|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
39-653 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1002.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQRD 118
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQSD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MKLAPYKIVNK-DGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVI 197
Cdd:PTZ00009 87 MKHWPFKVTTGgDDKPMIEVTYQ-GEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 198 AGLNVVRIINEPTAAAIAYGLDKKG-GEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKL 276
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKGdGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 277 IKKKH-GKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMED 355
Cdd:PTZ00009 246 FKRKNrGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEKVLKD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 356 AGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPNKGVNPDEAVAFGAAVQGGILSGEGGDETKDILLLDVAPLTLGI 435
Cdd:PTZ00009 326 AGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTPLSLGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 436 ETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEVTFEVDAN 515
Cdd:PTZ00009 406 ETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDAN 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 516 GILNVKAEDKASGKSEKITITNDKGRLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQINDkDKLADKL 595
Cdd:PTZ00009 486 GILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD-EKVKGKL 564
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1023970679 596 ESDEKEKIETATKEALEWMDDNQNAEKEDYEEKLKEVEAVCNPIITAVYQRSG-GAPGG 653
Cdd:PTZ00009 565 SDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQAAGgGMPGG 623
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
38-645 |
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: 946.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQR 117
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 118 DMKLAPYKIVNKD-GKPYIEVKIKDgetKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:pfam00012 81 DIKHLPYKVVKLPnGDAGVEVRYLG---ETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKL 276
Cdd:pfam00012 158 IAGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 277 IKKKHGKDISKDNRALGKLRRECERAKRALSS-QHQVRVEIESLF-DGIDFSEPLTRARFEELNNDLFRKTMGPVKKAME 354
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMaDGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 355 DAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSGEggDETKDILLLDVAPLTLG 434
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 435 IETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEVTFEVDA 514
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 515 NGILNVKAEDKASGKSEKITITNDKGrLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQINDKdklADK 594
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE---GDK 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1023970679 595 LESDEKEKIETatkeALEWMDDN-QNAEKEDYEEKLKEVEAVCNPIITAVYQ 645
Cdd:pfam00012 551 VPEAEKSKVES----AIEWLKDElEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
36-655 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 912.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 36 GTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDN-ERLIGEAAKNQAAVNPERTVFDVKRLIGRKfeDKE 114
Cdd:PRK00290 2 GKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 115 VQRDMKLAPYKIVNKDGKPYIeVKIKDgetKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDA 194
Cdd:PRK00290 80 VQKDIKLVPYKIVKADNGDAW-VEIDG---KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 195 GVIAGLNVVRIINEPTAAAIAYGLDKKGGEKnILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFI 274
Cdd:PRK00290 156 GKIAGLEVLRIINEPTAAALAYGLDKKGDEK-ILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 275 KLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVrvEIESLFDGIDFSEP------LTRARFEELNNDLFRKTMGP 348
Cdd:PRK00290 235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EINLPFITADASGPkhleikLTRAKFEELTEDLVERTIEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 349 VKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSGEggdeTKDILLLDV 428
Cdd:PRK00290 313 CKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVLLLDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 429 APLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEV 508
Cdd:PRK00290 388 TPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 509 TFEVDANGILNVKAEDKASGKSEKITITNDKGrLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQINDk 588
Cdd:PRK00290 468 TFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKE- 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1023970679 589 dkLADKLESDEKEKIETATKEALEWMDDNqnaEKEDYEEKLKEVEAVCNPIITAVYQRSGGAPGGKS 655
Cdd:PRK00290 546 --LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAG 607
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
36-412 |
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: 856.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 36 GTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEV 115
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 116 QRDMKLAPYKIVNKDGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAG 195
Cdd:cd10241 81 QKDIKLLPFKIVNKNGKPYIQVEVK-GEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 196 VIAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIK 275
Cdd:cd10241 160 TIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 276 LIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMED 355
Cdd:cd10241 240 LFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLED 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1023970679 356 AGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPNKGVNPDEAVAFGAAVQGGIL 412
Cdd:cd10241 320 AGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
38-645 |
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: 813.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDN-ERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEdkEVQ 116
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 RDMKLAPYKIVNKDGKPYIEVkikdgETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKV-----DGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKL 276
Cdd:TIGR02350 155 IAGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 277 IKKKHGKDISKDNRALGKLRRECERAKRALSSQHQvrVEIESLFDGIDFSEP------LTRARFEELNNDLFRKTMGPVK 350
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLS--TEINLPFITADASGPkhlemtLTRAKFEELTADLVERTKEPVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 351 KAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSGeggdETKDILLLDVAP 430
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKG----DVKDVLLLDVTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 431 LTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEVTF 510
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 511 EVDANGILNVKAEDKASGKSEKITITNDKGrLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQINDkdk 590
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--- 543
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1023970679 591 LADKLESDEKEKIETATKEALEWMDDNqnaEKEDYEEKLKEVEAVCNPIITAVYQ 645
Cdd:TIGR02350 544 AGDKLPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
39-412 |
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: 729.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQRD 118
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MKLAPYKIVNKDGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVIA 198
Cdd:cd10233 82 MKHWPFKVVSGGDKPKIQVEYK-GETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 199 GLNVVRIINEPTAAAIAYGLDKKG-GEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKLI 277
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGkGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 278 KKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMEDAG 357
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1023970679 358 LEKRQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPNKGVNPDEAVAFGAAVQGGIL 412
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
36-648 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 705.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 36 GTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFT-DNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKE 114
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTeDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 115 VQRDMKLAPYKIV-NKDGKPYIEvkikdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKD 193
Cdd:PTZ00400 121 TKKEQKILPYKIVrASNGDAWIE-----AQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 194 AGVIAGLNVVRIINEPTAAAIAYGLDKKGGeKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYF 273
Cdd:PTZ00400 196 AGKIAGLDVLRIINEPTAAALAFGMDKNDG-KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 274 IKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVrvEIESLFDGIDFSEP------LTRARFEELNNDLFRKTMG 347
Cdd:PTZ00400 275 IAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADQSGPkhlqikLSRAKLEELTHDLLKKTIE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 348 PVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSGEggdeTKDILLLD 427
Cdd:PTZ00400 353 PCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDLLLLD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 428 VAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIE 507
Cdd:PTZ00400 428 VTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 508 VTFEVDANGILNVKAEDKASGKSEKITITNDKGrLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQIND 587
Cdd:PTZ00400 508 VTFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD 586
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1023970679 588 -KDKLADKLESDEKEKIeTATKEALewmddnQNAEKEDYEEKLKEVEAVCNPIITAVYQRSG 648
Cdd:PTZ00400 587 lKDKISDADKDELKQKI-TKLRSTL------SSEDVDSIKDKTKQLQEASWKISQQAYKQGN 641
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
35-654 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 702.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 35 IGTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFT-DNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDK 113
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGkSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 114 EVQRDMklAPYKIV-NKDGKpyIEVKIKDgetKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATK 192
Cdd:PRK13411 81 EEERSR--VPYTCVkGRDDT--VNVQIRG---RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 193 DAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEY 272
Cdd:PRK13411 154 DAGTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 273 FIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSqhQVRVEIESLFDGIDFSEP------LTRARFEELNNDLFRKTM 346
Cdd:PRK13411 234 LVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSS--MLTTSINLPFITADETGPkhlemeLTRAKFEELTKDLVEATI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 347 GPVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPNKGVNPDEAVAFGAAVQGGILSGeggdETKDILLL 426
Cdd:PRK13411 312 EPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGG----EVKDLLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 427 DVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQI 506
Cdd:PRK13411 388 DVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 507 EVTFEVDANGILNVKAEDKASGKSEKITITNdKGRLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQIN 586
Cdd:PRK13411 468 EVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLK 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023970679 587 DKdklADKLESDEKEKIETAtKEALEWMDDNQNAEKEDYEEKLKEVEAVCNPIITAVYQRSGGAPGGK 654
Cdd:PRK13411 547 EN---GELISEELKQRAEQK-VEQLEAALTDPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDT 610
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
36-645 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 702.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 36 GTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDN-ERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEdkE 114
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 115 VQRDMKLAPYKiVNKDGKPYIEVK--IKDgetKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATK 192
Cdd:CHL00094 80 ISEEAKQVSYK-VKTDSNGNIKIEcpALN---KDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 193 DAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKnILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEY 272
Cdd:CHL00094 156 DAGKIAGLEVLRIINEPTAASLAYGLDKKNNET-ILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 273 FIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVE---IESLFDG-IDFSEPLTRARFEELNNDLFRKTMGP 348
Cdd:CHL00094 235 LIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 349 VKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSGEggdeTKDILLLDV 428
Cdd:CHL00094 315 VENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 429 APLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEV 508
Cdd:CHL00094 390 TPLSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 509 TFEVDANGILNVKAEDKASGKSEKITITNdKGRLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQINDk 588
Cdd:CHL00094 470 TFDIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE- 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 589 dkLADKLESDEKEKIETATKEAlewmddNQNAEKEDYE---EKLKEVEAVCNPIITAVYQ 645
Cdd:CHL00094 548 --LKDKISEEKKEKIENLIKKL------RQALQNDNYEsikSLLEELQKALMEIGKEVYS 599
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
38-551 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 700.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFT-DNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDkevq 116
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 rdmklapykivnkdgkpyIEVKIKDgetKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:COG0443 77 ------------------EATEVGG---KRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAAR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKL 276
Cdd:COG0443 136 IAGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 277 IKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIeSLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMEDA 356
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINL-PFSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 357 GLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSGEGGDetkdillLDVAPLTLGIE 436
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 437 TVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEVTFEVDANG 516
Cdd:COG0443 367 TLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANG 446
|
490 500 510
....*....|....*....|....*....|....*
gi 1023970679 517 ILNVKAEDKASGKSEKITItndkgrlsQEEIERMV 551
Cdd:COG0443 447 ILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
38-412 |
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: 694.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQR 117
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 118 DMKLAPYKIVNK-DGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:cd24028 81 DIKHWPFKVVEDeDGKPKIEVTYK-GEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDKK-GGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIK 275
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDKKsSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 276 LIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMED 355
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1023970679 356 AGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPNKGVNPDEAVAFGAAVQGGIL 412
Cdd:cd24028 320 AKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
36-651 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 668.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 36 GTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFT-DNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEdkE 114
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYD--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 115 VQRDMKLAPYKI-VNKDGKpyieVKIKDGET-KVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATK 192
Cdd:PRK13410 80 LDPESKRVPYTIrRNEQGN----VRIKCPRLeREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 193 DAGVIAGLNVVRIINEPTAAAIAYGLDKkGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEY 272
Cdd:PRK13410 156 DAGRIAGLEVERILNEPTAAALAYGLDR-SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 273 FIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVE---IESLFDG-IDFSEPLTRARFEELNNDLFRKTMGP 348
Cdd:PRK13410 235 LAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISlpfITATEDGpKHIETRLDRKQFESLCGDLLDRLLRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 349 VKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDyFDGKEPNKGVNPDEAVAFGAAVQGGILSGEggdeTKDILLLDV 428
Cdd:PRK13410 315 VKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRT-LIPREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLDV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 429 APLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEV 508
Cdd:PRK13410 390 TPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 509 TFEVDANGILNVKAEDKASGKSEKITITNdKGRLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQINDK 588
Cdd:PRK13410 470 AFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDA 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1023970679 589 D-KLADKLESDEKEKIETATKEALEWMDDNQNAEKEDYEEKLKEVEAVCNPIITAVYQRSGGAP 651
Cdd:PRK13410 549 AlEFGPYFAERQRRAVESAMRDVQDSLEQDDDRELDLAVADLQEALYGLNREVRAEYKEEDEGP 612
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
20-655 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 655.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 20 GSLLAFSIAKEEAEKI-GTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERT 98
Cdd:PTZ00186 10 AAASAARLARHESQKVqGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQST 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 99 VFDVKRLIGRKFEDKEVQRDMKLAPYKIVNK-DGKPYIEvkikDGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVV 177
Cdd:PTZ00186 90 FYAVKRLIGRRFEDEHIQKDIKNVPYKIVRAgNGDAWVQ----DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 178 TVPAYFNDAQRQATKDAGVIAGLNVVRIINEPTAAAIAYGLDKKGgEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGD 257
Cdd:PTZ00186 166 TCPAYFNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGMDKTK-DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 258 THLGGEDFDQRIMEYFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSE----PLTRAR 333
Cdd:PTZ00186 245 THLGGEDFDLALSDYILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQhiqmHISRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 334 FEELNNDLFRKTMGPVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILS 413
Cdd:PTZ00186 325 FEGITQRLIERSIAPCKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 414 GEggdeTKDILLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDL 493
Cdd:PTZ00186 404 GD----VKGLVLLDVTPLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 494 TGIPPAPRGTPQIEVTFEVDANGILNVKAEDKASGKSEKITITNDKGrLSQEEIERMVKEAEEFAEEDKKVKERIDARNS 573
Cdd:PTZ00186 480 VGIPPAPRGVPQIEVTFDIDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 574 LETYVYNMRNQINDKDKLADKlesdEKEKIETATKEALEWMdDNQNAEKEDYE---EKLKEVEAVCNpiiTAVYQRSGGA 650
Cdd:PTZ00186 559 AETQLTTAERQLGEWKYVSDA----EKENVKTLVAELRKAM-ENPNVAKDDLAaatDKLQKAVMECG---RTEYQQAAAA 630
|
....*
gi 1023970679 651 PGGKS 655
Cdd:PTZ00186 631 NSGSS 635
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
32-653 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 634.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 32 AEKigtVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDN-ERLIGEAAKNQAAVNPERTVFDVKRLIGRKF 110
Cdd:PLN03184 38 AEK---VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 111 EdkEVQRDMKLAPYKIVNKDGKpyiEVKIK-DGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQ 189
Cdd:PLN03184 115 S--EVDEESKQVSYRVVRDENG---NVKLDcPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 190 ATKDAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEkNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRI 269
Cdd:PLN03184 190 ATKDAGRIAGLEVLRIINEPTAASLAYGFEKKSNE-TILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 270 MEYFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVE---IESLFDG---IDFSepLTRARFEELNNDLFR 343
Cdd:PLN03184 269 VDWLASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhIDTT--LTRAKFEELCSDLLD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 344 KTMGPVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDyFDGKEPNKGVNPDEAVAFGAAVQGGILSGEggdeTKDI 423
Cdd:PLN03184 347 RCKTPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKK-LTGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 424 LLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGT 503
Cdd:PLN03184 422 VLLDVTPLSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGV 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 504 PQIEVTFEVDANGILNVKAEDKASGKSEKITITNdKGRLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRN 583
Cdd:PLN03184 502 PQIEVKFDIDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEK 580
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023970679 584 QINDkdkLADKLESDEKEKIETATKEALEWMDDNQNAEKEDYEEKL-KEVEAvcnpIITAVYQRSGGAPGG 653
Cdd:PLN03184 581 QLKE---LGDKVPADVKEKVEAKLKELKDAIASGSTQKMKDAMAALnQEVMQ----IGQSLYNQPGAGGAG 644
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
39-606 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 589.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDkeVQRD 118
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MKLAPYKIV-NKDGKPYIEVKikDGetkVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVI 197
Cdd:PRK05183 100 YPHLPYQFVaSENGMPLIRTA--QG---LKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 198 AGLNVVRIINEPTAAAIAYGLDKkGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYfiklI 277
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDS-GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADW----I 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 278 KKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIEsLFDGIdfsepLTRARFEELNNDLFRKTMGPVKKAMEDAG 357
Cdd:PRK05183 250 LEQAGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSVA-LWQGE-----ITREQFNALIAPLVKRTLLACRRALRDAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 358 LEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSGEGGDEtkDILLLDVAPLTLGIET 437
Cdd:PRK05183 324 VEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGLET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 438 VGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEVTFEVDANGI 517
Cdd:PRK05183 401 MGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 518 LNVKAEDKASGKSEKITITNDKGrLSQEEIERMVKEAEEFAEEDKK----VKERIDARNSLETYvynmrNQINDKDklAD 593
Cdd:PRK05183 481 LSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQaralAEQKVEAERVLEAL-----QAALAAD--GD 552
|
570
....*....|...
gi 1023970679 594 KLESDEKEKIETA 606
Cdd:PRK05183 553 LLSAAERAAIDAA 565
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
39-412 |
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: 571.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNgHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQRD 118
Cdd:cd24093 2 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MKLAPYKIVNKDGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVIA 198
Cdd:cd24093 81 MKTWPFKVIDVNGNPVIEVQYL-GETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 199 GLNVVRIINEPTAAAIAYGLDKKGGEK--NILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKL 276
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGAGKSEKerHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 277 IKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMEDA 356
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1023970679 357 GLEKRQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPNKGVNPDEAVAFGAAVQGGIL 412
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
38-413 |
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: 566.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFT-DNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQ 116
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTkDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 RDMKlaPYKiVNKDGKPYIEVKIKDgetKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:cd10234 81 RKQV--PYP-VVSAGNGDAWVEIGG---KEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDKKGGEKnILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKL 276
Cdd:cd10234 155 IAGLEVLRIINEPTAAALAYGLDKKKDEK-ILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 277 IKKKHGKDISKDNRALGKLRRECERAKRALSSQHQvrVEIESLFDGIDFSEP------LTRARFEELNNDLFRKTMGPVK 350
Cdd:cd10234 234 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLE--TEINLPFITADASGPkhlemkLTRAKFEELTEDLVERTIEPVE 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023970679 351 KAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILS 413
Cdd:cd10234 312 QALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
38-632 |
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: 565.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDN-ERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQ 116
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDgGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 rdmKLAPYKIV-NKDGKPYIEVKikDGETkvfSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAG 195
Cdd:TIGR01991 81 ---SILPYRFVdGPGEMVRLRTV--QGTV---TPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 196 VIAGLNVVRIINEPTAAAIAYGLDKkGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYfik 275
Cdd:TIGR01991 153 RLAGLNVLRLLNEPTAAAVAYGLDK-ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKW--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 276 lIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIEslFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMED 355
Cdd:TIGR01991 229 -ILKQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDFT--LDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 356 AGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSGEGGDEtkDILLLDVAPLTLGI 435
Cdd:TIGR01991 306 AGLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 436 ETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEVTFEVDAN 515
Cdd:TIGR01991 383 ETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDAD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 516 GILNVKAEDKASGKSEKITITNDKGrLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQINDKDKLadkL 595
Cdd:TIGR01991 463 GLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDL---L 538
|
570 580 590
....*....|....*....|....*....|....*..
gi 1023970679 596 ESDEKEKIETATKEALEWMDDNQNAEKEDYEEKLKEV 632
Cdd:TIGR01991 539 SEDERAAIDAAMEALQKALQGDDADAIKAAIEALEEA 575
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
36-412 |
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: 521.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 36 GTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFT-DNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKE 114
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 115 VQRDMKLAPYKIVN-KDGKPYIEVKikdgeTKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKD 193
Cdd:cd11733 81 VQKDIKMVPYKIVKaSNGDAWVEAH-----GKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 194 AGVIAGLNVVRIINEPTAAAIAYGLDKKGGeKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYF 273
Cdd:cd11733 156 AGQIAGLNVLRIINEPTAAALAYGLDKKDD-KIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 274 IKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQvrVEIESLFDGIDFSEP------LTRARFEELNNDLFRKTMG 347
Cdd:cd11733 235 VAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQ--TDINLPFITADASGPkhlnmkLTRAKFESLVGDLIKRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023970679 348 PVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGIL 412
Cdd:cd11733 313 PCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
36-414 |
1.06e-165 |
|
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: 479.63 E-value: 1.06e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 36 GTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFT-DNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKE 114
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 115 VQRDMKLAPYKIV-NKDGKPYIEVKIKDgetkvFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKD 193
Cdd:cd11734 81 VQRDIKEVPYKIVkHSNGDAWVEARGQK-----YSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 194 AGVIAGLNVVRIINEPTAAAIAYGLDKKgGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYF 273
Cdd:cd11734 156 AGQIAGLNVLRVINEPTAAALAYGLDKS-GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 274 IKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQvrVEIESLFDGIDFSEP------LTRARFEELNNDLFRKTMG 347
Cdd:cd11734 235 VSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQ--TDINLPFITADASGPkhinmkLTRAQFESLVKPLVDRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1023970679 348 PVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSG 414
Cdd:cd11734 313 PCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
38-414 |
2.77e-155 |
|
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: 452.44 E-value: 2.77e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLI-GEAAKNQAAVNPERTVFDVKRLIGRKFEDkeVQ 116
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 RDMKLAPYKIVNKDGkpyiEVKIKDGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:cd10236 82 EELPLLPYRLVGDEN----ELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDKKgGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKL 276
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQK-KEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 277 IkkkhGKDISKDNRALGKLRRECERAKRALSSQHQVRveIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMEDA 356
Cdd:cd10236 237 I----GIDARLDPAVQQALLQAARRAKEALSDADSAS--IEVEVEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1023970679 357 GLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSG 414
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; ... |
37-414 |
1.16e-150 |
|
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: 442.16 E-value: 1.16e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 37 TVIGIDLGTTYSCVGVYK--NGHVEIIANDQGNRITPSWVGFTDNER-LIGEAAKNQAAVNPERTVFDVKRLIGRKFEDK 113
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 114 EVQRDMKLAPYKIVN-KDGKPYIEVKiKDGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATK 192
Cdd:cd10237 103 ELEEEAKRYPFKVVNdNIGSAFFEVP-LNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 193 DAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEY 272
Cdd:cd10237 182 KAANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 273 FIKLIKKKHGKDIsKDNRALGKLRRECERAKRALSSQHQVRVEIE-----SLFDGIDFSEPLTRARFEELNNDLFRKTMG 347
Cdd:cd10237 262 LIDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqislPSAFKVKFKEEITRDLFETLNEDLFQRVLE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1023970679 348 PVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILSG 414
Cdd:cd10237 341 PIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
39-413 |
2.57e-148 |
|
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: 433.93 E-value: 2.57e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIA-NDQGNRITPSWVGFTDNER-LIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEvq 116
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDKDGEvLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 rdmklapykivNKDGKPYievkikdgetkvfSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:cd24029 79 -----------EIGGKEY-------------TPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKL 276
Cdd:cd24029 135 LAGLNVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 277 IKKKHGK-DISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMED 355
Cdd:cd24029 215 IGIETGIlDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1023970679 356 AGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILS 413
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; ... |
37-412 |
1.66e-141 |
|
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: 417.80 E-value: 1.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 37 TVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQ 116
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 RDMKLAPYKIVNKDGKPYIEVKIkDGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIEL-EEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGL--DKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFI 274
Cdd:cd10238 160 KAGFNVLRVISEPSAAALAYGIgqDDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 275 KLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAME 354
Cdd:cd10238 240 SEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1023970679 355 DAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPNKGVNPDEAVAFGAAVQGGIL 412
Cdd:cd10238 320 SAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
39-411 |
1.64e-132 |
|
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: 393.15 E-value: 1.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGF-TDNERLIGEAAKNQAAVNPERTVFDVKRLIGrkfEDKevqr 117
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMG---TDK---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 118 dmklaPYKIVNKdgkpyievkikdgetkVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVI 197
Cdd:cd10235 74 -----QYRLGNH----------------TFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGEL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 198 AGLNVVRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIkli 277
Cdd:cd10235 133 AGLKVERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFL--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 278 kKKHGKDISKDNRA-LGKLRRECERAKRALSSQHqvRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKAMEDA 356
Cdd:cd10235 210 -KKHRLDFTSLSPSeLAALRKRAEQAKRQLSSQD--SAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1023970679 357 GLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGI 411
Cdd:cd10235 287 GLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
39-408 |
1.75e-131 |
|
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: 391.92 E-value: 1.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQRD 118
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MKLAPYKIVN-KDGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVI 197
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYN-GEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 198 AGLNVVRIINEPTAAAIAYGLDKK----GGEKN-ILVF-DLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIME 271
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSdlleSEEKPrIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 272 YFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKK 351
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1023970679 352 AMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQ 408
Cdd:cd11732 320 ALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQ 375
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
39-408 |
2.67e-123 |
|
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: 370.84 E-value: 2.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQRD 118
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MKLAPYKIVN-KDGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVI 197
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYL-GEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 198 AGLNVVRIINEPTAAAIAYGLDKK----GGEK--NILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIME 271
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGIYKQdlpaEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 272 YFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSS-QHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVK 350
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLR 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1023970679 351 KAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQ 408
Cdd:cd10228 320 SALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
38-413 |
1.16e-119 |
|
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: 362.01 E-value: 1.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQR 117
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 118 DMKLAPYKIVN-KDGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGV 196
Cdd:cd24095 83 DLKLFPFKVTEgPDGEIGINVNYL-GEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDK----KGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEY 272
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGIYKtdlpETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 273 FIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKA 352
Cdd:cd24095 242 FAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023970679 353 MEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILS 413
Cdd:cd24095 322 LADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
37-409 |
3.69e-113 |
|
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: 344.09 E-value: 3.69e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 37 TVIGIDLGTTYSCVGVYKNGH-VEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGrkfedkev 115
Cdd:cd10230 1 AVLGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 116 qrdmklapykivnkdgkpyievkikdgetkvFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAG 195
Cdd:cd10230 73 -------------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 196 VIAGLNVVRIINEPTAAAIAYGLDKKGGE---KNILVFDLGGGTFDVSILTID------------NGVFEVLATNGDTHL 260
Cdd:cd10230 122 EIAGLNVLSLINDNTAAALNYGIDRRFENnepQNVLFYDMGASSTSATVVEFSsvkekdkgknktVPQVEVLGVGWDRTL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 261 GGEDFDQRIMEYFIKLIKKKHGK--DISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELN 338
Cdd:cd10230 202 GGLEFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELC 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023970679 339 NDLFRKTMGPVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPNKGVNPDEAVAFGAAVQG 409
Cdd:cd10230 282 ADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYA 352
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
38-645 |
2.06e-112 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 350.31 E-value: 2.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEaaknqaavnpERTVFDVKRLIGRKFedKEVQR 117
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTL--KEILN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 118 DMKL----APYKIVNKDgkpyiEVKIKDGEtKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKD 193
Cdd:PRK01433 89 TPALfslvKDYLDVNSS-----ELKLNFAN-KQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 194 AGVIAGLNVVRIINEPTAAAIAYGLDKkGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYF 273
Cdd:PRK01433 163 AAKIAGFEVLRLIAEPTAAAYAYGLNK-NQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 274 IKLIkkkhgkDISKDNRALgklrRECERAKRALSSQHQVRVEIESLfdgidfseplTRARFEELNNDLFRKTMGPVKKAM 353
Cdd:PRK01433 242 CNKF------DLPNSIDTL----QLAKKAKETLTYKDSFNNDNISI----------NKQTLEQLILPLVERTINIAQECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 354 EDAGLEkrQIDEIVLVGGSTRIPKIQQLLKDYFDgKEPNKGVNPDEAVAFGAAVQGGILSGEggdeTKDILLLDVAPLTL 433
Cdd:PRK01433 302 EQAGNP--NIDGVILVGGATRIPLIKDELYKAFK-VDILSDIDPDKAVVWGAALQAENLIAP----HTNSLLIDVVPLSL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 434 GIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSMTKDCRLLGKFDLTGIPPAPRGTPQIEVTFEVD 513
Cdd:PRK01433 375 GMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAID 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 514 ANGILNVKAEDKASGKSEKITITNDKGrLSQEEIERMVKEAEEFAEEDKKVKERIDARNSLETYVYNMRNQIndkDKLAD 593
Cdd:PRK01433 455 ADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAI---AELTT 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1023970679 594 KLESDEKEKIETA---TKEALEWMDDN--QNAEKEDYEEKLKEVEAVCNPIITAVYQ 645
Cdd:PRK01433 531 LLSESEISIINSLldnIKEAVHARDIIliNNSIKEFKSKIKKSMDTKLNIIINDLLK 587
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
39-413 |
3.48e-106 |
|
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: 327.02 E-value: 3.48e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQRD 118
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MKLAPYKIVNKDGKPYIEVKIKdGETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVIA 198
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYL-GEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 199 GLNVVRIINEPTAAAIAYGLDK----KGGEK--NILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEY 272
Cdd:cd24094 160 GLNPLRLMNDTTAAALGYGITKtdlpEPEEKprIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 273 FIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVKKA 352
Cdd:cd24094 240 FADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023970679 353 MEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILS 413
Cdd:cd24094 320 LAQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
37-412 |
9.68e-97 |
|
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: 301.59 E-value: 9.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 37 TVIGIDLGTTYSCVG-VYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGrkfedkev 115
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 116 qrdmklapykivnkdgkpyievkikdgeTKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAG 195
Cdd:cd10232 73 ----------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 196 VIAGLNVVRIINEPTAAAIAYGLDK-----KGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIM 270
Cdd:cd10232 125 AAAGLEVLQLIPEPAAAALAYDLRAetsgdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 271 EYFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGPVK 350
Cdd:cd10232 205 GHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVT 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023970679 351 KAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFDG---KEPNKGVNPDEAVAFGAAVQGGIL 412
Cdd:cd10232 285 DAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEstiIRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
37-411 |
6.29e-91 |
|
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: 287.61 E-value: 6.29e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 37 TVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQ 116
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 RDMKLAPYKIVN-KDGKPYIEVKIKDgETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAG 195
Cdd:cd11737 81 AEKPSLAYELVQlPTGTTGIKVMYME-EERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 196 VIAGLNVVRIINEPTAAAIAYGLDKKG------GEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRI 269
Cdd:cd11737 160 QIAGLNCLRLMNETTAVALAYGIYKQDlpapeeKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 270 MEYFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQ-HQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGP 348
Cdd:cd11737 240 VNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANaSDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023970679 349 VKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGI 411
Cdd:cd11737 320 LRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
37-408 |
1.90e-89 |
|
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: 283.68 E-value: 1.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 37 TVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQ 116
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 RDMKLAPYKIVN-KDGKPYIEVKIKDGEtKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAG 195
Cdd:cd11739 81 KEKENLSYDLVPlKNGGVGVKVMYLDEE-HHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 196 VIAGLNVVRIINEPTAAAIAYGLDKK---GGEKN--ILVF-DLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRI 269
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIYKQdlpAPDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 270 MEYFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQH-QVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGP 348
Cdd:cd11739 240 VEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSNStDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 349 VKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQ 408
Cdd:cd11739 320 LYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
37-413 |
1.84e-88 |
|
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: 281.04 E-value: 1.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 37 TVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQ 116
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 RDMKLAPYKIVN-KDGKPYIEVKIKDgETKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAG 195
Cdd:cd11738 81 AEKIKLPYELQKmPNGSTGVKVRYLD-EERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 196 VIAGLNVVRIINEPTAAAIAYGLDKKG------GEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRI 269
Cdd:cd11738 160 QIAGLNCLRLMNETTAVALAYGIYKQDlpaleeKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 270 MEYFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQ-HQVRVEIESLFDGIDFSEPLTRARFEELNNDLFRKTMGP 348
Cdd:cd11738 240 VDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANaSDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023970679 349 VKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAVQGGILS 413
Cdd:cd11738 320 LKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
39-407 |
3.55e-60 |
|
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: 204.65 E-value: 3.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDqgnrITPSWVGFTDNERLIgeaaknqaavnpertvfdvkrligrkfedkevqrd 118
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVV----LQLPWPGGDGGSSKV----------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 mklapykivnkdgkPyievkikdgeTKVfspeEVSAMILIKMKETAEAYLGKKIK-------DAVVTVPAYFNDAQRQAT 191
Cdd:cd10170 42 --------------P----------SVL----EVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREAL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 192 KDAGVIAGL----NVVRIINEPTAAAIAYGLDKKGGEK-----NILVFDLGGGTFDVSILTIDNG---VFEVLATNGDTH 259
Cdd:cd10170 94 REAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDLLPlkpgdVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 260 LGGEDFDQRIMEYFIKLIKKKHGKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGID---FSEPLTRARFEE 336
Cdd:cd10170 174 LGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEE 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1023970679 337 LNNDLFRKTMGPVKKAMEDAGLEK--RQIDEIVLVGGSTRIPKIQQLLKDYFDGKEPN---KGVNPDEAVAFGAAV 407
Cdd:cd10170 254 EIRDLFDPVIDKILELIEEQLEAKsgTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
39-407 |
3.36e-41 |
|
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: 155.12 E-value: 3.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNE------RLIGEAAKNQAAVNPE--RTVFDVKRLIGRKF 110
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEegRLIKSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 111 EDKEVqrdmklapykIVNKDgkpyievkikdgetkvFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQA 190
Cdd:cd10231 81 FDETT----------IFGRR----------------YPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 191 T-------KDAGVIAGLNVVRIINEPTAAAIAY--GLDKkggEKNILVFDLGGGTFDVSILTID----NGVFEVLATNGD 257
Cdd:cd10231 135 DaqaesrlRDAARRAGFRNVEFQYEPIAAALDYeqRLDR---EELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 258 tHLGGEDFDQRIM------------EYFIK-----------------------------LIKKKHGKDiSKDNRALGKLR 296
Cdd:cd10231 212 -GIGGDDFDRELAlkkvmphlgrgsTYVSGdkglpvpawlyadlsnwhaisllytkktlRLLLDLRRD-AADPEKIERLL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 297 ------------RECERAKRALSSQHQVRVEIESLFDGIDfsEPLTRARFEELNNDLFRKTMGPVKKAMEDAGLEKRQID 364
Cdd:cd10231 290 slvedqlghrlfRAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVD 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1023970679 365 EIVLVGGSTRIPKIQQLLKDYFdGKEPNKGVNPDEAVAFGAAV 407
Cdd:cd10231 368 RVFLTGGSSQSPAVRQALASLF-GQARLVEGDEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
38-406 |
5.19e-23 |
|
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: 101.20 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 38 VIGIDLGTTYSC-----VGVYKNGHVEIIANDQGNRI----TPSWVGFTDNERL--IGEAAKNQAAVNPERtvfdvkrli 106
Cdd:cd10229 2 VVAIDFGTTYSGyaysfITDPGDIHTMYNWWGAPTGVsspkTPTCLLLNPDGEFhsFGYEAREKYSDLAED--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 107 GRKFEDKEVQRDMKLAPYKIVNKDGKpyieVKIKDGetKVFSPEEVSAMILIKMKETAEAYLGKKIKDA--------VVT 178
Cdd:cd10229 73 EEHQWLYFFKFKMMLLSEKELTRDTK----VKAVNG--KSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 179 VPAYFNDAQRQATKDAGVIAGL------NVVRIINEPTAAAIAYGLDKKGGEKNI-------LVFDLGGGTFDVSILTI- 244
Cdd:cd10229 147 VPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKLLAEGEEKElkpgdkyLVVDCGGGTVDITVHEVl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 245 -DNGVFEVLATNGDtHLGGEDFDqrimEYFIKLIKKKHGKDISKDnralgkLRRECERAkralssqhqvRVEIESLFDGI 323
Cdd:cd10229 227 eDGKLEELLKASGG-PWGSTSVD----EEFEELLEEIFGDDFMEA------FKQKYPSD----------YLDLLQAFERK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 324 --DFSEPLTRARFEElnndLFRKTMGPVKKAMEDAgLEKRQ---IDEIVLVGGSTRIPKIQQLLKDYFDGK----EPnkg 394
Cdd:cd10229 286 krSFKLRLSPELMKS----LFDPVVKKIIEHIKEL-LEKPElkgVDYIFLVGGFAESPYLQKAVKEAFSTKvkiiIP--- 357
|
410
....*....|..
gi 1023970679 395 VNPDEAVAFGAA 406
Cdd:cd10229 358 PEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
39-407 |
5.10e-14 |
|
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: 73.28 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGhveIIANDqgnritPSWVGF-TDNERLI--GEAAKnqaavnpertvfdvkRLIGRKFEDKEV 115
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVdKNTGKVLavGEEAK---------------KMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 116 QRDMKlapykivnkDGkpyieVkIKDGETkvfspeeVSAMI--LIKMketaeAYLGKKIK--DAVVTVPAYFNDAQRQAT 191
Cdd:cd10225 58 IRPLR---------DG-----V-IADFEA-------TEAMLryFIRK-----AHRRRGFLrpRVVIGVPSGITEVERRAV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 192 KDAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKNiLVFDLGGGTFDVSILTIdNGVfeVLATNgdTHLGGEDFDQRIME 271
Cdd:cd10225 111 KEAAEHAGAREVYLIEEPMAAAIGAGLPIEEPRGS-MVVDIGGGTTEIAVISL-GGI--VTSRS--VRVAGDEMDEAIIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 272 YfiklIKKKHGKDISkdnralgklRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARfeELNNDLFRKTMGP--- 348
Cdd:cd10225 185 Y----VRRKYNLLIG---------ERTAERIKIEIGSAYPLDEELSMEVRGRDLVTGLPRTI--EITSEEVREALEEpvn 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023970679 349 -----VKKAMEDAGLEKRQ--IDE-IVLVGGSTRIPKIQQLLKDYFdgkepnkGV------NPDEAVAFGAAV 407
Cdd:cd10225 250 aiveaVRSTLERTPPELAAdiVDRgIVLTGGGALLRGLDELLREET-------GLpvhvadDPLTCVAKGAGK 315
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
39-384 |
1.84e-13 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 72.97 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDNErLIGEAAKNQAAVNPertvFDVKR--LIGRKfedKEVQ 116
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTRE-AVSEWLYRHLDVPA----YDDERqaLLRRA---IRYN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 117 RDMKLAPYKIVNKDGKPYIEVKIKDGET-------KVF------SPEEVS-------AMILiKMKETAEAYLGKKIKDAV 176
Cdd:PRK11678 75 REEDIDVTAQSVFFGLAALAQYLEDPEEvyfvkspKSFlgasglKPQQVAlfedlvcAMML-HIKQQAEAQLQAAITQAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 177 VTVPAYFN-----DAQRQAT---KDAGVIAGLNVVRIINEPTAAAIAY--GLDKkggEKNILVFDLGGGTFDVSILTI-- 244
Cdd:PRK11678 154 IGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTE---EKRVLVVDIGGGTTDCSMLLMgp 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 245 -----DNGVFEVLATNGdTHLGGEDFDqrIMEYFIKLI-------KKKHGK--------------DIS------------ 286
Cdd:PRK11678 231 swrgrADRSASLLGHSG-QRIGGNDLD--IALAFKQLMpllgmgsETEKGIalpslpfwnavainDVPaqsdfyslangr 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 287 ------KDNRA--------------LG-KLRRECERAKRALSSQHQVRVEIESLFDGIdfSEPLTRARFEELNNDLFRKT 345
Cdd:PRK11678 308 llndliRDAREpekvarllkvwrqrLSyRLVRSAEEAKIALSDQAETRASLDFISDGL--ATEISQQGLEEAISQPLARI 385
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1023970679 346 MGPVKKAMEDAGLekrQIDEIVLVGGSTRIP----KIQQLLKD 384
Cdd:PRK11678 386 LELVQLALDQAQV---KPDVIYLTGGSARSPliraALAQQLPG 425
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
39-282 |
5.03e-12 |
|
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also called envB) and the paralogous pair MreB and Mrl of Bacillus subtilis have all been shown to help determine cell shape. This protein is present in a wide variety of bacteria, including spirochetes, but is missing from the Mycoplasmas and from Gram-positive cocci. Most completed bacterial genomes have a single member of this family. In some species it is an essential gene. A close homolog is found in the Archaeon Methanobacterium thermoautotrophicum, and a more distant homolog in Archaeoglobus fulgidus. The family is related to cell division protein FtsA and heat shock protein DnaK. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129982 [Multi-domain] Cd Length: 333 Bit Score: 67.43 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGhveIIANDqgnritPSWVGFtdnERLIGEAAKNQAAVNPErtvfdVKRLIGRKFEDKEVQRD 118
Cdd:TIGR00904 5 IGIDLGTANTLVYVKGRG---IVLNE------PSVVAI---RTDRDAKTKSILAVGHE-----AKEMLGKTPGNIVAIRP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MklapykivnKDGkpyievKIKDGETkvfspeeVSAMI--LIKMKETAEAYLGKKIkdaVVTVPAYFNDAQRQATKDAGV 196
Cdd:TIGR00904 68 M---------KDG------VIADFEV-------TEKMIkyFIKQVHSRKSFFKPRI---VICVPSGITPVERRAVKESAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 197 IAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVfDLGGGTFDVSILTIdNGVfevlATNGDTHLGGEDFDQRIMEYfikl 276
Cdd:TIGR00904 123 SAGAREVYLIEEPMAAAIGAGLPVEEPTGSMVV-DIGGGTTEVAVISL-GGI----VVSRSIRVGGDEFDEAIINY---- 192
|
....*.
gi 1023970679 277 IKKKHG 282
Cdd:TIGR00904 193 IRRTYN 198
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
39-406 |
2.27e-11 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 65.48 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCVGVYKNGhveIIANDqgnritPSWVGF-TDNERLI--GEAAKnqaavnpertvfdvkRLIGRkfedkev 115
Cdd:COG1077 10 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAIdKKTGKVLavGEEAK---------------EMLGR------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 116 qrdmklAPYKIVN----KDGKpyievkIKDgetkvFspeevsamilikmkETAEAYLG---KKIKD--------AVVTVP 180
Cdd:COG1077 59 ------TPGNIVAirplKDGV------IAD-----F--------------EVTEAMLKyfiKKVHGrrsffrprVVICVP 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 181 AYFNDAQRQATKDAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVfDLGGGTFDVSILTIdNGVfeVLATNgdTHL 260
Cdd:COG1077 108 SGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTGNMVV-DIGGGTTEVAVISL-GGI--VVSRS--IRV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 261 GGEDFDQRIMEYfiklIKKKHGKDISkdnralgklRRECERAKRALSSQHQVRVEIESLFDGIDFSEPLTRARfeELNND 340
Cdd:COG1077 182 AGDELDEAIIQY----VRKKYNLLIG---------ERTAEEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTI--TITSE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 341 LFRKTMGPVKKAMEDA---GLEKRQ-------IDE-IVLVGGSTRIPKIQQLLKDYFdgkepnkGV------NPDEAVAF 403
Cdd:COG1077 247 EIREALEEPLNAIVEAiksVLEKTPpelaadiVDRgIVLTGGGALLRGLDKLLSEET-------GLpvhvaeDPLTCVAR 319
|
...
gi 1023970679 404 GAA 406
Cdd:COG1077 320 GTG 322
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
162-405 |
1.24e-09 |
|
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: 60.26 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 162 ETAEA---YLGKKIKDA--------VVTVPAYFNDAQRQATKDAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKNiLVF 230
Cdd:pfam06723 72 EVTEAmlkYFIKKVHGRrsfskprvVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGN-MVV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 231 DLGGGTFDVSILTIDNGVfevlaTNGDTHLGGEDFDQRImeyfIKLIKKKHgkdiskdNRALGKlrRECERAKRALSSQH 310
Cdd:pfam06723 151 DIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFDEAI----IKYIRKKY-------NLLIGE--RTAERIKIEIGSAY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 311 QVRVEIESLFDGIDFSEPLtrARFEELNNDLFRKTMGP--------VKKAMED--AGLEKRQIDE-IVLVGGSTRIPKIQ 379
Cdd:pfam06723 213 PTEEEEKMEIRGRDLVTGL--PKTIEISSEEVREALKEpvsaiveaVKEVLEKtpPELAADIVDRgIVLTGGGALLRGLD 290
|
250 260 270
....*....|....*....|....*....|..
gi 1023970679 380 QLLKDYFdgkepnkGV------NPDEAVAFGA 405
Cdd:pfam06723 291 KLLSDET-------GLpvhiaeDPLTCVALGT 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
175-406 |
2.93e-09 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 58.99 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 175 AVVTVPAYFNDAQRQATKDAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKNiLVFDLGGGTFDVSILTIdNGVfevlAT 254
Cdd:PRK13930 103 IVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPVTEPVGN-MVVDIGGGTTEVAVISL-GGI----VY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 255 NGDTHLGGEDFDQRIMEYfiklIKKKHGKDISKdnralgklrRECERAKRALSSQHQV----RVEIEslfdGIDFSEPLT 330
Cdd:PRK13930 177 SESIRVAGDEMDEAIVQY----VRRKYNLLIGE---------RTAEEIKIEIGSAYPLdeeeSMEVR----GRDLVTGLP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 331 RARfeELNNDLFRKTMGP--------VKKAMED------AGLekrqIDE-IVLVGGSTRIPKIQQLLKDYFdgkepnkGV 395
Cdd:PRK13930 240 KTI--EISSEEVREALAEplqqiveaVKSVLEKtppelaADI----IDRgIVLTGGGALLRGLDKLLSEET-------GL 306
|
250
....*....|....*..
gi 1023970679 396 ------NPDEAVAFGAA 406
Cdd:PRK13930 307 pvhiaeDPLTCVARGTG 323
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
141-387 |
3.63e-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: 58.46 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 141 DGETKVFSPEEVsAMILIKMKETAEAYLGKKIKDAVVTVP----AYFNDAQRqatkdagviAGLNVVRIINEPTAAAIAY 216
Cdd:cd24004 37 MGDGQIHDISKV-AESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPFAAANLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 217 gLDKKGGEKNILVFDLGGGTFDVSIltIDNGVfeVLATnGDTHLGGEDFDQRIMEyfiklikkkhGKDISKDnralgklr 296
Cdd:cd24004 107 -IPYDMRDLNIALVDIGAGTTDIAL--IRNGG--IEAY-RMVPLGGDDFTKAIAE----------GFLISFE-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 297 rECERAKRAlssqhqvrveiESLFDGIDFSEPLTRARFEELNNDLFRKTMGP----VKKAMEDAGLEKRQIDEIVLVGGS 372
Cdd:cd24004 163 -EAEKIKRT-----------YGIFLLIEAKDQLGFTINKKEVYDIIKPVLEElasgIANAIEEYNGKFKLPDAVYLVGGG 230
|
250
....*....|....*
gi 1023970679 373 TRIPKIQQLLKDYFD 387
Cdd:cd24004 231 SKLPGLNEALAEKLG 245
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
176-281 |
9.11e-09 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 57.60 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 176 VVTVPAYFNDAQRQATKDAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVfDLGGGTFDVSILTIDNGVfevlaTN 255
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVV-DIGGGTTDIAVLSLGGIV-----TS 172
|
90 100
....*....|....*....|....*.
gi 1023970679 256 GDTHLGGEDFDQRIMEYfiklIKKKH 281
Cdd:PRK13928 173 SSIKVAGDKFDEAIIRY----IRKKY 194
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
156-260 |
1.76e-07 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 52.65 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 156 ILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVIAGLNVVRIINEPTAAAIAYGLdkkggeKNILVFDLGGG 235
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI------RDGAVVDIGGG 121
|
90 100
....*....|....*....|....*....
gi 1023970679 236 TFDVSIltIDNGvfEVLAT----NGDTHL 260
Cdd:cd24047 122 TTGIAV--LKDG--KVVYTadepTGGTHL 146
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
176-282 |
5.08e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 52.01 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 176 VVTVPAYFNDAQRQATKDAGVIAGLNVVRIINEPTAAAIAYGLDKKGGEKNILVfDLGGGTFDVSILTIdNGVfevlATN 255
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVV-DIGGGTTEVAVISL-GGI----VYS 173
|
90 100
....*....|....*....|....*..
gi 1023970679 256 GDTHLGGEDFDQRIMEYfiklIKKKHG 282
Cdd:PRK13927 174 KSVRVGGDKFDEAIINY----VRRNYN 196
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
156-242 |
2.17e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 49.83 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 156 ILIKMKETAEAYLGKKIKDAVVTVPAyfndaqrqAT--KDAGVI------AGLNVVRIINEPTAAAIAYGLdkkggeKNI 227
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGI------DNG 137
|
90
....*....|....*
gi 1023970679 228 LVFDLGGGTFDVSIL 242
Cdd:PRK15080 138 AVVDIGGGTTGISIL 152
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
139-275 |
7.53e-06 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 48.36 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 139 IKDGetkVFSPEEVSAMILIKMKETAEAYLGKKIK--DAVVTVPAYFNDAQRQATKDAGVIAGLNVVRIINEPTAAAIAY 216
Cdd:PRK13929 66 MKDG---VIADYDMTTDLLKQIMKKAGKNIGMTFRkpNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGA 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1023970679 217 GLDKKGGEKNILVfDLGGGTFDVSILTidngvFEVLATNGDTHLGGEDFDQRIMEYFIK 275
Cdd:PRK13929 143 DLPVDEPVANVVV-DIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSFVRK 195
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
39-290 |
1.75e-05 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 46.75 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGttyscvgvykNGHVEIIANDQGNRITPSWVGFTDNERLIGEAAKNQAAVNPERTVFdvkrLIGrKFEDKEVQRD 118
Cdd:cd10227 1 IGIDIG----------NGNTKVVTGGGKEFKFPSAVAEARESSLDDGLLEDDIIVEYNGKRY----LVG-ELALREGGGG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 119 MKLAPYKIVNKDGKPYIEVKIKDgeTKVFSPEEVSAMILIKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATkdagvia 198
Cdd:cd10227 66 RSTGDDKKKSEDALLLLLAALAL--LGDDEEVDVNLVVGLPISEYKEEKKELKKKLLKGLHEFTFNGKERRIT------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 199 gLNVVRIINEPTAAAIAYGLDKKGGE-KNILVFDLGGGTfdVSILTIDNGvfEVLATNGDTHLGGEDFDQRIMEYFIKLI 277
Cdd:cd10227 137 -INDVKVLPEGAGAYLDYLLDDDELEdGNVLVIDIGGGT--TDILTFENG--KPIEESSDTLPGGEEALEKYADDILNEL 211
|
250
....*....|...
gi 1023970679 278 KKKHGKDISKDNR 290
Cdd:cd10227 212 LKKLGDELDSADK 224
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
39-405 |
9.28e-05 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 44.89 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 39 IGIDLGTTYSCvgvyknghveiIANDQGNRIT-PSWVGFTD---------NERLIGEAA-KNQAAVNpertvfdvkrlIG 107
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRFSfRSVVGYPKdiiarkllgKEVLFGDEAlENRLALD-----------LR 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 108 RKFEDKevqrdmklapykivnkdgkpyievKIKDGETKVFspeEVSAMILIKMKETAEAYLGKKIKdAVVTVPAYFNDAQ 187
Cdd:cd24009 62 RPLEDG------------------------VIKEGDDRDL---EAARELLQHLIELALPGPDDEIY-AVIGVPARASAEN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 188 RQATKDA--GVIAGlnvVRIINEPTAaaIAYGLDKKggeKNILVFDLGGGTFDVSILtidNGvfeVLATNGD---THLGG 262
Cdd:cd24009 114 KQALLEIarELVDG---VMVVSEPFA--VAYGLDRL---DNSLIVDIGAGTTDLCRM---KG---TIPTEEDqitLPKAG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 263 EDFDQRIMEyfikLIKKKH-GKDISKDnralgKLRRECERAKRA--LSSQHQVRVEIESLFDGIDFSEPLTRArFEELNN 339
Cdd:cd24009 180 DYIDEELVD----LIKERYpEVQLTLN-----MARRWKEKYGFVgdASEPVKVELPVDGKPVTYDITEELRIA-CESLVP 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 340 DLFRKTMGPVKKAMEDAGLEKRQidEIVLVGGSTRI----PKIQQLLKDYFDGKEPnKGVNPDEAVAFGA 405
Cdd:cd24009 250 DIVEGIKKLIASFDPEFQEELRN--NIVLAGGGSRIrgldTYIEKALKEYGGGKVT-CVDDPVFAGAEGA 316
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
198-387 |
1.28e-04 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 44.74 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 198 AGLNVVRIINEPTAAAIAYgLDKKGGEKNILVFDLGGGTFDVSIlTIDNGV--FEVLAtngdthLGGEDFDqrimeyfik 275
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTEDEKELGVALVDIGGGTTDIAV-FKDGALrhTAVIP------VGGDHIT--------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 276 likkkhgKDISkdnRALGKLRRECERAKR----ALSSQHQVRVEIEslFDGIDFSEPLT----------RARFEELnndl 341
Cdd:COG0849 237 -------NDIA---IGLRTPLEEAERLKIkygsALASLADEDETIE--VPGIGGRPPREisrkelaeiiEARVEEI---- 300
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1023970679 342 frktMGPVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFD 387
Cdd:COG0849 301 ----FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
352-418 |
3.74e-04 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 43.67 E-value: 3.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1023970679 352 AMEDAGLEkrqIDEIVLVGGSTRIPKIQQLLKDYFDgkEPNKGVNPDEAVAFGAAVQGGILSGEGGD 418
Cdd:COG1070 388 ALEEAGVK---IDRIRATGGGARSPLWRQILADVLG--RPVEVPEAEEGGALGAALLAAVGLGLYDD 449
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
198-404 |
4.54e-04 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; 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. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 42.90 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 198 AGLNVVRIINEPTAAAIAYgLDKKggEKN--ILVFDLGGGTFDVSILTidNGVF---EVLAtngdthLGGEDFDqrimey 272
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTED--EKElgVALIDIGGGTTDIAVFK--NGSLrytAVIP------VGGNHIT------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 273 fiklikkkhgKDISKdnrALGKLRRECERAKR----ALSSQHQVRVEIESLFDGIDFSEPLTR--------ARFEELnnd 340
Cdd:cd24048 235 ----------NDIAI---GLNTPFEEAERLKIkygsALSEEADEDEIIEIPGVGGREPREVSRrelaeiieARVEEI--- 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023970679 341 lFRKtmgpVKKAMEDAGLEKRQIDEIVLVGGSTRIPKIQQLLKDYFD-----GKEPNKGVNPDE------AVAFG 404
Cdd:cd24048 299 -LEL----VKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvriGRPKNIGGLPEEvndpayATAVG 368
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
174-236 |
4.91e-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: 40.53 E-value: 4.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1023970679 174 DAVVTVPAYFNDAQRQAT-----------KDAGVIAGLNVVRIINEPTAAAIAYGLDKKGGekNILVFDLGGGT 236
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPE--GLLVVDLGGGT 86
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
352-414 |
1.17e-03 |
|
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: 41.77 E-value: 1.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023970679 352 AMEDAGLEkrqIDEIVLVGGSTRIPKIQQLLKDYFDgkEPNKGVNPDEAVAFGAAVQGGILSG 414
Cdd:cd07809 386 ILRELGVE---IDEIRLIGGGSKSPVWRQILADVFG--VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
198-407 |
3.01e-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: 40.34 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 198 AGLNVVRIINEPTAAAIAYGLDK-KGGEKNILVFDLGGGTFDVSIltIDNGVFEVLATNGdthLGGEDFDQRIMEYF--- 273
Cdd:cd24049 148 AGLKPVAIDVESFALARALEYLLpDEEEETVALLDIGASSTTLVI--VKNGKLLFTRSIP---VGGNDITEAIAKALgls 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 274 ---IKLIKKKHGKDISKDNRALGKLRREcerakralssqhqVRVEIESLFDGIDFSEpltrarfeelnnDLFRKTMGpvk 350
Cdd:cd24049 223 feeAEELKREYGLLLEGEEGELKKVAEA-------------LRPVLERLVSEIRRSL------------DYYRSQNG--- 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1023970679 351 kamedagleKRQIDEIVLVGGSTRIPKIQQLLKDYFDGK----EPNKGVNPDE-------------AVAFGAAV 407
Cdd:cd24049 275 ---------GEPIDKIYLTGGGSLLPGLDEYLSERLGIPveilNPFSNIESKKsddeelkedaplfAVAIGLAL 339
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
535-633 |
5.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 535 ITNDKGRLSQEEIERMVKEAEEFAEEDKK-----VKERI-DARNSLETYVYNMRNQINDKDK-LADKlESDEKEKIETAT 607
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKealleAKEEIhKLRNEFEKELRERRNELQKLEKrLLQK-EENLDRKLELLE 106
|
90 100
....*....|....*....|....*...
gi 1023970679 608 K--EALEWMDDNQNAEKEDYEEKLKEVE 633
Cdd:PRK12704 107 KreEELEKKEKELEQKQQELEKKEEELE 134
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
532-632 |
6.07e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.03 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 532 KITITNDKGRLSQEEIERMVKEAEEFA--EEDKKVKERIDARNSLETYVYNMRNQ---INDKDKLADKLESdEKEKIEta 606
Cdd:TIGR01612 1611 KISDIKKKINDCLKETESIEKKISSFSidSQDTELKENGDNLNSLQEFLESLKDQkknIEDKKKELDELDS-EIEKIE-- 1687
|
90 100 110
....*....|....*....|....*....|
gi 1023970679 607 tkealewMDDNQNaeKEDYE----EKLKEV 632
Cdd:TIGR01612 1688 -------IDVDQH--KKNYEigiiEKIKEI 1708
|
|
| ASKHA_NBD_ParM_Alp7A-like |
cd24023 |
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar ... |
203-386 |
6.51e-03 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Bacillus subtilis actin-like protein Alp7A, a plasmid partitioning protein that functions in plasmid segregation. The subfamily also includes Bacillus thuringiensis ParM hybrid fusion protein.
Pssm-ID: 466873 [Multi-domain] Cd Length: 368 Bit Score: 39.24 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 203 VRIINEPTAAAIAYGLDKKGG------------EKNILVFDLGGGTFDVSIltIDNGVFEVLATNGdTHLGGEDfdqrIM 270
Cdd:cd24023 174 VKVLPEGVAALFALIYDEDGNervedtededlkEKNILIIDIGGGTTDVAV--FEGGKFDPDLSTG-IDLGIGT----AL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023970679 271 EYFIKLIKKKHGKDISKDNRALGKLRREceraKRALSSQHQVRVEIESLFDgidfsepltrARFEELNNDLFRKtmgpVK 350
Cdd:cd24023 247 DEIIKELKKEYGVEFDRRRLLFELIIKK----KEYKDKNRGKKVDLTDIVE----------KALEELAEEILDE----IE 308
|
170 180 190
....*....|....*....|....*....|....*.
gi 1023970679 351 KAMEDAgleKRQIDEIVLVGGSTripkiqQLLKDYF 386
Cdd:cd24023 309 KKWNKA---GNDIEVIYVYGGGS------ILLKDYL 335
|
|
| HyuA |
COG0145 |
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport ... |
194-251 |
6.82e-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: 39.69 E-value: 6.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1023970679 194 AGVIAglnvvriineptAAAIAygldKKGGEKNILVFDLGGGTFDVSIltIDNGVFEV 251
Cdd:COG0145 261 GGVVG------------AAALA----RAAGFDNVITFDMGGTSTDVSL--IEDGEPER 300
|
|
| |
