|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 982.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQ 110
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPK-ERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 QDIKFLPFKVVEK-KTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 189
Cdd:pfam00012 80 RDIKHLPYKVVKLpNGDAGVEVRYLG---ETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 190 TIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIK 269
Cdd:pfam00012 157 QIAGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 270 LYKKKTGKDVRKDNRAVQKLRREVEKAKRALSS-QHQARIEIESFFE-GEDFSETLTRAKFEELNMDLFRSTMKPVQKVL 347
Cdd:pfam00012 237 EFKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 348 EDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGI 427
Cdd:pfam00012 317 KDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVTPLSLGI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 428 ETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVN 507
Cdd:pfam00012 396 ETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDAN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 508 GILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKeklGGKL 587
Cdd:pfam00012 476 GILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE---GDKV 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 254540168 588 SSEDKEtmekAVEEKIEWLESH-QDADIEDFKAKKKELEEIVQPIISKLY 636
Cdd:pfam00012 552 PEAEKS----KVESAIEWLKDElEGDDKEEIEAKTEELAQVSQKIGERMY 597
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
32-645 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 962.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 111
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 DIKFLPFKVVEK-KTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:PTZ00009 86 DMKHWPFKVTTGgDDKPMIEVTYQG-EKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKR-EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIK 269
Cdd:PTZ00009 165 IAGLNVLRIINEPTAAAIAYGLDKKgDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 270 LYKKKT-GKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLE 348
Cdd:PTZ00009 245 DFKRKNrGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEKVLK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 349 DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQD--TGDLVLLDVCPLTLG 426
Cdd:PTZ00009 325 DAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSsqVQDLLLLDVTPLSLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 427 IETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDV 506
Cdd:PTZ00009 405 LETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDA 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 507 NGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDkEKLGGK 586
Cdd:PTZ00009 485 NGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD-EKVKGK 563
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 587 LSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLY-GSGGPPPTG 645
Cdd:PTZ00009 564 LSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYqAAGGGMPGG 623
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
29-654 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 916.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTwnDPS 108
Cdd:PRK00290 2 GKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFLPFKVVEKKTKPYIqVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:PRK00290 80 VQKDIKLVPYKIVKADNGDAW-VEIDG---KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKrEGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 268
Cdd:PRK00290 156 GKIAGLEVLRIINEPTAAALAYGLDK-KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 269 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFFEG-EDFSETLTRAKFEELNMDLFRSTMKPVQ 344
Cdd:PRK00290 235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINlpfITADASGpKHLEIKLTRAKFEELTEDLVERTIEPCK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 345 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPLT 424
Cdd:PRK00290 315 QALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD--VKDVLLLDVTPLS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 425 LGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEI 504
Cdd:PRK00290 392 LGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 505 DVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDkekLG 584
Cdd:PRK00290 472 DANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKE---LG 547
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254540168 585 GKLSSEDKETMEKAVEEkiewLES-HQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDE 654
Cdd:PRK00290 548 DKVPADEKEKIEAAIKE----LKEaLKGEDKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDD 614
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
29-406 |
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: 870.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPS 108
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFT-DGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFLPFKVVEKKTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:cd10241 80 VQKDIKLLPFKIVNKNGKPYIQVEVKG-EKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 268
Cdd:cd10241 159 GTIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 269 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLE 348
Cdd:cd10241 239 KLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 254540168 349 DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 406
Cdd:cd10241 319 DAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 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: 835.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsVQ 110
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 QDIKFLPFKVVEKKTKPYIQVDigggqTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKVD-----GKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 270
Cdd:TIGR02350 155 IAGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 YKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGED----FSETLTRAKFEELNMDLFRSTMKPVQKV 346
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVRQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 347 LEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGdqDTGDLVLLDVCPLTLG 426
Cdd:TIGR02350 315 LKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKG--DVKDVLLLDVTPLSLG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 427 IETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDV 506
Cdd:TIGR02350 392 IETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 507 NGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDkekLGGK 586
Cdd:TIGR02350 472 NGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE---AGDK 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 254540168 587 LSSEDKETMEKAVEEKIEWLEshqDADIEDFKAKKKELEEIVQPIISKLY 636
Cdd:TIGR02350 548 LPAEEKEKIEKAVAELKEALK---GEDVEEIKAKTEELQQALQKLAEAMY 594
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
32-406 |
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: 725.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 111
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 DIKFLPFKVVEKKTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 191
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKG-ETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 192 AGLNVMRIINEPTAAAIAYGLDKR-EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 270
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDKKgKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 YKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 350
Cdd:cd10233 240 FKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 254540168 351 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 406
Cdd:cd10233 320 KLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
29-653 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 719.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPS 108
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFLPFKVVEKKT-KPYIQvdiggGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 187
Cdd:PTZ00400 121 TKKEQKILPYKIVRASNgDAWIE-----AQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 188 AGTIAGLNVMRIINEPTAAAIAYGLDKREGeKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 267
Cdd:PTZ00400 196 AGKIAGLDVLRIINEPTAAALAFGMDKNDG-KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 268 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQarIEIESFFEGEDFSE------TLTRAKFEELNMDLFRSTMK 341
Cdd:PTZ00400 275 IAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQ--TEINLPFITADQSGpkhlqiKLSRAKLEELTHDLLKKTIE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 342 PVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVC 421
Cdd:PTZ00400 353 PCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE--IKDLLLLDVT 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 422 PLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVT 501
Cdd:PTZ00400 430 PLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVT 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 502 FEIDVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDke 581
Cdd:PTZ00400 510 FDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD-- 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 582 kLGGKLSSEDKETMekavEEKIEWLESH-QDADIEDFKAKKKELEEIVQPIISKLYGSG-------GPPPTGEEDTSEKD 653
Cdd:PTZ00400 587 -LKDKISDADKDEL----KQKITKLRSTlSSEDVDSIKDKTKQLQEASWKISQQAYKQGnsdnqqsEQSTNSEESEEKND 661
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
29-650 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 715.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDps 108
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFLPFKVVEKKTKPyIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:PRK13411 80 TEEERSRVPYTCVKGRDDT-VNVQIRG---RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 268
Cdd:PRK13411 156 GTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 269 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFFEGEDFSET-LTRAKFEELNMDLFRSTMKPVQ 344
Cdd:PRK13411 236 ENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINlpfITADETGPKHLEMeLTRAKFEELTKDLVEATIEPMQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 345 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDtgDLVLLDVCPLT 424
Cdd:PRK13411 316 QALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGEVK--DLLLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 425 LGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEI 504
Cdd:PRK13411 394 LGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 505 DVNGILRVTAEDKGTGNKNKITITNdQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLg 584
Cdd:PRK13411 474 DVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGEL- 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254540168 585 gkLSSEDKETMEKAVEEkIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTS 650
Cdd:PRK13411 552 --ISEELKQRAEQKVEQ-LEAALTDPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDTVEPT 614
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
31-543 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 713.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsvq 110
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 qdikflpfkvvekktkpyIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:COG0443 77 ------------------EATEVGG---KRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAAR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 270
Cdd:COG0443 136 IAGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 YKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIeSFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 350
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINL-PFSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 351 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTgdlvlLDVCPLTLGIETV 430
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-----LDVTPLSLGIETL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 431 GGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGIL 510
Cdd:COG0443 369 GGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGIL 448
|
490 500 510
....*....|....*....|....*....|...
gi 254540168 511 RVTAEDKGTGNKNKITITndqnrltpEEIERMV 543
Cdd:COG0443 449 SVSAKDLGTGKEQSITIK--------EEIERML 473
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
29-655 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 709.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDps 108
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFLPFKVVeKKTKPYIQVDIGGGQtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:CHL00094 80 ISEEAKQVSYKVK-TDSNGNIKIECPALN-KDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKREGEKnILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 268
Cdd:CHL00094 158 GKIAGLEVLRIINEPTAASLAYGLDKKNNET-ILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 269 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGED----FSETLTRAKFEELNMDLFRSTMKPVQ 344
Cdd:CHL00094 237 KEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTgpkhIEKTLTRAKFEELCSDLINRCRIPVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 345 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPLT 424
Cdd:CHL00094 317 NALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE--VKDILLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 425 LGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEI 504
Cdd:CHL00094 394 LGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 505 DVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIgdkEKLG 584
Cdd:CHL00094 474 DANGILSVTAKDKGTGKEQSITIQGAST-LPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQL---KELK 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254540168 585 GKLSSEDKETMEKAVEEKIEWLEShqdADIEDFKAKKKELEEIVQPIISKLYGSggppPTGEEDTSEKDEL 655
Cdd:CHL00094 550 DKISEEKKEKIENLIKKLRQALQN---DNYESIKSLLEELQKALMEIGKEVYSS----TSTTDPASNDDDV 613
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
31-406 |
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: 691.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQ 110
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFT-DGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 QDIKFLPFKVVEKKT-KPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 189
Cdd:cd24028 80 SDIKHWPFKVVEDEDgKPKIEVTYKG-EEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 190 TIAGLNVMRIINEPTAAAIAYGLDKR-EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 268
Cdd:cd24028 159 TIAGLNVLRIINEPTAAALAYGLDKKsSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 269 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLE 348
Cdd:cd24028 239 EEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 254540168 349 DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 406
Cdd:cd24028 319 DAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
29-615 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 678.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDps 108
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFLPFKVvekKTKPYIQVDIGGGQT-KTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 187
Cdd:PRK13410 80 LDPESKRVPYTI---RRNEQGNVRIKCPRLeREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 188 AGTIAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 267
Cdd:PRK13410 157 AGRIAGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 268 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGED----FSETLTRAKFEELNMDLFRSTMKPV 343
Cdd:PRK13410 236 AEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDgpkhIETRLDRKQFESLCGDLLDRLLRPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 344 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPL 423
Cdd:PRK13410 316 KRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE--LKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 424 TLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFE 503
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 504 IDVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKE-K 582
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQGAST-LSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAAlE 551
|
570 580 590
....*....|....*....|....*....|...
gi 254540168 583 LGGKLSSEDKETMEKAVEEKIEWLESHQDADIE 615
Cdd:PRK13410 552 FGPYFAERQRRAVESAMRDVQDSLEQDDDRELD 584
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
31-651 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 656.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsVQ 110
Cdd:PLN03184 41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 QDIKFLPFKVVeKKTKPYIQVD---IGggqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 187
Cdd:PLN03184 119 EESKQVSYRVV-RDENGNVKLDcpaIG----KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 188 AGTIAGLNVMRIINEPTAAAIAYGLDKREGEkNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 267
Cdd:PLN03184 194 AGRIAGLEVLRIINEPTAASLAYGFEKKSNE-TILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 268 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFFEGEDFSET-LTRAKFEELNMDLFRSTMKPV 343
Cdd:PLN03184 273 ASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGPKHIDTtLTRAKFEELCSDLLDRCKTPV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 344 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFfNGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPL 423
Cdd:PLN03184 353 ENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE--VSDIVLLDVTPL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 424 TLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFE 503
Cdd:PLN03184 430 SLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFD 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 504 IDVNGILRVTAEDKGTGNKNKITITNdQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIgdkEKL 583
Cdd:PLN03184 510 IDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQL---KEL 585
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254540168 584 GGKLSSEDKETMEKAVEEKIEWLEShqdADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSE 651
Cdd:PLN03184 586 GDKVPADVKEKVEAKLKELKDAIAS---GSTQKMKDAMAALNQEVMQIGQSLYNQPGAGGAGPAPGGE 650
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
29-628 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 620.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPS 108
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGS-EKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFLPFKVVEKKT-KPYIQvdigGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 187
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGNgDAWVQ----DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 188 AGTIAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 267
Cdd:PTZ00186 182 AGTIAGLNVIRVVNEPTAAALAYGMDKTK-DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 268 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSE----TLTRAKFEELNMDLFRSTMKPV 343
Cdd:PTZ00186 261 LEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQhiqmHISRSKFEGITQRLIERSIAPC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 344 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPL 423
Cdd:PTZ00186 341 KQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD--VKGLVLLDVTPL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 424 TLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFE 503
Cdd:PTZ00186 418 SLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFD 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 504 IDVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEkl 583
Cdd:PTZ00186 498 IDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWK-- 574
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 254540168 584 ggKLSSEDKETMEKAVEEKIEWLESHQDADiEDFKAKKKELEEIV 628
Cdd:PTZ00186 575 --YVSDAEKENVKTLVAELRKAMENPNVAK-DDLAAATDKLQKAV 616
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
31-407 |
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: 567.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQ 110
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 QDIKFLPfkvVEKKTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:cd10234 81 RKQVPYP---VVSAGNGDAWVEIGG---KEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKREGEKnILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 270
Cdd:cd10234 155 IAGLEVLRIINEPTAAALAYGLDKKKDEK-ILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 YKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGED----FSETLTRAKFEELNMDLFRSTMKPVQKV 346
Cdd:cd10234 234 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASgpkhLEMKLTRAKFEELTEDLVERTIEPVEQA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254540168 347 LEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 407
Cdd:cd10234 314 LKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
32-406 |
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: 561.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGrVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 111
Cdd:cd24093 2 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 DIKFLPFKVVEKKTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 191
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLG-ETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 192 AGLNVMRIINEPTAAAIAYGLD--KREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIK 269
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 270 LYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLED 349
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 254540168 350 SDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 406
Cdd:cd24093 319 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
31-634 |
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: 553.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPsvq 110
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 QDIKFLPFKVVEKKTKpYIQVDIGGGqTKTfaPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:TIGR01991 78 KTFSILPYRFVDGPGE-MVRLRTVQG-TVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIkl 270
Cdd:TIGR01991 154 LAGLNVLRLLNEPTAAAVAYGLDKAS-EGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 ykKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIEsfFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 350
Cdd:TIGR01991 231 --KQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDFT--LDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 351 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETV 430
Cdd:TIGR01991 307 GLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGIETM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 431 GGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGIL 510
Cdd:TIGR01991 386 GGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 511 RVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLggkLSSE 590
Cdd:TIGR01991 466 TVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDL---LSED 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 254540168 591 DKETMEKAVEEKIEWLeshQDADIEDFKAKKKELEEIVQPIISK 634
Cdd:TIGR01991 542 ERAAIDAAMEALQKAL---QGDDADAIKAAIEALEEATDNFAAR 582
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
32-615 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 545.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGeRLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsVQQ 111
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 DIKFLPFKVVEKK-TKPYIQVDIGggqTKTfaPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:PRK05183 99 RYPHLPYQFVASEnGMPLIRTAQG---LKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKl 270
Cdd:PRK05183 174 LAGLNVLRLLNEPTAAAIAYGLDSGQ-EGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILE- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 ykkKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIEsffegeDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 350
Cdd:PRK05183 252 ---QAGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSVA------LWQGEITREQFNALIAPLVKRTLLACRRALRDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 351 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETV 430
Cdd:PRK05183 323 GVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLETM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 431 GGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGIL 510
Cdd:PRK05183 402 GGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 511 RVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKK---LKE-RIDTRNELESYAYSLKnqigdkeKLGGK 586
Cdd:PRK05183 482 SVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQaraLAEqKVEAERVLEALQAALA-------ADGDL 553
|
570 580
....*....|....*....|....*....
gi 254540168 587 LSSEDKETMEKAVEEKIEWLESHQDADIE 615
Cdd:PRK05183 554 LSAAERAAIDAAMAALREVAQGDDADAIE 582
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
29-406 |
0e+00 |
|
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466839 [Multi-domain] Cd Length: 377 Bit Score: 520.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVF--KNGRVeiIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWND 106
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMegKTPKV--IENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 107 PSVQQDIKFLPFKVVeKKTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATK 186
Cdd:cd11733 79 PEVQKDIKMVPYKIV-KASNGDAWVEAHG---KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 187 DAGTIAGLNVMRIINEPTAAAIAYGLDKREGeKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEH 266
Cdd:cd11733 155 DAGQIAGLNVLRIINEPTAAALAYGLDKKDD-KIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 267 FIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIEsfFEGEDFSE------TLTRAKFEELNMDLFRSTM 340
Cdd:cd11733 234 LVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLP--FITADASGpkhlnmKLTRAKFESLVGDLIKRTV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254540168 341 KPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVL 406
Cdd:cd11733 312 EPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
29-408 |
3.42e-164 |
|
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: 475.40 E-value: 3.42e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPS 108
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFLPFKVVeKKTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:cd11734 81 VQRDIKEVPYKIV-KHSNGDAWVEARG---QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKrEGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 268
Cdd:cd11734 157 GQIAGLNVLRVINEPTAAALAYGLDK-SGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 269 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIEsfFEGEDFS------ETLTRAKFEELNMDLFRSTMKP 342
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLP--FITADASgpkhinMKLTRAQFESLVKPLVDRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254540168 343 VQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSG 408
Cdd:cd11734 314 CKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
31-408 |
2.51e-158 |
|
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: 459.76 E-value: 2.51e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsVQ 110
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 QDIKFLPFKVVEKkTKPYIQVDIGGGqtkTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:cd10236 82 EELPLLPYRLVGD-ENELPRFRTGAG---NLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKrEGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIkl 270
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQ-KKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWIL-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 ykKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIEsfFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 350
Cdd:cd10236 235 --KQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVE--VEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 254540168 351 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSG 408
Cdd:cd10236 311 GLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
30-408 |
2.68e-155 |
|
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: 453.72 E-value: 2.68e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 30 TVVGIDLGTTYSCVGVFK--NGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDP 107
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 108 SVQQDIKFLPFKVVEK---KTKPYIQVDiggGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQA 184
Cdd:cd10237 103 ELEEEAKRYPFKVVNDnigSAFFEVPLN---GSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 185 TKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVM 264
Cdd:cd10237 180 TRKAANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 265 EHFIKLYKKKTGKDVrKDNRAVQKLRREVEKAKRALSSQHQARIEIE-----SFFEGEDFSETLTRAKFEELNMDLFRST 339
Cdd:cd10237 260 QYLIDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqislPSAFKVKFKEEITRDLFETLNEDLFQRV 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540168 340 MKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSG 408
Cdd:cd10237 339 LEPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
32-407 |
2.50e-149 |
|
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: 436.24 E-value: 2.50e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIA-NDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSvq 110
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 qdikflpfkvvekktkpyiqvDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:cd24029 79 ---------------------EIGG---KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 270
Cdd:cd24029 135 LAGLNVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 YKKKTGK-DVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLED 349
Cdd:cd24029 215 IGIETGIlDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 254540168 350 SDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 407
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
30-406 |
9.94e-140 |
|
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: 412.79 E-value: 9.94e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 30 TVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSV 109
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDN-EKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 110 QQDIKFLPFKVVEKKTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 189
Cdd:cd10238 80 QELKKESKCKIIEKDGKPGYEIELEE-KKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 190 TIAGLNVMRIINEPTAAAIAYGL--DKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 267
Cdd:cd10238 159 EKAGFNVLRVISEPSAAALAYGIgqDDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 268 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVL 347
Cdd:cd10238 239 ASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 254540168 348 EDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 406
Cdd:cd10238 319 NSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
32-404 |
3.60e-135 |
|
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: 399.70 E-value: 3.60e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGrtwndpsvqq 111
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 dikflpfkvvekKTKPYIqvdIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 191
Cdd:cd10235 71 ------------TDKQYR---LGN---HTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGEL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 192 AGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLY 271
Cdd:cd10235 133 AGLKVERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 272 KKKTGKDVRKDNravQKLRREVEKAKRALSSQHQAriEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSD 351
Cdd:cd10235 213 RLDFTSLSPSEL---AALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAG 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 254540168 352 LKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAG 404
Cdd:cd10235 288 LKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAA 339
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
32-403 |
9.55e-128 |
|
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: 381.91 E-value: 9.55e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 111
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEK-ERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 DIKFLPFKVVE-KKTKPYIQVDIGGGQTkTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:cd11732 80 EIKLLPFKLVElEDGKVGIEVSYNGEEV-VFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKR-----EGEKNILVF-DLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVM 264
Cdd:cd11732 159 IAGLNCLRLINETTAAALDYGIYKSdllesEEKPRIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 265 EHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQ 344
Cdd:cd11732 239 EHFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 254540168 345 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQA 403
Cdd:cd11732 319 KALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
32-403 |
1.66e-126 |
|
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: 378.93 E-value: 1.66e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 111
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEK-NRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 DIKFLPFKVVEKKT-KPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 190
Cdd:cd10228 80 ELKHLPYKVVKLPNgSVGIKVQYLG-EEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 191 IAGLNVMRIINEPTAAAIAYGLDKR----EGEK--NILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVM 264
Cdd:cd10228 159 IAGLNCLRLLNDTTAVALAYGIYKQdlpaEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 265 EHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSS-QHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPV 343
Cdd:cd10228 239 EHFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 344 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQA 403
Cdd:cd10228 319 RSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
31-407 |
9.69e-118 |
|
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: 356.62 E-value: 9.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQ 110
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFG-EKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 QDIKFLPFKVVEKKT-KPYIQVDIGGGQtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 189
Cdd:cd24095 82 RDLKLFPFKVTEGPDgEIGINVNYLGEQ-KVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 190 TIAGLNVMRIINEPTAAAIAYGL---DKREGE-KNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVME 265
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIyktDLPETDpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 266 HFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQK 345
Cdd:cd24095 241 HFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540168 346 VLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 407
Cdd:cd24095 321 ALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
30-403 |
4.73e-109 |
|
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: 332.92 E-value: 4.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 30 TVVGIDLGTTYSCVGVFKNGR-VEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGrtwndps 108
Cdd:cd10230 1 AVLGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFR-NGERLFGDDALALATRFPENTFSYLKDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 vqqdikflpfkvvekktkpyiqvdigggqtktFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:cd10230 73 --------------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKR---EGEKNILVFDLGGGTFDVSLLTID------------NGVFEVVATNGDTH 253
Cdd:cd10230 121 AEIAGLNVLSLINDNTAAALNYGIDRRfenNEPQNVLFYDMGASSTSATVVEFSsvkekdkgknktVPQVEVLGVGWDRT 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 254 LGGEDFDQRVMEHFIKLY--KKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEEL 331
Cdd:cd10230 201 LGGLEFDLRLADHLADEFneKHKKDKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEEL 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540168 332 NMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQA 403
Cdd:cd10230 281 CADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYA 352
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
20-635 |
5.96e-106 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 333.36 E-value: 5.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 20 EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGerlIGDAAKNQLTSnpentvfdAKRL 99
Cdd:PRK01433 10 EQADFKQERQIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN---FTIGNNKGLRS--------IKRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 100 IGRT----WNDPSVQQDIK-FLPFKVVEKKTKpyiqvdiggGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVP 174
Cdd:PRK01433 79 FGKTlkeiLNTPALFSLVKdYLDVNSSELKLN---------FANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 175 AYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKreGEKNI-LVFDLGGGTFDVSLLTIDNGVFEVVATNGDTH 253
Cdd:PRK01433 150 AHFNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNK--NQKGCyLVYDLGGGTFDVSILNIQEGIFQVIATNGDNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 254 LGGEDFDQRVMEHFIKLYkkktgkDVRKDNRAVQKLRreveKAKRALSSQhqarieieSFFEGEDFSetLTRAKFEELNM 333
Cdd:PRK01433 228 LGGNDIDVVITQYLCNKF------DLPNSIDTLQLAK----KAKETLTYK--------DSFNNDNIS--INKQTLEQLIL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 334 DLFRSTMKPVQKVLEDSdlKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSrGINPDEAVAYGAAVQAGVLSGDQDtg 413
Cdd:PRK01433 288 PLVERTINIAQECLEQA--GNPNIDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLIAPHT-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 414 DLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPR 493
Cdd:PRK01433 363 NSLLIDVVPLSLGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 494 GVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSL 573
Cdd:PRK01433 443 GSIRAEVTFAIDADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNI 521
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254540168 574 KNQIGDKEklggKLSSEDKETMEKAVEEKIEWLESHQDA-----DIEDFKAK-KKELEEIVQPIISKL 635
Cdd:PRK01433 522 ERAIAELT----TLLSESEISIINSLLDNIKEAVHARDIilinnSIKEFKSKiKKSMDTKLNIIINDL 585
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
32-407 |
1.04e-105 |
|
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: 325.48 E-value: 1.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 111
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPK-SRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 DIKFLPFKVVEKKTKPYIQVDIGGGQTKtFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 191
Cdd:cd24094 80 EEKYFTAKLVDANGEVGAEVNYLGEKHV-FSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 192 AGLNVMRIINEPTAAAIAYGLDK------REGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVME 265
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKtdlpepEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 266 HFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQK 345
Cdd:cd24094 239 HFADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254540168 346 VLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 407
Cdd:cd24094 319 ALAQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
30-406 |
6.66e-99 |
|
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: 306.60 E-value: 6.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 30 TVVGIDLGTTYSCVG-VFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGrtwndps 108
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 vqqdikflpfkvvekktkpyiqvdigggqTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:cd10232 73 -----------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKREG-----EKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRV 263
Cdd:cd10232 124 AAAAGLEVLQLIPEPAAAALAYDLRAETSgdtikDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 264 MEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPV 343
Cdd:cd10232 204 VGHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLV 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254540168 344 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRG---INPDEAVAYGAAVQAGVL 406
Cdd:cd10232 284 TDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIRAptqINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
30-405 |
7.80e-96 |
|
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: 299.93 E-value: 7.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 30 TVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSV 109
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPK-NRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 110 QQDIKFLPFKVVEKKTKP------YIQvdigggQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQ 183
Cdd:cd11737 80 QAEKPSLAYELVQLPTGTtgikvmYME------EERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 184 ATKDAGTIAGLNVMRIINEPTAAAIAYGLDKR------EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGE 257
Cdd:cd11737 154 SVMDATQIAGLNCLRLMNETTAVALAYGIYKQdlpapeEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 258 DFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQ-HQARIEIESFFEGEDFSETLTRAKFEELNMDLF 336
Cdd:cd11737 234 KFDEVLVNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANaSDLPLNIECFMNDIDVSGTMNRGQFEEMCADLL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254540168 337 RSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGV 405
Cdd:cd11737 314 ARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
30-402 |
6.46e-90 |
|
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: 284.45 E-value: 6.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 30 TVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSV 109
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSK-NRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 110 QQDIKFLPFKVVE-KKTKPYIQVdIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:cd11739 80 QKEKENLSYDLVPlKNGGVGVKV-MYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKR-----EGEKNILVF-DLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQR 262
Cdd:cd11739 159 AQIVGLNCLRLMNDMTAVALNYGIYKQdlpapDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 263 VMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQH-QARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMK 341
Cdd:cd11739 239 LVEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSNStDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254540168 342 PVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQ 402
Cdd:cd11739 319 PLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
30-407 |
2.24e-87 |
|
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: 277.95 E-value: 2.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 30 TVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSV 109
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSR-NRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 110 QQDIKFLPFKVvEKKTKPYIQVDIGG-GQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 188
Cdd:cd11738 80 QAEKIKLPYEL-QKMPNGSTGVKVRYlDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVMRIINEPTAAAIAYGLDKR------EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQR 262
Cdd:cd11738 159 AQIAGLNCLRLMNETTAVALAYGIYKQdlpaleEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 263 VMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQ-HQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMK 341
Cdd:cd11738 239 LVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANaSDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254540168 342 PVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 407
Cdd:cd11738 319 PLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
32-401 |
5.55e-61 |
|
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: 206.57 E-value: 5.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVgvfkngrveiiandqgnritpSYVAFTPEGERLIGDAAKNQLTSNPENTVfdakrligrtwndPSVqq 111
Cdd:cd10170 1 VGIDFGTTYSGV---------------------AYALLGPGEPPLVVLQLPWPGGDGGSSKV-------------PSV-- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 112 dikflpfkvvekktkpyIQVdigggqtktfapeeiSAMVLTKMKETAEAYLGKKV-------THAVVTVPAYFNDAQRQA 184
Cdd:cd10170 45 -----------------LEV---------------VADFLRALLEHAKAELGDRIwelekapIEVVITVPAGWSDAAREA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 185 TKDAGTIAGL----NVMRIINEPTAAAIAYGLDKR-----EGEKNILVFDLGGGTFDVSLLTIDNG---VFEVVATNGDT 252
Cdd:cd10170 93 LREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGdllplKPGDVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 253 HLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEG---EDFSETLTRAKFE 329
Cdd:cd10170 173 LLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGglpELGLEKGTLLLTE 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254540168 330 ELNMDLFRSTMKPVQKVLED--SDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEP---SRGINPDEAVAYGAAV 401
Cdd:cd10170 253 EEIRDLFDPVIDKILELIEEqlEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIiivLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
32-401 |
6.81e-43 |
|
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: 159.75 E-value: 6.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERL-----IGDAAKNQLTSNPENTvfdakRLIgrtwnd 106
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGaesiyFGNDAIDAYLNDPEEG-----RLI------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 107 psvqQDIK-FLPFKVVEKKTKPyiqvdigggqTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQAT 185
Cdd:cd10231 70 ----KSVKsFLGSSLFDETTIF----------GRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 186 -------KDAGTIAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTID----NGVFEVVATNGDtHL 254
Cdd:cd10231 136 aqaesrlRDAARRAGFRNVEFQYEPIAAALDYEQRLDR-EELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 255 GGEDFDQRVM----------------------------------EHFIKLYKKKTGKDVRKDNRAVQK------------ 288
Cdd:cd10231 214 GGDDFDRELAlkkvmphlgrgstyvsgdkglpvpawlyadlsnwHAISLLYTKKTLRLLLDLRRDAADpekierllslve 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 289 ------LRREVEKAKRALSSQHQARIEIEsfFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVL 362
Cdd:cd10231 294 dqlghrLFRAVEQAKIALSSADEATLSFD--FIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFL 371
|
410 420 430
....*....|....*....|....*....|....*....
gi 254540168 363 VGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAV 401
Cdd:cd10231 372 TGGSSQSPAVRQALASLF-GQARLVEGDEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
31-400 |
5.51e-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: 104.28 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 31 VVGIDLGTTYSCVG---VFKNGRVEIIANDQG------NRITPSYVAFTPEGERL-IGDAAKNQLTSNPENtvfDAKRLI 100
Cdd:cd10229 2 VVAIDFGTTYSGYAysfITDPGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHsFGYEAREKYSDLAED---EEHQWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 101 GRtwndpsvQQDIKFLPFKvvEKKTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHA--------VVT 172
Cdd:cd10229 79 YF-------FKFKMMLLSE--KELTRDTKVKAVNG---KSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 173 VPAYFNDAQ----RQATKDAGTIAGLNVMR--IINEPTAAAIAYGLDKREGEKNI-------LVFDLGGGTFDVSLLTI- 238
Cdd:cd10229 147 VPAIWSDAAkqfmREAAVKAGLISEENSEQliIALEPEAAALYCQKLLAEGEEKElkpgdkyLVVDCGGGTVDITVHEVl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 239 -DNGVFEVVATNGDtHLGGEDFDQRvmehFIKLYKKKTGKDVRKDNR-----AVQKLRREVEKAKRAlssqhqarieies 312
Cdd:cd10229 227 eDGKLEELLKASGG-PWGSTSVDEE----FEELLEEIFGDDFMEAFKqkypsDYLDLLQAFERKKRS------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 313 ffegedFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKksDIDEIVLVGGSTRIPKIQQLVKEFFngkEPSRGI--- 389
Cdd:cd10229 289 ------FKLRLSPELMKSLFDPVVKKIIEHIKELLEKPELK--GVDYIFLVGGFAESPYLQKAVKEAF---STKVKIiip 357
|
410
....*....|..
gi 254540168 390 -NPDEAVAYGAA 400
Cdd:cd10229 358 pEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
32-401 |
7.29e-13 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 69.81 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGrveIIANDqgnritPSYVAFTPEGERLI--GDaaknqltsnpentvfDAKRLIGRTwndpsv 109
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVDKNTGKVLavGE---------------EAKKMLGRT------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 110 qqdikflpfkvvekktkpyiqvdigggqtktfaPEEISAM------VLTKMkETAEAYLG---KKV--------THAVVT 172
Cdd:cd10225 52 ---------------------------------PGNIVAIrplrdgVIADF-EATEAMLRyfiRKAhrrrgflrPRVVIG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 173 VPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNiLVFDLGGGTFDVSLLTIdNGvfeVVATNGdT 252
Cdd:cd10225 98 VPSGITEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPIEEPRGS-MVVDIGGGTTEIAVISL-GG---IVTSRS-V 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 253 HLGGEDFDQRVMEHFIKLYKKKTGkdvrkdnravqklRREVEKAKRALSSQHQARIEIESFFEGEDF------SETLTRA 326
Cdd:cd10225 172 RVAGDEMDEAIINYVRRKYNLLIG-------------ERTAERIKIEIGSAYPLDEELSMEVRGRDLvtglprTIEITSE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 327 KFEELNMDLFRSTMKPVQKVLEDS--DLkKSDIDE--IVLVGGSTRIPKIQQLVKEFFngkepsrGI------NPDEAVA 396
Cdd:cd10225 239 EVREALEEPVNAIVEAVRSTLERTppEL-AADIVDrgIVLTGGGALLRGLDELLREET-------GLpvhvadDPLTCVA 310
|
....*
gi 254540168 397 YGAAV 401
Cdd:cd10225 311 KGAGK 315
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
148-375 |
3.32e-12 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 69.12 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 148 AMVLtKMKETAEAYLGKKVTHAVVTVPAYFN-----DAQRQAT---KDAGTIAGLNVMRIINEPTAAAIAY--GLDKreg 217
Cdd:PRK11678 132 AMML-HIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTE--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 218 EKNILVFDLGGGTFDVSLLT-----IDNgvfevvaTNGDTHL--------GGEDFD-QRVMEHFIKLY----KKKTGK-- 277
Cdd:PRK11678 208 EKRVLVVDIGGGTTDCSMLLmgpswRGR-------ADRSASLlghsgqriGGNDLDiALAFKQLMPLLgmgsETEKGIal 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 278 ------------------------------DVRKDNRAVQKLRR---------------EVEKAKRALSSQHQARIEIeS 312
Cdd:PRK11678 281 pslpfwnavaindvpaqsdfyslangrllnDLIRDAREPEKVARllkvwrqrlsyrlvrSAEEAKIALSDQAETRASL-D 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254540168 313 FFEgEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKsdiDEIVLVGGSTRIP----KIQQL 375
Cdd:PRK11678 360 FIS-DGLATEISQQGLEEAISQPLARILELVQLALDQAQVKP---DVIYLTGGSARSPliraALAQQ 422
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
32-400 |
1.57e-09 |
|
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: 60.09 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGrveIIANDqgnritPSYVAFTPEGERLI--GDaaknqltsnpentvfDAKRLIGRTwndpsv 109
Cdd:COG1077 10 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAIDKKTGKVLavGE---------------EAKEMLGRT------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 110 qqdikflpfkvvekktkpyiqvdigggqtktfaPEEISAMvlTKMK-------ETAEAYLG---KKVT--------HAVV 171
Cdd:COG1077 60 ---------------------------------PGNIVAI--RPLKdgviadfEVTEAMLKyfiKKVHgrrsffrpRVVI 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 172 TVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVfDLGGGTFDVSLltIDNGvfEVVATNGd 251
Cdd:COG1077 105 CVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTGNMVV-DIGGGTTEVAV--ISLG--GIVVSRS- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 252 THLGGEDFDQRVMEHFIKLYKKKTGkdvrkdnravqklRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKfeEL 331
Cdd:COG1077 179 IRVAGDELDEAIIQYVRKKYNLLIG-------------ERTAEEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTI--TI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 332 NMDLFRSTMKP--------VQKVLEDS--DLkKSDIDE--IVLVGGSTRIPKIQQLVKEFFngkepsrGI------NPDE 393
Cdd:COG1077 244 TSEEIREALEEplnaiveaIKSVLEKTppEL-AADIVDrgIVLTGGGALLRGLDKLLSEET-------GLpvhvaeDPLT 315
|
....*..
gi 254540168 394 AVAYGAA 400
Cdd:COG1077 316 CVARGTG 322
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
120-381 |
1.92e-09 |
|
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: 59.23 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 120 VVEKKTKPYIQVDIGGGQTKTFA--------PEEIsAMVLTKMKETAEAYLGKKVTHAVVTVP----AYFNDAQRqatkd 187
Cdd:cd24004 14 VLEEDDENIEVLAFSSEEHPERAmgdgqihdISKV-AESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 188 agtiAGLNVMRIINEPTAAAIAYGLDKrEGEKNILVFDLGGGTFDVSLltIDNGVfeVVATnGDTHLGGEDFDQRVMEHF 267
Cdd:cd24004 88 ----AGLEPVGLTLEPFAAANLLIPYD-MRDLNIALVDIGAGTTDIAL--IRNGG--IEAY-RMVPLGGDDFTKAIAEGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 268 IKLYKkktgkdvrkdnravqklrrEVEKAKRALSSQhqarieiESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVL 347
Cdd:cd24004 158 LISFE-------------------EAEKIKRTYGIF-------LLIEAKDQLGFTINKKEVYDIIKPVLEELASGIANAI 211
|
250 260 270
....*....|....*....|....*....|....
gi 254540168 348 EDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFN 381
Cdd:cd24004 212 EEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
150-254 |
4.83e-08 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 54.19 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 150 VLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLdkregeKNILVFDLGGG 229
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI------RDGAVVDIGGG 121
|
90 100
....*....|....*....|....*....
gi 254540168 230 TFDVSLltIDNGvfEVVAT----NGDTHL 254
Cdd:cd24047 122 TTGIAV--LKDG--KVVYTadepTGGTHL 146
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
168-400 |
2.33e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 53.21 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 168 HAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNiLVFDLGGGTFDVSLLTIDNgvfevVA 247
Cdd:PRK13930 102 RIVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPVTEPVGN-MVVDIGGGTTEVAVISLGG-----IV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 248 TNGDTHLGGEDFDQRVMEHFIKLYKKKTGKdvrkdnravqklrREVEKAKR----ALSSQHQARIEIesffEGEDFSETL 323
Cdd:PRK13930 176 YSESIRVAGDEMDEAIVQYVRRKYNLLIGE-------------RTAEEIKIeigsAYPLDEEESMEV----RGRDLVTGL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 324 trAKFEELNMDLFRSTMKP--------VQKVLEDS--DLkKSDIDE--IVLVGGSTRIPKIQQLVKEFFngkepsrGI-- 389
Cdd:PRK13930 239 --PKTIEISSEEVREALAEplqqiveaVKSVLEKTppEL-AADIIDrgIVLTGGGALLRGLDKLLSEET-------GLpv 308
|
250
....*....|....*
gi 254540168 390 ----NPDEAVAYGAA 400
Cdd:PRK13930 309 hiaeDPLTCVARGTG 323
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
29-272 |
4.52e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 52.21 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 29 GTVVGIDLGTtySCVGVFKNGRvEIIANDqgnritPSYVAFtpegerligDAAKNQLTSNPEntvfDAKRLIGRTwndPS 108
Cdd:PRK13928 3 GRDIGIDLGT--ANVLVYVKGK-GIVLNE------PSVVAI---------DKNTNKVLAVGE----EARRMVGRT---PG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 109 VQQDIKFL------PFKVVEKKTKPYIQVdiGGGQTKTFAPEeisamvltkmketaeaylgkkvthAVVTVPAYFNDAQR 182
Cdd:PRK13928 58 NIVAIRPLrdgviaDYDVTEKMLKYFINK--ACGKRFFSKPR------------------------IMICIPTGITSVEK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 183 QATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVfDLGGGTFDVSLLTIDNGVfevvaTNGDTHLGGEDFDQR 262
Cdd:PRK13928 112 RAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVV-DIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFDEA 185
|
250
....*....|
gi 254540168 263 VMEHFIKLYK 272
Cdd:PRK13928 186 IIRYIRKKYK 195
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
30-271 |
2.06e-06 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 50.29 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 30 TVVGIDLGTTYSCVGVFKNGrveIIANDqgnritPSYVAFTPEGERLIGDAAknqltsnpentvfDAKRLIGRTwndpsv 109
Cdd:PRK13929 5 TEIGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKAVLAIGT-------------EAKNMIGKT------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 110 qqdikflPFKVVekKTKPYiqvdigggQTKTFAPEEISAMVLTKMKETAEAYLGKKV--THAVVTVPAYFNDAQRQATKD 187
Cdd:PRK13929 57 -------PGKIV--AVRPM--------KDGVIADYDMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAISD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 188 AGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVfDLGGGTFDVSLLTidngvFEVVATNGDTHLGGEDFDQRVMEHF 267
Cdd:PRK13929 120 AVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVV-DIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSFV 193
|
....
gi 254540168 268 IKLY 271
Cdd:PRK13929 194 RKKY 197
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
150-254 |
2.22e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 49.44 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 150 VLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLdkregeKNILVFDLGGG 229
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGI------DNGAVVDIGGG 145
|
90 100
....*....|....*....|....*....
gi 254540168 230 TFDVSLLtiDNGvfEVVAT----NGDTHL 254
Cdd:PRK15080 146 TTGISIL--KDG--KVVYSadepTGGTHM 170
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
32-399 |
6.57e-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: 48.71 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGTTYSCVGVFKNGrveIIANDqgnritPSYVAFTPEGERLI--GDaaknqltsnpentvfDAKRLIGRTwndpsv 109
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAINTKTKKVLavGN---------------EAKKMLGRT------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 110 qqdikflpfkvvekktkpyiqvdigggqtktfaPEEISAM------VLTKMkETAEA---YLGKKVTHA--------VVT 172
Cdd:pfam06723 54 ---------------------------------PGNIVAVrplkdgVIADF-EVTEAmlkYFIKKVHGRrsfskprvVIC 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 173 VPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNiLVFDLGGGTFDVSLLTIdNGVfeVVATNgdT 252
Cdd:pfam06723 100 VPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGN-MVVDIGGGTTEVAVISL-GGI--VTSKS--V 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 253 HLGGEDFDQRVMEHFIKLYKKKTGKdvrkdnravqklrREVEKAKRALSSQHQARIEIESFFEGEDFSETLTR------A 326
Cdd:pfam06723 174 RVAGDEFDEAIIKYIRKKYNLLIGE-------------RTAERIKIEIGSAYPTEEEEKMEIRGRDLVTGLPKtieissE 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254540168 327 KFEELNMDLFRSTMKPVQKVLEDS--DLkKSDIDE--IVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGA 399
Cdd:pfam06723 241 EVREALKEPVSAIVEAVKEVLEKTppEL-AADIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
169-267 |
2.87e-04 |
|
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: 41.30 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 169 AVVTVPAYFNDAQRQAT-----------KDAGTIAGLNVMRIINEPTAAAIAYGLDKREGekNILVFDLGGGTfdvsllt 237
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPE--GLLVVDLGGGT------- 86
|
90 100 110
....*....|....*....|....*....|
gi 254540168 238 idNGVFEVVATNGDTHLggEDFDQRVMEHF 267
Cdd:cd00012 87 --DISANVVLVGGGARN--NGLAKRLKELL 112
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
356-408 |
5.90e-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: 42.92 E-value: 5.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 254540168 356 DIDEIVLVGGSTRIPKIQQLVKEFFNgkEPSRGINPDEAVAYGAAVQAGVLSG 408
Cdd:cd07809 393 EIDEIRLIGGGSKSPVWRQILADVFG--VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| Hydantoinase_A |
pfam01968 |
Hydantoinase/oxoprolinase; This family includes the enzymes hydantoinase and oxoprolinase EC:3. ... |
146-246 |
9.30e-04 |
|
Hydantoinase/oxoprolinase; This family includes the enzymes hydantoinase and oxoprolinase EC:3.5.2.9. Both reactions involve the hydrolysis of 5-membered rings via hydrolysis of their internal imide bonds.
Pssm-ID: 396517 [Multi-domain] Cd Length: 288 Bit Score: 41.50 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 146 ISAMVLTKMKETAEAyLGKKVTHAVVTVPAYFNDAQRQATkDAGTIAGLNVMRIINEPTAAAIAYG-LDKREGEKNILVF 224
Cdd:pfam01968 7 VNAYLAPIMREYLEG-VEDSLEKVGSKAPVYVMQSDGGLV-SIDEARKRPVETILSGPAAGVVGAAyTGKLLGNKNLIGF 84
|
90 100
....*....|....*....|..
gi 254540168 225 DLGGGTFDVSLltIDNGVFEVV 246
Cdd:pfam01968 85 DMGGTSTDISP--IIDGEPEIT 104
|
|
| HyuA |
COG0145 |
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport ... |
205-256 |
1.05e-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: 42.38 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 254540168 205 AAAIAygldKREGEKNILVFDLGGGTFDVSLltIDNGVFEVVAtngDTHLGG 256
Cdd:COG0145 266 AAALA----RAAGFDNVITFDMGGTSTDVSL--IEDGEPERTT---ETEVAG 308
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
537-635 |
1.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 537 EEIERMVNDAEKFAEEDKKLK------ERIDTRNELESYAYSLKNQIGDKEK-LGGKLSSEDK--ETMEKAvEEKIEWLE 607
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEAlleakeEIHKLRNEFEKELRERRNELQKLEKrLLQKEENLDRklELLEKR-EEELEKKE 116
|
90 100
....*....|....*....|....*...
gi 254540168 608 SHQDADIEDFKAKKKELEEIVQPIISKL 635
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQEL 144
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
170-266 |
1.69e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 41.23 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 170 VVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVfDLGGGTFDVSLLTIdNGvfevVATN 249
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVV-DIGGGTTEVAVISL-GG----IVYS 173
|
90
....*....|....*..
gi 254540168 250 GDTHLGGEDFDQRVMEH 266
Cdd:PRK13927 174 KSVRVGGDKFDEAIINY 190
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
32-284 |
2.28e-03 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 40.20 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 32 VGIDLGttyscvgvfkNGRVEIIANDQGNRITPSYVAFTPEGERLIGDaaknqlTSNPENTVFDAKR-LIGrtwndpsvq 110
Cdd:cd10227 1 IGIDIG----------NGNTKVVTGGGKEFKFPSAVAEARESSLDDGL------LEDDIIVEYNGKRyLVG--------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 111 qdikflpfKVVEKKTKPYIQVDIGGGQTKTFApeeisAMVLTKMKETAEAYlgKKVTHAVVTVPA--YFNDAQRQATKDA 188
Cdd:cd10227 56 --------ELALREGGGGRSTGDDKKKSEDAL-----LLLLAALALLGDDE--EVDVNLVVGLPIseYKEEKKELKKKLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 189 GTIAGLNVM-----------RIINEPTAAAIAYGLDKREGE-KNILVFDLGGGTFDVslLTIDNGvfEVVATNGDTHLGG 256
Cdd:cd10227 121 KGLHEFTFNgkerritindvKVLPEGAGAYLDYLLDDDELEdGNVLVIDIGGGTTDI--LTFENG--KPIEESSDTLPGG 196
|
250 260
....*....|....*....|....*...
gi 254540168 257 EDFDQRVMEHFIKLYKKKTGKDVRKDNR 284
Cdd:cd10227 197 EEALEKYADDILNELLKKLGDELDSADK 224
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
192-401 |
4.52e-03 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 39.57 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 192 AGLNVMRIINEPTAAAIAYGLDKR-EGEKNILVFDLGGGTFDVSLltIDNGVFEVVATNGdthLGGEDFDQRVMEHFikl 270
Cdd:cd24049 148 AGLKPVAIDVESFALARALEYLLPdEEEETVALLDIGASSTTLVI--VKNGKLLFTRSIP---VGGNDITEAIAKAL--- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 271 ykkktgkDVRKDnravqklrrEVEKAKRalssqHQARIEIESFFEGEDFSETLTRAkFEELNMDLFRStmkpvqkvLE-- 348
Cdd:cd24049 220 -------GLSFE---------EAEELKR-----EYGLLLEGEEGELKKVAEALRPV-LERLVSEIRRS--------LDyy 269
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 349 DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGK----EPSRGINPDE-------------AVAYGAAV 401
Cdd:cd24049 270 RSQNGGEPIDKIYLTGGGSLLPGLDEYLSERLGIPveilNPFSNIESKKsddeelkedaplfAVAIGLAL 339
|
|
| ASKHA_NBD_PPX_GppA |
cd24006 |
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
118-331 |
4.96e-03 |
|
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466856 [Multi-domain] Cd Length: 294 Bit Score: 39.44 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 118 FKVVEKKTKPyiqVDIGGG--QTKTFAPEEISAMV--LTKMKETAEAYLGKKV----THAVvtvpayfndaqRQAtKDAG 189
Cdd:cd24006 23 FRILERLREP---VRLGEDvfTTGRISEEAIERAVeaLRRFKKLADEYGVKRIravaTSAV-----------REA-SNGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 190 TI-------AGLNVmRIINEP-----TAAAIAYGLDKreGEKNILVFDLGGGTFDVSLLtiDNGVFEVVATngdTHLGGe 257
Cdd:cd24006 88 EFlerikreTGIDV-EIISGEeearlIYLAVRSGLPL--GDGNALIVDIGGGSTELTLG--DNGEILFSES---LPLGA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254540168 258 dfdQRVMEHFIKLYkkktgkdvRKDNRAVQKLRREVEKAKRALSSQHQ--------------ARIEIESFFEGEDFSETL 323
Cdd:cd24006 159 ---VRLTERFLKDD--------PPSELLEEYLRSFVRSVLRPLPKRRKikfdvaigsggtilALAAMALARKGKPHGYEI 227
|
....*...
gi 254540168 324 TRAKFEEL 331
Cdd:cd24006 228 SREELKAL 235
|
|
| |
