|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-608 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1199.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGT----- 73
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFtKDGERLVGQPAKRQAVTNPeNTIFSIKRLMGRrdeev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 74 -----------------DYKVDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PRK00290 81 qkdiklvpykivkadngDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 137 LEVERIINEPTAAALAYGLDKtDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKK 216
Cdd:PRK00290 161 LEVLRIINEPTAAALAYGLDK-KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKD 296
Cdd:PRK00290 240 ENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 297 AGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIMGG 376
Cdd:PRK00290 320 AGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 377 RMNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNV 456
Cdd:PRK00290 400 VMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 457 TAKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSNAE 536
Cdd:PRK00290 480 SAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIE 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920606352 537 SKKDALKSALEGQDIEDIKAKKEELEKVIQDLSAKVYqqaqQAQQQAQEGTQQTQNDSNVEDAEFKEVNDDE 608
Cdd:PRK00290 560 AAIKELKEALKGEDKEAIKAKTEELTQASQKLGEAMY----QQAQAAQGAAGAAAKDDDVVDAEFEEVKDDK 627
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-573 |
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: 1030.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 3 KVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGT------- 73
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFtKNGERLVGQPAKRQAVTNPeNTIYSIKRFMGRrfdevte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 74 --------------DYKVDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:TIGR02350 81 eakrvpykvvgdggDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 140 ERIINEPTAAALAYGLDKTDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKENG 219
Cdd:TIGR02350 161 LRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKKEEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 220 VDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKDAGL 299
Cdd:TIGR02350 241 IDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKDAGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 300 STSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIMGGRMN 379
Cdd:TIGR02350 321 SASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGVMT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 380 TLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNVTAK 459
Cdd:TIGR02350 401 KLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 460 DLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSNAESKK 539
Cdd:TIGR02350 481 DKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKAV 560
|
570 580 590
....*....|....*....|....*....|....
gi 920606352 540 DALKSALEGQDIEDIKAKKEELEKVIQDLSAKVY 573
Cdd:TIGR02350 561 AELKEALKGEDVEEIKAKTEELQQALQKLAEAMY 594
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
4-573 |
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: 905.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY------- 75
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPkNTVFSVKRLIGRKFsdpvvqr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 -------------------KVDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:pfam00012 81 dikhlpykvvklpngdagvEVRYLGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 137 LEVERIINEPTAAALAYGLDKTDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKK 216
Cdd:pfam00012 161 LNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGvSQTQISLPFISAGESGpLHLEISLTRSKFEELADSLIRRTMEPTRQALKD 296
Cdd:pfam00012 241 KYGIDLSKDKRALQRLREAAEKAKIELSS-NQTNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVEKALKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 297 AGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITG--DVKDVVLLDVTPLSLGIEIM 374
Cdd:pfam00012 319 AGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIETL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 375 GGRMNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIV 454
Cdd:pfam00012 399 GGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGIL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 455 NVTAKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSN 534
Cdd:pfam00012 479 TVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSK 558
|
570 580 590
....*....|....*....|....*....|....*....
gi 920606352 535 AESKKDALKSALEGQDIEDIKAKKEELEKVIQDLSAKVY 573
Cdd:pfam00012 559 VESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMY 597
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-573 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 845.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMG------ 72
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFgKSGDRLVGQLAKRQAVTNAeNTVYSIKRFIGrrwddt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 73 ------TDYK----------VDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PRK13411 81 eeersrVPYTcvkgrddtvnVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 137 LEVERIINEPTAAALAYGLDKTDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKK 216
Cdd:PRK13411 161 LEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKD 296
Cdd:PRK13411 241 QEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 297 AGLSTSEIDEVILVGGSTRIPAVQEAVKKEI-GKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIMG 375
Cdd:PRK13411 321 AGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 376 GRMNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVN 455
Cdd:PRK13411 401 EVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 456 VTAKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSNA 535
Cdd:PRK13411 481 VSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRA 560
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 920606352 536 ESKKDALKSALEGQDI--EDIKAKKEELEKVIQDLSAKVY 573
Cdd:PRK13411 561 EQKVEQLEAALTDPNIslEELKQQLEEFQQALLAIGAEVY 600
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-603 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 844.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMG------ 72
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYtKKGDLLVGQIAKRQAVINPeNTFYSVKRFIGrkfsei 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 73 ------TDYKV--DIEG----------KSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:CHL00094 81 seeakqVSYKVktDSNGnikiecpalnKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 135 AGLEVERIINEPTAAALAYGLDKTdQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEF 214
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDKK-NNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 215 KKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQAL 294
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 295 KDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIM 374
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 375 GGRMNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIV 454
Cdd:CHL00094 400 GGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 455 NVTAKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSN 534
Cdd:CHL00094 480 SVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 920606352 535 AESKKDALKSALEGQDIEDIKAKKEELEKVIQDLSAKVYqqaqqaqqQAQEGTQQTQNDSNVEDAEFKE 603
Cdd:CHL00094 560 IENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVY--------SSTSTTDPASNDDDVIDTDFSE 620
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-568 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 801.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY--- 75
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFtKDGELLVGQLARRQLVLNPqNTFYNLKRFIGRRYdel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 -----------KVDIEG----------KSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:PRK13410 81 dpeskrvpytiRRNEQGnvrikcprleREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 135 AGLEVERIINEPTAAALAYGLDKTDqDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEF 214
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 215 KKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQAL 294
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 295 KDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIM 374
Cdd:PRK13410 320 KDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 375 GGRMNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIV 454
Cdd:PRK13410 400 GGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 455 NVTAKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQ------------------- 515
Cdd:PRK13410 480 QVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQaerrlrdaalefgpyfaer 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 920606352 516 ----VEKTITDLGDNISDDDKSNAESKKDALKSALEGQDIEDIKAKKEELEKVIQDL 568
Cdd:PRK13410 560 qrraVESAMRDVQDSLEQDDDRELDLAVADLQEALYGLNREVRAEYKEEDEGPLQGI 616
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
4-486 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 790.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK---VD 78
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFpKDGEVLVGEAAKRQAVTNPgRTIRSIKRLLGRSLFdeaTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 79 IEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKT 158
Cdd:COG0443 81 VGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 159 DQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKENGVDLSQDKMALQRLKDAAEK 238
Cdd:COG0443 161 KEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEEGIDLRLDPAALQRLREAAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 239 AKKDLSGVSQTQISLPFisageSGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKDAGLSTSEIDEVILVGGSTRIPA 318
Cdd:COG0443 241 AKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 319 VQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDvvlLDVTPLSLGIEIMGGRMNTLIERNTTIPTSKSQVYST 398
Cdd:COG0443 316 VRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIETLGGVFTKLIPRNTTIPTAKSQVFST 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 399 AADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNVTAKDLGTNKEQNITIqsssals 478
Cdd:COG0443 393 AADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITI------- 465
|
....*...
gi 920606352 479 DEEIDRMV 486
Cdd:COG0443 466 KEEIERML 473
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
4-573 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 779.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK----- 76
Cdd:PTZ00400 43 IVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFtEDGQRLVGIVAKRQAVTNPeNTVFATKRLIGRRYDedatk 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 77 -------------------VDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:PTZ00400 123 keqkilpykivrasngdawIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 138 EVERIINEPTAAALAYGLDKTDqDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKE 217
Cdd:PTZ00400 203 DVLRIINEPTAAALAFGMDKND-GKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEFKKQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 218 NGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKDA 297
Cdd:PTZ00400 282 QGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCEKCIKDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 298 GLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIMGGR 377
Cdd:PTZ00400 362 GVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGIETLGGV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 378 MNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNVT 457
Cdd:PTZ00400 442 FTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMNIS 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 458 AKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSNAES 537
Cdd:PTZ00400 522 AVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDELKQ 601
|
570 580 590
....*....|....*....|....*....|....*.
gi 920606352 538 KKDALKSALEGQDIEDIKAKKEELEKVIQDLSAKVY 573
Cdd:PTZ00400 602 KITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAY 637
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-603 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 742.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 3 KVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMG-------- 72
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYtKNGDRLVGQIAKRQAVVNPeNTFFSVKRFIGrkmsevde 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 73 ----TDYKVDIE------------GKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PLN03184 120 eskqVSYRVVRDengnvkldcpaiGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 137 LEVERIINEPTAAALAYGLDKTDqDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKK 216
Cdd:PLN03184 200 LEVLRIINEPTAASLAYGFEKKS-NETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKD 296
Cdd:PLN03184 279 DEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVENALRD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 297 AGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIMGG 376
Cdd:PLN03184 359 AKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLGLETLGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 377 RMNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNV 456
Cdd:PLN03184 439 VMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSV 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 457 TAKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSNAE 536
Cdd:PLN03184 519 SATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVE 598
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 920606352 537 SKKDALKSALEGQDIEDIKAKKEELEKVIQDLSAKVYQQAQQAQQ--------QAQEGTQQTQNDSNVEDAEFKE 603
Cdd:PLN03184 599 AKLKELKDAIASGSTQKMKDAMAALNQEVMQIGQSLYNQPGAGGAgpapggeaGSSSSSSSGGDGDDVIDADFTD 673
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
4-353 |
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: 696.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK----- 76
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFtKDGERLVGQPAKRQAVTNPeNTIFSIKRFMGRRYKeveve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 77 -----------------VDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:cd10234 81 rkqvpypvvsagngdawVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 140 ERIINEPTAAALAYGLDKtDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKENG 219
Cdd:cd10234 161 LRIINEPTAAALAYGLDK-KKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 220 VDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKDAGL 299
Cdd:cd10234 240 IDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAKL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 920606352 300 STSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVIT 353
Cdd:cd10234 320 SPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
4-573 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 676.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---------- 72
Cdd:PTZ00186 29 VIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPqSTFYAVKRLIGrrfedehiqk 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 73 ----TDYKV-----------DIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:PTZ00186 109 diknVPYKIvragngdawvqDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 138 EVERIINEPTAAALAYGLDKTdQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKE 217
Cdd:PTZ00186 189 NVIRVVNEPTAAALAYGMDKT-KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEFRKT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 218 NGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKDA 297
Cdd:PTZ00186 268 SGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPCKQCMKDA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 298 GLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIMGGR 377
Cdd:PTZ00186 348 GVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLGIETLGGV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 378 MNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNVT 457
Cdd:PTZ00186 428 FTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHVT 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 458 AKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLgDNISDDDKSNAES 537
Cdd:PTZ00186 508 AKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEW-KYVSDAEKENVKT 586
|
570 580 590
....*....|....*....|....*....|....*...
gi 920606352 538 KKDALKSALEGQDI--EDIKAKKEELEKVIQDLSAKVY 573
Cdd:PTZ00186 587 LVAELRKAMENPNVakDDLAAATDKLQKAVMECGRTEY 624
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-573 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 602.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY-------- 75
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPeNTVFDAKRLIGRKFddsvvqsd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 ------------------KVDIEG--KSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:PTZ00009 87 mkhwpfkvttggddkpmiEVTYQGekKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 136 GLEVERIINEPTAAALAYGLDKTDQDQK-VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEF 214
Cdd:PTZ00009 167 GLNVLRIINEPTAAAIAYGLDKKGDGEKnVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQDF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 215 KKEN-GVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGesgpLHLEISLTRSKFEELADSLIRRTMEPTRQA 293
Cdd:PTZ00009 247 KRKNrGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEG----IDYNVTISRARFEELCGDYFRNTLQPVEKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 294 LKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEI-GKDPHKGVNPDEVVAMGAAIQGGVITGD----VKDVVLLDVTPLS 368
Cdd:PTZ00009 323 LKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLDVTPLS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 369 LGIEIMGGRMNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDI 448
Cdd:PTZ00009 403 LGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 449 DKNGIVNVTAKDLGTNKEQNITIQSSSA-LSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITD--LGD 525
Cdd:PTZ00009 483 DANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDekVKG 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 920606352 526 NISDDDKSNAESK-KDALKSALEGQ--DIEDIKAKKEELEKVIQDLSAKVY 573
Cdd:PTZ00009 563 KLSDSDKATIEKAiDEALEWLEKNQlaEKEEFEHKQKEVESVCNPIMTKMY 613
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-571 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 570.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKVDIE 80
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPkNTISSVKRFMGrslADIQQRYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 81 GKSY-------------------TPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVER 141
Cdd:PRK05183 102 HLPYqfvasengmplirtaqglkSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNVLR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 142 IINEPTAAALAYGLDKTdQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLvsefKKENGVD 221
Cdd:PRK05183 182 LLNEPTAAAIAYGLDSG-QEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWI----LEQAGLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 222 LSQDKMALQRLKDAAEKAKKDLSGVSQTQISLpFISAGEsgplhleisLTRSKFEELADSLIRRTMEPTRQALKDAGLST 301
Cdd:PRK05183 257 PRLDPEDQRLLLDAARAAKEALSDADSVEVSV-ALWQGE---------ITREQFNALIAPLVKRTLLACRRALRDAGVEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 302 SEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDV--KDVVLLDVTPLSLGIEIMGGRMN 379
Cdd:PRK05183 327 DEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKpdSDMLLLDVIPLSLGLETMGGLVE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 380 TLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNVTAK 459
Cdd:PRK05183 407 KIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVTAM 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 460 DLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSNAESKK 539
Cdd:PRK05183 487 EKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERAAIDAAM 566
|
570 580 590
....*....|....*....|....*....|..
gi 920606352 540 DALKSALEGQDIEDIKAKKEELEKVIQDLSAK 571
Cdd:PRK05183 567 AALREVAQGDDADAIEAAIKALDKATQEFAAR 598
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
2-352 |
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: 569.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 2 SKVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK--- 76
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFtADGERLVGMPAKRQAVTNPeNTLYATKRLIGRRFDdpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 77 ---------------------VDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd11733 81 vqkdikmvpykivkasngdawVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 136 GLEVERIINEPTAAALAYGLDKTDqDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFK 215
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKKD-DKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 216 KENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALK 295
Cdd:cd11733 240 KEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 920606352 296 DAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd11733 320 DAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
4-571 |
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: 559.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYKvDIEG 81
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPkNTISSVKRLMGRSIE-DIKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 82 KSY----------------------TPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:TIGR01991 80 FSIlpyrfvdgpgemvrlrtvqgtvTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 140 ERIINEPTAAALAYGLDKTdQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVsefkKENG 219
Cdd:TIGR01991 160 LRLLNEPTAAAVAYGLDKA-SEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL----KQLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 220 VDLSQDKMALQRLKDAAEKAKKDLSGvsQTQISLPFISAGEsgplHLEISLTRSKFEELADSLIRRTMEPTRQALKDAGL 299
Cdd:TIGR01991 235 ISADLNPEDQRLLLQAARAAKEALTD--AESVEVDFTLDGK----DFKGKLTRDEFEALIQPLVQKTLSICRRALRDAGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 300 STSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDV--KDVVLLDVTPLSLGIEIMGGR 377
Cdd:TIGR01991 309 SVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRigNDLLLLDVTPLSLGIETMGGL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 378 MNTLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNVT 457
Cdd:TIGR01991 389 VEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTVS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 458 AKDLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSNAES 537
Cdd:TIGR01991 469 AQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAIDA 548
|
570 580 590
....*....|....*....|....*....|....
gi 920606352 538 KKDALKSALEGQDIEDIKAKKEELEKVIQDLSAK 571
Cdd:TIGR01991 549 AMEALQKALQGDDADAIKAAIEALEEATDNFAAR 582
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
4-354 |
2.45e-174 |
|
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: 499.67 E-value: 2.45e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKR------------ 69
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFtKDGERLVGVPAKRQAVVNPeNTLFATKRligrkfddaevq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 70 ------------HMGTDYKVDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:cd11734 83 rdikevpykivkHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 138 EVERIINEPTAAALAYGLDKTDqDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKE 217
Cdd:cd11734 163 NVLRVINEPTAAALAYGLDKSG-DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFKKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 218 NGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKDA 297
Cdd:cd11734 242 SGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALKDA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 920606352 298 GLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITG 354
Cdd:cd11734 322 GVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
4-352 |
8.57e-170 |
|
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: 487.79 E-value: 8.57e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKVDI 79
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPeNTIFDVKRLIGrkfDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 80 -------------------------EGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd24028 81 dikhwpfkvvededgkpkievtykgEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 135 AGLEVERIINEPTAAALAYGLDKTDQDQK-VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSE 213
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERnVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 214 FKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESgplhLEISLTRSKFEELADSLIRRTMEPTRQA 293
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGID----FETTITRAKFEELCEDLFKKCLEPVEKV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 294 LKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEI-GKDPHKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd24028 317 LKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
4-352 |
4.25e-166 |
|
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: 478.24 E-value: 4.25e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY------- 75
Cdd:cd10241 3 VIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPeNTVFDVKRLIGRKFddkevqk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 ------------------KVDIEG--KSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd10241 83 dikllpfkivnkngkpyiQVEVKGekKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 136 GLEVERIINEPTAAALAYGLDKTDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFK 215
Cdd:cd10241 163 GLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLFK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 216 KENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESgplhLEISLTRSKFEELADSLIRRTMEPTRQALK 295
Cdd:cd10241 243 KKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGED----FSETLTRAKFEELNMDLFRKTLKPVQKVLE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 920606352 296 DAGLSTSEIDEVILVGGSTRIPAVQEAVKKEI-GKDPHKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd10241 319 DAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
5-352 |
7.40e-157 |
|
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: 453.96 E-value: 7.40e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQ-NPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK--VDI 79
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFdKDGEVLVGEEAKNQALLDPeNTIYSVKRLMGRDTKdkEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 80 EGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTD 159
Cdd:cd24029 81 GGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNVLRLINEPTAAALAYGLDKEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 160 QDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKENGV-DLSQDKMALQRLKDAAEK 238
Cdd:cd24029 161 KDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETGIlDDKEDERARARLREAAEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 239 AKKDLSGVSQTQISLPFISAGEsgplHLEISLTRSKFEELADSLIRRTMEPTRQALKDAGLSTSEIDEVILVGGSTRIPA 318
Cdd:cd24029 241 AKIELSSSDSTDILILDDGKGG----ELEIEITREEFEELIAPLIERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPL 316
|
330 340 350
....*....|....*....|....*....|....
gi 920606352 319 VQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd24029 317 VREMLEEYFGREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
1-354 |
3.46e-152 |
|
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: 442.43 E-value: 3.46e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY--- 75
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYgEDGKITVGEKAKENAITDPeNTISSVKRLMGRSLadv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 -------------------KVDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd10236 81 keelpllpyrlvgdenelpRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 137 LEVERIINEPTAAALAYGLDKtDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYlvseFKK 216
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQ-KKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADW----ILK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLpfisagESGPLHLEISLTRSKFEELADSLIRRTMEPTRQALKD 296
Cdd:cd10236 236 QIGIDARLDPAVQQALLQAARRAKEALSDADSASIEV------EVEGKDWEREITREEFEELIQPLVKRTLEPCRRALKD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 920606352 297 AGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITG 354
Cdd:cd10236 310 AGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
5-352 |
5.70e-146 |
|
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: 427.05 E-value: 5.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKV--D 78
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPtNTVFDAKRLIGrkfDDPVVqsD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 79 I----------------------EGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd10233 82 MkhwpfkvvsggdkpkiqveykgETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 137 LEVERIINEPTAAALAYGLDKTDQDQK-VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFK 215
Cdd:cd10233 162 LNVLRIINEPTAAAIAYGLDKKGKGERnVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 216 KENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGesgpLHLEISLTRSKFEELADSLIRRTMEPTRQALK 295
Cdd:cd10233 242 RKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEG----IDFYTSITRARFEELCADLFRSTLEPVEKVLR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 920606352 296 DAGLSTSEIDEVILVGGSTRIPAVQEAVKKEI-GKDPHKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd10233 318 DAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
5-354 |
3.19e-140 |
|
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: 411.25 E-value: 3.19e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF-KNGETQVGEVAKRQAITNPN-TVQSIKRHMGTDYKVDIEGK 82
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDrTAASFKRFMGTDKQYRLGNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 83 SYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTDQDQ 162
Cdd:cd10235 81 TFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAALAYGLHKREDET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 163 KVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKENGVDLSQDKMALQRlkdAAEKAKKD 242
Cdd:cd10235 161 RFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDFTSLSPSELAALRK---RAEQAKRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 243 LSgvSQTQISLPFISAGESgplhLEISLTRSKFEELADSLIRRTMEPTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEA 322
Cdd:cd10235 238 LS--SQDSAEIRLTYRGEE----LEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPLVRQL 311
|
330 340 350
....*....|....*....|....*....|..
gi 920606352 323 VKKEIGKDPHKGVNPDEVVAMGAAIQGGVITG 354
Cdd:cd10235 312 IARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
4-566 |
2.51e-131 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 397.69 E-value: 2.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGevakrqaitNPNTVQSIKRHMGT---------- 73
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG---------NNKGLRSIKRLFGKtlkeilntpa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 74 ------DY--------KVDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:PRK01433 92 lfslvkDYldvnsselKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFEV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 140 ERIINEPTAAALAYGLDKtDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFkkeng 219
Cdd:PRK01433 172 LRLIAEPTAAAYAYGLNK-NQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNKF----- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 220 vDLSQDKMALQrlkdAAEKAKKDLSGVSQTQISlpfisagesgplhlEISLTRSKFEELADSLIRRTMEPTRQALKDAGl 299
Cdd:PRK01433 246 -DLPNSIDTLQ----LAKKAKETLTYKDSFNND--------------NISINKQTLEQLILPLVERTINIAQECLEQAG- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 300 sTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIMGGRMN 379
Cdd:PRK01433 306 -NPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGMELYGGIVE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 380 TLIERNTTIPTSKSQVYSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPPAPRGVPQIEVTFDIDKNGIVNVTAK 459
Cdd:PRK01433 385 KIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVSAY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 460 DLGTNKEQNITIQSSSALSDEEIDRMVKDAEENAEADKKRREEVDLRNEADSLVFQVEKTITDLGDNISDDDKSNAESKK 539
Cdd:PRK01433 465 EKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISIINSLL 544
|
570 580
....*....|....*....|....*..
gi 920606352 540 DALKSALEGQDIEDIKAKKEELEKVIQ 566
Cdd:PRK01433 545 DNIKEAVHARDIILINNSIKEFKSKIK 571
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
5-352 |
8.42e-129 |
|
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: 383.18 E-value: 8.42e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDePKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK------- 76
Cdd:cd24093 2 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPrNTVFDAKRLIGRRFDdesvqkd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 77 --------VDIEG------------KSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd24093 81 mktwpfkvIDVNGnpvievqylgetKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 137 LEVERIINEPTAAALAYGLD--KTDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEF 214
Cdd:cd24093 161 LNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 215 KKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESgplhLEISLTRSKFEELADSLIRRTMEPTRQAL 294
Cdd:cd24093 241 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED----FESSITRARFEDLNAALFKSTLEPVEQVL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 920606352 295 KDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEI-GKDPHKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd24093 317 KDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-354 |
2.85e-110 |
|
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: 337.00 E-value: 2.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 3 KVIGIDLGTTNSCVAVLE---GDEpKVIQNPEGARTTPSVVAFK-NGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY-- 75
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHavtGEV-EVIPDDDGHKSIPSVVAFTpDGGVLVGYDALAQAEHNPsNTIYDAKRFIGKTFtk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 -KVDIEGKSY-------------------------TPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATK 129
Cdd:cd10237 102 eELEEEAKRYpfkvvndnigsaffevplngstlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 130 DAGKIAGLEVERIINEPTAAALAYGLDKTDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDY 209
Cdd:cd10237 182 KAANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 210 LVSEFKKENGVDLSqDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESGPLHL-EISLTRSKFEELADSLIRRTME 288
Cdd:cd10237 262 LIDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKfKEEITRDLFETLNEDLFQRVLE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 920606352 289 PTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVITG 354
Cdd:cd10237 341 PIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
4-352 |
2.54e-98 |
|
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: 304.94 E-value: 2.54e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTD-------- 74
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNAsNTVVRVKQLLGRSfddpavqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 75 -----------------YKVDIEGKS--YTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd10238 82 lkkeskckiiekdgkpgYEIELEEKKklVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 136 GLEVERIINEPTAAALAYGLDKTDQDQK--VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSE 213
Cdd:cd10238 162 GFNVLRVISEPSAAALAYGIGQDDPTENsnVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLASE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 214 FKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLpfisagESgpLH----LEISLTRSKFEELADSLIRRTMEP 289
Cdd:cd10238 242 FKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSV------ES--LYdgmdFQCNVSRARFESLCSSLFQQCLEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 920606352 290 TRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEI-GKDPHKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd10238 314 IQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
5-348 |
2.78e-91 |
|
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: 286.76 E-value: 2.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKVDIE 80
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYkNTIRNFKRLIGlkfDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 81 GKS-------------------------YTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd11732 81 IKLlpfklveledgkvgievsyngeevvFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 136 GLEVERIINEPTAAALAYGLDKTDQD------QKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDY 209
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLeseekpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 210 LVSEFKKENGVDLSQDKMALQRLKDAAEKAKKDLsgvsqtqislpfiSAGESGPLHLE---------ISLTRSKFEELAD 280
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVL-------------SANGEAPLNVEclmedidfsGQIKREEFEELIQ 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 920606352 281 SLIRRTMEPTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQ 348
Cdd:cd11732 308 PLLARLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQ 375
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
1-349 |
1.04e-90 |
|
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: 285.74 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSkVIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG------- 72
Cdd:cd24095 1 MS-VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPkNTISQLKRLIGrkfddpe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 73 --TD-----YKVdIEG---------------KSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKD 130
Cdd:cd24095 80 vqRDlklfpFKV-TEGpdgeiginvnylgeqKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 131 AGKIAGLEVERIINEPTAAALAYGLDKTDQDQ----KVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVI 206
Cdd:cd24095 159 AAQIAGLNCLRLMNETTATALAYGIYKTDLPEtdptNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 207 IDYLVSEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISagESGPLHLEIslTRSKFEELADSLIRRT 286
Cdd:cd24095 239 FDHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLM--EDKDVKGMI--TREEFEELAAPLLERL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 920606352 287 MEPTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQG 349
Cdd:cd24095 315 LEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
4-349 |
3.05e-90 |
|
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: 283.23 E-value: 3.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLE-GDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGtdykvdieg 81
Cdd:cd10230 2 VLGIDLGSEFIKVALVKpGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPeNTFSYLKDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 82 ksYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKT--- 158
Cdd:cd10230 73 --YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAALNYGIDRRfen 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 159 DQDQKVLVFDLGGGTFDVSILE--------LGDGV----FEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKENG--VDLSQ 224
Cdd:cd10230 151 NEPQNVLFYDMGASSTSATVVEfssvkekdKGKNKtvpqVEVLGVGWDRTLGGLEFDLRLADHLADEFNEKHKkdKDVRT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 225 DKMALQRLKDAAEKAKKDLSGVSQTQISLpfisagESgpLHLEI----SLTRSKFEELADSLIRRTMEPTRQALKDAGLS 300
Cdd:cd10230 231 NPRAMAKLLKEANRVKEVLSANTEAPASI------ES--LYDDIdfrtKITREEFEELCADLFERVVAPIEEALEKAGLT 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 920606352 301 TSEIDEVILVGGSTRIPAVQEAVKKEIGKDP-HKGVNPDEVVAMGAAIQG 349
Cdd:cd10230 303 LDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
5-348 |
1.46e-86 |
|
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: 274.54 E-value: 1.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG----------- 72
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLkNTVSGFKRLLGrkfddpfvqke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 73 ---------------TDYKVDI--EGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd10228 81 lkhlpykvvklpngsVGIKVQYlgEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 136 GLEVERIINEPTAAALAYGLDKTD---QDQK---VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDY 209
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDlpaEEEKprnVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 210 LVSEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGvSQTQIslpfisagesgPLHLEI---------SLTRSKFEELAD 280
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSA-NATEL-----------PLNIECfmddkdvsgKMKRAEFEELCA 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 920606352 281 SLIRRTMEPTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQ 348
Cdd:cd10228 309 PLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-352 |
4.95e-84 |
|
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: 266.92 E-value: 4.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVL-EGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVqsikrhmgtDYKVDIEG 81
Cdd:cd10232 2 VIGISFGNSNSSIAIInKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPkNTV---------ANFRDLLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 82 KS-YTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDK--- 157
Cdd:cd10232 73 TTtLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDLRAets 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 158 --TDQDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKKENGVDLSQDKMALQRLKDA 235
Cdd:cd10232 153 gdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAKEFKKKTKTDPRKNARSLAKLRNA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 236 AEKAKKDLSGVSQTQISLPFISAGesgpLHLEISLTRSKFEELADSLIRRTMEPTRQALKDAGLSTSEIDEVILVGGSTR 315
Cdd:cd10232 233 AEITKRALSQGTSAPCSVESLADG----IDFHSSINRTRYELLASKVFQQFADLVTDAIEKAGLDPLDIDEVLLAGGASR 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 920606352 316 IPAVQEAVKKEIGKDPHK----GVNPDEVVAMGAAIQGGVI 352
Cdd:cd10232 309 TPKLASNFEYLFPESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
5-348 |
1.63e-80 |
|
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: 258.84 E-value: 1.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITN-PNTVQSIKRHMGTDYK------- 76
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNfKNTVGSLKRLIGRTFSdpevaee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 77 --------VDIEGK------------SYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd24094 81 ekyftaklVDANGEvgaevnylgekhVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 137 LEVERIINEPTAAALAYGLDKTD-----QDQKVLVF-DLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYL 210
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTDlpepeEKPRIVAFvDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 211 VSEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLpfisagESgpLHLEI----SLTRSKFEELADSLIRRT 286
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNV------ES--LMNDIdvssMLKREEFEELIAPLLERV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920606352 287 MEPTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQ 348
Cdd:cd24094 313 TAPLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFA 374
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
4-348 |
3.92e-71 |
|
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: 234.06 E-value: 3.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKVDI 79
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAkNTVQGFKRFHGrafSDPFVQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 80 -------------------------EGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11737 82 ekpslayelvqlptgttgikvmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 135 AGLEVERIINEPTAAALAYGLDKTD------QDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIID 208
Cdd:cd11737 162 AGLNCLRLMNETTAVALAYGIYKQDlpapeeKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 209 YLVSEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQtqiSLPFISAGESGPLHLEISLTRSKFEELADSLIRRTME 288
Cdd:cd11737 242 HFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANAS---DLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 289 PTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQ 348
Cdd:cd11737 319 PLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
4-348 |
5.00e-65 |
|
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: 218.19 E-value: 5.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY------- 75
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNAnNTVSNFKRFHGRAFndpfvqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 ---------------KVDI------EGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11739 82 ekenlsydlvplkngGVGVkvmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 135 AGLEVERIINEPTAAALAYGLDKTD-----QDQKVLVF-DLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIID 208
Cdd:cd11739 162 VGLNCLRLMNDMTAVALNYGIYKQDlpapdEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 209 YLVSEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSqtqISLPFISAGESGPLHLEISLTRSKFEELADSLIRRTME 288
Cdd:cd11739 242 HFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSNS---TDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 289 PTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQ 348
Cdd:cd11739 319 PLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
4-353 |
4.84e-64 |
|
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: 215.55 E-value: 4.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITN-PNTVQSIKRHMG---------- 72
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNaKNTIHGFKKFHGrafddpfvqa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 73 ----------------TDYKVDI--EGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11738 82 ekiklpyelqkmpngsTGVKVRYldEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 135 AGLEVERIINEPTAAALAYGLDKTD------QDQKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIID 208
Cdd:cd11738 162 AGLNCLRLMNETTAVALAYGIYKQDlpaleeKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 209 YLVSEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQtqiSLPFISAGESGPLHLEISLTRSKFEELADSLIRRTME 288
Cdd:cd11738 242 YFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANAS---DLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 920606352 289 PTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAIQGGVIT 353
Cdd:cd11738 319 PLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
5-347 |
9.59e-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: 202.33 E-value: 9.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVI---------QNPEGARTTPSVVafkngetqvgevakrqaitnpntvqsikrhmgtdy 75
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPlvvlqlpwpGGDGGSSKVPSVL----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 kvdiegksytpqEISAMVLQNLKNTAESYLGDKVD-------KAVITVPAYFNDAERQATKDAGKIAGLEVE----RIIN 144
Cdd:cd10170 46 ------------EVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALREAARAAGFGSDsdnvRLVS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 145 EPTAAALAYGLDKTDQ-----DQKVLVFDLGGGTFDVSILELGDG---VFEVLSTAGDNKLGGDDFDQVIIDYLVSEFKK 216
Cdd:cd10170 114 EPEAAALYALEDKGDLlplkpGDVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGALLGGTDIDEAFEKLLREKLGD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGESgPLHLEISLTRSKFEELADSLIRRTMEPTRQALKD 296
Cdd:cd10170 194 KGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGL-PELGLEKGTLLLTEEEIRDLFDPVIDKILELIEE 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 920606352 297 AGLSTS--EIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGV----NPDEVVAMGAAI 347
Cdd:cd10170 273 QLEAKSgtPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
5-346 |
5.23e-51 |
|
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: 181.32 E-value: 5.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAF------KNGETQVGEVAKRQAITNPNT---VQSIKRHMGTD- 74
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFprreeeGAESIYFGNDAIDAYLNDPEEgrlIKSVKSFLGSSl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 75 -YKVDIEGKSYTPQEISAMVLQNLKNTAESYLGDKVDKAVITVPAYF----NDAERQAT---KDAGKIAGLEVERIINEP 146
Cdd:cd10231 81 fDETTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFsgvgAEDDAQAEsrlRDAARRAGFRNVEFQYEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 147 TAAALAYGLDkTDQDQKVLVFDLGGGTFDVSILELG----DGVFEVLSTAGDnKLGGDDFDQVIIDYLVS-EF------- 214
Cdd:cd10231 161 IAAALDYEQR-LDREELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GIGGDDFDRELALKKVMpHLgrgstyv 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 215 ---------------------------------------------KKENGVDLSQDKMAlQRLKDAAEKAKKDLSGVSQT 249
Cdd:cd10231 239 sgdkglpvpawlyadlsnwhaisllytkktlrllldlrrdaadpeKIERLLSLVEDQLG-HRLFRAVEQAKIALSSADEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 250 QISLPFIsagesgPLHLEISLTRSKFEELADSLIRRTMEPTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGK 329
Cdd:cd10231 318 TLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQ 391
|
410
....*....|....*..
gi 920606352 330 DPHKGVNPDEVVAMGAA 346
Cdd:cd10231 392 ARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-354 |
1.65e-24 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 105.44 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNSCVA-VLEGDEPKVIQ--------NPEGARTTPSVVAFKNGETQV--GEVAKRQAITNPNTVQS-----I 67
Cdd:cd10229 2 VVAIDFGTTYSGYAySFITDPGDIHTmynwwgapTGVSSPKTPTCLLLNPDGEFHsfGYEAREKYSDLAEDEEHqwlyfF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 68 KRHMGTDYKVDIE---------GKSYTPQEISAMVLQNLKNTAESYLGDKVDKA--------VITVPAYFNDAERQATKD 130
Cdd:cd10229 82 KFKMMLLSEKELTrdtkvkavnGKSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTVPAIWSDAAKQFMRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 131 AGKIAGLEVE------RIINEPTAAALAYGLDKTDQ-------DQKVLVFDLGGGTFDVSILEL-GDGVFEVLSTAGDNK 196
Cdd:cd10229 162 AAVKAGLISEenseqlIIALEPEAAALYCQKLLAEGeekelkpGDKYLVVDCGGGTVDITVHEVlEDGKLEELLKASGGP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 197 LGGDDFDQVIIDYL--------VSEFKKENGVDlsqdkmaLQRLKDAAEKAKKDLSgvsqtqislpfisagesgplhleI 268
Cdd:cd10229 242 WGSTSVDEEFEELLeeifgddfMEAFKQKYPSD-------YLDLLQAFERKKRSFK-----------------------L 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 269 SLTRSKFEELADSLIRRTMEPTRQALKDAGLstSEIDEVILVGGSTRIPAVQEAVKKEIGKDpHKGVNPDEVVAmgAAIQ 348
Cdd:cd10229 292 RLSPELMKSLFDPVVKKIIEHIKELLEKPEL--KGVDYIFLVGGFAESPYLQKAVKEAFSTK-VKIIIPPEPGL--AVVK 366
|
....*.
gi 920606352 349 GGVITG 354
Cdd:cd10229 367 GAVLFG 372
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
5-331 |
2.94e-21 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 96.85 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGDEPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNPNTV--QSIKRHMGTDYKVDIEG- 81
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREAVSEWLYRHLDVPAYDDErqALLRRAIRYNREEDIDVt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 82 ---------------------------KSY------TPQEIS-------AMvLQNLKNTAESYLGDKVDKAVITVPAYFN 121
Cdd:PRK11678 83 aqsvffglaalaqyledpeevyfvkspKSFlgasglKPQQVAlfedlvcAM-MLHIKQQAEAQLQAAITQAVIGRPVNFQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 122 -----DAERQAT---KDAGKIAGLEVERIINEPTAAalayGLD---KTDQDQKVLVFDLGGGTFDVSILELG-------D 183
Cdd:PRK11678 162 glggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDfeaTLTEEKRVLVVDIGGGTTDCSMLLMGpswrgraD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 184 GVFEVLSTAGdNKLGGDDFDqviIDYLVSEF--------KKENGVDL----------------------SQDKMALQRL- 232
Cdd:PRK11678 238 RSASLLGHSG-QRIGGNDLD---IALAFKQLmpllgmgsETEKGIALpslpfwnavaindvpaqsdfysLANGRLLNDLi 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 233 KDA------------------------AEKAKKDLSGVSQTQISLPFISAGesgplhLEISLTRSKFEELADSLIRRTME 288
Cdd:PRK11678 314 RDArepekvarllkvwrqrlsyrlvrsAEEAKIALSDQAETRASLDFISDG------LATEISQQGLEEAISQPLARILE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 920606352 289 PTRQALKDAGLSTseiDEVILVGGSTRIPAVQEAVKKEIGKDP 331
Cdd:PRK11678 388 LVQLALDQAQVKP---DVIYLTGGSARSPLIRAALAQQLPGIP 427
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
5-347 |
6.98e-21 |
|
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: 93.69 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVlEGDEpkVIQNpEgarttPSVVAFKNGETQ---VGEVAKRQAITNPNTVQSIkRHM--G--TDYkv 77
Cdd:cd10225 2 IGIDLGTANTLVYV-KGKG--IVLN-E-----PSVVAVDKNTGKvlaVGEEAKKMLGRTPGNIVAI-RPLrdGviADF-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 78 diegksytpqEISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGL-EVeRIINEPTAAALAYGLD 156
Cdd:cd10225 70 ----------EATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAEHAGArEV-YLIEEPMAAAIGAGLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 157 kTDQDQKVLVFDLGGGTFDVSILELGdGVfeVLSTAgdNKLGGDDFDQVIIDYLvsefKKENGVDLSQdkmalqrlkDAA 236
Cdd:cd10225 139 -IEEPRGSMVVDIGGGTTEIAVISLG-GI--VTSRS--VRVAGDEMDEAIINYV----RRKYNLLIGE---------RTA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 237 EKAKKDLSGVSQTQISLPFISAG---ESGpLHLEISLTRSKFEELADSLIRRTMEPTRQALKDAGLSTSE--IDE-VILV 310
Cdd:cd10225 200 ERIKIEIGSAYPLDEELSMEVRGrdlVTG-LPRTIEITSEEVREALEEPVNAIVEAVRSTLERTPPELAAdiVDRgIVLT 278
|
330 340 350
....*....|....*....|....*....|....*..
gi 920606352 311 GGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAI 347
Cdd:cd10225 279 GGGALLRGLDELLREETGLPVHVADDPLTCVAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-347 |
1.16e-19 |
|
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: 90.52 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNSCVAVleGDEPKVIQnpEgarttPSVVAFKNGETQ---VGEVAKRqaitnpntvqsikrhMgtdykv 77
Cdd:COG1077 6 FSKDIGIDLGTANTLVYV--KGKGIVLN--E-----PSVVAIDKKTGKvlaVGEEAKE---------------M------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 78 diEGKsyTPQEISAM------VLQNLkNTAESYLGDKVDKA-----------VITVPAYFNDAERQATKDAGKIAGL-EV 139
Cdd:COG1077 56 --LGR--TPGNIVAIrplkdgVIADF-EVTEAMLKYFIKKVhgrrsffrprvVICVPSGITEVERRAVRDAAEQAGArEV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 140 eRIINEPTAAALAYGLDKTDqDQKVLVFDLGGGTFDVSILELGdGVfeVLSTAgdNKLGGDDFDQVIIDYLvsefKKENG 219
Cdd:COG1077 131 -YLIEEPMAAAIGAGLPIEE-PTGNMVVDIGGGTTEVAVISLG-GI--VVSRS--IRVAGDELDEAIIQYV----RKKYN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 220 VDLSqDKMalqrlkdaAEKAKKDLSGVSQTQISLPFISAG---ESG-PLHLEISltrskfeelaDSLIRRTMEPTRQALK 295
Cdd:COG1077 200 LLIG-ERT--------AEEIKIEIGSAYPLEEELTMEVRGrdlVTGlPKTITIT----------SEEIREALEEPLNAIV 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 920606352 296 DAGLSTSE----------IDE-VILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAI 347
Cdd:COG1077 261 EAIKSVLEktppelaadiVDRgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGTGK 323
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
2-347 |
1.26e-17 |
|
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: 84.14 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 2 SKVIGIDLGTTNSCVAVleGDEPKVIQNPegarttpSVVAFKNGETQ---VGEVAKRQAITNPNTVQSIkRHMGTDYKVD 78
Cdd:pfam06723 1 SKDIGIDLGTANTLVYV--KGKGIVLNEP-------SVVAINTKTKKvlaVGNEAKKMLGRTPGNIVAV-RPLKDGVIAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 79 IEgksytpqeISAMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDkT 158
Cdd:pfam06723 71 FE--------VTEAMLKYFIKKVHGRRSFSKPRVVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLP-V 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 159 DQDQKVLVFDLGGGTFDVSILELGDGVfevlsTAGDNKLGGDDFDQVIIDYLVSEFKKENGVdlsqdkmalqrlkDAAEK 238
Cdd:pfam06723 142 EEPTGNMVVDIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFDEAIIKYIRKKYNLLIGE-------------RTAER 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 239 AKKDLSGVSQTQISLPFISAG---ESGpLHLEISLTRSKFEELADSLIRRTMEPTRQALKD--AGLSTSEIDE-VILVGG 312
Cdd:pfam06723 204 IKIEIGSAYPTEEEEKMEIRGrdlVTG-LPKTIEISSEEVREALKEPVSAIVEAVKEVLEKtpPELAADIVDRgIVLTGG 282
|
330 340 350
....*....|....*....|....*....|....*
gi 920606352 313 STRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAI 347
Cdd:pfam06723 283 GALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-347 |
3.18e-17 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 83.26 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNSCVAVlEGDepKVIQNpEgarttPSVVAFKNGETQ---VGEVAKRQAITNPNTVQSIK--RHmGT-- 73
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYV-KGK--GIVLN-E-----PSVVAIDTKTGKvlaVGEEAKEMLGRTPGNIEAIRplKD-GVia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 74 DYKVdiegksytpqeISAMVLQNLKNTAESYLGDKVdKAVITVPAYFNDAERQATKDAGKIAGL-EVErIINEPTAAALA 152
Cdd:PRK13930 77 DFEA-----------TEAMLRYFIKKARGRRFFRKP-RIVICVPSGITEVERRAVREAAEHAGArEVY-LIEEPMAAAIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 153 YGLDKTDQDQKVLVfDLGGGTFDVSILELGDGVfevlsTAGDNKLGGDDFDQVIIDYLvsefKKENGVDLSQdkmalqrl 232
Cdd:PRK13930 144 AGLPVTEPVGNMVV-DIGGGTTEVAVISLGGIV-----YSESIRVAGDEMDEAIVQYV----RRKYNLLIGE-------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 233 kDAAEKAKKDLSGVSQtqislpfisagESGPLHLEIS----LT-RSKFEELADSLIRRTMEPTRQALKDAGLSTSE---- 303
Cdd:PRK13930 206 -RTAEEIKIEIGSAYP-----------LDEEESMEVRgrdlVTgLPKTIEISSEEVREALAEPLQQIVEAVKSVLEktpp 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 920606352 304 ------IDE-VILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMGAAI 347
Cdd:PRK13930 274 elaadiIDRgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGTGK 324
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
5-214 |
1.10e-16 |
|
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: 81.69 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVlEG-----DEPKVIQNPEG-ARTTPSVVAfkngetqVGEVAKRQAITNPNTVQSIkRHMGTDYKVD 78
Cdd:TIGR00904 5 IGIDLGTANTLVYV-KGrgivlNEPSVVAIRTDrDAKTKSILA-------VGHEAKEMLGKTPGNIVAI-RPMKDGVIAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 79 IEGksyTPQEISAMVLQNLKNtaESYLGDKVdkaVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLdKT 158
Cdd:TIGR00904 76 FEV---TEKMIKYFIKQVHSR--KSFFKPRI---VICVPSGITPVERRAVKESALSAGAREVYLIEEPMAAAIGAGL-PV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 920606352 159 DQDQKVLVFDLGGGTFDVSILELGdGVFEVLSTagdnKLGGDDFDQVIIDYLVSEF 214
Cdd:TIGR00904 147 EEPTGSMVVDIGGGTTEVAVISLG-GIVVSRSI----RVGGDEFDEAIINYIRRTY 197
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
1-214 |
1.37e-13 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 72.04 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNSCVAVleGDEPKVIQNPegarttpSVVAFKNGETQ---VGEVAKRqaitnpntvqsikrhMgtdykv 77
Cdd:PRK13927 4 FSNDLGIDLGTANTLVYV--KGKGIVLNEP-------SVVAIRTDTKKvlaVGEEAKQ---------------M------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 78 diEGKsyTPQEISAM------VLQNLKNTAE--SYLGDKVDKA-------VITVPAYFNDAERQATKDAGKIAGL-EVeR 141
Cdd:PRK13927 54 --LGR--TPGNIVAIrpmkdgVIADFDVTEKmlKYFIKKVHKNfrpsprvVICVPSGITEVERRAVRESALGAGArEV-Y 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 920606352 142 IINEPTAAALAYGLDKTDQdQKVLVFDLGGGTFDVSILELGdGVfeVLSTAgdNKLGGDDFDQVIIDYLVSEF 214
Cdd:PRK13927 129 LIEEPMAAAIGAGLPVTEP-TGSMVVDIGGGTTEVAVISLG-GI--VYSKS--VRVGGDKFDEAIINYVRRNY 195
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
1-215 |
2.64e-13 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 71.47 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 1 MSKVIGIDLGTTNscVAVLEGDEPKVIQNPegarttpSVVAFKNGETQ---VGEVAKRQaitnpntvqsIKRhmgtdykv 77
Cdd:PRK13928 2 FGRDIGIDLGTAN--VLVYVKGKGIVLNEP-------SVVAIDKNTNKvlaVGEEARRM----------VGR-------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 78 diegksyTPQEISAM------VLQNLKNTaESYLGDKVDKA-----------VITVPAYFNDAERQATKDAGKIAGLEVE 140
Cdd:PRK13928 55 -------TPGNIVAIrplrdgVIADYDVT-EKMLKYFINKAcgkrffskpriMICIPTGITSVEKRAVREAAEQAGAKKV 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 920606352 141 RIINEPTAAALAYGLDKTdQDQKVLVFDLGGGTFDVSILELGDGVfevlsTAGDNKLGGDDFDQVIIDYLVSEFK 215
Cdd:PRK13928 127 YLIEEPLAAAIGAGLDIS-QPSGNMVVDIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFDEAIIRYIRKKYK 195
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
5-344 |
1.37e-12 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 69.16 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAvleGDEPKVIQNpegartTPSVVAFkNGETQ----VGEVAKRQAITNPNTVQSIkRHMGTDYKVDIE 80
Cdd:PRK13929 7 IGIDLGTANILVY---SKNKGIILN------EPSVVAV-DTETKavlaIGTEAKNMIGKTPGKIVAV-RPMKDGVIADYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 81 gksytpqeISAMVLQNLKNTAESYLGDKVDK--AVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLdKT 158
Cdd:PRK13929 76 --------MTTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADL-PV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 159 DQDQKVLVFDLGGGTFDVSILELGdGVFEVLSTagdnKLGGDDFDQVIIDY-------LVSEFKKENgVDLSQDKMALQR 231
Cdd:PRK13929 147 DEPVANVVVDIGGGTTEVAIISFG-GVVSCHSI----RIGGDQLDEDIVSFvrkkynlLIGERTAEQ-VKMEIGYALIEH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 232 LKDAAEKAKKDL-SGVSQTqislpfisagesgplhleISLTRSKFEELADSLIRRTMEPTRQALKDA--GLSTSEIDE-V 307
Cdd:PRK13929 221 EPETMEVRGRDLvTGLPKT------------------ITLESKEIQGAMRESLLHILEAIRATLEDCppELSGDIVDRgV 282
|
330 340 350
....*....|....*....|....*....|....*..
gi 920606352 308 ILVGGSTRIPAVQEAVKKEIGKDPHKGVNPDEVVAMG 344
Cdd:PRK13929 283 ILTGGGALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
93-347 |
3.34e-09 |
|
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: 57.66 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 93 VLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTdqdqkvLVFDLGGG 172
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG------AVVDIGGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 173 TFDVSILELGdgvfEVLSTAgDNKLGGDDFDQVIIDYLvsefkkenGVDLSQdkmalqrlkdaAEKAKKDLSgvSQTQIs 252
Cdd:cd24047 122 TTGIAVLKDG----KVVYTA-DEPTGGTHLSLVLAGNY--------GISFEE-----------AEIIKRDPA--RHKEL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 253 LPFIsagesgplhleisltRSKFEELAdSLIRRtmeptrqalkdaGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPH 332
Cdd:cd24047 175 LPVV---------------RPVIEKMA-SIVKR------------HIKGYKVKDLYLVGGTCCLPGIEEVFEKETGLPVY 226
|
250
....*....|....*
gi 920606352 333 KGVNPDEVVAMGAAI 347
Cdd:cd24047 227 KPSNPLLVTPLGIAL 241
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
91-328 |
1.23e-08 |
|
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: 56.53 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 91 AMVLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKdagkiAGLEVERIINEPTAAALAYGLDKTdQDQKVLVFDLG 170
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPYDM-RDLNIALVDIG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 171 GGTFDVSILELGdgvfeVLSTAGDNKLGGDDFDQVIIDYLVSEFKKengvdlsqdkmalqrlkdaAEKAKKDLS-GVSQT 249
Cdd:cd24004 123 AGTTDIALIRNG-----GIEAYRMVPLGGDDFTKAIAEGFLISFEE-------------------AEKIKRTYGiFLLIE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 250 --QISLPFISAGESgplhleISLTRSKFEELADSLIRrtmeptrqALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEI 327
Cdd:cd24004 179 akDQLGFTINKKEV------YDIIKPVLEELASGIAN--------AIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKL 244
|
.
gi 920606352 328 G 328
Cdd:cd24004 245 G 245
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
4-328 |
5.63e-08 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 55.40 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 4 VIGIDLGTTNS-----------CVAVL---EGDEPKViqnpEGARTTPSVVAFKNGETQVGEVAKRQAI--TNPNTVQ-- 65
Cdd:cd11735 2 VVAIDFGTTSSgyaysftkepeCIHVMrrwEGGDPGV----SNQKTPTTILLTPERKFHSFGYAARDFYhdLDPNESKqw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 66 ------SIKRHMGTDYKVDIE-----GKSYTPQEISAMVLQNLKNTAESYLGDKVD--------KAVITVPAYFNDAERQ 126
Cdd:cd11735 78 lyfekfKMKLHTTGNLTMETDltaanGKKVKALEIFAYALQFFKEQALKELSDQAGsefdnsdvRWVITVPAIWKQPAKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 127 ATKDAGKIAGLEV----ERIIN--EPTAAALAYGLDKTDQDQKVLVFDLGGGTFDVSI--LELGDGVFEVLSTAGDNKLG 198
Cdd:cd11735 158 FMRQAAYKAGLASpenpEQLIIalEPEAASIYCRKLRLHQMDRYVVVDCGGGTVDLTVhqIRLPEGHLKELYKASGGPYG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 199 --GDDFD------QVIIDYLVSEFKKENGVDLSQDKMALQRLKDAAEKAKkdlsgVSQTQISLP--FISAGESGPLH-LE 267
Cdd:cd11735 238 slGVDYEfekllcKIFGEDFIDQFKIKRPAAWVDLMIAFESRKRAAAPDR-----TNPLNITLPfsFIDYYKKFRGHsVE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 920606352 268 ISLTRSKFE--------------ELADSLIRRTMEPTRQALKD--AGLSTSEIDEVILVGGSTRIPAVQEAVKKEIG 328
Cdd:cd11735 313 HALRKSNVDfvkwssqgmlrmspDAMNALFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAESPLLQQAVQNAFG 389
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
93-346 |
7.47e-08 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 54.07 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 93 VLQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTdqdqkvLVFDLGGG 172
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG------AVVDIGGG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 173 TFDVSILELGdgvfEVLSTAgDNKLGGDDFDQVIIDYLvsefkkenGVDLSQdkmalqrlkdaAEKAKKDLSGvsqtqis 252
Cdd:PRK15080 146 TTGISILKDG----KVVYSA-DEPTGGTHMSLVLAGAY--------GISFEE-----------AEQYKRDPKH------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 253 lpfisagesgplHLEI-SLTRSKFEELADSlirrtmepTRQALKDaglstSEIDEVILVGGSTRIPAVQEAVKKEIGKDP 331
Cdd:PRK15080 195 ------------HKEIfPVVKPVVEKMASI--------VARHIEG-----QDVEDIYLVGGTCCLPGFEEVFEKQTGLPV 249
|
250
....*....|....*
gi 920606352 332 HKGVNPDEVVAMGAA 346
Cdd:PRK15080 250 HKPQHPLFVTPLGIA 264
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
67-329 |
1.28e-05 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 47.65 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 67 IKRHMGTDYKVDIEGKSYTPQEISAMV-------------LQNLKNTAESYLGDKVDKAVITVPAYFNDAERQATKDAGK 133
Cdd:cd11736 85 MKIHSTSDLTMETELEAVNGKKVQALEvfahalrffkehaLQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 134 IAGL------EVERIINEPTAAALAygLDKTDqdqKVLVFDLGGGTFDVSI--LELGDGVFEVLSTAGDNKLGGddfdqv 205
Cdd:cd11736 165 LAGLvspenpEQLLIALEPEAASIY--CRKLD---RYIVADCGGGTVDLTVhqIEQPQGTLKELYKASGGPYGA------ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 206 iidylvsefkkeNGVDLSQDKMALQRLKD---AAEKAKKDLSGVSQTqisLPFISAGESGPLHLEISLTRSKFEELADSL 282
Cdd:cd11736 234 ------------VGVDLAFEKLLCQIFGEdfiATFKAKRPAAWVDLT---IAFEARKRTAALRMSSEAMNELFQPTISQI 298
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 920606352 283 IRRTmeptrqalkDAGLSTSEIDEV---ILVGGSTRIPAVQEAVKKEIGK 329
Cdd:cd11736 299 IQHI---------DDLMKKPEVKGIkflFLVGGFAESPMLQRAVQAAFGN 339
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
142-327 |
1.58e-05 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins; Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp9 forms a stable heterodimer with Arp7 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.
Pssm-ID: 466814 Cd Length: 356 Bit Score: 47.30 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 142 IINEPTAAALAYGLdktdqdQKVLVFDLGGGTFDVS-ILElgdgvFEVLSTAG-DNKLGGDDFDQviidYLVSEFKKENG 219
Cdd:cd10208 104 ILEAPLAALYAAGA------TSGIVVDIGHEKTDITpIVD-----SQVVPHALvSIPIGGQDCTA----HLAQLLKSDEP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 220 VDLSQDKMALQRLKDAAEKAKKdlSGVSQtqislpFISAG---ESGPlHLEISLTRSKFEE--LADSLIRRTMEPTRQAL 294
Cdd:cd10208 169 ELKSQAESGEEATLDLAEALKK--SPICE------VLSDGadlASGT-EITVGKERFRACEplFKPSSLRVDLLIAAIAG 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 920606352 295 KDAGLSTSEIDE-------VILVGGSTRIPAVQEAVKKEI 327
Cdd:cd10208 240 ALVLNASDEPDKrpalwenIIIVGGGSRIRGLKEALLSEL 279
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
5-347 |
1.00e-04 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 44.96 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLE--GDEPKV-----IQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNPNTVQSIKrhmGTDYKV 77
Cdd:cd24049 1 LGIDIGSSSIKAVELKrsGGGLVLvafaiIPLPEGAIVDGEIADPEALAEALKKLLKENKIKGKKVVVALP---GSDVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 78 -DIEGKSYTPQEISAMVlqnlKNTAESYLGDKVDKAVI---TVPAYFNDAERQ-----ATK--------DAGKIAGLEVE 140
Cdd:cd24049 78 rTIKLPKMPEKELEEAI----RFEAEQYLPFPLEEVVLdyqILGEVEEGGEKLevlvvAAPkeivesylELLKEAGLKPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 141 RIINEPTAAALAYGLDKTDQDQK-VLVFDLGGGTFDVSILElgDGVFEVLSTAgdnKLGGDDFDQVIIDYLvsefkkenG 219
Cdd:cd24049 154 AIDVESFALARALEYLLPDEEEEtVALLDIGASSTTLVIVK--NGKLLFTRSI---PVGGNDITEAIAKAL--------G 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 220 VDLsqdkmalqrlkDAAEKAKKDLSgvsqtqislpFISAGESGPLHLEISLTRSKFEELADSlIRRTMEPTRQALKDagl 299
Cdd:cd24049 221 LSF-----------EEAEELKREYG----------LLLEGEEGELKKVAEALRPVLERLVSE-IRRSLDYYRSQNGG--- 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 920606352 300 stSEIDEVILVGGSTRIPAVQEAVKKEIGK-----DPHKGVNPDEV-------------VAMGAAI 347
Cdd:cd24049 276 --EPIDKIYLTGGGSLLPGLDEYLSERLGIpveilNPFSNIESKKSddeelkedaplfaVAIGLAL 339
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
135-335 |
2.51e-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: 43.67 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 135 AGLEVERIINEPTAAALAYgLDKTDQDQKVLVFDLGGGTFDVSILElgDGVF---EVLStagdnkLGGDDFDQviidylv 211
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEKELGVALIDIGGGTTDIAVFK--NGSLrytAVIP------VGGNHITN------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 212 sefkkengvDLSqdkMALQRLKDAAEKAKKDLSGVSQTQIS--LPFISAGESGPLHLEISLtrskfeeladSLIRRTMEP 289
Cdd:cd24048 236 ---------DIA---IGLNTPFEEAERLKIKYGSALSEEADedEIIEIPGVGGREPREVSR----------RELAEIIEA 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 920606352 290 --------TRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGV 335
Cdd:cd24048 294 rveeilelVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGR 347
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
135-340 |
9.64e-04 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 42.04 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 135 AGLEVERIINEPTAAALAYgLDKTDQDQKVLVFDLGGGTFDVSILElgDGVF---EVLSTAGDNklggddfdqviidylV 211
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTEDEKELGVALVDIGGGTTDIAVFK--DGALrhtAVIPVGGDH---------------I 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 212 SEfkkengvDLSqdkMALQRLKDAAEKAKKDLSGVSQTQIS----LPFISAGESGPlhleISLTRSkfeELADSL---IR 284
Cdd:COG0849 236 TN-------DIA---IGLRTPLEEAERLKIKYGSALASLADedetIEVPGIGGRPP----REISRK---ELAEIIearVE 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 920606352 285 RTMEPTRQALKDAGLSTSEIDEVILVGGSTRIPAVQEAVKKEIGKDPHKGVnPDEV 340
Cdd:COG0849 299 EIFELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGR-PDGI 353
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
234-359 |
2.17e-03 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 40.97 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 234 DAAEKAKKDLSGVsqtqISLPFISaGESGPLH----------LEISLTRskfeelADsLIRRTME----PTRQ---ALKD 296
Cdd:COG1070 324 ALAAEVPPGADGL----LFLPYLS-GERTPHWdpnargaffgLTLSHTR------AH-LARAVLEgvafALRDgleALEE 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 920606352 297 AGLstsEIDEVILVGGSTRIPAVQEAV----KKEIGKdphkgVNPDEVVAMGAAIQGGVITGDVKDV 359
Cdd:COG1070 392 AGV---KIDRIRATGGGARSPLWRQILadvlGRPVEV-----PEAEEGGALGAALLAAVGLGLYDDL 450
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
5-226 |
5.10e-03 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 39.04 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 5 IGIDLGTTNSCVAVLEGD---------EPKVIQNPEGARTTPSVVAFKNGETQVGEVAKRQAITNpntvqsikRHMGTDY 75
Cdd:cd10227 1 IGIDIGNGNTKVVTGGGKefkfpsavaEARESSLDDGLLEDDIIVEYNGKRYLVGELALREGGGG--------RSTGDDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 76 KvdieGKSYTPQEISAMVLQNLKNTaesylgDKVDKAVITVPA--YFNDAERQATKDAGKIAGLEVE-----------RI 142
Cdd:cd10227 73 K----KSEDALLLLLAALALLGDDE------EVDVNLVVGLPIseYKEEKKELKKKLLKGLHEFTFNgkerritindvKV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920606352 143 INEPTAAALAYGLDKT-DQDQKVLVFDLGGGTFDVSILELGDGVFEvlstAGDNKLGGDDFDQVIIDYLVSEFKKENGVD 221
Cdd:cd10227 143 LPEGAGAYLDYLLDDDeLEDGNVLVIDIGGGTTDILTFENGKPIEE----SSDTLPGGEEALEKYADDILNELLKKLGDE 218
|
....*
gi 920606352 222 LSQDK 226
Cdd:cd10227 219 LDSAD 223
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
111-173 |
8.00e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.06 E-value: 8.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 920606352 111 KAVITVPAYFNDAERQAT-----------KDAGKIAGLEVERIINEPTAAALAYGLDKTDQDqkVLVFDLGGGT 173
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPEG--LLVVDLGGGT 86
|
|
| |
