|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
32-643 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 952.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQH 111
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 112 DIKFFPFKVVEK-NSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:PTZ00009 86 DMKHWPFKVTTGgDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKK-EGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKL 269
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKgDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 270 -YKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLED 348
Cdd:PTZ00009 246 fKRKNRGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEKVLKD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 349 ADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQAGVLSGEQD--TDAIVLLDVNPLTMGI 426
Cdd:PTZ00009 326 AGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSsqVQDLLLLDVTPLSLGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 427 ETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEIDAN 506
Cdd:PTZ00009 406 ETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDAN 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 507 GILQVSAEDKGTGNKEKIVITNDQNRLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDkDKLGAKL 586
Cdd:PTZ00009 486 GILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD-EKVKGKL 564
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 587 SDDEKNKLESAIDESIKWLEQNPDADPEEYKKQKKDLEAIVQPVIAKLYQGAGGAPP 643
Cdd:PTZ00009 565 SDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQAAGGGMP 621
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
31-636 |
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: 936.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQ 110
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFT-PKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HDIKFFPFKVVEK-NSKPHISVdtSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGV 189
Cdd:pfam00012 80 RDIKHLPYKVVKLpNGDAGVEV--RYLGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 190 IAGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKL 269
Cdd:pfam00012 158 IAGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 270 YKKKKGKDIRKDNRAVQKLRREVEKAKRALSG-SHQVRIEIESFFE-GDDFSETLTRAKFEELNLDLFRSTLKPVQKVLE 347
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 348 DADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLSGEQDTDAIVLLDVNPLTMGIE 427
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVTPLSLGIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 428 TVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEIDANG 507
Cdd:pfam00012 397 TLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 508 ILQVSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDKdklGAKLS 587
Cdd:pfam00012 477 ILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE---GDKVP 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 24641404 588 DDEKNKLESAIDesikWLEQN-PDADPEEYKKQKKDLEAIVQPVIAKLYQ 636
Cdd:pfam00012 553 EAEKSKVESAIE----WLKDElEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
29-651 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 893.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 29 GTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGRewSDTN 108
Cdd:PRK00290 2 GKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGR--RDEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 109 VQHDIKFFPFKVVE-KNSKPHISVDtsqgAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:PRK00290 80 VQKDIKLVPYKIVKaDNGDAWVEID----GKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 188 GVIAGLQVMRIINEPTAAAIAYGLDKKEGEKnVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFI 267
Cdd:PRK00290 156 GKIAGLEVLRIINEPTAAALAYGLDKKGDEK-ILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 268 KLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGDD-----FSETLTRAKFEELNLDLFRSTLKPV 342
Cdd:PRK00290 235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINL-PFITADAsgpkhLEIKLTRAKFEELTEDLVERTIEPC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 343 QKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGgKEPSRGINPDEAVAYGAAVQAGVLSGE-QDtdaIVLLDVNP 421
Cdd:PRK00290 314 KQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFG-KEPNKGVNPDEVVAIGAAIQGGVLAGDvKD---VLLLDVTP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 422 LTMGIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSF 501
Cdd:PRK00290 390 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 502 EIDANGILQVSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDkdk 581
Cdd:PRK00290 470 DIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKE--- 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 582 LGAKLSDDEKNKLESAIDESIKWLEQNpdaDPEEYKKQKKDLEAIVQPVIAKLYQGAGGAPPPEGGDDAD 651
Cdd:PRK00290 546 LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGAAAKD 612
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
29-405 |
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: 834.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 29 GTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTN 108
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFT-DGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 109 VQHDIKFFPFKVVEKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd10241 80 VQKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 189 VIAGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIK 268
Cdd:cd10241 160 TIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 269 LYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLED 348
Cdd:cd10241 240 LFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLED 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 349 ADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd10241 320 AGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
31-636 |
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: 811.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDtnVQ 110
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HDIKFFPFKVVEKNSKPHISVDTsqgaKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKVDG----KEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKLY 270
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 271 KKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGDD-----FSETLTRAKFEELNLDLFRSTLKPVQKV 345
Cdd:TIGR02350 236 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINL-PFITADAsgpkhLEMTLTRAKFEELTADLVERTKEPVRQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 346 LEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLSGE-QDtdaIVLLDVNPLTM 424
Cdd:TIGR02350 315 LKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGDvKD---VLLLDVTPLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 425 GIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEID 504
Cdd:TIGR02350 391 GIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDID 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 505 ANGILQVSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDkdkLGA 584
Cdd:TIGR02350 471 ANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE---AGD 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 24641404 585 KLSDDEKNKLESAIDESIKWLEQNpdaDPEEYKKQKKDLEAIVQPVIAKLYQ 636
Cdd:TIGR02350 547 KLPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
28-645 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 718.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 28 LGTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDT 107
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 108 NVQHdiKFFPFKVVEKNSKphiSVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:PRK13411 81 EEER--SRVPYTCVKGRDD---TVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 188 GVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFI 267
Cdd:PRK13411 156 GTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 268 KLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGDD-----FSETLTRAKFEELNLDLFRSTLKPV 342
Cdd:PRK13411 236 ENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINL-PFITADEtgpkhLEMELTRAKFEELTKDLVEATIEPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 343 QKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQAGVLSGEQDTdaIVLLDVNPL 422
Cdd:PRK13411 315 QQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGEVKD--LLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 423 TMGIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFE 502
Cdd:PRK13411 393 SLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 503 IDANGILQVSAEDKGTGNKEKIVITNdQNRLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDKdkl 582
Cdd:PRK13411 473 IDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKEN--- 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641404 583 GAKLSDDEKNKLESAIDEsIKWLEQNPDADPEEYKKQKKDLEAIVQPVIAKLYQGAGGAPPPE 645
Cdd:PRK13411 549 GELISEELKQRAEQKVEQ-LEAALTDPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDT 610
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
32-405 |
0e+00 |
|
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466831 [Multi-domain] Cd Length: 375 Bit Score: 704.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQH 111
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 112 DIKFFPFKVVEKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVIA 191
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 192 GLQVMRIINEPTAAAIAYGLDKK-EGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKLY 270
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKgKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 271 KKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDAD 350
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24641404 351 MNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
29-654 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 688.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 29 GTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTN 108
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 109 VQHDIKFFPFKVV-EKNSKPHISvdtSQGaKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:PTZ00400 121 TKKEQKILPYKIVrASNGDAWIE---AQG-KKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 188 GVIAGLQVMRIINEPTAAAIAYGLDKKEGeKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFI 267
Cdd:PTZ00400 197 GKIAGLDVLRIINEPTAAALAFGMDKNDG-KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 268 KLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGDD-----FSETLTRAKFEELNLDLFRSTLKPV 342
Cdd:PTZ00400 276 AEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINL-PFITADQsgpkhLQIKLSRAKLEELTHDLLKKTIEPC 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 343 QKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGgKEPSRGINPDEAVAYGAAVQAGVLSGEqdTDAIVLLDVNPL 422
Cdd:PTZ00400 355 EKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFG-KEPSKGVNPDEAVAMGAAIQAGVLKGE--IKDLLLLDVTPL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 423 TMGIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFE 502
Cdd:PTZ00400 432 SLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFD 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 503 IDANGILQVSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDkdkL 582
Cdd:PTZ00400 512 VDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD---L 587
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 583 GAKLSDDEKNKLESAIdESIKwlEQNPDADPEEYKKQKKDLEAIVQPVIAKLYQGAGGA-----PPPEGGDDADLKD 654
Cdd:PTZ00400 588 KDKISDADKDELKQKI-TKLR--STLSSEDVDSIKDKTKQLQEASWKISQQAYKQGNSDnqqseQSTNSEESEEKND 661
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
28-624 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 687.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 28 LGTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDT 107
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 108 NvqHDIKFFPFkVVEKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:PRK13410 81 D--PESKRVPY-TIRRNEQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 188 GVIAGLQVMRIINEPTAAAIAYGLDKKEgEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFI 267
Cdd:PRK13410 158 GRIAGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 268 KLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDD----FSETLTRAKFEELNLDLFRSTLKPVQ 343
Cdd:PRK13410 237 EQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDgpkhIETRLDRKQFESLCGDLLDRLLRPVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 344 KVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGgKEPSRGINPDEAVAYGAAVQAGVLSGE-QDtdaIVLLDVNPL 422
Cdd:PRK13410 317 RALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIP-REPNQNVNPDEVVAVGAAIQAGILAGElKD---LLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 423 TMGIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFE 502
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 503 IDANGILQVSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDKD-K 581
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQGAST-LSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAAlE 551
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 24641404 582 LGAKLSDDEKNKLESAIDESIKWLEQNpdaDPEEYKKQKKDLE 624
Cdd:PRK13410 552 FGPYFAERQRRAVESAMRDVQDSLEQD---DDRELDLAVADLQ 591
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
31-542 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 686.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQ 110
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HdikffpfkvveknskphisvdtsqGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:COG0443 81 V------------------------GGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKLY 270
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 271 KKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDAD 350
Cdd:COG0443 217 GKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINL-PFSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 351 MNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLSGEQDTdaivlLDVNPLTMGIETVG 430
Cdd:COG0443 296 LSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-----LDVTPLSLGIETLG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 431 GVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEIDANGILQ 510
Cdd:COG0443 370 GVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILS 449
|
490 500 510
....*....|....*....|....*....|..
gi 24641404 511 VSAEDKGTGNKEKIVITndqnrltpEDIDRMI 542
Cdd:COG0443 450 VSAKDLGTGKEQSITIK--------EEIERML 473
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
28-655 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 683.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 28 LGTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDt 107
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 108 nVQHDIKFFPFKVVeKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:CHL00094 80 -ISEEAKQVSYKVK-TDSNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 188 GVIAGLQVMRIINEPTAAAIAYGLDKKEGEKnVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFI 267
Cdd:CHL00094 158 GKIAGLEVLRIINEPTAASLAYGLDKKNNET-ILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 268 KLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGDD-----FSETLTRAKFEELNLDLFRSTLKPV 342
Cdd:CHL00094 237 KEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINL-PFITATQtgpkhIEKTLTRAKFEELCSDLINRCRIPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 343 QKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGgKEPSRGINPDEAVAYGAAVQAGVLSGEqdTDAIVLLDVNPL 422
Cdd:CHL00094 316 ENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLG-KKPNQSVNPDEVVAIGAAVQAGVLAGE--VKDILLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 423 TMGIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFE 502
Cdd:CHL00094 393 SLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 503 IDANGILQVSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIgdkDKL 582
Cdd:CHL00094 473 IDANGILSVTAKDKGTGKEQSITIQGAST-LPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQL---KEL 548
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 583 GAKLSDDEKNKLESAIDEsikwLEQNPDADP-EEYKKQKKDLEAIVQPVIAKLYQGAGGAPPPEGGD---DADLKDE 655
Cdd:CHL00094 549 KDKISEEKKEKIENLIKK----LRQALQNDNyESIKSLLEELQKALMEIGKEVYSSTSTTDPASNDDdviDTDFSET 621
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
31-405 |
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: 658.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQ 110
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFT-DGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HDIKFFPFKVVEKNS-KPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGV 189
Cdd:cd24028 80 SDIKHWPFKVVEDEDgKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 190 IAGLQVMRIINEPTAAAIAYGLDKK-EGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIK 268
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDKKsSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 269 LYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLED 348
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 349 ADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd24028 320 AKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
31-651 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 635.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDtnVQ 110
Cdd:PLN03184 41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HDIKFFPFKVVeKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:PLN03184 119 EESKQVSYRVV-RDENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKKEGEkNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKLY 270
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKKSNE-TILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 271 KKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIE---IESFFEGDDFSET-LTRAKFEELNLDLFRSTLKPVQKVL 346
Cdd:PLN03184 277 KKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGPKHIDTtLTRAKFEELCSDLLDRCKTPVENAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 347 EDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFfGGKEPSRGINPDEAVAYGAAVQAGVLSGEqdTDAIVLLDVNPLTMGI 426
Cdd:PLN03184 357 RDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE--VSDIVLLDVTPLSLGL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 427 ETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEIDAN 506
Cdd:PLN03184 434 ETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDAN 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 507 GILQVSAEDKGTGNKEKIVITNdQNRLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIgdkDKLGAKL 586
Cdd:PLN03184 514 GILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQL---KELGDKV 589
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641404 587 SDDEKNKLESAIDEsikwLEQNPDADPEEykKQKKDLEAIVQPVIA---KLYQ-----GAGGAPPPEGGDDAD 651
Cdd:PLN03184 590 PADVKEKVEAKLKE----LKDAIASGSTQ--KMKDAMAALNQEVMQigqSLYNqpgagGAGPAPGGEAGSSSS 656
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
29-651 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 631.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 29 GTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADgERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTN 108
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGS-EKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 109 VQHDIKFFPFKVVEKNSKPHISVDTSqgAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGNGDAWVQDGN--GKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 189 VIAGLQVMRIINEPTAAAIAYGLDKKEgEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIK 268
Cdd:PTZ00186 184 TIAGLNVIRVVNEPTAAALAYGMDKTK-DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 269 LYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSE----TLTRAKFEELNLDLFRSTLKPVQK 344
Cdd:PTZ00186 263 EFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQhiqmHISRSKFEGITQRLIERSIAPCKQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 345 VLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGgKEPSRGINPDEAVAYGAAVQAGVLSGeqDTDAIVLLDVNPLTM 424
Cdd:PTZ00186 343 CMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQ-KDPFRGVNPDEAVALGAATLGGVLRG--DVKGLVLLDVTPLSL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 425 GIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEID 504
Cdd:PTZ00186 420 GIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDID 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 505 ANGILQVSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDkdklGA 584
Cdd:PTZ00186 500 ANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGE----WK 574
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 585 KLSDDEKNKLESAIDESIKWLEqNPDADPEEYKKQKKDLEAIVQPVIAKLYQGAGGAPPPEGGDDAD 651
Cdd:PTZ00186 575 YVSDAEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQKAVMECGRTEYQQAAAANSGSSSNSGE 640
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
31-406 |
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: 556.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQ 110
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HDIKFFPFkVVEKNSKPHISVDTsqgaKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:cd10234 81 RKQVPYPV-VSAGNGDAWVEIGG----KEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKKEGEKnVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKLY 270
Cdd:cd10234 156 AGLEVLRIINEPTAAALAYGLDKKKDEK-ILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 271 KKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGDD-----FSETLTRAKFEELNLDLFRSTLKPVQKV 345
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINL-PFITADAsgpkhLEMKLTRAKFEELTEDLVERTIEPVEQA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641404 346 LEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd10234 314 LKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
32-633 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 547.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGeRLIGDAAKNQLTTNPENTVFDAKRLIGREWSDtnVQH 111
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 112 DIKFFPFKVVEknSKPH-ISVDTSQGAKvfAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:PRK05183 99 RYPHLPYQFVA--SENGmPLIRTAQGLK--SPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKKEgEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKLY 270
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDSGQ-EGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 271 KKKKGKDIRkDNRAVQKLRREvekAKRALSGSHQVRIEIEsffegdDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDAD 350
Cdd:PRK05183 254 GLSPRLDPE-DQRLLLDAARA---AKEALSDADSVEVSVA------LWQGEITREQFNALIAPLVKRTLLACRRALRDAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 351 MNKKDVHEIVLVGGSTRIPKVQQLVKDFFGgKEPSRGINPDEAVAYGAAVQAGVLSGEQDTDAIVLLDVNPLTMGIETVG 430
Cdd:PRK05183 324 VEADEVKEVVMVGGSTRVPLVREAVGEFFG-RTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLETMG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 431 GVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEIDANGILQ 510
Cdd:PRK05183 403 GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 511 VSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKK---LKE-RVESRNELESYAYSLKnqigdKDklGAKL 586
Cdd:PRK05183 483 VTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQaraLAEqKVEAERVLEALQAALA-----AD--GDLL 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 24641404 587 SDDEKNKLESAIDESIKWLEQNpdaDPEEYKKQKKDLEAIVQPVIAK 633
Cdd:PRK05183 555 SAAERAAIDAAMAALREVAQGD---DADAIEAAIKALDKATQEFAAR 598
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
31-633 |
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: 538.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQ 110
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HDIkffPFKVVEkNSKPHISVDTSQGAKvfAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:TIGR01991 81 SIL---PYRFVD-GPGEMVRLRTVQGTV--TPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKKEgEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIkly 270
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDKAS-EGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 271 kKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIEsfFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDAD 350
Cdd:TIGR01991 231 -KQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDFT--LDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 351 MNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLSGEQDTDAIVLLDVNPLTMGIETVG 430
Cdd:TIGR01991 308 LSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGIETMG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 431 GVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSFEIDANGILQ 510
Cdd:TIGR01991 387 GLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 511 VSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIGDKDKLgakLSDDE 590
Cdd:TIGR01991 467 VSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDL---LSEDE 542
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 24641404 591 KNKLESAIDESIKWLEQNpdaDPEEYKKQKKDLEAIVQPVIAK 633
Cdd:TIGR01991 543 RAAIDAAMEALQKALQGD---DADAIKAAIEALEEATDNFAAR 582
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
32-405 |
0e+00 |
|
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466943 [Multi-domain] Cd Length: 375 Bit Score: 536.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGrVEIIANDQGNRITPSYVAFTADgERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQH 111
Cdd:cd24093 2 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 112 DIKFFPFKVVEKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVIA 191
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 192 GLQVMRIINEPTAAAIAYGLD--KKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKL 269
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 270 YKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDA 349
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641404 350 DMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
29-405 |
6.09e-176 |
|
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: 505.26 E-value: 6.09e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 29 GTVIGIDLGTTYSCVGVY--KNGRVeiIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSD 106
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMegKTPKV--IENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 107 TNVQHDIKFFPFKVVE-KNSKPHISVdtsqGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATK 185
Cdd:cd11733 79 PEVQKDIKMVPYKIVKaSNGDAWVEA----HGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 186 DAGVIAGLQVMRIINEPTAAAIAYGLDKKEGeKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDH 265
Cdd:cd11733 155 DAGQIAGLNVLRIINEPTAAALAYGLDKKDD-KIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 266 FIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGD-----DFSETLTRAKFEELNLDLFRSTLK 340
Cdd:cd11733 234 LVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINL-PFITADasgpkHLNMKLTRAKFESLVGDLIKRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641404 341 PVQKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd11733 313 PCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
29-407 |
1.09e-158 |
|
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: 461.15 E-value: 1.09e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 29 GTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTN 108
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 109 VQHDIKFFPFKVVeknskPHISVDT--SQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 186
Cdd:cd11734 81 VQRDIKEVPYKIV-----KHSNGDAwvEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 187 AGVIAGLQVMRIINEPTAAAIAYGLDkKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHF 266
Cdd:cd11734 156 AGQIAGLNVLRVINEPTAAALAYGLD-KSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 267 IKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIeSFFEGD-----DFSETLTRAKFEELNLDLFRSTLKP 341
Cdd:cd11734 235 VSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINL-PFITADasgpkHINMKLTRAQFESLVKPLVDRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641404 342 VQKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLSG 407
Cdd:cd11734 314 CKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
31-407 |
3.15e-150 |
|
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: 439.34 E-value: 3.15e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDtnVQ 110
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HDIKFFPFKVVEkNSKPHISVDTSQGakVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:cd10236 82 EELPLLPYRLVG-DENELPRFRTGAG--NLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKKEgEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIkly 270
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQKK-EGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWIL--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 271 kKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIEsfFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDAD 350
Cdd:cd10236 235 -KQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVE--VEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDAG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 351 MNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLSG 407
Cdd:cd10236 312 LEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
30-407 |
6.80e-149 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187.
Pssm-ID: 466835 [Multi-domain] Cd Length: 409 Bit Score: 437.54 E-value: 6.80e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 30 TVIGIDLGTTYSCVGVYK--NGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDT 107
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 108 NVQHDIKFFPFKVVEKNS-KPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 186
Cdd:cd10237 103 ELEEEAKRYPFKVVNDNIgSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 187 AGVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHF 266
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 267 IKLYKKKKGKDIrKDNRAVQKLRREVEKAKRALS--GSHQVRIEIESFFEGDD---FSETLTRAKFEELNLDLFRSTLKP 341
Cdd:cd10237 263 IDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTnhNSASLSLPLQISLPSAFkvkFKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641404 342 VQKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLSG 407
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
32-406 |
1.28e-144 |
|
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: 424.30 E-value: 1.28e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIA-NDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGRewsdtnvq 110
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 hdikffpfkvvekNSKPHISVdtsqGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:cd24029 73 -------------DTKDKEEI----GGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKL- 269
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKi 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 270 YKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDA 349
Cdd:cd24029 216 GIETGILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKDA 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 350 DMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd24029 296 KLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
30-405 |
4.88e-132 |
|
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: 393.15 E-value: 4.88e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 30 TVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNV 109
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFT-DNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 110 QHDIKFFPFKVVEKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGV 189
Cdd:cd10238 80 QELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 190 IAGLQVMRIINEPTAAAIAYGL--DKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFI 267
Cdd:cd10238 160 KAGFNVLRVISEPSAAALAYGIgqDDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 268 KLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLE 347
Cdd:cd10238 240 SEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24641404 348 DADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd10238 320 SAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
32-403 |
2.18e-129 |
|
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: 385.06 E-value: 2.18e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERLIGDAAKNQLTTNPENTVFDAKRLIGrewSDTNVqh 111
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMG---TDKQY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 112 dikffpfkvveknskphisvdtSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVIA 191
Cdd:cd10235 76 ----------------------RLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 192 GLQVMRIINEPTAAAIAYGLDKKEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDHFIKLYK 271
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 272 KKKGKDIRKDNravQKLRREVEKAKRALSGSHQVriEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDADM 351
Cdd:cd10235 214 LDFTSLSPSEL---AALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAGL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24641404 352 NKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAG 403
Cdd:cd10235 289 KPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAA 339
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
32-402 |
1.48e-117 |
|
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: 355.81 E-value: 1.48e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQH 111
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFG-EKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 112 DIKFFPFKVVE-KNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:cd10228 80 ELKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKK----EGEK--NVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMD 264
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGIYKQdlpaEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 265 HFIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSG-SHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQ 343
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLR 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641404 344 KVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQA 402
Cdd:cd10228 320 SALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
32-402 |
1.23e-113 |
|
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: 345.70 E-value: 1.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQH 111
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFT-EKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 112 DIKFFPFKVVE-KNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVI 190
Cdd:cd11732 80 EIKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 191 AGLQVMRIINEPTAAAIAYGLDKK------EGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMD 264
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSdlleseEKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 265 HFIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQK 344
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24641404 345 VLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQA 402
Cdd:cd11732 320 ALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
31-406 |
2.51e-112 |
|
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: 342.75 E-value: 2.51e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQ 110
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFG-EKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 111 HDIKFFPFKVVE-KNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGV 189
Cdd:cd24095 82 RDLKLFPFKVTEgPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 190 IAGLQVMRIINEPTAAAIAYGL---DKKEGE-KNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDH 265
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGIyktDLPETDpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 266 FIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKV 345
Cdd:cd24095 242 FAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641404 346 LEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd24095 322 LADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
31-637 |
1.94e-104 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 329.51 E-value: 1.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGerligdaaknqLTTNPENTVFDAKRLIGR---EWSDT 107
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN-----------FTIGNNKGLRSIKRLFGKtlkEILNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 108 NVQhdikffpFKVVeknsKPHISVDTSQGAKVFA-----PEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQ 182
Cdd:PRK01433 90 PAL-------FSLV----KDYLDVNSSELKLNFAnkqlrIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 183 ATKDAGVIAGLQVMRIINEPTAAAIAYGLDKkeGEKNV-LVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQR 261
Cdd:PRK01433 159 EVMLAAKIAGFEVLRLIAEPTAAAYAYGLNK--NQKGCyLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 262 VMDHFIKLYkkkkgkDIRKDNRAVQKLRreveKAKRALSGshqvrieiESFFEGDDFSetLTRAKFEELNLDLFRSTLKP 341
Cdd:PRK01433 237 ITQYLCNKF------DLPNSIDTLQLAK----KAKETLTY--------KDSFNNDNIS--INKQTLEQLILPLVERTINI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 342 VQKVLEDAdmNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSrGINPDEAVAYGAAVQAGVLSGeQDTDAIvLLDVNP 421
Cdd:PRK01433 297 AQECLEQA--GNPNIDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLIA-PHTNSL-LIDVVP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 422 LTMGIETVGGVMTKLIPRNTVIPTKKSQVFSTASDNQHTVTIQVYEGERPMTKDNHLLGKFDLTGIPPAPRGIPQIEVSF 501
Cdd:PRK01433 372 LSLGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTF 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 502 EIDANGILQVSAEDKGTGNKEKIVITNDQNrLTPEDIDRMIRDAEKFADEDKKLKERVESRNELESYAYSLKNQIgdkDK 581
Cdd:PRK01433 452 AIDADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAI---AE 527
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641404 582 LGAKLSDDEKNKLESAID---ESIKWLEQNP-DADPEEYK-KQKKDLEAIVQPVIAKLYQG 637
Cdd:PRK01433 528 LTTLLSESEISIINSLLDnikEAVHARDIILiNNSIKEFKsKIKKSMDTKLNIIINDLLKG 588
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
30-402 |
3.35e-102 |
|
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: 315.20 E-value: 3.35e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 30 TVIGIDLGTTYSCVGVYKNGR-VEIIANDQGNRITPSYVAFtADGERLIGDAAKNQLTTNPENTVFDAKRLIGrewsdtn 108
Cdd:cd10230 1 AVLGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAF-RNGERLFGDDALALATRFPENTFSYLKDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 109 vqhdikffpfkvveknskphisvdtsqgakvFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd10230 73 -------------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 189 VIAGLQVMRIINEPTAAAIAYGLDKK---EGEKNVLVFDLGGGTFDVSLLTID------------NGVFEVVATNGDTHL 253
Cdd:cd10230 122 EIAGLNVLSLINDNTAAALNYGIDRRfenNEPQNVLFYDMGASSTSATVVEFSsvkekdkgknktVPQVEVLGVGWDRTL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 254 GGEDFDQRVMDHFIKL--YKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELN 331
Cdd:cd10230 202 GGLEFDLRLADHLADEfnEKHKKDKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELC 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641404 332 LDLFRSTLKPVQKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRGINPDEAVAYGAAVQA 402
Cdd:cd10230 282 ADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
32-406 |
8.35e-97 |
|
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: 302.76 E-value: 8.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFtADGERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNVQH 111
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGF-GPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 112 DIKFFPFKVVEKNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVIA 191
Cdd:cd24094 80 EEKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 192 GLQVMRIINEPTAAAIAYGLDK------KEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMDH 265
Cdd:cd24094 160 GLNPLRLMNDTTAAALGYGITKtdlpepEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 266 FIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKV 345
Cdd:cd24094 240 FADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641404 346 LEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd24094 320 LAQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
30-405 |
4.64e-91 |
|
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: 286.18 E-value: 4.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 30 TVIGIDLGTTYSCVG-VYKNGRVEIIANDQGNRITPSYVAFTaDGERLIGDAAKNQLTTNPENTVFDAKRLIGrewsdtn 108
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 109 vqhdikffpfkvveknskphisvdtsqgAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd10232 73 ----------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 189 VIAGLQVMRIINEPTAAAIAYGLDK-----KEGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVM 263
Cdd:cd10232 125 AAAGLEVLQLIPEPAAAALAYDLRAetsgdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 264 DHFIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSGSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQ 343
Cdd:cd10232 205 GHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVT 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641404 344 KVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFGGKEPSRG---INPDEAVAYGAAVQAGVL 405
Cdd:cd10232 285 DAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIRAptqINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
30-404 |
1.98e-90 |
|
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: 286.07 E-value: 1.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 30 TVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADgERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNV 109
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPK-NRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 110 QHDIKFFPFKVVE-KNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd11737 80 QAEKPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 189 VIAGLQVMRIINEPTAAAIAYGLDKK------EGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRV 262
Cdd:cd11737 160 QIAGLNCLRLMNETTAVALAYGIYKQdlpapeEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 263 MDHFIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSG-SHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKP 341
Cdd:cd11737 240 VNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641404 342 VQKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGV 404
Cdd:cd11737 320 LRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
30-401 |
5.26e-84 |
|
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: 269.04 E-value: 5.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 30 TVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADgERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNV 109
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSK-NRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 110 QHDIKFFPFKVVE-KNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd11739 80 QKEKENLSYDLVPlKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 189 VIAGLQVMRIINEPTAAAIAYGLDKK------EGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRV 262
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIYKQdlpapdEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 263 MDHFIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALS-GSHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKP 341
Cdd:cd11739 240 VEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSsNSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 342 VQKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQ 401
Cdd:cd11739 320 LYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
30-406 |
7.14e-84 |
|
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: 268.71 E-value: 7.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 30 TVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADgERLIGDAAKNQLTTNPENTVFDAKRLIGREWSDTNV 109
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSR-NRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 110 QHDIKFFPFKVVE-KNSKPHISVDTSQGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd11738 80 QAEKIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 189 VIAGLQVMRIINEPTAAAIAYGLDKK------EGEKNVLVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRV 262
Cdd:cd11738 160 QIAGLNCLRLMNETTAVALAYGIYKQdlpaleEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 263 MDHFIKLYKKKKGKDIRKDNRAVQKLRREVEKAKRALSG-SHQVRIEIESFFEGDDFSETLTRAKFEELNLDLFRSTLKP 341
Cdd:cd11738 240 VDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641404 342 VQKVLEDADMNKKDVHEIVLVGGSTRIPKVQQLVKDFFgGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd11738 320 LKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
144-400 |
1.30e-56 |
|
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: 195.02 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 144 EISAMVLGKMKETAEAYLGKKV-------THAVVTVPAYFNDAQRQATKDAGVIAGL----QVMRIINEPTAAAIAYGLD 212
Cdd:cd10170 46 EVVADFLRALLEHAKAELGDRIwelekapIEVVITVPAGWSDAAREALREAARAAGFgsdsDNVRLVSEPEAAALYALED 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 213 KK-----EGEKNVLVFDLGGGTFDVSLLTIDNG---VFEVVATNGDTHLGGEDFDQRVMDHFIKLYKKKKGKDIRKDNRA 284
Cdd:cd10170 126 KGdllplKPGDVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 285 VQKLRREVEKAKRALSGSHQVRIEIESFFEG---DDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDA--DMNKKDVHEI 359
Cdd:cd10170 206 LAKLLREFEEAKKRFSGGEEDERLVPSLLGGglpELGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQleAKSGTPPDAV 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24641404 360 VLVGGSTRIPKVQQLVKDFFGGKEP---SRGINPDEAVAYGAAV 400
Cdd:cd10170 286 VLVGGFSRSPYLRERLRERFGSAGIiivLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
32-400 |
3.11e-37 |
|
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: 143.57 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTADGERL-----IGDAAKNQLTTNPENTVF--DAKRLIGrew 104
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGaesiyFGNDAIDAYLNDPEEGRLikSVKSFLG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 105 sdtnvqhdIKFFPFKVVeknskphisvdtsqGAKVFAPEEISAMVLGKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQAT 184
Cdd:cd10231 78 --------SSLFDETTI--------------FGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 185 -------KDAGVIAGLQVMRIINEPTAAAIAYGLDKKEgEKNVLVFDLGGGTFDVSLLTID----NGVFEVVATNGDtHL 253
Cdd:cd10231 136 aqaesrlRDAARRAGFRNVEFQYEPIAAALDYEQRLDR-EELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 254 GGEDFDQRVMDH-------------------------------------FIKLYKKKKGKDIRKDNRAVQKLRR------ 290
Cdd:cd10231 214 GGDDFDRELALKkvmphlgrgstyvsgdkglpvpawlyadlsnwhaislLYTKKTLRLLLDLRRDAADPEKIERllslve 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 291 ---------EVEKAKRALSGSHQVRIEIEsfFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDADMNKKDVHEIVL 361
Cdd:cd10231 294 dqlghrlfrAVEQAKIALSSADEATLSFD--FIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFL 371
|
410 420 430
....*....|....*....|....*....|....*....
gi 24641404 362 VGGSTRIPKVQQLVKDFFGGkEPSRGINPDEAVAYGAAV 400
Cdd:cd10231 372 TGGSSQSPAVRQALASLFGQ-ARLVEGDEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
31-399 |
3.43e-24 |
|
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: 104.67 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVG---VYKNGRVEIIANDQG------NRITPSYVAFTADGERL-IGDAAKNQLTTNPENtvfDAKRLI 100
Cdd:cd10229 2 VVAIDFGTTYSGYAysfITDPGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHsFGYEAREKYSDLAED---EEHQWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 101 GREwsdtnvqhdiKFFPFKVVEKNSKPHISVDTSQGAKVFApEEISAMVLGKMKETAEAYLGKKVTHA--------VVTV 172
Cdd:cd10229 79 YFF----------KFKMMLLSEKELTRDTKVKAVNGKSMPA-LEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 173 PAYFNDAQRQATKDAGVIAGL------QVMRIINEPTAAAIAYGLDKKEGE-------KNVLVFDLGGGTFDVSLLTI-- 237
Cdd:cd10229 148 PAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKLLAEGEekelkpgDKYLVVDCGGGTVDITVHEVle 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 238 DNGVFEVVATNGDtHLGGEDFDQRVMdHFIKLYKKKKGKDIRKDNRAV--QKLRREVEKAKRALSgshqVRI---EIESF 312
Cdd:cd10229 228 DGKLEELLKASGG-PWGSTSVDEEFE-ELLEEIFGDDFMEAFKQKYPSdyLDLLQAFERKKRSFK----LRLspeLMKSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 313 FEgddfsetltrakfeelnlDLFRSTLKPVQKVLEDADMnkKDVHEIVLVGGSTRIPKVQQLVKDFFGGKepsRGI---- 388
Cdd:cd10229 302 FD------------------PVVKKIIEHIKELLEKPEL--KGVDYIFLVGGFAESPYLQKAVKEAFSTK---VKIiipp 358
|
410
....*....|.
gi 24641404 389 NPDEAVAYGAA 399
Cdd:cd10229 359 EPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
32-400 |
6.59e-11 |
|
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: 64.03 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVgvYKNGRvEIIANDqgnritPSYVAF-TADGERL-IGDaaknqlttnpentvfDAKRLIGRewsdtnv 109
Cdd:cd10225 2 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAVdKNTGKVLaVGE---------------EAKKMLGR------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 110 qhdikffpfkvveknskphisvdtsqgakvfAPEEISAM------VLGKMkETAEAYLG---KKV--------THAVVTV 172
Cdd:cd10225 51 -------------------------------TPGNIVAIrplrdgVIADF-EATEAMLRyfiRKAhrrrgflrPRVVIGV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 173 PAYFNDAQRQATKDAGVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNvLVFDLGGGTFDVSLLTIdNGvfeVVATNGdTH 252
Cdd:cd10225 99 PSGITEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPIEEPRGS-MVVDIGGGTTEIAVISL-GG---IVTSRS-VR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 253 LGGEDFDQRVMDHFiklykkkkgkdirKDNRAVQKLRREVEKAKralsgshqvrIEIESFFEGDDfSETLT--------- 323
Cdd:cd10225 173 VAGDEMDEAIINYV-------------RRKYNLLIGERTAERIK----------IEIGSAYPLDE-ELSMEvrgrdlvtg 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 324 RAKFEELNLDLFRSTLKP--------VQKVLED-----ADmnkkDVHE--IVLVGGSTRIPKVQQLVKDFFGgkEPSRGI 388
Cdd:cd10225 229 LPRTIEITSEEVREALEEpvnaiveaVRSTLERtppelAA----DIVDrgIVLTGGGALLRGLDELLREETG--LPVHVA 302
|
410
....*....|...
gi 24641404 389 -NPDEAVAYGAAV 400
Cdd:cd10225 303 dDPLTCVAKGAGK 315
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
136-380 |
1.23e-10 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 64.11 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 136 GAKVFAPEEIS-------AMVLgKMKETAEAYLGKKVTHAVVTVPAYFN-----DAQRQAT---KDAGVIAGLQVMRIIN 200
Cdd:PRK11678 114 GASGLKPQQVAlfedlvcAMML-HIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 201 EPTAAAIAY--GLDKkegEKNVLVFDLGGGTFDVSLLT-----IDNgvfevvaTNGDTHL--------GGEDFD-----Q 260
Cdd:PRK11678 193 EPVAAGLDFeaTLTE---EKRVLVVDIGGGTTDCSMLLmgpswRGR-------ADRSASLlghsgqriGGNDLDialafK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 261 RVMDH--------------------------------FIKLYKKKKGKDIRKDNRAVQKLRR---------------EVE 293
Cdd:PRK11678 263 QLMPLlgmgsetekgialpslpfwnavaindvpaqsdFYSLANGRLLNDLIRDAREPEKVARllkvwrqrlsyrlvrSAE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 294 KAKRALSGSHQVRIEIeSFFEgDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDADMnKKDVheIVLVGGSTRIP---- 369
Cdd:PRK11678 343 EAKIALSDQAETRASL-DFIS-DGLATEISQQGLEEAISQPLARILELVQLALDQAQV-KPDV--IYLTGGSARSPlira 417
|
330
....*....|....*...
gi 24641404 370 KVQQL-------VKDFFG 380
Cdd:PRK11678 418 ALAQQlpgipivGGDDFG 435
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
152-253 |
3.09e-07 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 51.88 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 152 KMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVIAGLQVMRIINEPTAAAIAYGLdkkegeKNVLVFDLGGGTFD 231
Cdd:cd24047 51 KLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI------RDGAVVDIGGGTTG 124
|
90 100
....*....|....*....|....*.
gi 24641404 232 VSLltIDNGvfEVVAT----NGDTHL 253
Cdd:cd24047 125 IAV--LKDG--KVVYTadepTGGTHL 146
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
32-266 |
4.33e-07 |
|
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: 52.39 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTtySCVGVYKNGRvEIIANDqgnritPSYVAFTADGERLI--GDaaknqlttnpentvfDAKRLIGRewsdtnv 109
Cdd:COG1077 10 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIDKKTGKVLavGE---------------EAKEMLGR------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 110 qhdikffpfkvveknskphisvdtsqgakvfAPEEISAM------VLGKMkETAEAYLG---KKVT--------HAVVTV 172
Cdd:COG1077 59 -------------------------------TPGNIVAIrplkdgVIADF-EVTEAMLKyfiKKVHgrrsffrpRVVICV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 173 PAYFNDAQRQATKDAGVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNvLVFDLGGGTFDVSLltIDNGvfEVVATNGdTH 252
Cdd:COG1077 107 PSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTGN-MVVDIGGGTTEVAV--ISLG--GIVVSRS-IR 180
|
250
....*....|....
gi 24641404 253 LGGEDFDQRVMDHF 266
Cdd:COG1077 181 VAGDELDEAIIQYV 194
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
28-266 |
5.25e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 52.06 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 28 LGTVIGIDLGTTYscVGVYKNGRvEIIANDqgnritPSYVAFTADGERL--IGDAAKNQLTTNPENTV------------ 93
Cdd:PRK13930 7 FSKDIGIDLGTAN--TLVYVKGK-GIVLNE------PSVVAIDTKTGKVlaVGEEAKEMLGRTPGNIEairplkdgviad 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 94 FDAkrligrewsdtnVQHDIKFFPFKVVEKNS--KPHIsvdtsqgakvfapeeisamvlgkmketaeaylgkkvthaVVT 171
Cdd:PRK13930 78 FEA------------TEAMLRYFIKKARGRRFfrKPRI---------------------------------------VIC 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 172 VPAYFNDAQRQATKDAGVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVfDLGGGTFDVSLLTIDNgvfevVATNGDT 251
Cdd:PRK13930 107 VPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPVTEPVGNMVV-DIGGGTTEVAVISLGG-----IVYSESI 180
|
250
....*....|....*
gi 24641404 252 HLGGEDFDQRVMDHF 266
Cdd:PRK13930 181 RVAGDEMDEAIVQYV 195
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
28-265 |
1.61e-06 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 50.67 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 28 LGTVIGIDLGTtySCVGVYKNGRvEIIANDqgnritPSYVAFTADGERLI--GDAAKNQLTTNPENTVfdAKRLIgREws 105
Cdd:PRK13928 2 FGRDIGIDLGT--ANVLVYVKGK-GIVLNE------PSVVAIDKNTNKVLavGEEARRMVGRTPGNIV--AIRPL-RD-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 106 dtNVQHDikffpFKVVEKNSKPHIsvDTSQGAKVFAPEEIsamvlgkmketaeaylgkkvthaVVTVPAYFNDAQRQATK 185
Cdd:PRK13928 68 --GVIAD-----YDVTEKMLKYFI--NKACGKRFFSKPRI-----------------------MICIPTGITSVEKRAVR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 186 DAGVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNvLVFDLGGGTFDVSLLTIDNGVfevvaTNGDTHLGGEDFDQRVMDH 265
Cdd:PRK13928 116 EAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGN-MVVDIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFDEAIIRY 189
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
149-253 |
2.15e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 49.83 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 149 VLGKMKETAEAYLGKKVTHAVVTVPAyfndaqrqAT--KDAGVI------AGLQVMRIINEPTAAAIAYGLdkkegeKNV 220
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGI------DNG 137
|
90 100 110
....*....|....*....|....*....|....*..
gi 24641404 221 LVFDLGGGTFDVSLLtiDNGvfEVVAT----NGDTHL 253
Cdd:PRK15080 138 AVVDIGGGTTGISIL--KDG--KVVYSadepTGGTHM 170
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
125-380 |
2.24e-06 |
|
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: 49.60 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 125 SKPHISVDTSQGAkVFAPEEIsAMVLGKMKETAEAYLGKKVTHAVVTVP----AYFNDAQRqatkdagviAGLQVMRIIN 200
Cdd:cd24004 29 SEEHPERAMGDGQ-IHDISKV-AESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 201 EPTAAAIAYGLDKKEgEKNVLVFDLGGGTFDVSLltIDNGVfeVVATnGDTHLGGEDFDQRVMDHFiklykkkkgkDIRK 280
Cdd:cd24004 98 EPFAAANLLIPYDMR-DLNIALVDIGAGTTDIAL--IRNGG--IEAY-RMVPLGGDDFTKAIAEGF----------LISF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 281 DnravqklrrEVEKAKRALSGShqvrieiESFFEGDDFSETLTRAKFEELNLDLFRSTLKPVQKVLEDADMNKKDVHEIV 360
Cdd:cd24004 162 E---------EAEKIKRTYGIF-------LLIEAKDQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKFKLPDAVY 225
|
250 260
....*....|....*....|
gi 24641404 361 LVGGSTRIPKVQQLVKDFFG 380
Cdd:cd24004 226 LVGGGSKLPGLNEALAEKLG 245
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
32-236 |
2.71e-06 |
|
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: 49.86 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGTTYSCVgvYKNGRvEIIANDqgnritPSYVAFTADGERLI--GDAAKNQLTTNPENTVfdAKR-LIGREWSD-T 107
Cdd:pfam06723 4 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAINTKTKKVLavGNEAKKMLGRTPGNIV--AVRpLKDGVIADfE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 108 NVQHDIKFFPFKVVEKNSKPHISVdtsqgakvfapeeisamvlgkmketaeaylgkkvthaVVTVPAYFNDAQRQATKDA 187
Cdd:pfam06723 73 VTEAMLKYFIKKVHGRRSFSKPRV-------------------------------------VICVPSGITEVERRAVKEA 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24641404 188 GVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNvLVFDLGGGTFDVSLLT 236
Cdd:pfam06723 116 AKNAGAREVFLIEEPMAAAIGAGLPVEEPTGN-MVVDIGGGTTEVAVIS 163
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
139-265 |
7.85e-06 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 48.36 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 139 VFAPEEISAMVLGKMKETAEAYLGKKV--THAVVTVPAYFNDAQRQATKDAGVIAGLQVMRIINEPTAAAIAYGLDKKEG 216
Cdd:PRK13929 70 VIADYDMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEP 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24641404 217 EKNVLVfDLGGGTFDVSLLTidngvFEVVATNGDTHLGGEDFDQRVMDH 265
Cdd:PRK13929 150 VANVVV-DIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSF 192
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
355-407 |
1.88e-04 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 44.46 E-value: 1.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 24641404 355 DVHEIVLVGGSTRIPKVQQLVKDFFGgkEPSRGINPDEAVAYGAAVQAGVLSG 407
Cdd:cd07809 393 EIDEIRLIGGGSKSPVWRQILADVFG--VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
31-380 |
2.58e-04 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 43.80 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 31 VIGIDLGTTYSCVGVYKNGRVEII-------ANDQG--NRITPSYVAFTADGE-RLIGDAAKNQL-TTNPENtvfdakrl 99
Cdd:cd11736 2 VVAIDFGTTSSGYAFSFSSDPEAIhmmrkweGGDPGvaNQKTPTSLLLTPDGAfHSFGYTARDYYhDLDPEE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 100 iGREWsdtnvqhdIKFFPFKVvEKNSKPHISVDTS----QGAKVFAPEEISAMV-------LGKMKETAEAYLGKKVTHA 168
Cdd:cd11736 74 -ARDW--------LYFEKFKM-KIHSTSDLTMETEleavNGKKVQALEVFAHALrffkehaLQELKDQSPSLPEKDAVRW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 169 VVTVPAYFNDAQRQATKDAGVIAGL------QVMRIINEPTAAAI-AYGLDKkegeknVLVFDLGGGTFDVSLLTID--N 239
Cdd:cd11736 144 VLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR------YIVADCGGGTVDLTVHQIEqpQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 240 GVF-EVVATNGD---------------THLGGEDFdqrvMDHFiklykkkkgkdirkdnravqklrreveKAKRALSGsh 303
Cdd:cd11736 218 GTLkELYKASGGpygavgvdlafekllCQIFGEDF----IATF---------------------------KAKRPAAW-- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 304 qvrIEIESFFEGDDFSETLtRAKFEELNlDLFRSTLKPVQKVLEDAdMNKKDVHEI---VLVGGSTRIPKVQQLVKDFFG 380
Cdd:cd11736 265 ---VDLTIAFEARKRTAAL-RMSSEAMN-ELFQPTISQIIQHIDDL-MKKPEVKGIkflFLVGGFAESPMLQRAVQAAFG 338
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
355-411 |
1.01e-03 |
|
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: 42.13 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641404 355 DVHEIVLVGGSTRIPKVQQLVKDFFGgkEPSRGINPDEAVAYGAAVQAGVLSGEQDT 411
Cdd:COG1070 395 KIDRIRATGGGARSPLWRQILADVLG--RPVEVPEAEEGGALGAALLAAVGLGLYDD 449
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
169-265 |
1.15e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 41.61 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 169 VVTVPAYFNDAQRQATKDAGVIAGLQVMRIINEPTAAAIAYGLDKKEGEKNVLVfDLGGGTFDVSLLTIdNGvfevVATN 248
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVV-DIGGGTTEVAVISL-GG----IVYS 173
|
90
....*....|....*..
gi 24641404 249 GDTHLGGEDFDQRVMDH 265
Cdd:PRK13927 174 KSVRVGGDKFDEAIINY 190
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
168-266 |
1.33e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 39.37 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 168 AVVTVPAYFNDAQRQAT-----------KDAGVIAGLQVMRIINEPTAAAIAYGLDKKEGekNVLVFDLGGGTfdvsllt 236
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPE--GLLVVDLGGGT------- 86
|
90 100 110
....*....|....*....|....*....|
gi 24641404 237 idNGVFEVVATNGDTHLggEDFDQRVMDHF 266
Cdd:cd00012 87 --DISANVVLVGGGARN--NGLAKRLKELL 112
|
|
| HyuA |
COG0145 |
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport ... |
187-255 |
1.48e-03 |
|
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 439915 [Multi-domain] Cd Length: 678 Bit Score: 41.61 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641404 187 AGVIAglqvmriineptAAAIAygldKKEGEKNVLVFDLGGGTFDVSLltIDNGVFEVVAtngDTHLGG 255
Cdd:COG0145 261 GGVVG------------AAALA----RAAGFDNVITFDMGGTSTDVSL--IEDGEPERTT---ETEVAG 308
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
32-283 |
3.12e-03 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 39.81 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 32 IGIDLGttyscvgvykNGRVEIIANDQGNRITPSYVAfTADGERLIGDAAKNQLTTNPENTVF----DAKRLIGREWSDT 107
Cdd:cd10227 1 IGIDIG----------NGNTKVVTGGGKEFKFPSAVA-EARESSLDDGLLEDDIIVEYNGKRYlvgeLALREGGGGRSTG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 108 NVQHDIKFFPFKVveknsKPHISVDTSQGAKVFApeeisaMVLG------KMKETAEAYLGKKVTHAVVtvpayFNDAQR 181
Cdd:cd10227 70 DDKKKSEDALLLL-----LAALALLGDDEEVDVN------LVVGlpiseyKEEKKELKKKLLKGLHEFT-----FNGKER 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641404 182 QAT-KDAGVIAglqvmriinEPTAAAIAYGLDKKEGE-KNVLVFDLGGGTFDVslLTIDNGvfEVVATNGDTHLGGEDFD 259
Cdd:cd10227 134 RITiNDVKVLP---------EGAGAYLDYLLDDDELEdGNVLVIDIGGGTTDI--LTFENG--KPIEESSDTLPGGEEAL 200
|
250 260
....*....|....*....|....
gi 24641404 260 QRVMDHFIKLYKKKKGKDIRKDNR 283
Cdd:cd10227 201 EKYADDILNELLKKLGDELDSADK 224
|
|
| |
