|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-636 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1250.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 1 MAKVIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDN-ERLVGQPAKRQAVTNPENTIFAVKRLIGRQigSK 79
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 80 EVKKDQKLVPYNIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:PRK00290 79 EVQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFK 239
Cdd:PRK00290 159 AGLEVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 240 KETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQAA 319
Cdd:PRK00290 239 KENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASG--PKHLEIKLTRAKFEELTEDLVERTIEPCKQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 320 LKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGIET 399
Cdd:PRK00290 317 LKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIET 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 400 LGGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGI 479
Cdd:PRK00290 397 LGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 480 VEVGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTIE 559
Cdd:PRK00290 477 VHVSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270302485 560 VIEMALANLTEQLETDDTDKIKSG*QNLTESAMKLGEAIYKSQQETAGDG*MGgeeeprGVDDDIVDADFEDLDENK 636
Cdd:PRK00290 557 KIEAAIKELKEALKGEDKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGAA------AKDDDVVDAEFEEVKDDK 627
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-600 |
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: 1014.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 3 KVIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDN-ERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGskEV 81
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 82 KKDQKLVPYNIVdGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAG 161
Cdd:TIGR02350 79 TEEAKRVPYKVV-GDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 162 LEVLRIINEPTAAALAYGLDK-KETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKK 240
Cdd:TIGR02350 158 LEVLRIINEPTAAALAYGLDKsKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 241 ETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQAAL 320
Cdd:TIGR02350 238 EEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASG--PKHLEMTLTRAKFEELTADLVERTKEPVRQAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 321 KDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGIETL 400
Cdd:TIGR02350 316 KDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 401 GGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGIV 480
Cdd:TIGR02350 396 GGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGIL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 481 EVGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTIEV 560
Cdd:TIGR02350 476 HVSAKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEK 555
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1270302485 561 IEMALANLTEQLETDDTDKIKSG*QNLTESAMKLGEAIYK 600
Cdd:TIGR02350 556 IEKAVAELKEALKGEDVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
4-600 |
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: 968.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVDGGNGDAWVEAS--GEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAG 161
Cdd:pfam00012 81 DIKHLPYKVVKLPNGDAGVEVRylGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 162 LEVLRIINEPTAAALAYGLDKKET-QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKK 240
Cdd:pfam00012 161 LNVLRIVNEPTAAALAYGLDKTDKeRNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 241 ETGVDLTKDKMALQRLKEAAEKAKIELSSSQqTEINQPFISMDPNGgqpLHMVLKLTRAKLESLVGDLIKATIKPCQAAL 320
Cdd:pfam00012 241 KYGIDLSKDKRALQRLREAAEKAKIELSSNQ-TNINLPFITAMADG---KDVSGTLTRAKFEELVADLFERTLEPVEKAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 321 KDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQG--DVKDVVLLDVTPLSLGIE 398
Cdd:pfam00012 317 KDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 399 TLGGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANG 478
Cdd:pfam00012 397 TLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 479 IVEVGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTI 558
Cdd:pfam00012 477 ILTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEK 556
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1270302485 559 EVIEMALANLTEQLETDDTDKIKSG*QNLTESAMKLGEAIYK 600
Cdd:pfam00012 557 SKVESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
4-606 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 947.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFT-DNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVK 82
Cdd:PTZ00400 43 IVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTeDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 KDQKLVPYNIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:PTZ00400 123 KEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKKET 242
Cdd:PTZ00400 203 DVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEFKKQQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 243 GVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQAALKD 322
Cdd:PTZ00400 283 GIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSG--PKHLQIKLSRAKLEELTHDLLKKTIEPCEKCIKD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 323 AGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGIETLGG 402
Cdd:PTZ00400 361 AGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGIETLGG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 403 VFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGIVEV 482
Cdd:PTZ00400 441 VFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMNI 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 483 GAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTIEVIE 562
Cdd:PTZ00400 521 SAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDELK 600
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1270302485 563 MALANLTEQLETDDTDKIKSG*QNLTESAMKLGEAIYKSQQETA 606
Cdd:PTZ00400 601 QKITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYKQGNSDN 644
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-629 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 862.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 1 MAKVIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDN-ERLVGQPAKRQAVTNPENTIFAVKRLIGRQigSK 79
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRK--FS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 80 EVKKDQKLVPYNIVDGGNGDAWVEAS--GEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAG 157
Cdd:CHL00094 79 EISEEAKQVSYKVKTDSNGNIKIECPalNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 158 KIAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADE 237
Cdd:CHL00094 159 KIAGLEVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 238 FKKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQ 317
Cdd:CHL00094 239 FKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTG--PKHIEKTLTRAKFEELCSDLINRCRIPVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 318 AALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGI 397
Cdd:CHL00094 317 NALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 398 ETLGGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDAN 477
Cdd:CHL00094 397 ETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDAN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 478 GIVEVGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTT 557
Cdd:CHL00094 477 GILSVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEK 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270302485 558 IEVIEMALANLTEQLETDDTDKIKSG*QNLTESAMKLGEAIYKSQQETagdg*mggeeEPRGVDDDIVDADF 629
Cdd:CHL00094 557 KEKIENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYSSTSTT----------DPASNDDDVIDTDF 618
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-623 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 829.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 1 MAKVIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFT-DNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSK 79
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGkSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 80 EVKKDQklVPYNIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:PRK13411 81 EEERSR--VPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKKET-QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEF 238
Cdd:PRK13411 159 AGLEVLRIINEPTAAALAYGLDKQDQeQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 239 KKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQA 318
Cdd:PRK13411 239 QQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETG--PKHLEMELTRAKFEELTKDLVEATIEPMQQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 319 ALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFF-GKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGI 397
Cdd:PRK13411 317 ALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 398 ETLGGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDAN 477
Cdd:PRK13411 397 ETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 478 GIVEVGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTT 557
Cdd:PRK13411 477 GILKVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEEL 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270302485 558 IEVIEMALANLTEQLETDD--TDKIKSG*QNLTESAMKLGEAIYKSQQETAGDG*MGGEEEPRGVDDD 623
Cdd:PRK13411 557 KQRAEQKVEQLEAALTDPNisLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDTVEPTSDTLITATMN 624
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-590 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 810.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 1 MAKVIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFT-DNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGsk 79
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 80 EVKKDQKLVPYNIV--DGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAG 157
Cdd:PRK13410 79 ELDPESKRVPYTIRrnEQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 158 KIAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADE 237
Cdd:PRK13410 159 RIAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 238 FKKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQ 317
Cdd:PRK13410 239 FLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDG--PKHIETRLDRKQFESLCGDLLDRLLRPVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 318 AALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGI 397
Cdd:PRK13410 317 RALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 398 ETLGGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDAN 477
Cdd:PRK13410 397 ETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDAN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 478 GIVEVGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTT 557
Cdd:PRK13410 477 GILQVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAALEFGPYF 556
|
570 580 590
....*....|....*....|....*....|....*..
gi 1270302485 558 IE----VIEMALANLTEQLETDDTDKIKSG*QNLTES 590
Cdd:PRK13410 557 AErqrrAVESAMRDVQDSLEQDDDRELDLAVADLQEA 593
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
4-606 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 797.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:PTZ00186 29 VIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVDGGNGDAWVE-ASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:PTZ00186 109 DIKNVPYKIVRAGNGDAWVQdGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKKET 242
Cdd:PTZ00186 189 NVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEFRKTS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 243 GVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGGQplHMVLKLTRAKLESLVGDLIKATIKPCQAALKD 322
Cdd:PTZ00186 269 GIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQ--HIQMHISRSKFEGITQRLIERSIAPCKQCMKD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 323 AGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGIETLGG 402
Cdd:PTZ00186 347 AGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLGIETLGG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 403 VFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGIVEV 482
Cdd:PTZ00186 427 VFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHV 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 483 GAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTiEVIE 562
Cdd:PTZ00186 507 TAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSDAEK-ENVK 585
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1270302485 563 MALANLTEQLETDDT--DKIKSG*QNLTESAMKLGEAIYksQQETA 606
Cdd:PTZ00186 586 TLVAELRKAMENPNVakDDLAAATDKLQKAVMECGRTEY--QQAAA 629
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-631 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 778.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 3 KVIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDN-ERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGskEV 81
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMS--EV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 82 KKDQKLVPYNIVDGGNGDAWVE--ASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:PLN03184 118 DEESKQVSYRVVRDENGNVKLDcpAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFK 239
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 240 KETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQAA 319
Cdd:PLN03184 278 KDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADG--PKHIDTTLTRAKFEELCSDLLDRCKTPVENA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 320 LKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGIET 399
Cdd:PLN03184 356 LRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLGLET 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 400 LGGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGI 479
Cdd:PLN03184 436 LGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGI 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 480 VEVGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTIE 559
Cdd:PLN03184 516 LSVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKE 595
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270302485 560 VIEMALANLTEQLETDDTDKIKSG*QNLTESAMKLGEAIYKSQQ------ETAGDG*MGGEEEPRGVDDDIVDADFED 631
Cdd:PLN03184 596 KVEAKLKELKDAIASGSTQKMKDAMAALNQEVMQIGQSLYNQPGaggagpAPGGEAGSSSSSSSGGDGDDVIDADFTD 673
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
4-512 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 777.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFT-DNERLVGQPAKRQAVTNPENTIFAVKRLIGRqigskevk 82
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 kdqklvpynivdgGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:COG0443 73 -------------SLFDEATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDKKET-QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKKE 241
Cdd:COG0443 140 EVLRLLNEPTAAALAYGLDKGKEeETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 242 TGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFismdpngGQPLHMVLKLTRAKLESLVGDLIKATIKPCQAALK 321
Cdd:COG0443 220 EGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-------SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 322 DAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDvvlLDVTPLSLGIETLG 401
Cdd:COG0443 293 DAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIETLG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 402 GVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGIVE 481
Cdd:COG0443 370 GVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILS 449
|
490 500 510
....*....|....*....|....*....|.
gi 1270302485 482 VGAKDKGTGKEQNITIqasgglnDDEIEAMV 512
Cdd:COG0443 450 VSAKDLGTGKEQSITI-------KEEIERML 473
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
4-378 |
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: 736.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFT-DNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVK 82
Cdd:cd11733 3 VIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 KDQKLVPYNIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:cd11733 83 KDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKKET 242
Cdd:cd11733 163 NVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFKKEQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 243 GVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQAALKD 322
Cdd:cd11733 243 GIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASG--PKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLKD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1270302485 323 AGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd11733 321 AGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
4-379 |
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: 729.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFT-DNERLVGQPAKRQAVTNPENTIFAVKRLIGRQigSKEVK 82
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTkDGERLVGQPAKRQAVTNPENTIFSIKRFMGRR--YKEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 KDQKLVPYNIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:cd10234 79 VERKQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKKET 242
Cdd:cd10234 159 EVLRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 243 GVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQAALKD 322
Cdd:cd10234 239 GIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASG--PKHLEMKLTRAKFEELTEDLVERTIEPVEQALKD 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1270302485 323 AGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQ 379
Cdd:cd10234 317 AKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-577 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 652.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKKD 84
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQSD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 QKLVPYNIVDGGNGDAWVEAS--GEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIA 160
Cdd:PTZ00009 87 MKHWPFKVTTGGDDKPMIEVTyqGEKktFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 161 GLEVLRIINEPTAAALAYGLDKKET--QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEF 238
Cdd:PTZ00009 167 GLNVLRIINEPTAAAIAYGLDKKGDgeKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQDF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 239 K-KETGVDLTKDKMALQRLKEAAEKAKIELSSSQQT--EINQPFISMDPNggqplhmvLKLTRAKLESLVGDLIKATIKP 315
Cdd:PTZ00009 247 KrKNRGKDLSSNQRALRRLRTQCERAKRTLSSSTQAtiEIDSLFEGIDYN--------VTISRARFEELCGDYFRNTLQP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 316 CQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFF-GKEANKGVNPDEVVAMGAAIQAGVLQGD----VKDVVLLDV 390
Cdd:PTZ00009 319 VEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLDV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 391 TPLSLGIETLGGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEV 470
Cdd:PTZ00009 399 TPLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 471 TFDIDANGIVEVGAKDKGTGKEQNITIQASGG-LNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEH 549
Cdd:PTZ00009 479 TFDIDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDE 558
|
570 580 590
....*....|....*....|....*....|
gi 1270302485 550 --KDKVDPTTIEVIEMALANLTEQLETDDT 577
Cdd:PTZ00009 559 kvKGKLSDSDKATIEKAIDEALEWLEKNQL 588
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
4-380 |
0e+00 |
|
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: 633.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFT-DNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVK 82
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAEVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 KDQKLVPYNIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:cd11734 83 RDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKKET 242
Cdd:cd11734 163 NVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFKKES 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 243 GVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGgqPLHMVLKLTRAKLESLVGDLIKATIKPCQAALKD 322
Cdd:cd11734 243 GIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASG--PKHINMKLTRAQFESLVKPLVDRTVEPCKKALKD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1270302485 323 AGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQG 380
Cdd:cd11734 321 AGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-589 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 621.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRqiGSKEVKKD 84
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGR--SLADIQQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 QKLVPYNIVDGGNG-DAWVEASGEKySPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGLE 163
Cdd:PRK05183 100 YPHLPYQFVASENGmPLIRTAQGLK-SPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 164 VLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLadefKKETG 243
Cdd:PRK05183 179 VLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWI----LEQAG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 244 VDLTKDKMALQRLKEAAEKAKIELSSSQQTEINqpfiSMDPNGgqplhmvlKLTRAKLESLVGDLIKATIKPCQAALKDA 323
Cdd:PRK05183 255 LSPRLDPEDQRLLLDAARAAKEALSDADSVEVS----VALWQG--------EITREQFNALIAPLVKRTLLACRRALRDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 324 GLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDV--KDVVLLDVTPLSLGIETLG 401
Cdd:PRK05183 323 GVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKpdSDMLLLDVIPLSLGLETMG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 402 GVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGIVE 481
Cdd:PRK05183 403 GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 482 VGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTIEVI 561
Cdd:PRK05183 483 VTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERAAI 562
|
570 580
....*....|....*....|....*...
gi 1270302485 562 EMALANLTEQLETDDTDKIKSG*QNLTE 589
Cdd:PRK05183 563 DAAMAALREVAQGDDADAIEAAIKALDK 590
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
4-591 |
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: 601.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDN-ERLVGQPAKRQAVTNPENTIFAVKRLIGRqigSKEVK 82
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDgGVEVGKEALAAAAEDPKNTISSVKRLMGR---SIEDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 KDQKLVPYNIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:TIGR01991 78 KTFSILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYladeFKKET 242
Cdd:TIGR01991 158 NVLRLLNEPTAAAVAYGLDKASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKW----ILKQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 243 GVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINqpfisMDPNGGqplHMVLKLTRAKLESLVGDLIKATIKPCQAALKD 322
Cdd:TIGR01991 234 GISADLNPEDQRLLLQAARAAKEALTDAESVEVD-----FTLDGK---DFKGKLTRDEFEALIQPLVQKTLSICRRALRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 323 AGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDV--KDVVLLDVTPLSLGIETL 400
Cdd:TIGR01991 306 AGLSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRigNDLLLLDVTPLSLGIETM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 401 GGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGIV 480
Cdd:TIGR01991 386 GGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 481 EVGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTIEV 560
Cdd:TIGR01991 466 TVSAQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAA 545
|
570 580 590
....*....|....*....|....*....|.
gi 1270302485 561 IEMALANLTEQLETDDTDKIKSG*QNLTESA 591
Cdd:TIGR01991 546 IDAAMEALQKALQGDDADAIKAAIEALEEAT 576
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
4-378 |
0e+00 |
|
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The HSPA1-like family includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10), HSPA13 (also known as 70-kDa heat shock protein 13; STCH; microsomal stress-70 protein ATPase core; stress-70 protein chaperone microsome-associated 60 kDa protein), as well as Saccharmoyces cerevisiae Hsp70 chaperone Ssb1-2 and heat shock protein Ssa1-4. HSPA1A/1B, HSPA1L, HSPA2 and HSPA6-8 are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). HSPA13 has peptide-independent ATPase activity. All family members belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466878 [Multi-domain] Cd Length: 376 Bit Score: 549.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVDGGNGDAWVEAS--GEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:cd24028 81 DIKHWPFKVVEDEDGKPKIEVTykGEEktFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKKE--TQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADE 237
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSsgERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 238 FKKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINqpfiSMDPNGGQPLHMvlKLTRAKLESLVGDLIKATIKPCQ 317
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIE----IDSLYDGIDFET--TITRAKFEELCEDLFKKCLEPVE 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270302485 318 AALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFF-GKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd24028 315 KVLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
4-378 |
0e+00 |
|
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 536.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:cd10241 3 VIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVD-GGNGDAWVEASGEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIA 160
Cdd:cd10241 83 DIKLLPFKIVNkNGKPYIQVEVKGEKktFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 161 GLEVLRIINEPTAAALAYGLDKKET-QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFK 239
Cdd:cd10241 163 GLNVLRIINEPTAAAIAYGLDKKGGeKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLFK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 240 KETGVDLTKDKMALQRLKEAAEKAKIELSSSQQT--EINQPFISMDpnggqplhMVLKLTRAKLESLVGDLIKATIKPCQ 317
Cdd:cd10241 243 KKTGKDISKDKRAVQKLRREVEKAKRALSSQHQAriEIESLFDGED--------FSETLTRAKFEELNMDLFRKTLKPVQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270302485 318 AALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFF-GKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd10241 315 KVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
5-378 |
1.06e-171 |
|
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: 493.68 E-value: 1.06e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKKD 84
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 QKLVPYNIVDGGNGDAW-VEASGEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAG 161
Cdd:cd10233 82 MKHWPFKVVSGGDKPKIqVEYKGETktFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 162 LEVLRIINEPTAAALAYGLDKKET--QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFK 239
Cdd:cd10233 162 LNVLRIINEPTAAAIAYGLDKKGKgeRNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 240 KETGVDLTKDKMALQRLKEAAEKAKIELSSSQQT--EINQPFISMDPNGgqplhmvlKLTRAKLESLVGDLIKATIKPCQ 317
Cdd:cd10233 242 RKHKKDISGNPRALRRLRTACERAKRTLSSSTQAsiEIDSLFEGIDFYT--------SITRARFEELCADLFRSTLEPVE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270302485 318 AALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFF-GKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd10233 314 KVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
1-380 |
4.83e-163 |
|
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: 471.32 E-value: 4.83e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 1 MAKVIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERL-VGQPAKRQAVTNPENTIFAVKRLIGRQIgsK 79
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKItVGEKAKENAITDPENTISSVKRLMGRSL--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 80 EVKKDQKLVPYNIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:cd10236 79 DVKEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYladeFK 239
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADW----IL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 240 KETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFismdpnGGQPLHmvLKLTRAKLESLVGDLIKATIKPCQAA 319
Cdd:cd10236 235 KQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV------EGKDWE--REITREEFEELIQPLVKRTLEPCRRA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270302485 320 LKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQG 380
Cdd:cd10236 307 LKDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
5-378 |
1.40e-151 |
|
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: 441.24 E-value: 1.40e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVI-ENAEGARTTPSVVAFTDNER-LVGQPAKRQAVTNPENTIFAVKRLIGRQigSKEVK 82
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPSVVYFDKDGEvLVGEEAKNQALLDPENTIYSVKRLMGRD--TKDKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 KdqklvpynivdggngdawveASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:cd24029 79 E--------------------IGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDK-KETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKKE 241
Cdd:cd24029 139 NVLRLINEPTAAALAYGLDKeGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 242 TGV-DLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFismDPNGGqplHMVLKLTRAKLESLVGDLIKATIKPCQAAL 320
Cdd:cd24029 219 TGIlDDKEDERARARLREAAEEAKIELSSSDSTDILILD---DGKGG---ELEIEITREEFEELIAPLIERTIDLLEKAL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1270302485 321 KDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd24029 293 KDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
5-378 |
1.27e-140 |
|
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: 414.38 E-value: 1.27e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQpRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKKD 84
Cdd:cd24093 2 IGIDLGTTYSCVATYESSV-EIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 QKLVPYNIVD-GGNGDAWVEASGEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAG 161
Cdd:cd24093 81 MKTWPFKVIDvNGNPVIEVQYLGETktFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 162 LEVLRIINEPTAAALAYGLDKKET---QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEF 238
Cdd:cd24093 161 LNVLRIINEPTAAAIAYGLGAGKSekeRHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 239 KKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQT--EINQPFISMDPNggqplhmvLKLTRAKLESLVGDLIKATIKPC 316
Cdd:cd24093 241 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTtvEVDSLFDGEDFE--------SSITRARFEDLNAALFKSTLEPV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270302485 317 QAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFF-GKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd24093 313 EQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
5-380 |
9.93e-127 |
|
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: 377.74 E-value: 9.93e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAF-TDNERLVGQPAKRQAVTNPENTIFAVKRLIGRqigskevkk 83
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMGT--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 dqklvpynivdggngDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGLE 163
Cdd:cd10235 72 ---------------DKQYRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 164 VLRIINEPTAAALAYGLDKKET-QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFKKET 242
Cdd:cd10235 137 VERLINEPTAAALAYGLHKREDeTRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 243 GVDLTKDKMALQRlkeAAEKAKIELSSSQQTEInqPFISMDPNGGqplhmvLKLTRAKLESLVGDLIKATIKPCQAALKD 322
Cdd:cd10235 217 TSLSPSELAALRK---RAEQAKRQLSSQDSAEI--RLTYRGEELE------IELTREEFEELCAPLLERLRQPIERALRD 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1270302485 323 AGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQG 380
Cdd:cd10235 286 AGLKPSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-380 |
3.50e-126 |
|
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: 378.61 E-value: 3.50e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 3 KVIGIDLGTTNSCVAI---MDGsQPRVIENAEGARTTPSVVAFTDNER-LVGQPAKRQAVTNPENTIFAVKRLIGRQIGS 78
Cdd:cd10237 23 KIVGIDLGTTYSCVGVyhaVTG-EVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 79 KEVKKDQKLVPYNIVDGGNGDAWVEASGEKY----SPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATK 154
Cdd:cd10237 102 EELEEEAKRYPFKVVNDNIGSAFFEVPLNGStlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 155 DAGKIAGLEVLRIINEPTAAALAYGLDKKE-TQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKY 233
Cdd:cd10237 182 KAANLAGLEVLRVINEPTAAAMAYGLHKKSdVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 234 LADEFKKETGVDLTkDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGGQPLHMvLKLTRAKLESLVGDLIKATI 313
Cdd:cd10237 262 LIDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKFK-EEITRDLFETLNEDLFQRVL 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270302485 314 KPCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQG 380
Cdd:cd10237 340 EPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
4-587 |
2.15e-124 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 380.74 E-value: 2.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQpakrqavtnpENTIFAVKRLIGRQIgsKEVKK 83
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTL--KEILN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPY--NIVDGGNGDAWVEASGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAG 161
Cdd:PRK01433 89 TPALFSLvkDYLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 162 LEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADEFkke 241
Cdd:PRK01433 169 FEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNKF--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 242 tgvDLTKDKMALQRLKEAAEkakielsssqqTEINQPFISMDpnggqplhmVLKLTRAKLESLVGDLIKATIKPCQAALK 321
Cdd:PRK01433 246 ---DLPNSIDTLQLAKKAKE-----------TLTYKDSFNND---------NISINKQTLEQLILPLVERTINIAQECLE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 322 DAGLSigDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGIETLG 401
Cdd:PRK01433 303 QAGNP--NIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGMELYG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 402 GVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTLRVFQGEREMAADNKMLGQFNLEDIPPAPRGLPQIEVTFDIDANGIVE 481
Cdd:PRK01433 381 GIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 482 VGAKDKGTGKEQNITIQASGGLNDDEIEAMVKEAEENAEADKDRKDLVEARNQAESLIHSTEKSMEEHKDKVDPTTIEVI 561
Cdd:PRK01433 461 VSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISII 540
|
570 580
....*....|....*....|....*.
gi 1270302485 562 EMALANLTEQLETDDTDKIKSG*QNL 587
Cdd:PRK01433 541 NSLLDNIKEAVHARDIILINNSIKEF 566
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
4-378 |
2.30e-112 |
|
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: 341.91 E-value: 2.30e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVD-GGNGDAWVEASGEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIA 160
Cdd:cd10238 82 LKKESKCKIIEkDGKPGYEIELEEKKklVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 161 GLEVLRIINEPTAAALAYGL---DKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLADE 237
Cdd:cd10238 162 GFNVLRVISEPSAAALAYGIgqdDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLASE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 238 FKKETGVDLTKDKMALQRLKEAAEKAKIELSSSQ--QTEINQPFISMDPNGgqplhmvlKLTRAKLESLVGDLIKATIKP 315
Cdd:cd10238 242 FKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNtaTCSVESLYDGMDFQC--------NVSRARFESLCSSLFQQCLEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270302485 316 CQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFF-GKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd10238 314 IQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
5-375 |
3.96e-107 |
|
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: 328.36 E-value: 3.96e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKKD 84
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 QKLVPYNIVDGGNGDAWVEAS--GEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIA 160
Cdd:cd11732 81 IKLLPFKLVELEDGKVGIEVSynGEEvvFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 161 GLEVLRIINEPTAAALAYGLDKK-------ETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKY 233
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSdlleseeKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 234 LADEFKKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFIS--MDPNGgqplhmvlKLTRAKLESLVGDLIKA 311
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMedIDFSG--------QIKREEFEELIQPLLAR 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270302485 312 TIKPCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQA 375
Cdd:cd11732 313 LEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
5-375 |
6.19e-97 |
|
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: 302.27 E-value: 6.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKKD 84
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 QKLVPYNIVDGGNGDAWVEAS--GEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIA 160
Cdd:cd10228 81 LKHLPYKVVKLPNGSVGIKVQylGEEhvFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 161 GLEVLRIINEPTAAALAYGLDKKET-------QTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKY 233
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDLpaeeekpRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 234 LADEFKKETGVDLTKDKMALQRLKEAAEKAKiELSSSQQTEInqP-----FIS-MDPNGgqplhmvlKLTRAKLESLVGD 307
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATEL--PlniecFMDdKDVSG--------KMKRAEFEELCAP 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270302485 308 LIKATIKPCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQA 375
Cdd:cd10228 310 LFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
4-379 |
1.80e-96 |
|
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: 301.15 E-value: 1.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVDGGNGDAWVEAS--GEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:cd24095 83 DLKLFPFKVTEGPDGEIGINVNylGEQkvFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYG-----LDKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYL 234
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGiyktdLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 235 ADEFKKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNggqpLHMVlkLTRAKLESLVGDLIKATIK 314
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKD----VKGM--ITREEFEELAAPLLERLLE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270302485 315 PCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVLQ 379
Cdd:cd24095 317 PLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
4-375 |
1.67e-89 |
|
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: 1.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIM-DGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGrqigskevk 82
Cdd:cd10230 2 VLGIDLGSEFIKVALVkPGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 kdqklvpynivdggngdawveasgekYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:cd10230 73 --------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGLDKK----ETQTIAVFDLGGGTFDITILEI------DDGL------FEVKSTNGDTFLGGEDF 226
Cdd:cd10230 127 NVLSLINDNTAAALNYGIDRRfennEPQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLGGLEF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 227 DMRIVKYLADEF--KKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTeinqpFISMdpnggQPLHMVL----KLTRAK 300
Cdd:cd10230 207 DLRLADHLADEFneKHKKDKDVRTNPRAMAKLLKEANRVKEVLSANTEA-----PASI-----ESLYDDIdfrtKITREE 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270302485 301 LESLVGDLIKATIKPCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEA-NKGVNPDEVVAMGAAIQA 375
Cdd:cd10230 277 FEELCADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
5-378 |
6.11e-88 |
|
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: 278.87 E-value: 6.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKKD 84
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 QKLVPYNIVDGgNGDAWVEAS--GEK--YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIA 160
Cdd:cd24094 81 EKYFTAKLVDA-NGEVGAEVNylGEKhvFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 161 GLEVLRIINEPTAAALAYGLDK------KETQTIAVF-DLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKY 233
Cdd:cd24094 160 GLNPLRLMNDTTAAALGYGITKtdlpepEEKPRIVAFvDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 234 LADEFKKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFISMDPNGGQplhmvlKLTRAKLESLVGDLIKATI 313
Cdd:cd24094 240 FADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSS------MLKREEFEELIAPLLERVT 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270302485 314 KPCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd24094 314 APLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-378 |
6.25e-76 |
|
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: 246.50 E-value: 6.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQ-PRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRqigskevk 82
Cdd:cd10232 2 VIGISFGNSNSSIAIINKDGrAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGT-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 83 kdqklvpynivdggngdawveasgEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL 162
Cdd:cd10232 74 ------------------------TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 163 EVLRIINEPTAAALAYGL------DKKETQTIAVFDLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVKYLAD 236
Cdd:cd10232 130 EVLQLIPEPAAAALAYDLraetsgDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 237 EFKKETGVDLTKDKMALQRLKEAAEKAKIELS--SSQQTEINQPFISMDPNGgqplhmvlKLTRAKLESLVGDLIKATIK 314
Cdd:cd10232 210 EFKKKTKTDPRKNARSLAKLRNAAEITKRALSqgTSAPCSVESLADGIDFHS--------SINRTRYELLASKVFQQFAD 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270302485 315 PCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANK----GVNPDEVVAMGAAIQAGVL 378
Cdd:cd10232 282 LVTDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
4-374 |
8.96e-76 |
|
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: 247.08 E-value: 8.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVDGGNGDAWVEA----SGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:cd11739 82 EKENLSYDLVPLKNGGVGVKVmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKK------ETQTIAVF-DLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVK 232
Cdd:cd11739 162 VGLNCLRLMNDMTAVALNYGIYKQdlpapdEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 233 YLADEFKKETGVDLTKDKMALQRLKEAAEKAKiELSSSQQTEIN---QPFIS-MDPNGgqplhmvlKLTRAKLESLVGDL 308
Cdd:cd11739 242 HFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLPlniECFMNdKDVSG--------KMNRSQFEELCADL 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270302485 309 IKATIKPCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQ 374
Cdd:cd11739 313 LQRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
4-377 |
4.70e-74 |
|
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: 242.54 E-value: 4.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVDGGNGDAWVEAS---GEK-YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:cd11737 82 EKPSLAYELVQLPTGTTGIKVMymeEERnFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKK------ETQTIAVF-DLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVK 232
Cdd:cd11737 162 AGLNCLRLMNETTAVALAYGIYKQdlpapeEKPRNVVFvDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 233 YLADEFKKETGVDLTKDKMALQRLKEAAEKAKIELSS-SQQTEIN-QPFIS-MDPNGgqplhmvlKLTRAKLESLVGDLI 309
Cdd:cd11737 242 HFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNiECFMNdIDVSG--------TMNRGQFEEMCADLL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270302485 310 KATIKPCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGV 377
Cdd:cd11737 314 ARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
4-378 |
4.34e-70 |
|
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: 232.12 E-value: 4.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENTIFAVKRLIGRQIGSKEVKK 83
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 84 DQKLVPYNIVDGGNGDAWVEA---SGEK-YSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKI 159
Cdd:cd11738 82 EKIKLPYELQKMPNGSTGVKVrylDEERvFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKKETQTI------AVF-DLGGGTFDITILEIDDGLFEVKSTNGDTFLGGEDFDMRIVK 232
Cdd:cd11738 162 AGLNCLRLMNETTAVALAYGIYKQDLPALeekprnVVFvDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 233 YLADEFKKETGVDLTKDKMALQRLKEAAEKAKIELSS-SQQTEINQPFISMDpnggqpLHMVLKLTRAKLESLVGDLIKA 311
Cdd:cd11738 242 YFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMND------IDVSSKMNRAQFEELCASLLAR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270302485 312 TIKPCQAALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAIQAGVL 378
Cdd:cd11738 316 VEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
5-373 |
1.68e-53 |
|
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: 186.16 E-value: 1.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIenaegarttpsvvaftdnerlvgqpakrqavtnpenTIFAVKRLIGRQIGSKEVkkd 84
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPP------------------------------------LVVLQLPWPGGDGGSSKV--- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 qklvpynivdggngdawveasgekysPSQISAF--ILQKMKETAESYLGEDV-------TQAVITVPAYFNDAQRQATKD 155
Cdd:cd10170 42 --------------------------PSVLEVVadFLRALLEHAKAELGDRIwelekapIEVVITVPAGWSDAAREALRE 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 156 AGKIAGL----EVLRIINEPTAAALAYGLDK------KETQTIAVFDLGGGTFDITILEIDDGLFEVK---STNGDTFLG 222
Cdd:cd10170 96 AARAAGFgsdsDNVRLVSEPEAAALYALEDKgdllplKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALLG 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 223 GEDFDMRIVKYLADEFKKETGVDLTKDKMALQRLKEAAEKAKIELSSSQQTEINQPFIsmdPNGGQPLHMVLKLTRAKLE 302
Cdd:cd10170 176 GTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSL---LGGGLPELGLEKGTLLLTE 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270302485 303 SLVGDLIKATIKPCQAALKDAGLS--IGDIDEVVMVGGMTRMPKVTEEVSKFFG----KEANKGVNPDEVVAMGAAI 373
Cdd:cd10170 253 EEIRDLFDPVIDKILELIEEQLEAksGTPPDAVVLVGGFSRSPYLRERLRERFGsagiIIVLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
5-372 |
8.64e-40 |
|
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: 150.89 E-value: 8.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNE------RLVGQPAKRQAVTNPENTIF--AVKRLIGrqi 76
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 77 gskevkkdqklvpynivDGGNGDAWVeaSGEKYSPSQISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQAT--- 153
Cdd:cd10231 78 -----------------SSLFDETTI--FGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqa 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 154 ----KDAGKIAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEID----DGLFEVKSTNGDtFLGGED 225
Cdd:cd10231 139 esrlRDAARRAGFRNVEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GIGGDD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 226 FDMRIV-KYLADEF----------------------------------------------------KKETGVDLTKDKMA 252
Cdd:cd10231 218 FDRELAlKKVMPHLgrgstyvsgdkglpvpawlyadlsnwhaisllytkktlrllldlrrdaadpeKIERLLSLVEDQLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 253 lQRLKEAAEKAKIELSSSQQTEINQPFIsmdpnggqPLHMVLKLTRAKLESLVGDLIKATIKPCQAALKDAGLSIGDIDE 332
Cdd:cd10231 298 -HRLFRAVEQAKIALSSADEATLSFDFI--------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDR 368
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1270302485 333 VVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAA 372
Cdd:cd10231 369 VFLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-373 |
6.33e-26 |
|
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: 110.06 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 4 VIGIDLGTTNSCVAIM---DGSQPRVIENAEGA------RTTPSVVAFTDNERLV--GQPAKRQAvtnpentifavKRLI 72
Cdd:cd10229 2 VVAIDFGTTYSGYAYSfitDPGDIHTMYNWWGAptgvssPKTPTCLLLNPDGEFHsfGYEAREKY-----------SDLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 73 GRQIGSKEVKKDQKLVPYNIVDGGNGDAWVEASGEKYSP--------SQISAFILQKMKETAESYLGEDVTQAVITVPAY 144
Cdd:cd10229 71 EDEEHQWLYFFKFKMMLLSEKELTRDTKVKAVNGKSMPAlevfaealRYLKDHALKELRDRSGSSLDEDDIRWVLTVPAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 145 FNDAQRQATKDAGKIAGL------EVLRIINEPTAAALAYGLDKKETQTIA--------VFDLGGGTFDITILEI--DDG 208
Cdd:cd10229 151 WSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKLLAEGEEKElkpgdkylVVDCGGGTVDITVHEVleDGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 209 LFEVKSTNGDTFlGGEDFDMRIVKYLADEFKKETGVDL-TKDKMALQRLKEAAEKAKIelsssqqteinqpfismdpngg 287
Cdd:cd10229 231 LEELLKASGGPW-GSTSVDEEFEELLEEIFGDDFMEAFkQKYPSDYLDLLQAFERKKR---------------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 288 qplHMVLKLTRAKLESLVGDLIKATIkpcqAALKD--AGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEanKGV---- 361
Cdd:cd10229 288 ---SFKLRLSPELMKSLFDPVVKKII----EHIKEllEKPELKGVDYIFLVGGFAESPYLQKAVKEAFSTK--VKIiipp 358
|
410
....*....|..
gi 1270302485 362 NPDEVVAMGAAI 373
Cdd:cd10229 359 EPGLAVVKGAVL 370
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
5-343 |
1.83e-11 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 66.42 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSQPRVIENAEGARTTPSVVAFTDNERLVGQPAKRQAVTNPENtifAVKRLIGRQIGSKEvKKD 84
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREAVSEWLYRHLDVPAYDD---ERQALLRRAIRYNR-EED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 85 QKLVPYNIVDGGNG-DAWVE----------------ASGEKysPSQISAF------ILQKMKETAESYLGEDVTQAVITV 141
Cdd:PRK11678 79 IDVTAQSVFFGLAAlAQYLEdpeevyfvkspksflgASGLK--PQQVALFedlvcaMMLHIKQQAEAQLQAAITQAVIGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 142 PAYFN-----DAQRQAT---KDAGKIAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIDDGlFEVK 213
Cdd:PRK11678 157 PVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSMLLMGPS-WRGR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 214 STNGDTFL-------GGEDFDMrivkYLAdeFK-----------KETGV------------------------------- 244
Cdd:PRK11678 236 ADRSASLLghsgqriGGNDLDI----ALA--FKqlmpllgmgseTEKGIalpslpfwnavaindvpaqsdfyslangrll 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 245 -DLTKDKM---ALQRLKE------------AAEKAKIELSSSQQTEINQPFISMDpnggqpLHmvLKLTRAKLESLVGDL 308
Cdd:PRK11678 310 nDLIRDARepeKVARLLKvwrqrlsyrlvrSAEEAKIALSDQAETRASLDFISDG------LA--TEISQQGLEEAISQP 381
|
410 420 430
....*....|....*....|....*....|....*
gi 1270302485 309 IKATIKPCQAALKDAGLSigdIDEVVMVGGMTRMP 343
Cdd:PRK11678 382 LARILELVQLALDQAQVK---PDVIYLTGGSARSP 413
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
118-373 |
1.18e-10 |
|
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: 62.28 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 118 ILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKetqtiAVFDLGGGT 197
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG-----AVVDIGGGT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 198 FDITILEiddglfevkstNGDtflggedfdmriVKYLADEFKKETGVDLTkdkMALQRLKEAAEKAKIELSSSQQTEInq 277
Cdd:cd24047 123 TGIAVLK-----------DGK------------VVYTADEPTGGTHLSLV---LAGNYGISFEEAEIIKRDPARHKEL-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 278 pfismdpnggqplhmvLKLTRAKLESlVGDLIKATIKPcqaalkdaglsiGDIDEVVMVGGMTRMPKVTEEVSKFFGKEA 357
Cdd:cd24047 175 ----------------LPVVRPVIEK-MASIVKRHIKG------------YKVKDLYLVGGTCCLPGIEEVFEKETGLPV 225
|
250
....*....|....*.
gi 1270302485 358 NKGVNPDEVVAMGAAI 373
Cdd:cd24047 226 YKPSNPLLVTPLGIAL 241
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
5-373 |
1.83e-10 |
|
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: 62.57 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDgsqpRVIENAEgarttPSVVAF-TDNERL--VGQPAKRQAVTNPENtIFAVKRLIGRQIGSKEV 81
Cdd:pfam06723 4 IGIDLGTANTLVYVKG----KGIVLNE-----PSVVAInTKTKKVlaVGNEAKKMLGRTPGN-IVAVRPLKDGVIADFEV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 82 KkdQKLVPYNIVDGGNGDAWVEAsgekyspsqisafilqkmketaesylgedvtQAVITVPAYFNDAQRQATKDAGKIAG 161
Cdd:pfam06723 74 T--EAMLKYFIKKVHGRRSFSKP-------------------------------RVVICVPSGITEVERRAVKEAAKNAG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 162 LEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIdDGLFEVKSTNgdtfLGGEDFDMRIVKYLADEFKKE 241
Cdd:pfam06723 121 AREVFLIEEPMAAAIGAGLPVEEPTGNMVVDIGGGTTEVAVISL-GGIVTSKSVR----VAGDEFDEAIIKYIRKKYNLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 242 TGVdltkdkmalqrlkEAAEKAKIELSSSQQTEINQpfiSMDPNG-----GQPLHMVLK---LTRAKLESL--VGDLIKA 311
Cdd:pfam06723 196 IGE-------------RTAERIKIEIGSAYPTEEEE---KMEIRGrdlvtGLPKTIEISseeVREALKEPVsaIVEAVKE 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270302485 312 TIKPCQAALkdaglsIGDIDE--VVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMGAAI 373
Cdd:pfam06723 260 VLEKTPPEL------AADIVDrgIVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-373 |
5.84e-10 |
|
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: 61.25 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 1 MAKVIGIDLGTTNSCVAImdGSQPRVIEnaEgarttPSVVAFTDNErlvgqpakrqavtnpeNTIFAV----KRLIGRqi 76
Cdd:COG1077 6 FSKDIGIDLGTANTLVYV--KGKGIVLN--E-----PSVVAIDKKT----------------GKVLAVgeeaKEMLGR-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 77 gskevkkdqklVPYNIV------DGgngdawVeasgekyspsqISAFilqkmkETAESYLGEDVTQA-----------VI 139
Cdd:COG1077 59 -----------TPGNIVairplkDG------V-----------IADF------EVTEAMLKYFIKKVhgrrsffrprvVI 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 140 TVPAYFNDAQRQATKDAGKIAGL-EVlRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIdDGLFEVKSTNgd 218
Cdd:COG1077 105 CVPSGITEVERRAVRDAAEQAGArEV-YLIEEPMAAAIGAGLPIEEPTGNMVVDIGGGTTEVAVISL-GGIVVSRSIR-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 219 tfLGGEDFDMRIVKYLadefKKETGVdLTKDKMalqrlkeaAEKAKIELSSSQQTEINQpfiSMDPNG-----GQPLHMV 293
Cdd:COG1077 181 --VAGDELDEAIIQYV----RKKYNL-LIGERT--------AEEIKIEIGSAYPLEEEL---TMEVRGrdlvtGLPKTIT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 294 LK---LTRAKLESL--VGDLIKATIKPCQAALkdaglsIGDIDE--VVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEV 366
Cdd:COG1077 243 ITseeIREALEEPLnaIVEAIKSVLEKTPPEL------AADIVDrgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTC 316
|
....*..
gi 1270302485 367 VAMGAAI 373
Cdd:COG1077 317 VARGTGK 323
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
5-269 |
8.83e-10 |
|
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: 60.56 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAImDGSqpRVIENaEgarttPSVVAFTDNErlvgqpakrqavtnpeNTIFAV----KRLIGRqigske 80
Cdd:cd10225 2 IGIDLGTANTLVYV-KGK--GIVLN-E-----PSVVAVDKNT----------------GKVLAVgeeaKKMLGR------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 81 vkkdqklVPYNIV------DGgngdawVEASGEkyspsqISAFILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATK 154
Cdd:cd10225 51 -------TPGNIVairplrDG------VIADFE------ATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 155 DAGKIAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIdDGLFEVKSTNgdtfLGGEDFDMRIVKYL 234
Cdd:cd10225 112 EAAEHAGAREVYLIEEPMAAAIGAGLPIEEPRGSMVVDIGGGTTEIAVISL-GGIVTSRSVR----VAGDEMDEAIINYV 186
|
250 260 270
....*....|....*....|....*....|....*
gi 1270302485 235 ADEFKKETGvdltkdkmalqrlKEAAEKAKIELSS 269
Cdd:cd10225 187 RRKYNLLIG-------------ERTAERIKIEIGS 208
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
118-395 |
1.74e-09 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 59.23 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 118 ILQKMKETAESYLGEDVTQAVITVP----AYFNDAQRqatkdagkiAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDL 193
Cdd:cd24004 51 SIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 194 GGGTFDITILEiDDGLFEVKSTNgdtfLGGEDFdmriVKYLADEFKketgVDLtkdkmalqrlkEAAEKAKIELSSSQQT 273
Cdd:cd24004 122 GAGTTDIALIR-NGGIEAYRMVP----LGGDDF----TKAIAEGFL----ISF-----------EEAEKIKRTYGIFLLI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 274 EINQPFIsmdpnGGQPLHMVLKLTRAKLESLVGDLIKatikpcqaALKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFF 353
Cdd:cd24004 178 EAKDQLG-----FTINKKEVYDIIKPVLEELASGIAN--------AIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1270302485 354 GKEANKGVNPDEVVAMGAAIQAGVLQGDvkdvvlLDVTPLSL 395
Cdd:cd24004 245 GLPVERIAPRNIGAISDITDETSKAKGP------EFVTPLGI 280
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
118-204 |
5.37e-09 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 57.53 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 118 ILQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKetqtiAVFDLGGGT 197
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG-----AVVDIGGGT 146
|
....*..
gi 1270302485 198 FDITILE 204
Cdd:PRK15080 147 TGISILK 153
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
119-281 |
1.88e-08 |
|
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: 56.90 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 119 LQKMKETAESYLGEDVTQAVITVPAYFNDAQRQATKDAGKIAGL------EVLRIINEPTAAAL-AYGLDKketqtIAVF 191
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR-----YIVA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 192 DLGGGTFDITILEIDD---GLFEVKSTNGDTFlGGEDFDMRIVKYLA--------DEFKKE---TGVDLTkdkMALQRLK 257
Cdd:cd11736 200 DCGGGTVDLTVHQIEQpqgTLKELYKASGGPY-GAVGVDLAFEKLLCqifgedfiATFKAKrpaAWVDLT---IAFEARK 275
|
170 180
....*....|....*....|....
gi 1270302485 258 EAaekAKIELSSSQQTEINQPFIS 281
Cdd:cd11736 276 RT---AALRMSSEAMNELFQPTIS 296
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
138-239 |
1.95e-08 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 56.45 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 138 VITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIdDGLFEVKSTNg 217
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVVDIGGGTTDIAVLSL-GGIVTSSSIK- 176
|
90 100
....*....|....*....|..
gi 1270302485 218 dtfLGGEDFDMRIVKYLADEFK 239
Cdd:PRK13928 177 ---VAGDKFDEAIIRYIRKKYK 195
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-269 |
3.26e-08 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 55.91 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 1 MAKVIGIDLGTTNSCVAIMD-GsqprVIENaEgarttPSVVAF-TDNERL--VGQPAKRQAVTNPENtIFAVKRLigrqi 76
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYVKGkG----IVLN-E-----PSVVAIdTKTGKVlaVGEEAKEMLGRTPGN-IEAIRPL----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 77 gSKEVkkdqklvpynIVDggngdawVEASGEkyspsQISAFILQKMKETAESYLgedvtQAVITVPAYFNDAQRQATKDA 156
Cdd:PRK13930 71 -KDGV----------IAD-------FEATEA-----MLRYFIKKARGRRFFRKP-----RIVICVPSGITEVERRAVREA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 157 GKIAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIdDGLFEVKSTNgdtfLGGEDFDMRIVKYLAD 236
Cdd:PRK13930 123 AEHAGAREVYLIEEPMAAAIGAGLPVTEPVGNMVVDIGGGTTEVAVISL-GGIVYSESIR----VAGDEMDEAIVQYVRR 197
|
250 260 270
....*....|....*....|....*....|...
gi 1270302485 237 EFKKETGvDLTkdkmalqrlkeaAEKAKIELSS 269
Cdd:PRK13930 198 KYNLLIG-ERT------------AEEIKIEIGS 217
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
5-370 |
1.36e-06 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 50.68 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 5 IGIDLGTTNSCVAIMDGSqprVIENAegarttPSVVAFTDNER---LVGQPAKRQAVTNPENtIFAVKRLigrqigskev 81
Cdd:PRK13929 7 IGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGK-IVAVRPM---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 82 kKDQKLVPYNIvdggngdawveasgekyspsqiSAFILQKMKETAESYLGEDVTQ--AVITVPAYFNDAQRQATKDAGKI 159
Cdd:PRK13929 67 -KDGVIADYDM----------------------TTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAVKN 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIdDGLFEVKSTNgdtfLGGEDFDMRIVKYLADEFK 239
Cdd:PRK13929 124 CGAKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEVAIISF-GGVVSCHSIR----IGGDQLDEDIVSFVRKKYN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 240 KETGvdltkdkmalqrlKEAAEKAKIELSSSQqteINQPFISMDPNG-----GQPLHMVL---KLTRAKLESLVGDL--I 309
Cdd:PRK13929 199 LLIG-------------ERTAEQVKMEIGYAL---IEHEPETMEVRGrdlvtGLPKTITLeskEIQGAMRESLLHILeaI 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270302485 310 KATIKPCQAALKdaglsiGDIDE--VVMVGGMTRMPKVTEEVSKFFGKEANKGVNPDEVVAMG 370
Cdd:PRK13929 263 RATLEDCPPELS------GDIVDrgVILTGGGALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
104-283 |
7.40e-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: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 104 ASGEKYSPSQISAFILQKMKETAESYL----GEDVTQA----VITVPAYFNDAQRQATKDAGKIAGL------EVLRIIN 169
Cdd:cd11735 102 ANGKKVKALEIFAYALQFFKEQALKELsdqaGSEFDNSdvrwVITVPAIWKQPAKQFMRQAAYKAGLaspenpEQLIIAL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 170 EPTAAAL-AYGLDKKETQTIAVFDLGGGTFDITILEI---DDGLFEVKSTNGDTF--LGGE-DFDMRIVKYLADEF---- 238
Cdd:cd11735 182 EPEAASIyCRKLRLHQMDRYVVVDCGGGTVDLTVHQIrlpEGHLKELYKASGGPYgsLGVDyEFEKLLCKIFGEDFidqf 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1270302485 239 ---KKETGVDLTkdkMALQRLKEAAEKAKIelsssQQTEINQPFISMD 283
Cdd:cd11735 262 kikRPAAWVDLM---IAFESRKRAAAPDRT-----NPLNITLPFSFID 301
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
160-361 |
1.72e-05 |
|
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: 47.53 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAAALAYgLDKKETQT-IAVFDLGGGTFDITILEidDGlfEVKSTngDTF-LGGEDFdmrivkylade 237
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEKELgVALIDIGGGTTDIAVFK--NG--SLRYT--AVIpVGGNHI----------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 238 fkketgvdlTKD-KMALQRLKEAAEKAKIELSSSQQTEI-NQPFISMDPNGGQPLHMVLKLT-----RAKLESLVgDLIK 310
Cdd:cd24048 234 ---------TNDiAIGLNTPFEEAERLKIKYGSALSEEAdEDEIIEIPGVGGREPREVSRRElaeiiEARVEEIL-ELVK 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1270302485 311 ATIkpcqaalKDAGLSIGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGV 361
Cdd:cd24048 304 KEL-------KESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGR 347
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|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
160-368 |
3.35e-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: 43.42 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 160 AGLEVLRIINEPTAA--ALAYGLDKKETQTIAVFDLGGGTFDITILEiDDGLFEVKSTNgdtfLGGEDFDMRIVKYLade 237
Cdd:cd24049 148 AGLKPVAIDVESFALarALEYLLPDEEEETVALLDIGASSTTLVIVK-NGKLLFTRSIP----VGGNDITEAIAKAL--- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 238 fkketGVDLtkdkmalqrlkEAAEKAKIELSSSqqteinqpfismDPNGGQPLHMVLKLTRAKLESLVGDlIKATIKPCQ 317
Cdd:cd24049 220 -----GLSF-----------EEAEELKREYGLL------------LEGEEGELKKVAEALRPVLERLVSE-IRRSLDYYR 270
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1270302485 318 AALKDaglsiGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKGvNPDEVVA 368
Cdd:cd24049 271 SQNGG-----EPIDKIYLTGGGSLLPGLDEYLSERLGIPVEIL-NPFSNIE 315
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|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
296-385 |
4.61e-04 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 43.28 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 296 LTRAKLESLVGDLikatiKPCQAALKDAGlsiGDIDEVVMVGGMTRMPKVTEEVSKFFGKEANKgVNPDEVVAMGAAIQA 375
Cdd:COG1070 370 LARAVLEGVAFAL-----RDGLEALEEAG---VKIDRIRATGGGARSPLWRQILADVLGRPVEV-PEAEEGGALGAALLA 440
|
90
....*....|
gi 1270302485 376 GVLQGDVKDV 385
Cdd:COG1070 441 AVGLGLYDDL 450
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
137-197 |
7.70e-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: 40.14 E-value: 7.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270302485 137 AVITVPAYFNDAQRQAT-----------KDAGKIAGLEVLRIINEPTAAALAYGLDKKETqTIAVFDLGGGT 197
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPE-GLLVVDLGGGT 86
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
1-269 |
3.24e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 40.07 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 1 MAKVIGIDLGTTNSCVaIMDGsqpRVIENAEgarttPSVVAFtDNERlvgqpakrqavtnpeNTIFAV----KRLIGRqi 76
Cdd:PRK13927 4 FSNDLGIDLGTANTLV-YVKG---KGIVLNE-----PSVVAI-RTDT---------------KKVLAVgeeaKQMLGR-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 77 gskevkkdqklVPYNIV------DGgngdawVEA---SGEKyspsQISAFILQKMKETAESylgedvTQAVITVPAYFND 147
Cdd:PRK13927 57 -----------TPGNIVairpmkDG------VIAdfdVTEK----MLKYFIKKVHKNFRPS------PRVVICVPSGITE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 148 AQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKETQTIAVFDLGGGTFDITILEIdDGLFEVKSTNgdtfLGGEDFD 227
Cdd:PRK13927 110 VERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVVDIGGGTTEVAVISL-GGIVYSKSVR----VGGDKFD 184
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1270302485 228 MRIVKYLadefKKETGVdLTKDKMalqrlkeaAEKAKIELSS 269
Cdd:PRK13927 185 EAIINYV----RRNYNL-LIGERT--------AERIKIEIGS 213
|
|
| ASKHA_NBD_ParM_pCBH-like |
cd24025 |
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ... |
166-338 |
5.62e-03 |
|
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium botulinum pCBH plasmid segregation protein ParM, an actin-like polymerizing motor. pCBH ParM filament structure is far more complex in comparison to the known filament structures of actin, MreB, and other ParMs. It is bipolar and stiff and like microtubules. The 15 polymerizing strands are likely to exert greater combined force relative to typical two-stranded actin-like filaments.
Pssm-ID: 466875 [Multi-domain] Cd Length: 326 Bit Score: 39.19 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 166 RIINEPTAAALAYGLDKK--------ETQTIAVFDLGGGTFDITILEIDDGLFEVKStngdtflGGEDFDMR-IVKYLAD 236
Cdd:cd24025 150 RVFPQGAGALYDALLDDDgqiidkalAKGRVGVIDIGYRTTDYVVFEDGEFLVPELS-------GSLETGMStAYRAIAN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270302485 237 EFKKETGVDLTkdkmaLQRLKEAAEKAKIELSssqqteinqpfismdpngGQPLHMVLKLTRAKLEslVGDLIKATIkpc 316
Cdd:cd24025 223 ALEEEYGIDLD-----LHELDRALREGKIRVR------------------GKEIDLSDLIDEALKE--LARQIANEI--- 274
|
170 180
....*....|....*....|..
gi 1270302485 317 QAALKDAglsIGDIDEVVMVGG 338
Cdd:cd24025 275 RSLWGDG---LGDLDAIILAGG 293
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