:cd24047 43 IGAIrIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG-----AVVD 117
|
90
....*....|..
gi 408360268 245 LGGGTFDISILE 256
Cdd:cd24047 118 IGGGTTGIAVLK 129
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
166-256 |
3.19e-07 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 52.14 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 166 IGAF-VLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSedkviAVYD 244
Cdd:PRK15080 67 IGAVtIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG-----AVVD 141
|
90
....*....|..
gi 408360268 245 LGGGTFDISILE 256
Cdd:PRK15080 142 IGGGTTGISILK 153
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
173-393 |
1.01e-05 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 47.67 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 173 KMKETAENYLGHTAKNAVITVPAYFNDSQRQATKdagqiSGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDI 252
Cdd:cd24004 54 ELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 253 SIleIQKGVFEVKSTNGdtfLGGEDFDQALLRHIvkefkretGVDLtkdnmalqrvrEAAEKAKCELSSSvqtDINLPYL 332
Cdd:cd24004 129 AL--IRNGGIEAYRMVP---LGGDDFTKAIAEGF--------LISF-----------EEAEKIKRTYGIF---LLIEAKD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 408360268 333 TMDASGPKHLNMKLTRAQFEGIVTDlIKRTIapcqkamqdAEVSKSD--IGEVILVGGMTRMP 393
Cdd:cd24004 182 QLGFTINKKEVYDIIKPVLEELASG-IANAI---------EEYNGKFklPDAVYLVGGGSKLP 234
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
285-430 |
6.28e-05 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 46.04 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 285 HIVKEFKRETGVDLTKDNMALQRVREAAEKakcelSSSVqtdINLPYLTMDASGPKHLNMK--------------LTRAQ 350
Cdd:cd07773 301 ALLEWFRDLFGGDESDLAAADELAEAAPPG-----PTGL---LFLPHLSGSGTPDFDPDARgaflgltlgttradLLRAI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 351 FEGIvTDLIKRTIAPCQKAMQDaevsksdIGEVILVGGMTRMPKVQQTVQDLFGRaPSKAVNPDEAVAIGAAIQGGVLAG 430
Cdd:cd07773 373 LEGL-AFELRLNLEALEKAGIP-------IDEIRAVGGGARSPLWLQLKADILGR-PIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
346-429 |
1.38e-04 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 43.47 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 346 LTRAQFEGIVtdLIKRTIAPCQKAMQDAEVSKsdigeVILVGGMTRMPKVQQTVQDLFGRaPSKAVNPDEAVAIGAAIQG 425
Cdd:pfam02782 122 LYRAILESLA--LQLRQILEALTKQEGHPIDT-----IHVSGGGSRNPLLLQLLADALGL-PVVVPGPDEATALGAALLA 193
|
....
gi 408360268 426 GVLA 429
Cdd:pfam02782 194 AVAA 197
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
346-430 |
1.56e-04 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They 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: 466798 [Multi-domain] Cd Length: 433 Bit Score: 44.82 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 346 LTRAQFEGIVTDlIKRTIapcqKAMQDAEVsksDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPdEAVAIGAAIQG 425
Cdd:cd07779 329 LARAILEGIAFE-LRDNL----EAMEKAGV---PIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETS-EATALGAAILA 399
|
....*
gi 408360268 426 GVLAG 430
Cdd:cd07779 400 AVGAG 404
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
214-302 |
1.78e-04 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 43.67 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 214 LNVLRVINEPTAAALAYGLDKSE--DKVIAVYDLGGGTFDISILEIQKGVFEvkstNGDTFLGGEDFDQALLRHIVKEFK 291
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDDEleDGNVLVIDIGGGTTDILTFENGKPIEE----SSDTLPGGEEALEKYADDILNELL 212
|
90
....*....|.
gi 408360268 292 RETGVDLTKDN 302
Cdd:cd10227 213 KKLGDELDSAD 223
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
212-423 |
1.91e-04 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 44.19 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 212 SGLNVLRVINEPTAA--ALAYGLDKSEDKVIAVYDLGGGTFDISIleIQKGVFE-VKSTNgdtfLGGEDFDQALlrhivk 288
Cdd:cd24049 148 AGLKPVAIDVESFALarALEYLLPDEEEETVALLDIGASSTTLVI--VKNGKLLfTRSIP----VGGNDITEAI------ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 289 efKRETGVDLtkdnmalqrvrEAAEKAKCELSSSVQTDINLPYLTMDAsgpkhlnmklTRAQFEGIVTDlIKRTIAPCQK 368
Cdd:cd24049 216 --AKALGLSF-----------EEAEELKREYGLLLEGEEGELKKVAEA----------LRPVLERLVSE-IRRSLDYYRS 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 408360268 369 AMQDAEVSKsdigeVILVGGMTRMPKVQQTVQDLFGrAPSKAVNPDE-------------------AVAIGAAI 423
Cdd:cd24049 272 QNGGEPIDK-----IYLTGGGSLLPGLDEYLSERLG-IPVEILNPFSnieskksddeelkedaplfAVAIGLAL 339
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
295-420 |
1.88e-03 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 39.62 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 295 GVDLTKDNM-ALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHlnmKLTRAQFEGI-------VTDLIKRTIAPC 366
Cdd:pfam14450 30 GNGITKDIAiGLRTAVEEAERLKIKYGSALASLADEDEVPGVGGREPR---EISRKELAEIiearveeILELVRAELEDR 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408360268 367 QKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAV-------NPDEAVAIG 420
Cdd:pfam14450 107 EVLPGEYVRLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSpdgiggrNPAYATALG 167
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
371-430 |
3.17e-03 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. 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: 466804 [Multi-domain] Cd Length: 448 Bit Score: 40.67 E-value: 3.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 371 QDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPdEAVAIGAAIQGGVLAG 430
Cdd:cd07798 390 QLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGR-EASALGAAICAAVGAG 448
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
190-290 |
3.73e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 40.07 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 190 VITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQkGVFEVKSTNg 269
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVVDIGGGTTEVAVISLG-GIVYSKSVR- 177
|
90 100
....*....|....*....|.
gi 408360268 270 dtfLGGEDFDQALLRHIVKEF 290
Cdd:PRK13927 178 ---VGGDKFDEAIINYVRRNY 195
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
329-435 |
4.95e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 39.83 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360268 329 LPYLT------MDAS------------GPKHLnmklTRAQFEGIVTDLikrtiAPCQKAMQDAEVsksDIGEVILVGGMT 390
Cdd:cd07808 336 LPYLSgertpyWDPNargsffglslshTRAHL----ARAVLEGVAFSL-----RDSLEVLKELGI---KVKEIRLIGGGA 403
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 408360268 391 RMPKVQQTVQDLFGRaPSKAVNPDEAVAIGAAIQGGVLAGDVTDV 435
Cdd:cd07808 404 KSPLWRQILADVLGV-PVVVPAEEEGSAYGAALLAAVGAGVFDDL 447
|
|
| |
