|
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: 1182.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGT----- 73
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFtKDGERLVGQPAKRQAVTNPeNTIFSIKRLMGRrdeev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 74 -----------------DYKVDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PRK00290 81 qkdiklvpykivkadngDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLDKtDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKK 216
Cdd:PRK00290 161 LEVLRIINEPTAAALAYGLDK-KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKD 296
Cdd:PRK00290 240 ENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 297 AGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEILGG 376
Cdd:PRK00290 320 AGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 377 RMNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNV 456
Cdd:PRK00290 400 VMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 457 TAKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKSAE 536
Cdd:PRK00290 480 SAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIE 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612675601 537 EKKDALKTALEGQDIEDIKSKKEELEKVIQELSAKVYEqaaqQQQQAQGANAGQNNDSTVEDAEFKEVKDDD 608
Cdd:PRK00290 560 AAIKELKEALKGEDKEAIKAKTEELTQASQKLGEAMYQ----QAQAAQGAAGAAAKDDDVVDAEFEEVKDDK 627
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-574 |
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: 1019.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 3 KIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGT------- 73
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFtKNGERLVGQPAKRQAVTNPeNTIYSIKRFMGRrfdevte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 74 --------------DYKVDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:TIGR02350 81 eakrvpykvvgdggDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 140 ERIINEPTAAALAYGLDKTDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKENG 219
Cdd:TIGR02350 161 LRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKKEEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 220 VDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDAGL 299
Cdd:TIGR02350 241 IDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKDAGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 300 TNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEILGGRMN 379
Cdd:TIGR02350 321 SASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGVMT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 380 TLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNVTAK 459
Cdd:TIGR02350 401 KLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 460 DLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKSAEEKK 539
Cdd:TIGR02350 481 DKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKAV 560
|
570 580 590
....*....|....*....|....*....|....*
gi 612675601 540 DALKTALEGQDIEDIKSKKEELEKVIQELSAKVYE 574
Cdd:TIGR02350 561 AELKEALKGEDVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
4-574 |
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: 882.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY------- 75
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPkNTVFSVKRLIGRKFsdpvvqr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 -------------------KVDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:pfam00012 81 dikhlpykvvklpngdagvEVRYLGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLDKTDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKK 216
Cdd:pfam00012 161 LNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGvSQTQISLPFISAGENGpLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKD 296
Cdd:pfam00012 241 KYGIDLSKDKRALQRLREAAEKAKIELSS-NQTNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVEKALKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 297 AGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITG--DVKDVVLLDVTPLSLGIEIL 374
Cdd:pfam00012 319 AGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIETL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 375 GGRMNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIV 454
Cdd:pfam00012 399 GGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGIL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 455 NVTAKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKS 534
Cdd:pfam00012 479 TVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSK 558
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 612675601 535 AEEKKDALKTALEGQDIEDIKSKKEELEKVIQELSAKVYE 574
Cdd:pfam00012 559 VESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-603 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 835.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMG------ 72
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYtKKGDLLVGQIAKRQAVINPeNTFYSVKRFIGrkfsei 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 73 ------TDYKV--DIEG----------KSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:CHL00094 81 seeakqVSYKVktDSNGnikiecpalnKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 135 AGLEVERIINEPTAAALAYGLDKTDkDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEF 214
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDKKN-NETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 215 KKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAM 294
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 295 KDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIL 374
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 375 GGRMNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIV 454
Cdd:CHL00094 400 GGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 455 NVTAKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKS 534
Cdd:CHL00094 480 SVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612675601 535 AEEKKDALKTALEGQDIEDIKSKKEELEKVIQELSAKVYEqaaqqqqqAQGANAGQNNDSTVEDAEFKE 603
Cdd:CHL00094 560 IENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYS--------STSTTDPASNDDDVIDTDFSE 620
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-574 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 833.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMG------ 72
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFgKSGDRLVGQLAKRQAVTNAeNTVYSIKRFIGrrwddt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 73 ------TDYK----------VDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PRK13411 81 eeersrVPYTcvkgrddtvnVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLDKTDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKK 216
Cdd:PRK13411 161 LEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKD 296
Cdd:PRK13411 241 QEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 297 AGLTNSDIDEVILVGGSTRIPAVQEAVKKEI-GKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEILG 375
Cdd:PRK13411 321 AGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 376 GRMNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVN 455
Cdd:PRK13411 401 EVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 456 VTAKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKSA 535
Cdd:PRK13411 481 VSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRA 560
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 612675601 536 EEKKDALKTALEGQDI--EDIKSKKEELEKVIQELSAKVYE 574
Cdd:PRK13411 561 EQKVEQLEAALTDPNIslEELKQQLEEFQQALLAIGAEVYQ 601
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-572 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 803.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY--- 75
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFtKDGELLVGQLARRQLVLNPqNTFYNLKRFIGRRYdel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 -----------KVDIEG----------KSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:PRK13410 81 dpeskrvpytiRRNEQGnvrikcprleREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 135 AGLEVERIINEPTAAALAYGLDKTDkDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEF 214
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 215 KKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAM 294
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 295 KDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEIL 374
Cdd:PRK13410 320 KDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 375 GGRMNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIV 454
Cdd:PRK13410 400 GGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 455 NVTAKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTD----LGENIGEE 530
Cdd:PRK13410 480 QVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDaaleFGPYFAER 559
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 612675601 531 DKKSAEEKKDALKTALEGQDIEDIKSKKEELEKVIQELSAKV 572
Cdd:PRK13410 560 QRRAVESAMRDVQDSLEQDDDRELDLAVADLQEALYGLNREV 601
|
|
| 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: 782.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK---VD 78
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFpKDGEVLVGEAAKRQAVTNPgRTIRSIKRLLGRSLFdeaTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 79 IEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKT 158
Cdd:COG0443 81 VGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 159 DKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKENGVDLSQDKMALQRLKDAAEK 238
Cdd:COG0443 161 KEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEEGIDLRLDPAALQRLREAAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 239 AKKDLSGVSQTQISLPFisageNGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDAGLTNSDIDEVILVGGSTRIPA 318
Cdd:COG0443 241 AKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 319 VQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDvvlLDVTPLSLGIEILGGRMNTLIERNTTIPTSKSQIYST 398
Cdd:COG0443 316 VRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIETLGGVFTKLIPRNTTIPTAKSQVFST 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 399 AVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNVTAKDLGTNKEQRITIqssssls 478
Cdd:COG0443 393 AADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITI------- 465
|
....*...
gi 612675601 479 DEEIDRMV 486
Cdd:COG0443 466 KEEIERML 473
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
4-574 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 754.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK----- 76
Cdd:PTZ00400 43 IVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFtEDGQRLVGIVAKRQAVTNPeNTVFATKRLIGRRYDedatk 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 77 -------------------VDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:PTZ00400 123 keqkilpykivrasngdawIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 138 EVERIINEPTAAALAYGLDKTDkDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKE 217
Cdd:PTZ00400 203 DVLRIINEPTAAALAFGMDKND-GKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEFKKQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 218 NGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDA 297
Cdd:PTZ00400 282 QGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCEKCIKDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 298 GLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEILGGR 377
Cdd:PTZ00400 362 GVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGIETLGGV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 378 MNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNVT 457
Cdd:PTZ00400 442 FTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMNIS 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 458 AKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKSAEE 537
Cdd:PTZ00400 522 AVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDELKQ 601
|
570 580 590
....*....|....*....|....*....|....*..
gi 612675601 538 KKDALKTALEGQDIEDIKSKKEELEKVIQELSAKVYE 574
Cdd:PTZ00400 602 KITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYK 638
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-573 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 727.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 3 KIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMG-------- 72
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYtKNGDRLVGQIAKRQAVVNPeNTFFSVKRFIGrkmsevde 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 73 ----TDYKVDIE------------GKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PLN03184 120 eskqVSYRVVRDengnvkldcpaiGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLDKTdKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKK 216
Cdd:PLN03184 200 LEVLRIINEPTAASLAYGFEKK-SNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKD 296
Cdd:PLN03184 279 DEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVENALRD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 297 AGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEILGG 376
Cdd:PLN03184 359 AKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLGLETLGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 377 RMNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNV 456
Cdd:PLN03184 439 VMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSV 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 457 TAKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKSAE 536
Cdd:PLN03184 519 SATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVE 598
|
570 580 590
....*....|....*....|....*....|....*..
gi 612675601 537 EKKDALKTALEGQDIEDIKSKKEELEKVIQELSAKVY 573
Cdd:PLN03184 599 AKLKELKDAIASGSTQKMKDAMAALNQEVMQIGQSLY 635
|
|
| 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: 693.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK----- 76
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFtKDGERLVGQPAKRQAVTNPeNTIFSIKRFMGRRYKeveve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 77 -----------------VDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:cd10234 81 rkqvpypvvsagngdawVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 140 ERIINEPTAAALAYGLDKtDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKENG 219
Cdd:cd10234 161 LRIINEPTAAALAYGLDK-KKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 220 VDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDAGL 299
Cdd:cd10234 240 IDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAKL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 612675601 300 TNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVIT 353
Cdd:cd10234 320 SPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
4-574 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 653.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---------- 72
Cdd:PTZ00186 29 VIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPqSTFYAVKRLIGrrfedehiqk 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 73 ----TDYKV-----------DIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:PTZ00186 109 diknVPYKIvragngdawvqDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 138 EVERIINEPTAAALAYGLDKTdKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKE 217
Cdd:PTZ00186 189 NVIRVVNEPTAAALAYGMDKT-KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEFRKT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 218 NGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDA 297
Cdd:PTZ00186 268 SGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPCKQCMKDA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 298 GLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEILGGR 377
Cdd:PTZ00186 348 GVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLGIETLGGV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 378 MNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNVT 457
Cdd:PTZ00186 428 FTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHVT 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 458 AKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLgENIGEEDKKSAEE 537
Cdd:PTZ00186 508 AKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEW-KYVSDAEKENVKT 586
|
570 580 590
....*....|....*....|....*....|....*....
gi 612675601 538 KKDALKTALEGQDI--EDIKSKKEELEKVIQELSAKVYE 574
Cdd:PTZ00186 587 LVAELRKAMENPNVakDDLAAATDKLQKAVMECGRTEYQ 625
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-574 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 588.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY-------- 75
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPeNTVFDAKRLIGRKFddsvvqsd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 ------------------KVDIEG--KSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:PTZ00009 87 mkhwpfkvttggddkpmiEVTYQGekKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 136 GLEVERIINEPTAAALAYGLDKTDKDEK-VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEF 214
Cdd:PTZ00009 167 GLNVLRIINEPTAAAIAYGLDKKGDGEKnVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQDF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 215 KKEN-GVDLSQDKMALQRLKDAAEKAKKDLSgvSQTQISLPFISAGENgpLHLEVNLTRSKFEELSDSLIRRTMEPTRQA 293
Cdd:PTZ00009 247 KRKNrGKDLSSNQRALRRLRTQCERAKRTLS--SSTQATIEIDSLFEG--IDYNVTISRARFEELCGDYFRNTLQPVEKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 294 MKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEI-GKEPNKGVNPDEVVAMGAAIQGGVITGD----VKDVVLLDVTPLS 368
Cdd:PTZ00009 323 LKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLDVTPLS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 369 LGIEILGGRMNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDI 448
Cdd:PTZ00009 403 LGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 449 DKNGIVNVTAKDLGTNKEQRITIQSSSS-LSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTD--LGE 525
Cdd:PTZ00009 483 DANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDekVKG 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 612675601 526 NIGEEDKKSAEEK-KDALKTALEGQ--DIEDIKSKKEELEKVIQELSAKVYE 574
Cdd:PTZ00009 563 KLSDSDKATIEKAiDEALEWLEKNQlaEKEEFEHKQKEVESVCNPIMTKMYQ 614
|
|
| 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: 558.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 2 SKIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK--- 76
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFtADGERLVGMPAKRQAVTNPeNTLYATKRLIGRRFDdpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 77 ---------------------VDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd11733 81 vqkdikmvpykivkasngdawVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 136 GLEVERIINEPTAAALAYGLDKTDkDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFK 215
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKKD-DKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 216 KENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMK 295
Cdd:cd11733 240 KEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 612675601 296 DAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd11733 320 DAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-571 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 551.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKVDIE 80
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPkNTISSVKRFMGrslADIQQRYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 81 GKSY-------------------TPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVER 141
Cdd:PRK05183 102 HLPYqfvasengmplirtaqglkSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNVLR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 142 IINEPTAAALAYGLDKtdKDEKV-LVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLvaefKKENGV 220
Cdd:PRK05183 182 LLNEPTAAAIAYGLDS--GQEGViAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWI----LEQAGL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 221 DLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLpFISAGEngplhlevnLTRSKFEELSDSLIRRTMEPTRQAMKDAGLT 300
Cdd:PRK05183 256 SPRLDPEDQRLLLDAARAAKEALSDADSVEVSV-ALWQGE---------ITREQFNALIAPLVKRTLLACRRALRDAGVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 301 NSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDV--KDVVLLDVTPLSLGIEILGGRM 378
Cdd:PRK05183 326 ADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKpdSDMLLLDVIPLSLGLETMGGLV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 379 NTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNVTA 458
Cdd:PRK05183 406 EKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVTA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 459 KDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKSAEEK 538
Cdd:PRK05183 486 MEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERAAIDAA 565
|
570 580 590
....*....|....*....|....*....|...
gi 612675601 539 KDALKTALEGQDIEDIKSKKEELEKVIQELSAK 571
Cdd:PRK05183 566 MAALREVAQGDDADAIEAAIKALDKATQEFAAR 598
|
|
| 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: 546.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCV-TVLEGdEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYKvDIE 80
Cdd:TIGR01991 1 AVGIDLGTTNSLVaSVRSG-VPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPkNTISSVKRLMGRSIE-DIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 81 GKSY----------------------TPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLE 138
Cdd:TIGR01991 79 TFSIlpyrfvdgpgemvrlrtvqgtvTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 139 VERIINEPTAAALAYGLDKTdKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVaefkKEN 218
Cdd:TIGR01991 159 VLRLLNEPTAAAVAYGLDKA-SEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL----KQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 219 GVDLSQDKMALQRLKDAAEKAKKDLSGvsQTQISLPFISAGENgplhLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDAG 298
Cdd:TIGR01991 234 GISADLNPEDQRLLLQAARAAKEALTD--AESVEVDFTLDGKD----FKGKLTRDEFEALIQPLVQKTLSICRRALRDAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 299 LTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDV--KDVVLLDVTPLSLGIEILGG 376
Cdd:TIGR01991 308 LSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRigNDLLLLDVTPLSLGIETMGG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 377 RMNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNV 456
Cdd:TIGR01991 388 LVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 457 TAKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKSAE 536
Cdd:TIGR01991 468 SAQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAID 547
|
570 580 590
....*....|....*....|....*....|....*
gi 612675601 537 EKKDALKTALEGQDIEDIKSKKEELEKVIQELSAK 571
Cdd:TIGR01991 548 AAMEALQKALQGDDADAIKAAIEALEEATDNFAAR 582
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
4-354 |
2.72e-171 |
|
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: 491.58 E-value: 2.72e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKR------------ 69
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFtKDGERLVGVPAKRQAVVNPeNTLFATKRligrkfddaevq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 70 ------------HMGTDYKVDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:cd11734 83 rdikevpykivkHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 138 EVERIINEPTAAALAYGLDKTDkDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKE 217
Cdd:cd11734 163 NVLRVINEPTAAALAYGLDKSG-DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFKKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 218 NGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDA 297
Cdd:cd11734 242 SGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALKDA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 612675601 298 GLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITG 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 |
1.45e-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: 489.72 E-value: 1.45e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKVDI 79
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPeNTIFDVKRLIGrkfDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 80 -------------------------EGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd24028 81 dikhwpfkvvededgkpkievtykgEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 135 AGLEVERIINEPTAAALAYGLDKTDKDEK-VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAE 213
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERnVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 214 FKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENgplhLEVNLTRSKFEELSDSLIRRTMEPTRQA 293
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGID----FETTITRAKFEELCEDLFKKCLEPVEKV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 294 MKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEI-GKEPNKGVNPDEVVAMGAAIQGGVI 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 |
2.00e-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: 479.40 E-value: 2.00e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY------- 75
Cdd:cd10241 3 VIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPeNTVFDVKRLIGRKFddkevqk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 ------------------KVDIEG--KSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd10241 83 dikllpfkivnkngkpyiQVEVKGekKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 136 GLEVERIINEPTAAALAYGLDKTDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFK 215
Cdd:cd10241 163 GLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLFK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 216 KENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENgplhLEVNLTRSKFEELSDSLIRRTMEPTRQAMK 295
Cdd:cd10241 243 KKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGED----FSETLTRAKFEELNMDLFRKTLKPVQKVLE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 612675601 296 DAGLTNSDIDEVILVGGSTRIPAVQEAVKKEI-GKEPNKGVNPDEVVAMGAAIQGGVI 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 |
2.98e-156 |
|
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: 452.42 E-value: 2.98e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQ-NPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK--VDI 79
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFdKDGEVLVGEEAKNQALLDPeNTIYSVKRLMGRDTKdkEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 80 EGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTD 159
Cdd:cd24029 81 GGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNVLRLINEPTAAALAYGLDKEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 160 KDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKENGV-DLSQDKMALQRLKDAAEK 238
Cdd:cd24029 161 KDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETGIlDDKEDERARARLREAAEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 239 AKKDLSGVSQTQISLPFISAGEngplHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDAGLTNSDIDEVILVGGSTRIPA 318
Cdd:cd24029 241 AKIELSSSDSTDILILDDGKGG----ELEIEITREEFEELIAPLIERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPL 316
|
330 340 350
....*....|....*....|....*....|....
gi 612675601 319 VQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVI 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 |
6.23e-151 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.
Pssm-ID: 466834 [Multi-domain] Cd Length: 367 Bit Score: 439.34 E-value: 6.23e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY--- 75
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYgEDGKITVGEKAKENAITDPeNTISSVKRLMGRSLadv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 -------------------KVDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd10236 81 keelpllpyrlvgdenelpRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLDKtDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYlvaeFKK 216
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQ-KKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADW----ILK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFisagenGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKD 296
Cdd:cd10236 236 QIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV------EGKDWEREITREEFEELIQPLVKRTLEPCRRALKD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 612675601 297 AGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITG 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 |
4.69e-148 |
|
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: 432.44 E-value: 4.69e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKV--D 78
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPtNTVFDAKRLIGrkfDDPVVqsD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 79 I----------------------EGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd10233 82 MkhwpfkvvsggdkpkiqveykgETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLDKTDKDEK-VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFK 215
Cdd:cd10233 162 LNVLRIINEPTAAAIAYGLDKKGKGERnVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 216 KENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGengpLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMK 295
Cdd:cd10233 242 RKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEG----IDFYTSITRARFEELCADLFRSTLEPVEKVLR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 612675601 296 DAGLTNSDIDEVILVGGSTRIPAVQEAVKKEI-GKEPNKGVNPDEVVAMGAAIQGGVI 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 |
5.42e-139 |
|
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: 407.79 E-value: 5.42e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF-KNGETQVGEVAKRQAITNPN-TVQSIKRHMGTDYKVDIEGK 82
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDrTAASFKRFMGTDKQYRLGNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 83 SYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTDKDE 162
Cdd:cd10235 81 TFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAALAYGLHKREDET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 163 KVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKENGVDLSQDKMALQRlkdAAEKAKKD 242
Cdd:cd10235 161 RFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDFTSLSPSELAALRK---RAEQAKRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 243 LSgvSQTQISLPFISAGENgplhLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEA 322
Cdd:cd10235 238 LS--SQDSAEIRLTYRGEE----LEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPLVRQL 311
|
330 340 350
....*....|....*....|....*....|..
gi 612675601 323 VKKEIGKEPNKGVNPDEVVAMGAAIQGGVITG 354
Cdd:cd10235 312 IARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
5-352 |
1.30e-128 |
|
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: 382.79 E-value: 1.30e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDePKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDYK------- 76
Cdd:cd24093 2 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPrNTVFDAKRLIGRRFDdesvqkd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 77 --------VDIEG------------KSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd24093 81 mktwpfkvIDVNGnpvievqylgetKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLD--KTDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEF 214
Cdd:cd24093 161 LNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 215 KKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENgplhLEVNLTRSKFEELSDSLIRRTMEPTRQAM 294
Cdd:cd24093 241 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED----FESSITRARFEDLNAALFKSTLEPVEQVL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 612675601 295 KDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEI-GKEPNKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd24093 317 KDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
5-567 |
2.84e-122 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 374.19 E-value: 2.84e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGevakrqaitNPNTVQSIKRHMGT----------- 73
Cdd:PRK01433 22 VGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG---------NNKGLRSIKRLFGKtlkeilntpal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 74 -----DY--------KVDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVE 140
Cdd:PRK01433 93 fslvkDYldvnsselKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFEVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 141 RIINEPTAAALAYGLDKTDKDeKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFkkengv 220
Cdd:PRK01433 173 RLIAEPTAAAYAYGLNKNQKG-CYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNKF------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 221 DLSQDKMALQrlkdAAEKAKKDLS---GVSQTQISLpfisagengplhlevnlTRSKFEELSDSLIRRTMEPTRQAMKDA 297
Cdd:PRK01433 246 DLPNSIDTLQ----LAKKAKETLTykdSFNNDNISI-----------------NKQTLEQLILPLVERTINIAQECLEQA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 298 GltNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIEILGGR 377
Cdd:PRK01433 305 G--NPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGMELYGGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 378 MNTLIERNTTIPTSKSQIYSTAVDNQPSVDVHVLQGERPMAADNKTLGRFQLTDIPPAERGKPQIEVTFDIDKNGIVNVT 457
Cdd:PRK01433 383 VEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 458 AKDLGTNKEQRITIQSSSSLSDEEIDRMVKDAEVNAEADKKRREEVDLRNEADSLVFQVEKTLTDLGENIGEEDKKSAEE 537
Cdd:PRK01433 463 AYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISIINS 542
|
570 580 590
....*....|....*....|....*....|
gi 612675601 538 KKDALKTALEGQDIEDIKSKKEELEKVIQE 567
Cdd:PRK01433 543 LLDNIKEAVHARDIILINNSIKEFKSKIKK 572
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-354 |
5.00e-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: 336.23 E-value: 5.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 3 KIIGIDLGTTNSCVTVLE---GDEpKVIQNPEGSRTTPSVVAFK-NGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY-- 75
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHavtGEV-EVIPDDDGHKSIPSVVAFTpDGGVLVGYDALAQAEHNPsNTIYDAKRFIGKTFtk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 -KVDIEGKSY-------------------------TPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATK 129
Cdd:cd10237 102 eELEEEAKRYpfkvvndnigsaffevplngstlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 130 DAGKIAGLEVERIINEPTAAALAYGLDKTDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDY 209
Cdd:cd10237 182 KAANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 210 LVAEFKKENGVDLSqDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENGPLHL-EVNLTRSKFEELSDSLIRRTME 288
Cdd:cd10237 262 LIDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKfKEEITRDLFETLNEDLFQRVLE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612675601 289 PTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVITG 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; ... |
5-352 |
2.13e-100 |
|
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: 310.33 E-value: 2.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTD--------- 74
Cdd:cd10238 3 FGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNAsNTVVRVKQLLGRSfddpavqel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 75 ----------------YKVDIEGKS--YTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd10238 83 kkeskckiiekdgkpgYEIELEEKKklVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLDKTDKDEK--VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEF 214
Cdd:cd10238 163 FNVLRVISEPSAAALAYGIGQDDPTENsnVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLASEF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 215 KKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPfiSAGENgpLHLEVNLTRSKFEELSDSLIRRTMEPTRQAM 294
Cdd:cd10238 243 KRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVE--SLYDG--MDFQCNVSRARFESLCSSLFQQCLEPIQEVL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 612675601 295 KDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEI-GKEPNKGVNPDEVVAMGAAIQGGVI 352
Cdd:cd10238 319 NSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 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 |
2.49e-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: 2.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKVDIE 80
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYkNTIRNFKRLIGlkfDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 81 GKS-------------------------YTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd11732 81 IKLlpfklveledgkvgievsyngeevvFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 136 GLEVERIINEPTAAALAYGLDK------TDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDY 209
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKsdllesEEKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 210 LVAEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENgplhLEVNLTRSKFEELSDSLIRRTMEP 289
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDID----FSGQIKREEFEELIQPLLARLEAP 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 612675601 290 TRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQ 348
Cdd:cd11732 317 IKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQ 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 |
5.15e-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: 283.82 E-value: 5.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSkIIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG------- 72
Cdd:cd24095 1 MS-VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPkNTISQLKRLIGrkfddpe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 73 --TD-----YKVdIEG---------------KSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKD 130
Cdd:cd24095 80 vqRDlklfpFKV-TEGpdgeiginvnylgeqKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 131 AGKIAGLEVERIINEPTAAALAYGLDKTDKDE----KVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVI 206
Cdd:cd24095 159 AAQIAGLNCLRLMNETTATALAYGIYKTDLPEtdptNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 207 IDYLVAEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISagENGPLHLEVnlTRSKFEELSDSLIRRT 286
Cdd:cd24095 239 FDHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLM--EDKDVKGMI--TREEFEELAAPLLERL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612675601 287 MEPTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQG 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 |
6.28e-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: 282.08 E-value: 6.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLE-GDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGtdykvdieg 81
Cdd:cd10230 2 VLGIDLGSEFIKVALVKpGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPeNTFSYLKDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 82 ksYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKT--- 158
Cdd:cd10230 73 --YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAALNYGIDRRfen 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 159 DKDEKVLVFDLGGGTFDVSILE--------LGDGV----FEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKENG--VDLSQ 224
Cdd:cd10230 151 NEPQNVLFYDMGASSTSATVVEfssvkekdKGKNKtvpqVEVLGVGWDRTLGGLEFDLRLADHLADEFNEKHKkdKDVRT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 225 DKMALQRLKDAAEKAKKDLSGVSQTQISLpfisagENgpLHLEVNL----TRSKFEELSDSLIRRTMEPTRQAMKDAGLT 300
Cdd:cd10230 231 NPRAMAKLLKEANRVKEVLSANTEAPASI------ES--LYDDIDFrtkiTREEFEELCADLFERVVAPIEEALEKAGLT 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 612675601 301 NSDIDEVILVGGSTRIPAVQEAVKKEIGKEP-NKGVNPDEVVAMGAAIQG 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 |
7.03e-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: 272.61 E-value: 7.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG----------- 72
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLkNTVSGFKRLLGrkfddpfvqke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 73 ---------------TDYKVDI--EGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd10228 81 lkhlpykvvklpngsVGIKVQYlgEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 136 GLEVERIINEPTAAALAYGLDKTD---KDEK---VLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDY 209
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDlpaEEEKprnVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 210 LVAEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGvSQTQIslpfisagengPLHLEV---------NLTRSKFEELSD 280
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSA-NATEL-----------PLNIECfmddkdvsgKMKRAEFEELCA 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612675601 281 SLIRRTMEPTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQ 348
Cdd:cd10228 309 PLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-352 |
2.34e-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: 267.69 E-value: 2.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVL-EGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVqsikrhmgtDYKVDIEG 81
Cdd:cd10232 2 VIGISFGNSNSSIAIInKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPkNTV---------ANFRDLLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 82 KS-YTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDK--- 157
Cdd:cd10232 73 TTtLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDLRAets 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 158 --TDKDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKKENGVDLSQDKMALQRLKDA 235
Cdd:cd10232 153 gdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAKEFKKKTKTDPRKNARSLAKLRNA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 236 AEKAKKDLSGVSQTQISLPFISAGENgpLHLEVNLTRskFEELSDSLIRRTMEPTRQAMKDAGLTNSDIDEVILVGGSTR 315
Cdd:cd10232 233 AEITKRALSQGTSAPCSVESLADGID--FHSSINRTR--YELLASKVFQQFADLVTDAIEKAGLDPLDIDEVLLAGGASR 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 612675601 316 IPAVQEAVKKEIGKEPNK----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 |
3.00e-79 |
|
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: 255.38 E-value: 3.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITN-PNTVQSIKRHMGTDYK------- 76
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNfKNTVGSLKRLIGRTFSdpevaee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 77 --------VDIEGK------------SYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd24094 81 ekyftaklVDANGEvgaevnylgekhVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 137 LEVERIINEPTAAALAYGLDKTD------KDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIIDYL 210
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTDlpepeeKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 211 VAEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLpfisagENGPLHLEVN--LTRSKFEELSDSLIRRTME 288
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNV------ESLMNDIDVSsmLKREEFEELIAPLLERVTA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 289 PTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQ 348
Cdd:cd24094 315 PLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFA 374
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
4-348 |
3.63e-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: 234.45 E-value: 3.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMG---TDYKVDI 79
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAkNTVQGFKRFHGrafSDPFVQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 80 -------------------------EGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11737 82 ekpslayelvqlptgttgikvmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 135 AGLEVERIINEPTAAALAYGLDKTD------KDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIID 208
Cdd:cd11737 162 AGLNCLRLMNETTAVALAYGIYKQDlpapeeKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 209 YLVAEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQtqiSLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTME 288
Cdd:cd11737 242 HFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANAS---DLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 289 PTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQ 348
Cdd:cd11737 319 PLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
4-353 |
5.34e-65 |
|
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: 218.25 E-value: 5.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITN-PNTVQSIKRHMG---------- 72
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNaKNTIHGFKKFHGrafddpfvqa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 73 ----------------TDYKVDI--EGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11738 82 ekiklpyelqkmpngsTGVKVRYldEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 135 AGLEVERIINEPTAAALAYGLDKTD------KDEKVLVFDLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIID 208
Cdd:cd11738 162 AGLNCLRLMNETTAVALAYGIYKQDlpaleeKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 209 YLVAEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQtqiSLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTME 288
Cdd:cd11738 242 YFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANAS---DLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612675601 289 PTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQGGVIT 353
Cdd:cd11738 319 PLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
4-348 |
6.43e-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: 217.81 E-value: 6.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNP-NTVQSIKRHMGTDY------- 75
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNAnNTVSNFKRFHGRAFndpfvqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 ---------------KVDI------EGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11739 82 ekenlsydlvplkngGVGVkvmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 135 AGLEVERIINEPTAAALAYGLDKTD---KDEK--VLVF-DLGGGTFDVSILELGDGVFEVLSTAGDNKLGGDDFDQVIID 208
Cdd:cd11739 162 VGLNCLRLMNDMTAVALNYGIYKQDlpaPDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 209 YLVAEFKKENGVDLSQDKMALQRLKDAAEKAKKDLSGVSqtqISLPFISAGENGPLHLEVNLTRSKFEELSDSLIRRTME 288
Cdd:cd11739 242 HFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSNS---TDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 289 PTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAIQ 348
Cdd:cd11739 319 PLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
5-347 |
8.31e-59 |
|
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: 200.02 E-value: 8.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVI---------QNPEGSRTTPSVVafkngetqvgevakrqaitnpntvqsikrhmgtdy 75
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPlvvlqlpwpGGDGGSSKVPSVL----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 kvdiegksytpqEISAMILQNLKNTAESYLGEKVD-------KAVITVPAYFNDAERQATKDAGKIAGLEVE----RIIN 144
Cdd:cd10170 46 ------------EVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALREAARAAGFGSDsdnvRLVS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 145 EPTAAALAYGLDKTD-----KDEKVLVFDLGGGTFDVSILELGDG---VFEVLSTAGDNKLGGDDFDQVIIDYLVAEFKK 216
Cdd:cd10170 114 EPEAAALYALEDKGDllplkPGDVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGALLGGTDIDEAFEKLLREKLGD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 217 ENGVDLSQDKMALQRLKDAAEKAKKDLSGVSQTQISLPFISAGENgPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKD 296
Cdd:cd10170 194 KGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGL-PELGLEKGTLLLTEEEIRDLFDPVIDKILELIEE 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 612675601 297 AGLT--NSDIDEVILVGGSTRIPAVQEAVKKEIGKEPNKGV----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 |
1.71e-52 |
|
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: 185.17 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAF------KNGETQVGEVAKRQAITNPNT---VQSIKRHMGTD- 74
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFprreeeGAESIYFGNDAIDAYLNDPEEgrlIKSVKSFLGSSl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 75 -YKVDIEGKSYTPQEISAMILQNLKNTAESYLGEKVDKAVITVPAYF----NDAERQAT---KDAGKIAGLEVERIINEP 146
Cdd:cd10231 81 fDETTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFsgvgAEDDAQAEsrlRDAARRAGFRNVEFQYEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 147 TAAALAYGLDkTDKDEKVLVFDLGGGTFDVSILELG----DGVFEVLSTAGDnKLGGDDFDQVIIDYLVA-EF------- 214
Cdd:cd10231 161 IAAALDYEQR-LDREELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GIGGDDFDRELALKKVMpHLgrgstyv 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 215 ---------------------------------------------KKENGVDLSQDKMAlQRLKDAAEKAKKDLSGVSQT 249
Cdd:cd10231 239 sgdkglpvpawlyadlsnwhaisllytkktlrllldlrrdaadpeKIERLLSLVEDQLG-HRLFRAVEQAKIALSSADEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 250 QISLPFIsagengPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGK 329
Cdd:cd10231 318 TLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQ 391
|
410
....*....|....*..
gi 612675601 330 EPNKGVNPDEVVAMGAA 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 |
7.63e-23 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 100.82 E-value: 7.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNSCVT-VLEGDEPKVIQ--------NPEGSRTTPSVVAFKNGETQV--GEVAKRQAITNPNTVQS-----I 67
Cdd:cd10229 2 VVAIDFGTTYSGYAySFITDPGDIHTmynwwgapTGVSSPKTPTCLLLNPDGEFHsfGYEAREKYSDLAEDEEHqwlyfF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 68 KRHMGTDYKVDIE---------GKSYTPQEISAMILQNLKNTAESYLGEKVDKA--------VITVPAYFNDAERQATKD 130
Cdd:cd10229 82 KFKMMLLSEKELTrdtkvkavnGKSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTVPAIWSDAAKQFMRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 131 AGKIAGLEVE------RIINEPTAAALAYG-------LDKTDKDEKVLVFDLGGGTFDVSILEL-GDGVFEVLSTAGDNK 196
Cdd:cd10229 162 AAVKAGLISEenseqlIIALEPEAAALYCQkllaegeEKELKPGDKYLVVDCGGGTVDITVHEVlEDGKLEELLKASGGP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 197 LGGDDFDQVIIDYLVAEFKKENGVDL-SQDKMALQRLKDAAEKAKKDLSgvsqtqislpfisagengpLHLEVNLTRSKF 275
Cdd:cd10229 242 WGSTSVDEEFEELLEEIFGDDFMEAFkQKYPSDYLDLLQAFERKKRSFK-------------------LRLSPELMKSLF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 276 EELSDSLIrrtmeptrQAMKD--AGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEpNKGVNPDEVVAmgAAIQGGVIT 353
Cdd:cd10229 303 DPVVKKII--------EHIKEllEKPELKGVDYIFLVGGFAESPYLQKAVKEAFSTK-VKIIIPPEPGL--AVVKGAVLF 371
|
.
gi 612675601 354 G 354
Cdd:cd10229 372 G 372
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
5-331 |
5.56e-22 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 99.17 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGDEPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNPNTV--QSIKRHMGTDYKVDIEG- 81
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREAVSEWLYRHLDVPAYDDErqALLRRAIRYNREEDIDVt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 82 ---------------------------KSY------TPQEIS-------AMILqNLKNTAESYLGEKVDKAVITVPAYFN 121
Cdd:PRK11678 83 aqsvffglaalaqyledpeevyfvkspKSFlgasglKPQQVAlfedlvcAMML-HIKQQAEAQLQAAITQAVIGRPVNFQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 122 -----DAERQAT---KDAGKIAGLEVERIINEPTAAalayGLD---KTDKDEKVLVFDLGGGTFDVSILELG-------D 183
Cdd:PRK11678 162 glggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDfeaTLTEEKRVLVVDIGGGTTDCSMLLMGpswrgraD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 184 GVFEVLSTAGdNKLGGDDFDqviIDYLVAEF--------KKENGVDL----------------------SQDKMALQRL- 232
Cdd:PRK11678 238 RSASLLGHSG-QRIGGNDLD---IALAFKQLmpllgmgsETEKGIALpslpfwnavaindvpaqsdfysLANGRLLNDLi 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 233 KDA------------------------AEKAKKDLSGVSQTQISLPFISAGengplhLEVNLTRSKFEELSDSLIRRTME 288
Cdd:PRK11678 314 RDArepekvarllkvwrqrlsyrlvrsAEEAKIALSDQAETRASLDFISDG------LATEISQQGLEEAISQPLARILE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 612675601 289 PTRQAMKDAGLTNsdiDEVILVGGSTRIPAVQEAVKKEIGKEP 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 |
3.93e-20 |
|
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: 91.38 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVlEGDEpkVIQNpEgsrttPSVVAFKNGETQ---VGEVAKRQAITNPNTVQSIkRHM--G--TDYkv 77
Cdd:cd10225 2 IGIDLGTANTLVYV-KGKG--IVLN-E-----PSVVAVDKNTGKvlaVGEEAKKMLGRTPGNIVAI-RPLrdGviADF-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 78 diegksytpqEISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGL-EVeRIINEPTAAALAYGLD 156
Cdd:cd10225 70 ----------EATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAEHAGArEV-YLIEEPMAAAIGAGLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 157 KTDKdEKVLVFDLGGGTFDVSILELGdGVfeVLSTAgdNKLGGDDFDQVIIDYLvaefKKENGVDLSQdkmalqrlkDAA 236
Cdd:cd10225 139 IEEP-RGSMVVDIGGGTTEIAVISLG-GI--VTSRS--VRVAGDEMDEAIINYV----RRKYNLLIGE---------RTA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 237 EKAKKDLSGVSQTQISLPFISAGENgplhLEVNLTRSkfEELSDSLIRRTMEPTRQAMKDAgLTN----------SDIDE 306
Cdd:cd10225 200 ERIKIEIGSAYPLDEELSMEVRGRD----LVTGLPRT--IEITSEEVREALEEPVNAIVEA-VRStlertppelaADIVD 272
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 612675601 307 --VILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAI 347
Cdd:cd10225 273 rgIVLTGGGALLRGLDELLREETGLPVHVADDPLTCVAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-347 |
3.46e-18 |
|
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: 86.28 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNSCVTVleGDEPKVIQnpEgsrttPSVVAFKNGETQ---VGEVAKRqaitnpntvqsikrhMgtdykv 77
Cdd:COG1077 6 FSKDIGIDLGTANTLVYV--KGKGIVLN--E-----PSVVAIDKKTGKvlaVGEEAKE---------------M------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 78 diEGKsyTPQEISAMilQNLKN-------TAESYLGEKVDKA-----------VITVPAYFNDAERQATKDAGKIAGL-E 138
Cdd:COG1077 56 --LGR--TPGNIVAI--RPLKDgviadfeVTEAMLKYFIKKVhgrrsffrprvVICVPSGITEVERRAVRDAAEQAGArE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 139 VeRIINEPTAAALAYGLDKTDkDEKVLVFDLGGGTFDVSILELGdGVfeVLSTAgdNKLGGDDFDQVIIDYLvaefKKEN 218
Cdd:COG1077 130 V-YLIEEPMAAAIGAGLPIEE-PTGNMVVDIGGGTTEVAVISLG-GI--VVSRS--IRVAGDELDEAIIQYV----RKKY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 219 GVDLSqDKMalqrlkdaAEKAKKDLSGVSQTQISLPFISAGengpLHLEVNLTRSKfeELSDSLIRRTMEPTRQAMKDAg 298
Cdd:COG1077 199 NLLIG-ERT--------AEEIKIEIGSAYPLEEELTMEVRG----RDLVTGLPKTI--TITSEEIREALEEPLNAIVEA- 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612675601 299 LTN----------SDIDE--VILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAI 347
Cdd:COG1077 263 IKSvlektppelaADIVDrgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGTGK 323
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-347 |
7.29e-18 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 85.18 E-value: 7.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNSCVTVlEGDepKVIQNpEgsrttPSVVAFKNGETQ---VGEVAKRQAITNPNTVQSIK--RHmGT-- 73
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYV-KGK--GIVLN-E-----PSVVAIDTKTGKvlaVGEEAKEMLGRTPGNIEAIRplKD-GVia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 74 DYKVdiegksytpqeISAMILQNLKNTAESYLGEKVdKAVITVPAYFNDAERQATKDAGKIAGL-EVErIINEPTAAALA 152
Cdd:PRK13930 77 DFEA-----------TEAMLRYFIKKARGRRFFRKP-RIVICVPSGITEVERRAVREAAEHAGArEVY-LIEEPMAAAIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 153 YGLDKTdkdEKV--LVFDLGGGTFDVSILELGDGVfevlsTAGDNKLGGDDFDQVIIDYLvaefKKENGVDLSQdkmalq 230
Cdd:PRK13930 144 AGLPVT---EPVgnMVVDIGGGTTEVAVISLGGIV-----YSESIRVAGDEMDEAIVQYV----RRKYNLLIGE------ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 231 rlkDAAEKAKKDLSGVSQtqislpfisagENGPLHLEV---NLTRS--KFEELSDSLIRRTMEPTRQAMKDA---GLTN- 301
Cdd:PRK13930 206 ---RTAEEIKIEIGSAYP-----------LDEEESMEVrgrDLVTGlpKTIEISSEEVREALAEPLQQIVEAvksVLEKt 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 612675601 302 -----SDIDE--VILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAI 347
Cdd:PRK13930 272 ppelaADIIDrgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGTGK 324
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
5-210 |
1.26e-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: 81.30 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVlEG-----DEPKVIQNPEG-SRTTPSVVAfkngetqVGEVAKRQAITNPNTVQSIkRHMGTDYKVD 78
Cdd:TIGR00904 5 IGIDLGTANTLVYV-KGrgivlNEPSVVAIRTDrDAKTKSILA-------VGHEAKEMLGKTPGNIVAI-RPMKDGVIAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 79 IEGksyTPQEISAMILQNLKNtaESYLGEKVdkaVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKT 158
Cdd:TIGR00904 76 FEV---TEKMIKYFIKQVHSR--KSFFKPRI---VICVPSGITPVERRAVKESALSAGAREVYLIEEPMAAAIGAGLPVE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 612675601 159 DKDEKvLVFDLGGGTFDVSILELGdGVFEVLSTagdnKLGGDDFDQVIIDYL 210
Cdd:TIGR00904 148 EPTGS-MVVDIGGGTTEVAVISLG-GIVVSRSI----RVGGDEFDEAIINYI 193
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
2-347 |
1.27e-16 |
|
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: 81.45 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 2 SKIIGIDLGTTNSCVTVleGDEPKVIQNPegsrttpSVVAFKNGETQ---VGEVAKRQAITNPNTVQSIkRHMGTDYKVD 78
Cdd:pfam06723 1 SKDIGIDLGTANTLVYV--KGKGIVLNEP-------SVVAINTKTKKvlaVGNEAKKMLGRTPGNIVAV-RPLKDGVIAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 79 IEgksytpqeISAMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDkT 158
Cdd:pfam06723 71 FE--------VTEAMLKYFIKKVHGRRSFSKPRVVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLP-V 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 159 DKDEKVLVFDLGGGTFDVSILELGDGVfevlsTAGDNKLGGDDFDQVIIDYLVAEFKKENGVdlsqdkmalqrlkDAAEK 238
Cdd:pfam06723 142 EEPTGNMVVDIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFDEAIIKYIRKKYNLLIGE-------------RTAER 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 239 AKKDLSGVSQTQISLPFISAGENgplhLEVNLTRSKfeELSDSLIRRTMEPTRQAMKDAGLT---------NSDIDE--V 307
Cdd:pfam06723 204 IKIEIGSAYPTEEEEKMEIRGRD----LVTGLPKTI--EISSEEVREALKEPVSAIVEAVKEvlektppelAADIVDrgI 277
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 612675601 308 ILVGGSTRIPAVQEAVKKEIGKEPNKGVNPDEVVAMGAAI 347
Cdd:pfam06723 278 VLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
1-210 |
7.31e-13 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 70.12 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNSCVTVleGDEPKVIQNPegsrttpSVVAFKNGETQ---VGEVAKRQAITNPNTVQSIkRHM--G--T 73
Cdd:PRK13927 4 FSNDLGIDLGTANTLVYV--KGKGIVLNEP-------SVVAIRTDTKKvlaVGEEAKQMLGRTPGNIVAI-RPMkdGviA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 74 DYKVdiegksyTPQEISAMILQNLKNTAESylgekvDKAVITVPAYFNDAERQATKDAGKIAGL-EVeRIINEPTAAALA 152
Cdd:PRK13927 74 DFDV-------TEKMLKYFIKKVHKNFRPS------PRVVICVPSGITEVERRAVRESALGAGArEV-YLIEEPMAAAIG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612675601 153 YGLDKTDKdEKVLVFDLGGGTFDVSILELGdGVfeVLSTAgdNKLGGDDFDQVIIDYL 210
Cdd:PRK13927 140 AGLPVTEP-TGSMVVDIGGGTTEVAVISLG-GI--VYSKS--VRVGGDKFDEAIINYV 191
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
1-215 |
7.56e-13 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 69.93 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 1 MSKIIGIDLGTTNscVTVLEGDEPKVIQNPegsrttpSVVAFKNGETQ---VGEVAKRQaitnpntvqsIKRhmgtdykv 77
Cdd:PRK13928 2 FGRDIGIDLGTAN--VLVYVKGKGIVLNEP-------SVVAIDKNTNKvlaVGEEARRM----------VGR-------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 78 diegksyTPQEISAMilQNLKN-------TAESYLGEKVDKA-----------VITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:PRK13928 55 -------TPGNIVAI--RPLRDgviadydVTEKMLKYFINKAcgkrffskpriMICIPTGITSVEKRAVREAAEQAGAKK 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612675601 140 ERIINEPTAAALAYGLDKTdKDEKVLVFDLGGGTFDVSILELGDGVfevlsTAGDNKLGGDDFDQVIIDYLVAEFK 215
Cdd:PRK13928 126 VYLIEEPLAAAIGAGLDIS-QPSGNMVVDIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFDEAIIRYIRKKYK 195
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
5-344 |
1.37e-10 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 63.00 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTvleGDEPKVIQNpegsrtTPSVVAFkNGETQ----VGEVAKRQAITNPNTVQSIkRHMGTDYKVDIE 80
Cdd:PRK13929 7 IGIDLGTANILVY---SKNKGIILN------EPSVVAV-DTETKavlaIGTEAKNMIGKTPGKIVAV-RPMKDGVIADYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 81 gksytpqeISAMILQNLKNTAESYLGEKVDK--AVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLdKT 158
Cdd:PRK13929 76 --------MTTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADL-PV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 159 DKDEKVLVFDLGGGTFDVSILELGdGVFEVLSTagdnKLGGDDFDQVIIDYLVAEFKKENGvdlsqdkmalqrlKDAAEK 238
Cdd:PRK13929 147 DEPVANVVVDIGGGTTEVAIISFG-GVVSCHSI----RIGGDQLDEDIVSFVRKKYNLLIG-------------ERTAEQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 239 AKKDLSGVSQTQISLPFISAGENGPLHLEVNLTRSKFE---ELSDSLIrRTMEPTRQAMKDA--GLTNSDIDE-VILVGG 312
Cdd:PRK13929 209 VKMEIGYALIEHEPETMEVRGRDLVTGLPKTITLESKEiqgAMRESLL-HILEAIRATLEDCppELSGDIVDRgVILTGG 287
|
330 340 350
....*....|....*....|....*....|..
gi 612675601 313 STRIPAVQEAVKKEIGKEPNKGVNPDEVVAMG 344
Cdd:PRK13929 288 GALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
91-369 |
6.98e-09 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 57.30 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 91 AMILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKdagkiAGLEVERIINEPTAAALAYGLDKTdKDEKVLVFDLG 170
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPYDM-RDLNIALVDIG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 171 GGTFDVSILELGdgvfeVLSTAGDNKLGGDDFDQVIIDYLVAEFKKengvdlsqdkmalqrlkdaAEKAKKDLS-GVSQT 249
Cdd:cd24004 123 AGTTDIALIRNG-----GIEAYRMVPLGGDDFTKAIAEGFLISFEE-------------------AEKIKRTYGiFLLIE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 250 --QISLPFISAGENgplhleVNLTRSKFEELSDSLIRRTMEPTRQAMKdagltnsdIDEVILVGGSTRIPAVQEAVKKEI 327
Cdd:cd24004 179 akDQLGFTINKKEV------YDIIKPVLEELASGIANAIEEYNGKFKL--------PDAVYLVGGGSKLPGLNEALAEKL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 612675601 328 GKEPNKgVNPDEVVAMgaaiqGGVITGDVKDVVLLDVTPLSL 369
Cdd:cd24004 245 GLPVER-IAPRNIGAI-----SDITDETSKAKGPEFVTPLGI 280
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
93-347 |
1.45e-08 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 55.74 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 93 ILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTdkdekvLVFDLGGG 172
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG------AVVDIGGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 173 TFDVSILELGdgvfEVLSTAgDNKLGGDDFDQVIIDYLvaefkkenGVDLSQdkmalqrlkdaAEKAKKDLSgvSQTQIs 252
Cdd:cd24047 122 TTGIAVLKDG----KVVYTA-DEPTGGTHLSLVLAGNY--------GISFEE-----------AEIIKRDPA--RHKEL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 253 LPFIsagengplhlevnltRSKFEELSdSLIRRtmeptrqamkdaGLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPN 332
Cdd:cd24047 175 LPVV---------------RPVIEKMA-SIVKR------------HIKGYKVKDLYLVGGTCCLPGIEEVFEKETGLPVY 226
|
250
....*....|....*
gi 612675601 333 KGVNPDEVVAMGAAI 347
Cdd:cd24047 227 KPSNPLLVTPLGIAL 241
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
93-346 |
1.14e-07 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 53.30 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 93 ILQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTdkdekvLVFDLGGG 172
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG------AVVDIGGG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 173 TFDVSILELGdgvfEVLSTAgDNKLGGDDFDQVIIDYLvaefkkenGVDLSQdkmalqrlkdaAEKAKKDlsgvsqtqis 252
Cdd:PRK15080 146 TTGISILKDG----KVVYSA-DEPTGGTHMSLVLAGAY--------GISFEE-----------AEQYKRD---------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 253 lpfisaGENGPLHLEVnlTRSKFEELSdSLIRRTmeptrqamkdagLTNSDIDEVILVGGSTRIPAVQEAVKKEIGKEPN 332
Cdd:PRK15080 192 ------PKHHKEIFPV--VKPVVEKMA-SIVARH------------IEGQDVEDIYLVGGTCCLPGFEEVFEKQTGLPVH 250
|
250
....*....|....
gi 612675601 333 KGVNPDEVVAMGAA 346
Cdd:PRK15080 251 KPQHPLFVTPLGIA 264
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
4-330 |
6.10e-06 |
|
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: 48.85 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 4 IIGIDLGTTNS-----------CVTVL---EGDEPKViqnpEGSRTTPSVVAFKNGETQVGEVAKRQAI--TNPNTVQ-- 65
Cdd:cd11735 2 VVAIDFGTTSSgyaysftkepeCIHVMrrwEGGDPGV----SNQKTPTTILLTPERKFHSFGYAARDFYhdLDPNESKqw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 66 ------SIKRHMGTDYKVDIE-----GKSYTPQEISAMILQNLKNTAESYL----GEKVDKA----VITVPAYFNDAERQ 126
Cdd:cd11735 78 lyfekfKMKLHTTGNLTMETDltaanGKKVKALEIFAYALQFFKEQALKELsdqaGSEFDNSdvrwVITVPAIWKQPAKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 127 ATKDAGKIAGLEV----ERIIN--EPTAAALAYGLDKTDKDEKVLVFDLGGGTFDVSI--LELGDGVFEVLSTAGDNKLG 198
Cdd:cd11735 158 FMRQAAYKAGLASpenpEQLIIalEPEAASIYCRKLRLHQMDRYVVVDCGGGTVDLTVhqIRLPEGHLKELYKASGGPYG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 199 --GDDFD------QVIIDYLVAEFKKENGVDLSQDKMALQRLKDAAEKAKkdlsgVSQTQISLP---------------- 254
Cdd:cd11735 238 slGVDYEfekllcKIFGEDFIDQFKIKRPAAWVDLMIAFESRKRAAAPDR-----TNPLNITLPfsfidyykkfrghsve 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 255 ---------FISAGENGPLHLEVNLTRSKFEELSDSLIRRTMEPTRQAmkdaglTNSDIDEVILVGGSTRIPAVQEAVKK 325
Cdd:cd11735 313 halrksnvdFVKWSSQGMLRMSPDAMNALFKPTIDHIIQHLTDLFQKP------EVSGVKFLFLVGGFAESPLLQQAVQN 386
|
....*
gi 612675601 326 EIGKE 330
Cdd:cd11735 387 AFGDQ 391
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
67-329 |
1.72e-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: 47.27 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 67 IKRHMGTDYKVDIEGKSYTPQEISAMI-------------LQNLKNTAESYLGEKVDKAVITVPAYFNDAERQATKDAGK 133
Cdd:cd11736 85 MKIHSTSDLTMETELEAVNGKKVQALEvfahalrffkehaLQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 134 IAGL------EVERIINEPTAAALAygldkTDKDEKVLVFDLGGGTFDVSI--LELGDGVFEVLSTAGDNKLGGddfdqv 205
Cdd:cd11736 165 LAGLvspenpEQLLIALEPEAASIY-----CRKLDRYIVADCGGGTVDLTVhqIEQPQGTLKELYKASGGPYGA------ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 206 iidylvaefkkeNGVDLSQDKMALQRLKD---AAEKAKKDLSGVSQTqisLPFISAGENGPLHlevnLTRSKFEELSDSL 282
Cdd:cd11736 234 ------------VGVDLAFEKLLCQIFGEdfiATFKAKRPAAWVDLT---IAFEARKRTAALR----MSSEAMNELFQPT 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 612675601 283 IRRTMEPTRQAMKDAGLTNsdIDEVILVGGSTRIPAVQEAVKKEIGK 329
Cdd:cd11736 295 ISQIIQHIDDLMKKPEVKG--IKFLFLVGGFAESPMLQRAVQAAFGN 339
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
5-347 |
1.05e-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: 44.58 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNscVTVLEGdepkviqnpEGSRTTPSVVAFKNGETQVGEVAKRQAITNPNTVQSIKRHMGtdyKVDIEGKSY 84
Cdd:cd24049 1 LGIDIGSSS--IKAVEL---------KRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALAEALKKLLK---ENKIKGKKV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 85 ---------------TPQEISAMILQNLKNTAESYLGEKVDKAVI---TVPAYFNDAERQ-----ATK--------DAGK 133
Cdd:cd24049 67 vvalpgsdvivrtikLPKMPEKELEEAIRFEAEQYLPFPLEEVVLdyqILGEVEEGGEKLevlvvAAPkeivesylELLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 134 IAGLEVERIINEPTAAALAYGLDKTDKDEK-VLVFDLGGGTFDVSILElgDGVFEVLSTAgdnKLGGDDFDQVIIDYLva 212
Cdd:cd24049 147 EAGLKPVAIDVESFALARALEYLLPDEEEEtVALLDIGASSTTLVIVK--NGKLLFTRSI---PVGGNDITEAIAKAL-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 213 efkkenGVDLsqdkmalqrlkDAAEKAKKDLSgvsqtqislpFISAGENGPLHLEVNLTRSKFEELSDSlIRRTMEPTRQ 292
Cdd:cd24049 220 ------GLSF-----------EEAEELKREYG----------LLLEGEEGELKKVAEALRPVLERLVSE-IRRSLDYYRS 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612675601 293 AMKDagltnSDIDEVILVGGSTRIPAVQEAVKKEIGKE-----PNKGVNPDEV-------------VAMGAAI 347
Cdd:cd24049 272 QNGG-----EPIDKIYLTGGGSLLPGLDEYLSERLGIPveilnPFSNIESKKSddeelkedaplfaVAIGLAL 339
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
135-344 |
1.30e-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: 44.44 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 135 AGLEVERIINEPTAAALAYgLDKTDKDEKVLVFDLGGGTFDVSILElgDGVF---EVLStagdnkLGGDDFDQviidylv 211
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEKELGVALIDIGGGTTDIAVFK--NGSLrytAVIP------VGGNHITN------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 212 aefkkengvDLSqdkMALQRLKDAAEKAKKDLSGVSQTQISlpfisagENGPLHLEVNLTRSKfEELSDSLIRRTMEP-- 289
Cdd:cd24048 236 ---------DIA---IGLNTPFEEAERLKIKYGSALSEEAD-------EDEIIEIPGVGGREP-REVSRRELAEIIEArv 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612675601 290 ------TRQAMKDAGLTNSDIDEVILVGGSTRIPAVQEAVKK------EIGKEPNKGVNPDEV------VAMG 344
Cdd:cd24048 296 eeilelVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEvfgmpvRIGRPKNIGGLPEEVndpayaTAVG 368
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
142-327 |
1.52e-04 |
|
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: 44.22 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 142 IINEPTAAALAYGLdktdkdEKVLVFDLGGGTFDVS-ILElgdgvFEVLSTAG-DNKLGGDDFDQviidYLVAEFKKENG 219
Cdd:cd10208 104 ILEAPLAALYAAGA------TSGIVVDIGHEKTDITpIVD-----SQVVPHALvSIPIGGQDCTA----HLAQLLKSDEP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 220 VDLSQDKMALQRLKDAAEKAKKDlsgvsqtqiSLPFISAGENGPLH---LEVNLTRSKFEE--LSDSLIRRTMEPTRQAM 294
Cdd:cd10208 169 ELKSQAESGEEATLDLAEALKKS---------PICEVLSDGADLASgteITVGKERFRACEplFKPSSLRVDLLIAAIAG 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 612675601 295 KDAGLTNSDIDE-------VILVGGSTRIPAVQEAVKKEI 327
Cdd:cd10208 240 ALVLNASDEPDKrpalwenIIIVGGGSRIRGLKEALLSEL 279
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
111-173 |
5.49e-04 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 40.53 E-value: 5.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612675601 111 KAVITVPAYFNDAERQAT-----------KDAGKIAGLEVERIINEPTAAALAYGLdkTDKDEKVLVFDLGGGT 173
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALL--TLGPEGLLVVDLGGGT 86
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
234-359 |
1.01e-03 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 42.13 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 234 DAAEKAKKDLSGVsqtqISLPFISaGENGPL---------------HLEVNLTRSKFEELSDSLiRRTMEptrqAMKDAG 298
Cdd:COG1070 324 ALAAEVPPGADGL----LFLPYLS-GERTPHwdpnargaffgltlsHTRAHLARAVLEGVAFAL-RDGLE----ALEEAG 393
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612675601 299 LtnsDIDEVILVGGSTRIPAVQEAV----KKEIGKepnkgVNPDEVVAMGAAIQGGVITGDVKDV 359
Cdd:COG1070 394 V---KIDRIRATGGGARSPLWRQILadvlGRPVEV-----PEAEEGGALGAALLAAVGLGLYDDL 450
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
5-226 |
1.07e-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: 41.35 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 5 IGIDLGTTNSCVTVLEGD---------EPKVIQNPEGSRTTPSVVAFKNGETQVGEVAKRQAITNpntvqsikRHMGTDY 75
Cdd:cd10227 1 IGIDIGNGNTKVVTGGGKefkfpsavaEARESSLDDGLLEDDIIVEYNGKRYLVGELALREGGGG--------RSTGDDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 76 KvdieGKSYTPQEISAMILQNLKNTaesylgEKVDKAVITVPA--YFNDAERQATKDAGKIAGLEVE-----------RI 142
Cdd:cd10227 73 K----KSEDALLLLLAALALLGDDE------EVDVNLVVGLPIseYKEEKKELKKKLLKGLHEFTFNgkerritindvKV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612675601 143 INEPTAAALAYGLDKT-DKDEKVLVFDLGGGTFDVSILELGDGVFEvlstAGDNKLGGDDFDQVIIDYLVAEFKKENGVD 221
Cdd:cd10227 143 LPEGAGAYLDYLLDDDeLEDGNVLVIDIGGGTTDILTFENGKPIEE----SSDTLPGGEEALEKYADDILNELLKKLGDE 218
|
....*
gi 612675601 222 LSQDK 226
Cdd:cd10227 219 LDSAD 223
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
135-195 |
2.80e-03 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 40.50 E-value: 2.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612675601 135 AGLEVERIINEPTAAALAYgLDKTDKDEKVLVFDLGGGTFDVSILElgDGVF---EVLSTAGDN 195
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTEDEKELGVALVDIGGGTTDIAVFK--DGALrhtAVIPVGGDH 234
|
|
| |
