|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
54-658 |
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 2099396667 54 KGAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDds 133
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRRDE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 134 EVKKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQI 213
Cdd:PRK00290 79 EVQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 214 SGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFK 293
Cdd:PRK00290 159 AGLEVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 294 RETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQ 373
Cdd:PRK00290 239 KENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 374 DAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLG 453
Cdd:PRK00290 319 DAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 454 GVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIVH 533
Cdd:PRK00290 399 GVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 534 VSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKMEEFKDQLPADECNKL 613
Cdd:PRK00290 479 VSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKI 558
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2099396667 614 KEEIAKMRELLARKDTETgenIRQAATSLQQASLKLFEMAYKKMA 658
Cdd:PRK00290 559 EAAIKELKEALKGEDKEA---IKAKTEELTQASQKLGEAMYQQAQ 600
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
57-655 |
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: 1010.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDdsEVK 136
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 KDIKNVPFKiVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGL 216
Cdd:TIGR02350 80 EEAKRVPYK-VVGDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 217 NVLRVINEPTAAALAYGLDKS-EDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKRE 295
Cdd:TIGR02350 159 EVLRIINEPTAAALAYGLDKSkKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 296 TGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQDA 375
Cdd:TIGR02350 239 EGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 376 EVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGV 455
Cdd:TIGR02350 319 GLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 456 FTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIVHVS 535
Cdd:TIGR02350 399 MTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 536 AKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKMEEFKDQLPADECNKLKE 615
Cdd:TIGR02350 479 AKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEK 558
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2099396667 616 EIAKMRELLARKDTetgENIRQAATSLQQASLKLFEMAYK 655
Cdd:TIGR02350 559 AVAELKEALKGEDV---EEIKAKTEELQQALQKLAEAMYQ 595
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
39-656 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 996.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 39 VLRAASSRKYASEAIKGAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNT 118
Cdd:PTZ00400 25 AMRSLCTSAIRFAKATGDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 119 FYATKRLIGRRFDDSEVKKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAY 198
Cdd:PTZ00400 105 VFATKRLIGRRYDEDATKKEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 199 FNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGE 278
Cdd:PTZ00400 185 FNDSQRQATKDAGKIAGLDVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 279 DFDQALLQYIVKEFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVA 358
Cdd:PTZ00400 265 DFDQRILNYLIAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTH 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 359 DLIKRTVAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVL 438
Cdd:PTZ00400 345 DLLKKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 439 LLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVP 518
Cdd:PTZ00400 425 LLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVP 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 519 QIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKM 598
Cdd:PTZ00400 505 QIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQL 584
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2099396667 599 EEFKDQLPADECNKLKEEIAKMRELLARKDTETgenIRQAATSLQQASLKLFEMAYKK 656
Cdd:PTZ00400 585 SDLKDKISDADKDELKQKITKLRSTLSSEDVDS---IKDKTKQLQEASWKISQQAYKQ 639
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
57-655 |
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: 979.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEVK 136
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFT-PKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 KDIKNVPFKIVRASNGDAWVEAH--GKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQIS 214
Cdd:pfam00012 80 RDIKHLPYKVVKLPNGDAGVEVRylGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 215 GLNVLRVINEPTAAALAYGLDKSE-DKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFK 293
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDkERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 294 RETGVDLTKDNMALQRVREASEKAKCELSSSvQTDINLPYLTMDASGpKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQ 373
Cdd:pfam00012 240 KKYGIDLSKDKRALQRLREAAEKAKIELSSN-QTNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 374 DAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG--DVTDVLLLDVTPLSLGIET 451
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIET 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 452 LGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGI 531
Cdd:pfam00012 398 LGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 532 VHVSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKMEEFKDQLPADECN 611
Cdd:pfam00012 478 LTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKS 557
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2099396667 612 KLKEEIAKMRELLARKDTetgENIRQAATSLQQASLKLFEMAYK 655
Cdd:pfam00012 558 KVESAIEWLKDELEGDDK---EEIEAKTEELAQVSQKIGERMYQ 598
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
40-675 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 867.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 40 LRAASSRKYASEAIKGAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADgERLVGMPAKRQAVTNPHNTF 119
Cdd:PTZ00186 12 ASAARLARHESQKVQGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGS-EKLVGLAAKRQAITNPQSTF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 120 YATKRLIGRRFDDSEVKKDIKNVPFKIVRASNGDAWVE-AHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAY 198
Cdd:PTZ00186 91 YAVKRLIGRRFEDEHIQKDIKNVPYKIVRAGNGDAWVQdGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 199 FNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGE 278
Cdd:PTZ00186 171 FNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 279 DFDQALLQYIVKEFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVA 358
Cdd:PTZ00186 251 DFDLALSDYILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 359 DLIKRTVAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVL 438
Cdd:PTZ00186 331 RLIERSIAPCKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 439 LLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVP 518
Cdd:PTZ00186 411 LLDVTPLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVP 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 519 QIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKM 598
Cdd:PTZ00186 491 QIEVTFDIDANGICHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQL 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 599 EEFKDQLPADECNkLKEEIAKMRELLARKDTeTGENIRQAATSLQQASLKLFEMAYKKMASE---RESSGSSGDQKEEKQ 675
Cdd:PTZ00186 571 GEWKYVSDAEKEN-VKTLVAELRKAMENPNV-AKDDLAAATDKLQKAVMECGRTEYQQAAAAnsgSSSNSGEQQQQQQQQ 648
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
55-431 |
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: 863.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 55 GAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSE 134
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 VKKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQIS 214
Cdd:cd11733 81 VQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 215 GLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKR 294
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 295 ETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQD 374
Cdd:cd11733 241 EQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLKD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099396667 375 AEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 431
Cdd:cd11733 321 AGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVLA 377
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
55-654 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 843.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 55 GAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDdsE 134
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 VKKDIKNVPFKIVRASNGDAWVE--AHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQ 212
Cdd:CHL00094 80 ISEEAKQVSYKVKTDSNGNIKIEcpALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 213 ISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEF 292
Cdd:CHL00094 160 IAGLEVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 293 KRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAM 372
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 373 QDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETL 452
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 453 GGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIV 532
Cdd:CHL00094 400 GGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 533 HVSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKMEEFKDQLPADECNK 612
Cdd:CHL00094 480 SVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEK 559
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2099396667 613 LKEEIAKMRELLarkDTETGENIRQAATSLQQASLKLFEMAY 654
Cdd:CHL00094 560 IENLIKKLRQAL---QNDNYESIKSLLEELQKALMEIGKEVY 598
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
55-656 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 837.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 55 GAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSE 134
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 VKKdiKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQIS 214
Cdd:PRK13411 82 EER--SRVPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 215 GLNVLRVINEPTAAALAYGLDK-SEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFK 293
Cdd:PRK13411 160 GLEVLRIINEPTAAALAYGLDKqDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 294 RETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQ 373
Cdd:PRK13411 240 QQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 374 DAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETL 452
Cdd:PRK13411 320 DAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 453 GGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIV 532
Cdd:PRK13411 400 GEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 533 HVSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKMEEFKDQLPADECNK 612
Cdd:PRK13411 480 KVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQR 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2099396667 613 LKEEIAKMRELLARKDTETgENIRQAATSLQQASLKLFEMAYKK 656
Cdd:PRK13411 560 AEQKVEQLEAALTDPNISL-EELKQQLEEFQQALLAIGAEVYQQ 602
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
55-652 |
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 2099396667 55 GAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDdsE 134
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYD--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 VKKDIKNVPFKIVRASNGDAWVE--AHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQ 212
Cdd:PRK13410 80 LDPESKRVPYTIRRNEQGNVRIKcpRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 213 ISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEF 292
Cdd:PRK13410 160 IAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 293 KRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAM 372
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 373 QDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETL 452
Cdd:PRK13410 320 KDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 453 GGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIV 532
Cdd:PRK13410 400 GGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 533 HVSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKME----EFKDQLPAD 608
Cdd:PRK13410 480 QVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRdaalEFGPYFAER 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2099396667 609 ECNKLKEEIAKMRELLARKDTetgENIRQAATSLQQAslkLFEM 652
Cdd:PRK13410 560 QRRAVESAMRDVQDSLEQDDD---RELDLAVADLQEA---LYGL 597
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
57-564 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 770.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDsevk 136
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 kdiknvpfkivrasngdAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGL 216
Cdd:COG0443 77 -----------------EATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 217 NVLRVINEPTAAALAYGLDK-SEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKRE 295
Cdd:COG0443 140 EVLRLLNEPTAAALAYGLDKgKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 296 TGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYltmdaSGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQDA 375
Cdd:COG0443 220 EGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 376 EVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDvllLDVTPLSLGIETLGGV 455
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIETLGGV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 456 FTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIVHVS 535
Cdd:COG0443 372 FTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVS 451
|
490 500
....*....|....*....|....*....
gi 2099396667 536 AKDKGTGREQQIVIqssgglsKDEIENMV 564
Cdd:COG0443 452 AKDLGTGKEQSITI-------KEEIERML 473
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
18-654 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 752.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 18 GGPVPAVPGLAQTFWNGLSQNVLRAASSRKYASEAIKGAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTA 97
Cdd:PLN03184 2 GGRLAPFSTPTAAFLKMGKRRGNGARRRAGGPLRVVAEKVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 98 DGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDdsEVKKDIKNVPFKIVRASNGDAWVE--AHGKLYSPSQIGAFVLMK 175
Cdd:PLN03184 82 NGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMS--EVDEESKQVSYRVVRDENGNVKLDcpAIGKQFAAEEISAQVLRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 176 MKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDIS 255
Cdd:PLN03184 160 LVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLEVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 256 ILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLT 335
Cdd:PLN03184 240 VLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 336 MDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNP 415
Cdd:PLN03184 320 ATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 416 DEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREM 495
Cdd:PLN03184 400 DEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 496 ASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDR 575
Cdd:PLN03184 480 VRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDK 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099396667 576 RRKERVEAVNLAEGIIHDTESKMEEFKDQLPADECNKLKEEIAKMRELLARKDTETgenIRQAATSLQQASLKLFEMAY 654
Cdd:PLN03184 560 EKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVEAKLKELKDAIASGSTQK---MKDAMAALNQEVMQIGQSLY 635
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
57-431 |
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: 730.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEVK 136
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 KDIknVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGL 216
Cdd:cd10234 81 RKQ--VPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 217 NVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKRET 296
Cdd:cd10234 159 EVLRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 297 GVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQDAE 376
Cdd:cd10234 239 GIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2099396667 377 VSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 431
Cdd:cd10234 319 LSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
55-432 |
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: 729.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 55 GAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSE 134
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 VKKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQIS 214
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 215 GLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKR 294
Cdd:cd11734 161 GLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 295 ETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQD 374
Cdd:cd11734 241 ESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALKD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2099396667 375 AEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG 432
Cdd:cd11734 321 AGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
54-633 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 671.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 54 KGAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDS 133
Cdd:PTZ00009 3 KGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 134 EVKKDIKNVPFKIVRASNGDAWVEAH----GKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKD 209
Cdd:PTZ00009 82 VVQSDMKHWPFKVTTGGDDKPMIEVTyqgeKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 210 AGQISGLNVLRVINEPTAAALAYGLDKSED--KIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQY 287
Cdd:PTZ00009 162 AGTIAGLNVLRIINEPTAAAIAYGLDKKGDgeKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 288 IVKEFKRET-GVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGpkhlNMKLSRSQFEGIVADLIKRTVA 366
Cdd:PTZ00009 242 CVQDFKRKNrGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDY----NVTISRARFEELCGDYFRNTLQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 367 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVLAGD----VTDVLLLD 441
Cdd:PTZ00009 318 PVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 442 VTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIE 521
Cdd:PTZ00009 398 VTPLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 522 VTFDIDANGIVHVSAKDKGTGREQQIVIQSSGG-LSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKMEE 600
Cdd:PTZ00009 478 VTFDIDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD 557
|
570 580 590
....*....|....*....|....*....|....*
gi 2099396667 601 --FKDQLPADECNKLKEEIAKMRELLARKDTETGE 633
Cdd:PTZ00009 558 ekVKGKLSDSDKATIEKAIDEALEWLEKNQLAEKE 592
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
58-646 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 606.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGeRLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDseVKK 137
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 DIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGLN 217
Cdd:PRK05183 99 RYPHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 218 VLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKefkrETG 297
Cdd:PRK05183 179 VLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILE----QAG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 298 VDLTKDNMALQRVREASEKAKCELSSSVQTDINLpyltMDASGpkhlnmKLSRSQFEGIVADLIKRTVAPCQKAMQDAEV 377
Cdd:PRK05183 255 LSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV----ALWQG------EITREQFNALIAPLVKRTLLACRRALRDAGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 378 SKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVT--DVLLLDVTPLSLGIETLGGV 455
Cdd:PRK05183 325 EADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKPdsDMLLLDVIPLSLGLETMGGL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 456 FTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIVHVS 535
Cdd:PRK05183 405 VEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVT 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 536 AKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEED---RRRKE-RVEAVNLAEGiihdTESKMEEFKDQLPADECN 611
Cdd:PRK05183 485 AMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDmqaRALAEqKVEAERVLEA----LQAALAADGDLLSAAERA 560
|
570 580 590
....*....|....*....|....*....|....*
gi 2099396667 612 KLKEEIAKMRELLARKDTETgenIRQAATSLQQAS 646
Cdd:PRK05183 561 AIDAAMAALREVAQGDDADA---IEAAIKALDKAT 592
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
57-646 |
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: 599.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDseVK 136
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIED--IK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 KdIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGL 216
Cdd:TIGR01991 79 T-FSILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 217 NVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKRET 296
Cdd:TIGR01991 158 NVLRLLNEPTAAAVAYGLDKASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQLGISA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 297 GVDLTKDNMALQRVREASEKakceLSSSVQTDINLPYLTMDASGpkhlnmKLSRSQFEGIVADLIKRTVAPCQKAMQDAE 376
Cdd:TIGR01991 238 DLNPEDQRLLLQAARAAKEA----LTDAESVEVDFTLDGKDFKG------KLTRDEFEALIQPLVQKTLSICRRALRDAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 377 VSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVT--DVLLLDVTPLSLGIETLGG 454
Cdd:TIGR01991 308 LSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIgnDLLLLDVTPLSLGIETMGG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 455 VFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANGIVHV 534
Cdd:TIGR01991 388 LVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 535 SAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKMEEFKDQLPADECNKLK 614
Cdd:TIGR01991 468 SAQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAID 547
|
570 580 590
....*....|....*....|....*....|..
gi 2099396667 615 EEIAKMRELLARKDTETgenIRQAATSLQQAS 646
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 ... |
57-430 |
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: 541.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEVK 136
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFT-DGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 KDIKNVPFKIVRASNGDAWVEAHG----KLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQ 212
Cdd:cd24028 80 SDIKHWPFKVVEDEDGKPKIEVTYkgeeKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 213 ISGLNVLRVINEPTAAALAYGLDK--SEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVK 290
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDKksSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 291 EFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASgpkhLNMKLSRSQFEGIVADLIKRTVAPCQK 370
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGID----FETTITRAKFEELCEDLFKKCLEPVEK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099396667 371 AMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVL 430
Cdd:cd24028 316 VLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
55-430 |
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: 533.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 55 GAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSE 134
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFT-DGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 VKKDIKNVPFKIVRaSNGDAWVEAHG----KLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDA 210
Cdd:cd10241 80 VQKDIKLLPFKIVN-KNGKPYIQVEVkgekKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 211 GQISGLNVLRVINEPTAAALAYGLDKSED-KIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIV 289
Cdd:cd10241 159 GTIAGLNVLRIINEPTAAAIAYGLDKKGGeKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 290 KEFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLT--MDASGPkhlnmkLSRSQFEGIVADLIKRTVAP 367
Cdd:cd10241 239 KLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFdgEDFSET------LTRAKFEELNMDLFRKTLKP 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099396667 368 CQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVL 430
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; ... |
58-430 |
2.66e-172 |
|
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: 496.38 E-value: 2.66e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEVKK 137
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 DIKNVPFKIVraSNGDA---WVEAHG--KLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQ 212
Cdd:cd10233 81 DMKHWPFKVV--SGGDKpkiQVEYKGetKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 213 ISGLNVLRVINEPTAAALAYGLDK--SEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVK 290
Cdd:cd10233 159 IAGLNVLRIINEPTAAAIAYGLDKkgKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 291 EFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYL--TMDasgpkhLNMKLSRSQFEGIVADLIKRTVAPC 368
Cdd:cd10233 239 EFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLfeGID------FYTSITRARFEELCADLFRSTLEPV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099396667 369 QKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVL 430
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 ... |
58-431 |
1.78e-163 |
|
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: 473.22 E-value: 1.78e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVL-ENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEvk 136
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 kdiknvpfkivrasngdawvEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGL 216
Cdd:cd24029 79 --------------------EIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 217 NVLRVINEPTAAALAYGLDK-SEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKRE 295
Cdd:cd24029 139 NVLRLINEPTAAALAYGLDKeGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 296 TGV-DLTKDNMALQRVREASEKAKCELSSSVQTDINLPyltmDASGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQD 374
Cdd:cd24029 219 TGIlDDKEDERARARLREAAEEAKIELSSSDSTDILIL----DDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099396667 375 AEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 431
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
57-432 |
1.96e-159 |
|
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: 463.23 E-value: 1.96e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDseVK 136
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 KDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGL 216
Cdd:cd10236 82 EELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 217 NVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKefkrET 296
Cdd:cd10236 162 NVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILK----QI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 297 GVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPkhlnmkLSRSQFEGIVADLIKRTVAPCQKAMQDAE 376
Cdd:cd10236 238 GIDARLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWERE------ITREEFEELIQPLVKRTLEPCRRALKDAG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2099396667 377 VSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG 432
Cdd:cd10236 312 LEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
58-430 |
5.88e-148 |
|
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: 434.41 E-value: 5.88e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGkQAKVLENSEGARTTPSVVAFTADgERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEVKK 137
Cdd:cd24093 2 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 DIKNVPFKIVRaSNGDAWVEAH----GKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQI 213
Cdd:cd24093 80 DMKTWPFKVID-VNGNPVIEVQylgeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 214 SGLNVLRVINEPTAAALAYGLD--KSE-DKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVK 290
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGagKSEkERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 291 EFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLtmdaSGPKHLNMKLSRSQFEGIVADLIKRTVAPCQK 370
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSL----FDGEDFESSITRARFEDLNAALFKSTLEPVEQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099396667 371 AMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLF-GRAPSKAVNPDEAVAIGAAIQGGVL 430
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; ... |
57-432 |
4.39e-132 |
|
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: 395.17 E-value: 4.39e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGK--QAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSE 134
Cdd:cd10237 24 IVGIDLGTTYSCVGVYHAVtgEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 VKKDIKNVPFKIVRASNGDAWVEAHG----KLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDA 210
Cdd:cd10237 104 LEEEAKRYPFKVVNDNIGSAFFEVPLngstLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 211 GQISGLNVLRVINEPTAAALAYGLDKSED-KIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIV 289
Cdd:cd10237 184 ANLAGLEVLRVINEPTAAAMAYGLHKKSDvNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 290 KEFKRETGVDLTkDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHL-NMKLSRSQFEGIVADLIKRTVAPC 368
Cdd:cd10237 264 DRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKfKEEITRDLFETLNEDLFQRVLEPI 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099396667 369 QKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG 432
Cdd:cd10237 343 RQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
58-432 |
3.71e-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: 377.36 E-value: 3.71e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERLVGMPAKRQAVTNPHNTFYATKRLIGRrfddsevkk 137
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMGT--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 diknvpfkivrasngDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGLN 217
Cdd:cd10235 72 ---------------DKQYRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 218 VLRVINEPTAAALAYGLDK-SEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVKEFKRET 296
Cdd:cd10235 137 VERLINEPTAAALAYGLHKrEDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 297 GVDLTKDNMALqrvREASEKAKCELSSSVQTDINLPYltmdasGPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQDAE 376
Cdd:cd10235 217 TSLSPSELAAL---RKRAEQAKRQLSSQDSAEIRLTY------RGEELEIELTREEFEELCAPLLERLRQPIERALRDAG 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2099396667 377 VSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAG 432
Cdd:cd10235 288 LKPSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
57-656 |
2.68e-116 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 360.71 E-value: 2.68e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGerlvgmpakrqAVTNPHNTFYATKRLIGRRFddsevk 136
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN-----------FTIGNNKGLRSIKRLFGKTL------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 137 KDIKNVP--FKIVR----ASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDA 210
Cdd:PRK01433 84 KEILNTPalFSLVKdyldVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 211 GQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYIVK 290
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 291 EFkretgvDLTKDNMALQRVREASEkakcelsssvqtdinlpYLTMDASGpKHLNMKLSRSQFEGIVADLIKRTVAPCQK 370
Cdd:PRK01433 244 KF------DLPNSIDTLQLAKKAKE-----------------TLTYKDSF-NNDNISINKQTLEQLILPLVERTINIAQE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 371 AMQDAevSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIE 450
Cdd:PRK01433 300 CLEQA--GNPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGME 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 451 TLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMASDNKLLGQFTLVGIPPAPRGVPQIEVTFDIDANG 530
Cdd:PRK01433 378 LYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 531 IVHVSAKDKGTGREQQIVIQSSGGLSKDEIENMVKNAEKYAEEDRRRKERVEAVNLAEGIIHDTESKMEEFKDQLPADEC 610
Cdd:PRK01433 458 ILSVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEI 537
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2099396667 611 NKLKEEIAKMRELLARKDtetgenirqaaTSLQQASLKLFEMAYKK 656
Cdd:PRK01433 538 SIINSLLDNIKEAVHARD-----------IILINNSIKEFKSKIKK 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 ... |
58-426 |
8.14e-110 |
|
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466838 [Multi-domain] Cd Length: 377 Bit Score: 336.45 E-value: 8.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEVKK 137
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFT-EKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 DIKNVPFKIVRASNGDAWVEAHGK----LYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQI 213
Cdd:cd11732 80 EIKLLPFKLVELEDGKVGIEVSYNgeevVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 214 SGLNVLRVINEPTAAALAYGLDKS-----EDK--IIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQ 286
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSdllesEEKprIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 287 YIVKEFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDasgpKHLNMKLSRSQFEGIVADLIKRTVA 366
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMED----IDFSGQIKREEFEELIQPLLARLEA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 367 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQ 426
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; ... |
56-430 |
1.43e-104 |
|
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: 323.04 E-value: 1.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 56 AVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEV 135
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFT-DNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 136 KKDIKNVPFKIVRaSNGDAW--VEAHGK--LYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAG 211
Cdd:cd10238 80 QELKKESKCKIIE-KDGKPGyeIELEEKkkLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 212 QISGLNVLRVINEPTAAALAYGL---DKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYI 288
Cdd:cd10238 159 EKAGFNVLRVISEPSAAALAYGIgqdDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 289 VKEFKRETGVDLTKDNMALQRVREASEKAKCELSS--SVQTDINLPYLTMDasgpkhLNMKLSRSQFEGIVADLIKRTVA 366
Cdd:cd10238 239 ASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTlnTATCSVESLYDGMD------FQCNVSRARFESLCSSLFQQCLE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099396667 367 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFgraPSKAV----NPDEAVAIGAAIQGGVL 430
Cdd:cd10238 313 PIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLF---PSAEVlssiPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
58-426 |
7.59e-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: 7.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEVKK 137
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFG-EKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 DIKNVPFKIVRASNGDAWVEAH----GKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQI 213
Cdd:cd10228 80 ELKHLPYKVVKLPNGSVGIKVQylgeEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 214 SGLNVLRVINEPTAAALAYG-----LDKSEDK--IIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQ 286
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGiykqdLPAEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 287 YIVKEFKRETGVDLTKDNMALQRVREASEKAKcELSSSVQTDI--NLPYLTMDasgpKHLNMKLSRSQFEGIVADLIKRT 364
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATELplNIECFMDD----KDVSGKMKRAEFEELCAPLFARV 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099396667 365 VAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQ 426
Cdd:cd10228 315 EVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
55-430 |
2.27e-102 |
|
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: 317.72 E-value: 2.27e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 55 GAVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSE 134
Cdd:cd24095 1 MSVVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFG-EKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 VKKDIKNVPFKIVRASNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDA 210
Cdd:cd24095 80 VQRDLKLFPFKVTEGPDGEIGINVnylgEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 211 GQISGLNVLRVINEPTAAALAYG-----LDKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALL 285
Cdd:cd24095 160 AQIAGLNCLRLMNETTATALAYGiyktdLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 286 QYIVKEFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDasgpKHLNMKLSRSQFEGIVADLIKRTV 365
Cdd:cd24095 240 DHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMED----KDVKGMITREEFEELAAPLLERLL 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099396667 366 APCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVL 430
Cdd:cd24095 316 EPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
58-431 |
4.89e-90 |
|
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: 285.42 E-value: 4.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFtADGERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEVKK 137
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGF-GPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 DIKNVPFKIVRAsNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQI 213
Cdd:cd24094 80 EEKYFTAKLVDA-NGEVGAEVnylgEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 214 SGLNVLRVINEPTAAALAYGLDKS-----EDK--IIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQ 286
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKTdlpepEEKprIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 287 YIVKEFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLT--MDASGpkhlnmKLSRSQFEGIVADLIKRT 364
Cdd:cd24094 239 HFADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMndIDVSS------MLKREEFEELIAPLLERV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099396667 365 VAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 431
Cdd:cd24094 313 TAPLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
56-427 |
2.09e-85 |
|
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: 272.06 E-value: 2.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 56 AVIGIDLGTTNSCVA-VMEGKQAKVLENSEGARTTPSVVAFtADGERLVGMPAKRQAVTNPHNTFYATKRLIGrrfddse 134
Cdd:cd10230 1 AVLGIDLGSEFIKVAlVKPGVPFEIVLNEESKRKTPSAVAF-RNGERLFGDDALALATRFPENTFSYLKDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 vkkdiknvpfkivrasngdawveahgklYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQIS 214
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 215 GLNVLRVINEPTAAALAYGLDK----SEDKIIAVYDLGGGTFDISILEIQ------------KGVFEVKSTNGDTFLGGE 278
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRrfenNEPQNVLFYDMGASSTSATVVEFSsvkekdkgknktVPQVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 279 DFDQALLQYIVKEFKRETG--VDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDasgpKHLNMKLSRSQFEGI 356
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKkdKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDD----IDFRTKITREEFEEL 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099396667 357 VADLIKRTVAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAP-SKAVNPDEAVAIGAAIQG 427
Cdd:cd10230 281 CADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
56-426 |
1.72e-81 |
|
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: 262.87 E-value: 1.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 56 AVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADgERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEV 135
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSK-NRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 136 KKDIKNVPFKIVRASNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAG 211
Cdd:cd11739 80 QKEKENLSYDLVPLKNGGVGVKVmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 212 QISGLNVLRVINEPTAAALAYGLDKSE-------DKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQAL 284
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIYKQDlpapdekPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 285 LQYIVKEFKRETGVDLTKDNMALQRVREASEKAKcELSSSVQTDI--NLPYLTMDasgpKHLNMKLSRSQFEGIVADLIK 362
Cdd:cd11739 240 VEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLplNIECFMND----KDVSGKMNRSQFEELCADLLQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099396667 363 RTVAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQ 426
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; ... |
56-426 |
4.01e-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: 249.09 E-value: 4.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 56 AVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADgERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEV 135
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPK-NRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 136 KKDIKNVPFKIVRASNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAG 211
Cdd:cd11737 80 QAEKPSLAYELVQLPTGTTGIKVmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 212 QISGLNVLRVINEPTAAALAYGLDKS-----EDK--IIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQAL 284
Cdd:cd11737 160 QIAGLNCLRLMNETTAVALAYGIYKQdlpapEEKprNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 285 LQYIVKEFKRETGVDLTKDNMALQRVREASEKAKCELS---SSVQTDINLPYLTMDASGpkhlnmKLSRSQFEGIVADLI 361
Cdd:cd11737 240 VNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSanaSDLPLNIECFMNDIDVSG------TMNRGQFEEMCADLL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099396667 362 KRTVAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQ 426
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; ... |
56-431 |
1.53e-75 |
|
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: 247.52 E-value: 1.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 56 AVIGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADgERLVGMPAKRQAVTNPHNTFYATKRLIGRRFDDSEV 135
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSR-NRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 136 KKDIKNVPFKIVRASNGDAWVEA----HGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAG 211
Cdd:cd11738 80 QAEKIKLPYELQKMPNGSTGVKVryldEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 212 QISGLNVLRVINEPTAAALAYGLDK-----SEDKI--IAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQAL 284
Cdd:cd11738 160 QIAGLNCLRLMNETTAVALAYGIYKqdlpaLEEKPrnVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 285 LQYIVKEFKRETGVDLTKDNMALQRVREASEKAKCELS---SSVQTDINLPYLTMDASGpkhlnmKLSRSQFEGIVADLI 361
Cdd:cd11738 240 VDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSanaSDLPLNIECFMNDIDVSS------KMNRAQFEELCASLL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 362 KRTVAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLA 431
Cdd:cd11738 314 ARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
56-430 |
1.61e-71 |
|
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: 235.72 E-value: 1.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 56 AVIGIDLGTTNSCVAVMEGKQ-AKVLENSEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPHNTFYATKRLIGRrfddse 134
Cdd:cd10232 1 VVIGISFGNSNSSIAIINKDGrAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLGT------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 135 vkkdiknvpfkivrasngdawveahgKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQIS 214
Cdd:cd10232 74 --------------------------TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 215 GLNVLRVINEPTAAALAYGL------DKSEDKIIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLQYI 288
Cdd:cd10232 128 GLEVLQLIPEPAAAALAYDLraetsgDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 289 VKEFKRETGVDLTKDNMALQRVREASEKAKCELS--SSVQTDINLPYLTMDASGpkhlnmKLSRSQFEGIVADLIKRTVA 366
Cdd:cd10232 208 AKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSqgTSAPCSVESLADGIDFHS------SINRTRYELLASKVFQQFAD 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099396667 367 PCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSK----AVNPDEAVAIGAAIQGGVL 430
Cdd:cd10232 282 LVTDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
58-425 |
5.76e-53 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 185.39 E-value: 5.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLE---------NSEGARTTPSVVAFTADgerlvgmpakrqavtnphntfyatkrligr 128
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLvvlqlpwpgGDGGSSKVPSVLEVVAD------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 129 rfddsevkkdiknvpfkivrasngdawveahgklyspsqigafVLMKMKETAENYLGH-------PAKNAVITVPAYFND 201
Cdd:cd10170 51 -------------------------------------------FLRALLEHAKAELGDriwelekAPIEVVITVPAGWSD 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 202 SQRQATKDAGQISGL----NVLRVINEPTAAALAYGLDKS------EDKIIAVYDLGGGTFDISILEIQKGVFEVK---S 268
Cdd:cd10170 88 AAREALREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGdllplkPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevA 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 269 TNGDTFLGGEDFDQALLQYIVKEFKRETGVDLTKDNMALQRVREASEKAKCELSSSVQTDINLPYLTMDASGPKHLNmKL 348
Cdd:cd10170 168 PGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPELGLE-KG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 349 SRSQFEGIVADLIKRTVAPCQKAMQDA--EVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAV----NPDEAVAIG 422
Cdd:cd10170 247 TLLLTEEEIRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARG 326
|
...
gi 2099396667 423 AAI 425
Cdd:cd10170 327 AAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
58-424 |
4.21e-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: 137.79 E-value: 4.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVVAFTADGERL-----VGMPAKRQAVTNPHNTFY--ATKRLIG-RR 129
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGaesiyFGNDAIDAYLNDPEEGRLikSVKSFLGsSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 130 FDDSEVkkdiknvpfkivrasngdawveaHGKLYSPSQIGAFVLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQAT-- 207
Cdd:cd10231 81 FDETTI-----------------------FGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaq 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 208 -----KDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEI----QKGVFEVKSTNGDtFLGGE 278
Cdd:cd10231 138 aesrlRDAARRAGFRNVEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLgpnrTDRRADILATSGV-GIGGD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 279 DFDQALL------------QYIVK-----------------------------EFKRETGVD------------LTKDNM 305
Cdd:cd10231 217 DFDRELAlkkvmphlgrgsTYVSGdkglpvpawlyadlsnwhaisllytkktlRLLLDLRRDaadpekierllsLVEDQL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 306 AlQRVREASEKAKCELSSSVQTDINLPYLtmdasgPKHLNMKLSRSQFEGIVADLIKRTVAPCQKAMQDAEVSKSDIGEV 385
Cdd:cd10231 297 G-HRLFRAVEQAKIALSSADEATLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420 430
....*....|....*....|....*....|....*....
gi 2099396667 386 ILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAA 424
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
56-427 |
1.29e-18 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 88.10 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 56 AVIGIDLGTTNSCVAVM-EGKQAKVL--------ENSEGARTTPSVVAFTADGErLV--GMPAKRQAVTNPHNTfyATKR 124
Cdd:cd10229 1 VVVAIDFGTTYSGYAYSfITDPGDIHtmynwwgaPTGVSSPKTPTCLLLNPDGE-FHsfGYEAREKYSDLAEDE--EHQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 125 LigRRFDDSEVKKDIKNVPF-KIVRASNGDaWVEAHGKL-YSPSQIGAFVLMKMKETAENYLghPAKNA--VITVPAYFN 200
Cdd:cd10229 78 L--YFFKFKMMLLSEKELTRdTKVKAVNGK-SMPALEVFaEALRYLKDHALKELRDRSGSSL--DEDDIrwVLTVPAIWS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 201 DSQ----RQATKDAGQISGLN--VLRVINEPTAAALAYGLDKSE---------DKIIaVYDLGGGTFDISILEIQK--GV 263
Cdd:cd10229 153 DAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCQKLLAEgeekelkpgDKYL-VVDCGGGTVDITVHEVLEdgKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 264 FEVKSTNGDTFlGGEDFDQALLQYI--------VKEFKRETGVDLTKdnmaLQRvreASEKAKCelsssvqtdinlpylT 335
Cdd:cd10229 232 EELLKASGGPW-GSTSVDEEFEELLeeifgddfMEAFKQKYPSDYLD----LLQ---AFERKKR---------------S 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 336 MDasgpkhlnMKLSRSQFEGIVADLIKRTVAPCQKAMQDAEVSKSDIgeVILVGGMTRMPKVQQTVQDLFGR-----APs 410
Cdd:cd10229 289 FK--------LRLSPELMKSLFDPVVKKIIEHIKELLEKPELKGVDY--IFLVGGFAESPYLQKAVKEAFSTkvkiiIP- 357
|
410
....*....|....*..
gi 2099396667 411 kaVNPDEAVAIGAAIQG 427
Cdd:cd10229 358 --PEPGLAVVKGAVLFG 372
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
58-425 |
1.31e-13 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 72.12 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVmeGKQAKVLenSEgarttPSVVAF-TADGERL-VGMPAKRqavtnphntfyatkrLIGRRFDDSEV 135
Cdd:cd10225 2 IGIDLGTANTLVYV--KGKGIVL--NE-----PSVVAVdKNTGKVLaVGEEAKK---------------MLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 136 KKDIKN---VPFKIVRAsngdawveahgklyspsQIGAFVlmkmkETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQ 212
Cdd:cd10225 58 IRPLRDgviADFEATEA-----------------MLRYFI-----RKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 213 ISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGGEDFDQALLQYIVKEF 292
Cdd:cd10225 116 HAGAREVYLIEEPMAAAIGAGLPIEEPRGSMVVDIGGGTTEIAVISLG-GIVTSRSVR----VAGDEMDEAIINYVRRKY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 293 KRETGvdltkDNMAlqrvreasEKAKCELSSSVQTDINlpyLTMDASG-------PKhlNMKLSRSQFEGIVADLIKRTV 365
Cdd:cd10225 191 NLLIG-----ERTA--------ERIKIEIGSAYPLDEE---LSMEVRGrdlvtglPR--TIEITSEEVREALEEPVNAIV 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099396667 366 APCQKAMQDA--EVSkSDIGE--VILVGGMTRMPKVQQTVQDLFG----RAPskavNPDEAVAIGAAI 425
Cdd:cd10225 253 EAVRSTLERTppELA-ADIVDrgIVLTGGGALLRGLDELLREETGlpvhVAD----DPLTCVAKGAGK 315
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
58-425 |
4.75e-12 |
|
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: 67.58 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVmEGKQAKVLEnsegarttPSVVAFTADGERLVgmpakrqAVTNphntfyATKRLIGRrfddsevkk 137
Cdd:pfam06723 4 IGIDLGTANTLVYV-KGKGIVLNE--------PSVVAINTKTKKVL-------AVGN------EAKKMLGR--------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 diknVPFKIVrasngdawveahgkLYSPSQIGAFVLMKMKETAENYLGHPAKNA--------VITVPAYFNDSQRQATKD 209
Cdd:pfam06723 53 ----TPGNIV--------------AVRPLKDGVIADFEVTEAMLKYFIKKVHGRrsfskprvVICVPSGITEVERRAVKE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 210 AGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGGEDFDQALLQYIV 289
Cdd:pfam06723 115 AAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGNMVVDIGGGTTEVAVISLG-GIVTSKSVR----VAGDEFDEAIIKYIR 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 290 KEFKRETGvdltkdnmalqrVREAsEKAKCELSSSVQTDINlpyLTMDASG-------PKHLNMKLS------RSQFEGI 356
Cdd:pfam06723 190 KKYNLLIG------------ERTA-ERIKIEIGSAYPTEEE---EKMEIRGrdlvtglPKTIEISSEevrealKEPVSAI 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099396667 357 VaDLIKRTVAPCQkamqdAEVSkSDIGE--VILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAI 425
Cdd:pfam06723 254 V-EAVKEVLEKTP-----PELA-ADIVDrgIVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
58-425 |
8.47e-12 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 67.03 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVmEGKQaKVLenSEgarttPSVVAFTADGERL--VGMPAKRQAVTNPHNT-------------FYAT 122
Cdd:COG1077 10 IGIDLGTANTLVYV-KGKG-IVL--NE-----PSVVAIDKKTGKVlaVGEEAKEMLGRTPGNIvairplkdgviadFEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 123 KRLIgRRFddseVKKdiknvpfkivrasngdawveAHGKlyspsqigafvlmkmketaeNYLGHPakNAVITVPAYFNDS 202
Cdd:COG1077 81 EAML-KYF----IKK--------------------VHGR--------------------RSFFRP--RVVICVPSGITEV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 203 QRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGGEDFDQ 282
Cdd:COG1077 114 ERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTGNMVVDIGGGTTEVAVISLG-GIVVSRSIR----VAGDELDE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 283 ALLQYIVKEFKRETGvdltkDNMAlqrvreasEKAKCELSSSVQTDINlpyLTMDASG-------PKHLNMKLS------ 349
Cdd:COG1077 189 AIIQYVRKKYNLLIG-----ERTA--------EEIKIEIGSAYPLEEE---LTMEVRGrdlvtglPKTITITSEeireal 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099396667 350 RSQFEGIVaDLIKRTVAPCQkamqdAEVSkSDIGE--VILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAI 425
Cdd:COG1077 253 EEPLNAIV-EAIKSVLEKTP-----PELA-ADIVDrgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGTGK 323
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
58-409 |
6.18e-10 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 61.80 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQAKVLENSEGARTTPSVV-AFTAD------GERLVGMP--AKRQAVTNphntfyatkRLI-G 127
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLcAPTREavsewlYRHLDVPAydDERQALLR---------RAIrY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 128 RRFDDSEVkkDIKNVPFKivRASNgDAWVEAHGKLY--------------SPSQIGAF------VLMKMKETAENYLGHP 187
Cdd:PRK11678 74 NREEDIDV--TAQSVFFG--LAAL-AQYLEDPEEVYfvkspksflgasglKPQQVALFedlvcaMMLHIKQQAEAQLQAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 188 AKNAVITVPAYFN-----DSQRQAT---KDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEI 259
Cdd:PRK11678 149 ITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSMLLM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 260 QKGvFEVKSTNGDTFL-------GGEDFDQALlqyIVKEF--------KRETGV-------------------------- 298
Cdd:PRK11678 229 GPS-WRGRADRSASLLghsgqriGGNDLDIAL---AFKQLmpllgmgsETEKGIalpslpfwnavaindvpaqsdfysla 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 299 ------DLTKDN---------MALQR-------VREAsEKAKCELSSSVQTDINLPYLTmdasgpKHLNMKLSRSQFEGI 356
Cdd:PRK11678 305 ngrllnDLIRDArepekvarlLKVWRqrlsyrlVRSA-EEAKIALSDQAETRASLDFIS------DGLATEISQQGLEEA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2099396667 357 VADLIKRTVAPCQKAMQDAEVsKSDIgeVILVGGMTRMPKVQQTVQDLFGRAP 409
Cdd:PRK11678 378 ISQPLARILELVQLALDQAQV-KPDV--IYLTGGSARSPLIRAALAQQLPGIP 427
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
58-425 |
6.74e-10 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 60.92 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVmegKQAKVLENSegarttPSVVAFTADGERL--VGMPAKRqavtnphntfyatkrLIGRRFDDSEV 135
Cdd:PRK13930 11 IGIDLGTANTLVYV---KGKGIVLNE------PSVVAIDTKTGKVlaVGEEAKE---------------MLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 136 KKDIKN---VPFKIVRAsngdawveahgklyspsQIGAFVlmkmkETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQ 212
Cdd:PRK13930 67 IRPLKDgviADFEATEA-----------------MLRYFI-----KKARGRRFFRKPRIVICVPSGITEVERRAVREAAE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 213 ISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGGEDFDQALLQYIVKEF 292
Cdd:PRK13930 125 HAGAREVYLIEEPMAAAIGAGLPVTEPVGNMVVDIGGGTTEVAVISLG-GIVYSESIR----VAGDEMDEAIVQYVRRKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 293 KRETGvdltkDNMAlqrvreasEKAKCELSSSVQTDinlPYLTMDASG-------PKhlNMKLSRSQFEGIVADLIKRTV 365
Cdd:PRK13930 200 NLLIG-----ERTA--------EEIKIEIGSAYPLD---EEESMEVRGrdlvtglPK--TIEISSEEVREALAEPLQQIV 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099396667 366 APCQKAMQD--AEVSkSDIGE--VILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAI 425
Cdd:PRK13930 262 EAVKSVLEKtpPELA-ADIIDrgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGTGK 324
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
192-293 |
2.88e-09 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 59.15 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 192 VITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIqKGVFEVKSTNg 271
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVVDIGGGTTDIAVLSL-GGIVTSSSIK- 176
|
90 100
....*....|....*....|..
gi 2099396667 272 dtfLGGEDFDQALLQYIVKEFK 293
Cdd:PRK13928 177 ---VAGDKFDEAIIRYIRKKYK 195
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
168-258 |
6.10e-08 |
|
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: 54.19 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 168 IGAF-VLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSedkiiAVYD 246
Cdd:cd24047 43 IGAIrIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG-----AVVD 117
|
90
....*....|..
gi 2099396667 247 LGGGTFDISILE 258
Cdd:cd24047 118 IGGGTTGIAVLK 129
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
57-432 |
1.64e-07 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 54.24 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 57 VIGIDLGTTNSCVAVMEGKQAK---VLENSEGA------RTTPSVVAFTADGERlvgmpakrqavtnpHNTFYATKRLIg 127
Cdd:cd11735 2 VVAIDFGTTSSGYAYSFTKEPEcihVMRRWEGGdpgvsnQKTPTTILLTPERKF--------------HSFGYAARDFY- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 128 RRFDDSEVKKDIKNVPFKIVRASNGDAWVE-----AHGKLYSPSQIGAFVLMKMKETAENYL----GHPAKNA----VIT 194
Cdd:cd11735 67 HDLDPNESKQWLYFEKFKMKLHTTGNLTMEtdltaANGKKVKALEIFAYALQFFKEQALKELsdqaGSEFDNSdvrwVIT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 195 VPAYFNDSQRQATKDAGQISGLNV------LRVINEPTAAAL------AYGLDKsedkiIAVYDLGGGTFDISILEIQ-- 260
Cdd:cd11735 147 VPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIycrklrLHQMDR-----YVVVDCGGGTVDLTVHQIRlp 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 261 KGVFE--VKSTNGDTFLGGEDFD-QALLQYIVKE-------FKRETG-VDLTkdnMALQRVREASEKAKCElsssvQTDI 329
Cdd:cd11735 222 EGHLKelYKASGGPYGSLGVDYEfEKLLCKIFGEdfidqfkIKRPAAwVDLM---IAFESRKRAAAPDRTN-----PLNI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 330 NLPYLTMD----------ASGPKHLNMKLSRSQFEGIVA-------DLIKRTVAPCQKAMQDAeVSKSDIGEV---ILVG 389
Cdd:cd11735 294 TLPFSFIDyykkfrghsvEHALRKSNVDFVKWSSQGMLRmspdamnALFKPTIDHIIQHLTDL-FQKPEVSGVkflFLVG 372
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2099396667 390 GMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIgaaIQGGVLAG 432
Cdd:cd11735 373 GFAESPLLQQAVQNAFGDQCRVIIPHDVGLTI---LKGAVLFG 412
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
176-422 |
3.16e-07 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 52.99 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 176 MKETAENY-LGHPAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDI 254
Cdd:PRK13929 85 MKKAGKNIgMTFRKPNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 255 SILEIqKGVFEVKSTNgdtfLGGEDFDQALLQYIVKEFKRETGvdltkdnmalqrvREASEKAKCELSSSVqtdINLPYL 334
Cdd:PRK13929 165 AIISF-GGVVSCHSIR----IGGDQLDEDIVSFVRKKYNLLIG-------------ERTAEQVKMEIGYAL---IEHEPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 335 TMDASGPKHLN-----MKLSRSQFEGIVADLIKRTVAPCQKAMQDAEVSKS-DIGE--VILVGGMTRMPKVQQTVQDLFG 406
Cdd:PRK13929 224 TMEVRGRDLVTglpktITLESKEIQGAMRESLLHILEAIRATLEDCPPELSgDIVDrgVILTGGGALLNGIKEWLSEEIV 303
|
250
....*....|....*.
gi 2099396667 407 RAPSKAVNPDEAVAIG 422
Cdd:PRK13929 304 VPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
348-432 |
3.19e-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: 53.32 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 348 LSRSQFEGIVAdlikrTVAPCQKAMQDAEVsksDIGEVILVGGMTRMPKVQQTVQDLFGrAPSKAVNPDEAVAIGAAIQG 427
Cdd:cd07809 368 LARAALEGATF-----GLRYGLDILRELGV---EIDEIRLIGGGSKSPVWRQILADVFG-VPVVVPETGEGGALGAALQA 438
|
....*
gi 2099396667 428 GVLAG 432
Cdd:cd07809 439 AWGAG 443
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
350-437 |
4.72e-07 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 52.91 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 350 RSQFEGIVADLikrtvAPCQKAMQDAEVsksDIGEVILVGGMTRMPKVQQTVQDLFGRaPSKAVNPDEAVAIGAAIQGGV 429
Cdd:COG1070 372 RAVLEGVAFAL-----RDGLEALEEAGV---KIDRIRATGGGARSPLWRQILADVLGR-PVEVPEAEEGGALGAALLAAV 442
|
....*...
gi 2099396667 430 LAGDVTDV 437
Cdd:COG1070 443 GLGLYDDL 450
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
168-258 |
5.93e-07 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 51.37 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 168 IGAF-VLMKMKETAENYLGHPAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSedkiiAVYD 246
Cdd:PRK15080 67 IGAVtIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG-----AVVD 141
|
90
....*....|..
gi 2099396667 247 LGGGTFDISILE 258
Cdd:PRK15080 142 IGGGTTGISILK 153
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
58-304 |
2.53e-05 |
|
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: 46.36 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQ-------AKVLENSEGARTTPSVVAFTADGER-LVGMPAKRQAVTNPHNTFYatkrligrr 129
Cdd:cd10227 1 IGIDIGNGNTKVVTGGGKEfkfpsavAEARESSLDDGLLEDDIIVEYNGKRyLVGELALREGGGGRSTGDD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 130 fddsevKKDIKNVPFKIVRASngdawveahgKLYSPSQIGAFVLMkmketaenyLGHPAKNavitvpaYFNDSQRQATKD 209
Cdd:cd10227 72 ------KKKSEDALLLLLAAL----------ALLGDDEEVDVNLV---------VGLPISE-------YKEEKKELKKKL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 210 AGQISG-----------LNVLRVINEPTAAALAYGLDKSE--DKIIAVYDLGGGTFDISILEIQKGVFEvkstNGDTFLG 276
Cdd:cd10227 120 LKGLHEftfngkerritINDVKVLPEGAGAYLDYLLDDDEleDGNVLVIDIGGGTTDILTFENGKPIEE----SSDTLPG 195
|
250 260
....*....|....*....|....*...
gi 2099396667 277 GEDFDQALLQYIVKEFKRETGVDLTKDN 304
Cdd:cd10227 196 GEEALEKYADDILNELLKKLGDELDSAD 223
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
58-316 |
3.19e-05 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 46.44 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVMEGKQakvlensegaRTTPSVVAFTADgerlvgmpakrqavtnphntfyatkrLIGRRFddseVKK 137
Cdd:cd24009 4 IGIDLGTSRSAVVTSRGKR----------FSFRSVVGYPKD--------------------------IIARKL----LGK 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 138 DiknVPFkivrasnGDAWVE--AHGKLYSPSQIG--AFVLMKMKETAENYLGH------PAKN----AVITVPAYFNDSQ 203
Cdd:cd24009 44 E---VLF-------GDEALEnrLALDLRRPLEDGviKEGDDRDLEAARELLQHlielalPGPDdeiyAVIGVPARASAEN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 204 RQATKDAGQISGLNVLrVINEPTAAAlaYGLDKSEDKIIAvyDLGGGTFDISILeiqKGVFevkSTNGD---TFLGGEDF 280
Cdd:cd24009 114 KQALLEIARELVDGVM-VVSEPFAVA--YGLDRLDNSLIV--DIGAGTTDLCRM---KGTI---PTEEDqitLPKAGDYI 182
|
250 260 270
....*....|....*....|....*....|....*.
gi 2099396667 281 DQALLQYIVKEFKretGVDLTKdNMalqrVREASEK 316
Cdd:cd24009 183 DEELVDLIKERYP---EVQLTL-NM----ARRWKEK 210
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
58-292 |
9.52e-05 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 45.08 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 58 IGIDLGTTNSCVAVmEGKqAKVLenSEgarttPSVVAFTADGERL--VGMPAKRQAVTNPHNT-------------FYAT 122
Cdd:PRK13927 8 LGIDLGTANTLVYV-KGK-GIVL--NE-----PSVVAIRTDTKKVlaVGEEAKQMLGRTPGNIvairpmkdgviadFDVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 123 KRLIgRRFddsevkkdIKNVPfkivrasngdawveaHGKLYSPsqigafvlmkmketaenylghpakNAVITVPAYFNDS 202
Cdd:PRK13927 79 EKML-KYF--------IKKVH---------------KNFRPSP------------------------RVVICVPSGITEV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 203 QRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDISILEIQkGVFEVKSTNgdtfLGGEDFDQ 282
Cdd:PRK13927 111 ERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVVDIGGGTTEVAVISLG-GIVYSKSVR----VGGDKFDE 185
|
250
....*....|
gi 2099396667 283 ALLQYIVKEF 292
Cdd:PRK13927 186 AIINYVRRNY 195
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
292-432 |
2.56e-04 |
|
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: 44.12 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 292 FKRETGVDLTKDNMALQRVREASEKakcelSSSVqtdINLPYLTMDASGPKHLNMK--------------LSRSQFEGIv 357
Cdd:cd07773 306 FRDLFGGDESDLAAADELAEAAPPG-----PTGL---LFLPHLSGSGTPDFDPDARgaflgltlgttradLLRAILEGL- 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099396667 358 ADLIKRTVAPCQKAMQDaevsksdIGEVILVGGMTRMPKVQQTVQDLFGRaPSKAVNPDEAVAIGAAIQGGVLAG 432
Cdd:cd07773 377 AFELRLNLEALEKAGIP-------IDEIRAVGGGARSPLWLQLKADILGR-PIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
350-431 |
4.85e-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: 41.93 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 350 RSQFEGIVAdlikrTVAPCQKAMQDAEvsKSDIGEVILVGGMTRMPKVQQTVQDLFGRaPSKAVNPDEAVAIGAAIQGGV 429
Cdd:pfam02782 124 RAILESLAL-----QLRQILEALTKQE--GHPIDTIHVSGGGSRNPLLLQLLADALGL-PVVVPGPDEATALGAALLAAV 195
|
..
gi 2099396667 430 LA 431
Cdd:pfam02782 196 AA 197
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
350-432 |
1.45e-03 |
|
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: 41.74 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 350 RSQFEGIVADlIKRTVapcqKAMQDAEVsksDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPdEAVAIGAAIQGGV 429
Cdd:cd07779 331 RAILEGIAFE-LRDNL----EAMEKAGV---PIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETS-EATALGAAILAAV 401
|
...
gi 2099396667 430 LAG 432
Cdd:cd07779 402 GAG 404
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
175-395 |
1.88e-03 |
|
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: 40.74 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 175 KMKETAENYLGHPAKNAVITVPAYFNDSQRQATKdagqiSGLNVLRVINEPTAAALAYGLDKSEDKIIAVYDLGGGTFDI 254
Cdd:cd24004 54 ELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 255 SIleIQKGVFEVKSTNGdtfLGGEDFDQAllqyIVKEFKretgVDLtkdnmalqrvrEASEKAKCELSSSvqtDINLPYL 334
Cdd:cd24004 129 AL--IRNGGIEAYRMVP---LGGDDFTKA----IAEGFL----ISF-----------EEAEKIKRTYGIF---LLIEAKD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099396667 335 TMDASGPKHLNMKLSRSQFEGIVADLIkrtvapcqKAMQDAEVSKSDIGEVILVGGMTRMP 395
Cdd:cd24004 182 QLGFTINKKEVYDIIKPVLEELASGIA--------NAIEEYNGKFKLPDAVYLVGGGSKLP 234
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
373-432 |
3.15e-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: 3.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099396667 373 QDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPdEAVAIGAAIQGGVLAG 432
Cdd:cd07798 390 QLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGR-EASALGAAICAAVGAG 448
|
|
| |
