|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-638 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1224.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 1 MGKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAV 80
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRRDEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 81 KDEAHRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAG 160
Cdd:PRK00290 81 QKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 161 LKVQRIVNEPTAAALAYGLDKShKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFKN 240
Cdd:PRK00290 161 LEVLRIINEPTAAALAYGLDKK-GDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 241 DEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKD 320
Cdd:PRK00290 240 ENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 321 AGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLGIETMGG 400
Cdd:PRK00290 320 AGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 401 VMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIVNV 480
Cdd:PRK00290 400 VMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 481 SAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKSQIE 560
Cdd:PRK00290 480 SAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIE 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080686173 561 AELEKLKEAHKAQDVAAIDSALSGLNAIMQQMSQEMYANAgadagaqpgpdmgAQGGASDQGTKSDDHVTDADFEEVK 638
Cdd:PRK00290 560 AAIKELKEALKGEDKEAIKAKTEELTQASQKLGEAMYQQA-------------QAAQGAAGAAAKDDDVVDAEFEEVK 624
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-598 |
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: 1041.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 3 KIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAVKD 82
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDEVTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKlVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLK 162
Cdd:TIGR02350 81 EAKRVPYK-VVGDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 163 VQRIVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFKNDE 242
Cdd:TIGR02350 160 VLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKKEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 243 GVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYI-MPVDGvPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKDA 321
Cdd:TIGR02350 240 GIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFItADASG-PKHLEMTLTRAKFEELTADLVERTKEPVRQALKDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 322 GLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLGIETMGGV 401
Cdd:TIGR02350 319 GLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 402 MTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIVNVS 481
Cdd:TIGR02350 399 MTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 482 AKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKSQIEA 561
Cdd:TIGR02350 479 AKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEK 558
|
570 580 590
....*....|....*....|....*....|....*..
gi 1080686173 562 ELEKLKEAHKAQDVAAIDSALSGLNAIMQQMSQEMYA 598
Cdd:TIGR02350 559 AVAELKEALKGEDVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
4-598 |
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: 904.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVK 81
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPK-ERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSdpVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 82 DEAHRLPYKLVEGENDTP--RVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:pfam00012 80 RDIKHLPYKVVKLPNGDAgvEVRYLGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 160 GLKVQRIVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFK 239
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 240 NDEGVDLRKDPMALQRLKEAAEKAKIELSSsTSTEINLPYIMpVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALK 319
Cdd:pfam00012 240 KKYGIDLSKDKRALQRLREAAEKAKIELSS-NQTNINLPFIT-AMADGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 320 DAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSG--DVKDVLLLDVTPLSLGIET 397
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIET 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 398 MGGVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGI 477
Cdd:pfam00012 398 LGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 478 VNVSAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKS 557
Cdd:pfam00012 478 LTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKS 557
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1080686173 558 QIEAELEKLKEAHKAQDVAAIDSALSGLNAIMQQMSQEMYA 598
Cdd:pfam00012 558 KVESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-636 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 896.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 1 MGKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAV 80
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 81 KDEAHRLPYKLVEGENDTPRVD--IDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:CHL00094 81 SEEAKQVSYKVKTDSNGNIKIEcpALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLDKSHKDmKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDKKNNE-TILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 239 KNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQAL 318
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 319 KDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLGIETM 398
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 399 GGVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIV 478
Cdd:CHL00094 400 GGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 479 NVSAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKSQ 558
Cdd:CHL00094 480 SVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEK 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080686173 559 IEAELEKLKEAHKAQDVAAIDSALSGLNAIMQQMSQEMYANAgadagaqpgpdmgaqggASDQGTKSDDHVTDADFEE 636
Cdd:CHL00094 560 IENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYSST-----------------STTDPASNDDDVIDTDFSE 620
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-634 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 885.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 1 MGKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAV 80
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 81 KDEAHRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAG 160
Cdd:PRK13411 81 EEERSRVPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 161 LKVQRIVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFKN 240
Cdd:PRK13411 161 LEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 241 DEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKD 320
Cdd:PRK13411 241 QEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 321 AGLAPSDVDEVILVGGSTRIPAVQEMVAKIF-GREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLGIETMG 399
Cdd:PRK13411 321 AGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 400 GVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIVN 479
Cdd:PRK13411 401 EVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 480 VSAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKSQI 559
Cdd:PRK13411 481 VSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRA 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080686173 560 EAELEKLKEAHKAQDV--AAIDSALSGLNAIMQQMSQEMYANAGADAGAQPGPDMGAQGGASDQGTKSDDHVTDADF 634
Cdd:PRK13411 561 EQKVEQLEAALTDPNIslEELKQQLEEFQQALLAIGAEVYQQGGSQTTDTVEPTSDTLITATMNSSNETTLIDEFNF 637
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-585 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 841.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 1 MGKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAV 80
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 81 KDEAHRLPYKLVEGENDTPRV--DIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:PRK13410 81 DPESKRVPYTIRRNEQGNVRIkcPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLDKShKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDRS-SSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 239 KNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQAL 318
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 319 KDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLGIETM 398
Cdd:PRK13410 320 KDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 399 GGVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIV 478
Cdd:PRK13410 400 GGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 479 NVSAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEI----GDKMPAD 554
Cdd:PRK13410 480 QVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAalefGPYFAER 559
|
570 580 590
....*....|....*....|....*....|.
gi 1080686173 555 KKSQIEAELEKLKEAHKAQDVAAIDSALSGL 585
Cdd:PRK13410 560 QRRAVESAMRDVQDSLEQDDDRELDLAVADL 590
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-636 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 819.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 3 KIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAVKD 82
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSEVDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKLVEGENDTPRVDID--GRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAG 160
Cdd:PLN03184 120 ESKQVSYRVVRDENGNVKLDCPaiGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 161 LKVQRIVNEPTAAALAYGLDKSHKDMkIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFKN 240
Cdd:PLN03184 200 LEVLRIINEPTAASLAYGFEKKSNET-ILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 241 DEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKD 320
Cdd:PLN03184 279 DEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVENALRD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 321 AGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLGIETMGG 400
Cdd:PLN03184 359 AKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLGLETLGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 401 VMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIVNV 480
Cdd:PLN03184 439 VMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSV 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 481 SAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKSQIE 560
Cdd:PLN03184 519 SATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVE 598
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080686173 561 AELEKLKEAHKAQDVAAIDSALSGLNAIMQQMSQEMYANAGAdAGAQPGPDMGAQGGASDQGTKSDDHVTDADFEE 636
Cdd:PLN03184 599 AKLKELKDAIASGSTQKMKDAMAALNQEVMQIGQSLYNQPGA-GGAGPAPGGEAGSSSSSSSGGDGDDVIDADFTD 673
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
4-510 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 798.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYsavkde 83
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 84 ahrlpyklvegenDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLKV 163
Cdd:COG0443 75 -------------FDEATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 164 QRIVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFKNDEG 243
Cdd:COG0443 142 LRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEEG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 244 VDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYimpvdGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKDAGL 323
Cdd:COG0443 222 IDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 324 APSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDvllLDVTPLSLGIETMGGVMT 403
Cdd:COG0443 297 SPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIETLGGVFT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 404 KLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIVNVSAK 483
Cdd:COG0443 374 KLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAK 453
|
490 500
....*....|....*....|....*..
gi 1080686173 484 DKGTGKEQKIRIeassglsDADIERMK 510
Cdd:COG0443 454 DLGTGKEQSITI-------KEEIERML 473
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
2-628 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 796.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 2 GKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--A 79
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDedA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 80 VKDEAHRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:PTZ00400 121 TKKEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 160 GLKVQRIVNEPTAAALAYGLDKShkDMK-IAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDKN--DGKtIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 239 KNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQAL 318
Cdd:PTZ00400 279 KKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCEKCI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 319 KDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLGIETM 398
Cdd:PTZ00400 359 KDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGIETL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 399 GGVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIV 478
Cdd:PTZ00400 439 GGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIM 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 479 NVSAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKSQ 558
Cdd:PTZ00400 519 NISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDE 598
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 559 IEAELEKLKEAHKAQDVAAIDSALSGLNAIMQQMSQEMYANAGADAGAQpgpdmGAQGGASDQGTKSDDH 628
Cdd:PTZ00400 599 LKQKITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYKQGNSDNQQS-----EQSTNSEESEEKNDNA 663
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
4-377 |
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: 721.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAVKDE 83
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 84 AHRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLKV 163
Cdd:cd10234 81 RKQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 164 QRIVNEPTAAALAYGLDKShKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFKNDEG 243
Cdd:cd10234 161 LRIINEPTAAALAYGLDKK-KDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 244 VDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKDAGL 323
Cdd:cd10234 240 IDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAKL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1080686173 324 APSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLS 377
Cdd:cd10234 320 SPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
2-627 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 684.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 2 GKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFvENGERKVGDPAKRQAITNPQHTVYSIKRFMGERY--SA 79
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAF-KGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFedEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 80 VKDEAHRLPYKLVEGENDTPRV-DIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGNGDAWVqDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLDKShKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:PTZ00186 186 AGLNVIRVVNEPTAAALAYGMDKT-KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 239 KNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQAL 318
Cdd:PTZ00186 265 RKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPCKQCM 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 319 KDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLGIETM 398
Cdd:PTZ00186 345 KDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLGIETL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 399 GGVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIV 478
Cdd:PTZ00186 425 GGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGIC 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 479 NVSAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKS- 557
Cdd:PTZ00186 505 HVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSDAEKENv 584
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080686173 558 -QIEAELEKLKEAHKA--QDVAAIDSALSglNAIMQQMSQEMYANAGADAGAQPGPDMGAQGGASDQGTKSDD 627
Cdd:PTZ00186 585 kTLVAELRKAMENPNVakDDLAAATDKLQ--KAVMECGRTEYQQAAAANSGSSSNSGEQQQQQQQQQQQNSEE 655
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-633 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 631.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERY--SAVKD 82
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVARNPENTVFDAKRLIGRKFddSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKLVEGENDTPRVDIDGR----HYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:PTZ00009 86 DMKHWPFKVTTGGDDKPMIEVTYQgekkTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLDKSHK-DMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEE 237
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKGDgEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 238 FKN-DEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMpvDGVPKHLvrTLSRAKFEQLSDRYIQACRGPVAQ 316
Cdd:PTZ00009 246 FKRkNRGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLF--EGIDYNV--TISRARFEELCGDYFRNTLQPVEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 317 ALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIF-GREPSKGVNPDEVVALGAAIQGGVLSGD----VKDVLLLDVTPL 391
Cdd:PTZ00009 322 VLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLDVTPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 392 SLGIETMGGVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFD 471
Cdd:PTZ00009 402 SLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 472 IDANGIVNVSAKDKGTGKEQKIRIEASSG-LSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKE--IG 548
Cdd:PTZ00009 482 IDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDekVK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 549 DKMPADKKSQIEAE-------LEKLKEAHKAQDVAAIDSALSGLNAIMQQMSQEMyanAGADAGAQPG---PDMGAQGGA 618
Cdd:PTZ00009 562 GKLSDSDKATIEKAidealewLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQAA---GGGMPGGMPGgmpGGMPGGAGP 638
|
650
....*....|....*
gi 1080686173 619 SDQGTKSDDHVTDAD 633
Cdd:PTZ00009 639 AGAGASSGPTVEEVD 653
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-587 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 628.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGeRKVGDPAKRQAITNPQHTVYSIKRFMGERYSAVKDEA 84
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLADIQQRY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 85 HRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLKVQ 164
Cdd:PRK05183 101 PHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 165 RIVNEPTAAALAYGLDkSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEfkndEGV 244
Cdd:PRK05183 181 RLLNEPTAAAIAYGLD-SGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQ----AGL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 245 DLRKDPMALQRLKEAAEKAKIELSSSTSTEINlpyIMPVDGvpkhlvrTLSRAKFEQ----LSDRYIQACRgpvaQALKD 320
Cdd:PRK05183 256 SPRLDPEDQRLLLDAARAAKEALSDADSVEVS---VALWQG-------EITREQFNAliapLVKRTLLACR----RALRD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 321 AGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDV--KDVLLLDVTPLSLGIETM 398
Cdd:PRK05183 322 AGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKpdSDMLLLDVIPLSLGLETM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 399 GGVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIV 478
Cdd:PRK05183 402 GGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 479 NVSAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKSQ 558
Cdd:PRK05183 482 SVTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERAA 561
|
570 580
....*....|....*....|....*....
gi 1080686173 559 IEAELEKLKEAHKAQDVAAIDSALSGLNA 587
Cdd:PRK05183 562 IDAAMAALREVAQGDDADAIEAAIKALDK 590
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
4-585 |
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: 612.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAVKdE 83
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIK-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 84 AHRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLKV 163
Cdd:TIGR01991 80 FSILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 164 QRIVNEPTAAALAYGLDKSHKDMkIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEfkndEG 243
Cdd:TIGR01991 160 LRLLNEPTAAAVAYGLDKASEGI-YAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQ----LG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 244 VDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPyimpVDGvpKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKDAGL 323
Cdd:TIGR01991 235 ISADLNPEDQRLLLQAARAAKEALTDAESVEVDFT----LDG--KDFKGKLTRDEFEALIQPLVQKTLSICRRALRDAGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 324 APSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDV--KDVLLLDVTPLSLGIETMGGV 401
Cdd:TIGR01991 309 SVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRigNDLLLLDVTPLSLGIETMGGL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 402 MTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDANGIVNVS 481
Cdd:TIGR01991 389 VEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTVS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 482 AKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPADKKSQIEA 561
Cdd:TIGR01991 469 AQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAIDA 548
|
570 580
....*....|....*....|....
gi 1080686173 562 ELEKLKEAHKAQDVAAIDSALSGL 585
Cdd:TIGR01991 549 AMEALQKALQGDDADAIKAAIEAL 572
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
2-376 |
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: 595.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 2 GKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERY--SA 79
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFddPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 80 VKDEAHRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:cd11733 81 VQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 160 GLKVQRIVNEPTAAALAYGLDKShKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFK 239
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKK-DDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 240 NDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALK 319
Cdd:cd11733 240 KEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080686173 320 DAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVL 376
Cdd:cd11733 320 DAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
2-378 |
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: 535.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 2 GKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--A 79
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDdaE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 80 VKDEAHRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 160 GLKVQRIVNEPTAAALAYGLDKShKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFK 239
Cdd:cd11734 161 GLNVLRVINEPTAAALAYGLDKS-GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 240 NDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALK 319
Cdd:cd11734 240 KESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080686173 320 DAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSG 378
Cdd:cd11734 320 DAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
4-376 |
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: 518.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVK 81
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDG-ERLVGEAAKNQAASNPENTIFDVKRLIGRKFDdpSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 82 DEAHRLPYKLVEGENDTP--RVDIDG--RHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd24028 80 SDIKHWPFKVVEDEDGKPkiEVTYKGeeKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 158 IAGLKVQRIVNEPTAAALAYGLD-KSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAE 236
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDkKSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 237 EFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMpvDGVPkhLVRTLSRAKFEQLSDRYIQACRGPVAQ 316
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLY--DGID--FETTITRAKFEELCEDLFKKCLEPVEK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080686173 317 ALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIF-GREPSKGVNPDEVVALGAAIQGGVL 376
Cdd:cd24028 316 VLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
1-378 |
3.32e-175 |
|
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: 502.13 E-value: 3.32e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 1 MGKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSAV 80
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 81 KDEAHRLPYKLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAG 160
Cdd:cd10236 81 KEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 161 LKVQRIVNEPTAAALAYGLDKsHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFkn 240
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQ-KKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQI-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 241 deGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPyimpvDGVPKHLvRTLSRAKFEQLSDRYIQACRGPVAQALKD 320
Cdd:cd10236 238 --GIDARLDPAVQQALLQAARRAKEALSDADSASIEVE-----VEGKDWE-REITREEFEELIQPLVKRTLEPCRRALKD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080686173 321 AGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSG 378
Cdd:cd10236 310 AGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
2-376 |
2.58e-173 |
|
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: 497.89 E-value: 2.58e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 2 GKIIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVEnGERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--A 79
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTD-GERLIGDAAKNQATSNPENTVFDVKRLIGRKFDdkE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 80 VKDEAHRLPYKLVEgENDTPRVDIDG----RHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEA 155
Cdd:cd10241 80 VQKDIKLLPFKIVN-KNGKPYIQVEVkgekKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 156 GEIAGLKVQRIVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLA 235
Cdd:cd10241 159 GTIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 236 EEFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMpvDGVpkHLVRTLSRAKFEQLSDRYIQACRGPVA 315
Cdd:cd10241 239 KLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLF--DGE--DFSETLTRAKFEELNMDLFRKTLKPVQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080686173 316 QALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIF-GREPSKGVNPDEVVALGAAIQGGVL 376
Cdd:cd10241 315 KVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
5-377 |
2.19e-159 |
|
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: 461.27 E-value: 2.19e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEP-VVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGErysavkde 83
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAeVIIENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 84 ahrlpyklvegeNDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLKV 163
Cdd:cd24029 73 ------------DTKDKEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 164 QRIVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFKNDEG 243
Cdd:cd24029 141 LRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 244 V-DLRKDPMALQRLKEAAEKAKIELSSSTSTEInlpyIMPVDGVPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKDAG 322
Cdd:cd24029 221 IlDDKEDERARARLREAAEEAKIELSSSDSTDI----LILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKDAK 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1080686173 323 LAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLS 377
Cdd:cd24029 297 LSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
5-376 |
9.58e-154 |
|
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: 447.85 E-value: 9.58e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVKD 82
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDdpVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKLVEGEnDTPRVDI----DGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd10233 81 DMKHWPFKVVSGG-DKPKIQVeykgETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLDKSHK-DMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEE 237
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDKKGKgERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 238 FKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYImpVDGVpkHLVRTLSRAKFEQLSDRYIQACRGPVAQA 317
Cdd:cd10233 240 FKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSL--FEGI--DFYTSITRARFEELCADLFRSTLEPVEKV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 318 LKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIF-GREPSKGVNPDEVVALGAAIQGGVL 376
Cdd:cd10233 316 LRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
5-374 |
6.08e-138 |
|
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: 406.24 E-value: 6.08e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGerysavkdea 84
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 85 hrlpyklvegeNDTPrVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLKVQ 164
Cdd:cd10235 71 -----------TDKQ-YRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 165 RIVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEEFKNDEGV 244
Cdd:cd10235 139 RLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDFTS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 245 DlrkDPMALQRLKEAAEKAKIELSSSTSTEINLPYimpvDGvpKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKDAGLA 324
Cdd:cd10235 219 L---SPSELAALRKRAEQAKRQLSSQDSAEIRLTY----RG--EELEIELTREEFEELCAPLLERLRQPIERALRDAGLK 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1080686173 325 PSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGG 374
Cdd:cd10235 290 PSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAA 339
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
5-376 |
1.78e-131 |
|
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: 390.88 E-value: 1.78e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVvIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVKD 82
Cdd:cd24093 2 IGIDLGTTYSCVATYESSVEI-IANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDdeSVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKLVEgENDTPRVDI----DGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd24093 80 DMKTWPFKVID-VNGNPVIEVqylgETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLD--KSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAE 236
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 237 EFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMpvDGvpKHLVRTLSRAKFEQLSDRYIQACRGPVAQ 316
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLF--DG--EDFESSITRARFEDLNAALFKSTLEPVEQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080686173 317 ALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIF-GREPSKGVNPDEVVALGAAIQGGVL 376
Cdd:cd24093 315 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
5-582 |
1.12e-118 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 365.72 E-value: 1.12e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENGerkvgdpakrqAITNPQHTVYSIKRFMGER-------- 76
Cdd:PRK01433 22 VGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN-----------FTIGNNKGLRSIKRLFGKTlkeilntp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 77 --YSAVKDeahrlpykLVEGENDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKE 154
Cdd:PRK01433 91 alFSLVKD--------YLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 155 AGEIAGLKVQRIVNEPTAAALAYGLDKSHKDMKIaVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWL 234
Cdd:PRK01433 163 AAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYL-VYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 235 AEEFkndegvDLRKDPMALQrlkeAAEKAKIELSSSTSTEINLPYImpvdgvpkhlvrtlSRAKFEQLSDRYIQACRGPV 314
Cdd:PRK01433 242 CNKF------DLPNSIDTLQ----LAKKAKETLTYKDSFNNDNISI--------------NKQTLEQLILPLVERTINIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 315 AQALKDAGlaPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDVKDVLLLDVTPLSLG 394
Cdd:PRK01433 298 QECLEQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 395 IETMGGVMTKLIDANTTIPTKKSQIFTTAADNQPSVEIHVLQGERPMAKDNKSLGKFNLDGIPAAMRGVPQIEVTFDIDA 474
Cdd:PRK01433 376 MELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 475 NGIVNVSAKDKGTGKEQKIRIEASSGLSDADIERMKAEAEANAEADKKERERVDKINEADSVIFQTEKQLKEIGDKMPAD 554
Cdd:PRK01433 456 DGILSVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSES 535
|
570 580
....*....|....*....|....*...
gi 1080686173 555 KKSQIEAELEKLKEAHKAQDVAAIDSAL 582
Cdd:PRK01433 536 EISIINSLLDNIKEAVHARDIILINNSI 563
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-378 |
8.57e-115 |
|
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: 349.33 E-value: 8.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 3 KIIGIDLGTTNSVVAVLEG--NEPVVIANSEGKRTTPSVVAFVENGERKVGDPAKRQAITNPQHTVYSIKRFMGERYSA- 79
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 80 -VKDEAHRLPYKLVEGENDTPRVDIDGR----HYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKE 154
Cdd:cd10237 103 eLEEEAKRYPFKVVNDNIGSAFFEVPLNgstlVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 155 AGEIAGLKVQRIVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWL 234
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 235 AEEFKNDEGVDLrKDPMALQRLKEAAEKAKIELSSSTSTEINLPyiMPVDGVPKHLVR---TLSRAKFEQLSDRYIQACR 311
Cdd:cd10237 263 IDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLP--LQISLPSAFKVKfkeEITRDLFETLNEDLFQRVL 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080686173 312 GPVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSG 378
Cdd:cd10237 340 EPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
5-372 |
2.25e-108 |
|
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: 331.45 E-value: 2.25e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVKD 82
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEK-ERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDdpEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKLVEGENDTP--RVDIDG--RHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd11732 80 EIKLLPFKLVELEDGKVgiEVSYNGeeVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLDKS----HKD--MKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIID 232
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSdlleSEEkpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 233 WLAEEFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMP-VDgvpkhLVRTLSRAKFEQLSDRYIQACR 311
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEdID-----FSGQIKREEFEELIQPLLARLE 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080686173 312 GPVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQ 372
Cdd:cd11732 315 APIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQ 375
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-376 |
8.58e-108 |
|
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: 329.97 E-value: 8.58e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVKD 82
Cdd:cd10238 3 FGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDN-EKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDdpAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKLVEgENDTPRVDID----GRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd10238 82 LKKESKCKIIE-KDGKPGYEIEleekKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLDKS--HKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAE 236
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDdpTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 237 EFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMpvDGVPKHLvrTLSRAKFEQLSDRYIQACRGPVAQ 316
Cdd:cd10238 241 EFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLY--DGMDFQC--NVSRARFESLCSSLFQQCLEPIQE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080686173 317 ALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIF-GREPSKGVNPDEVVALGAAIQGGVL 376
Cdd:cd10238 317 VLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
5-372 |
7.06e-98 |
|
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: 304.58 E-value: 7.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVKD 82
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEK-NRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDdpFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKLVEGENDTPRVDID----GRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd10228 80 ELKHLPYKVVKLPNGSVGIKVQylgeEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYGLDKS------HKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIID 232
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGIYKQdlpaeeEKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 233 WLAEEFKNDEGVDLRKDPMALQRLKEAAEKAKiELSSSTSTEI--NLPYIM---PVDGvpkhlvrTLSRAKFEQLSDRYI 307
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATELplNIECFMddkDVSG-------KMKRAEFEELCAPLF 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080686173 308 QACRGPVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQ 372
Cdd:cd10228 312 ARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
4-377 |
1.34e-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: 301.54 E-value: 1.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYSA--VK 81
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEK-QRFLGEAAAASILMNPKNTISQLKRLIGRKFDDpeVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 82 DEAHRLPYKLVEGENDTPRVDI----DGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd24095 82 RDLKLFPFKVTEGPDGEIGINVnylgEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 158 IAGLKVQRIVNEPTAAALAYGLDKSHKD----MKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDW 233
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGIYKTDLPetdpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 234 LAEEFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMpvDGVPKHLVrtLSRAKFEQLSDRYIQACRGP 313
Cdd:cd24095 242 FAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLM--EDKDVKGM--ITREEFEELAAPLLERLLEP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080686173 314 VAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLS 377
Cdd:cd24095 318 LEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
5-377 |
4.36e-89 |
|
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: 281.96 E-value: 4.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVKD 82
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPK-SRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSdpEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 EAHRLPYKLVEGENDT-PRVDIDG--RHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:cd24094 80 EEKYFTAKLVDANGEVgAEVNYLGekHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 160 GLKVQRIVNEPTAAALAYGLDKS------HKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDW 233
Cdd:cd24094 160 GLNPLRLMNDTTAAALGYGITKTdlpepeEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 234 LAEEFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLvrtlSRAKFEQLSDRYIQACRGP 313
Cdd:cd24094 240 FADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSML----KREEFEELIAPLLERVTAP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080686173 314 VAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLS 377
Cdd:cd24094 316 LEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
4-373 |
4.23e-83 |
|
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: 265.13 E-value: 4.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIA-NSEGKRTTPSVVAFvENGERKVGDPAKRQAITNPQHTVYSIKRFMGerysavkd 82
Cdd:cd10230 2 VLGIDLGSEFIKVALVKPGVPFEIVlNEESKRKTPSAVAF-RNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 eahrlpyklvegendtprvdidgrhYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLK 162
Cdd:cd10230 73 -------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 163 VQRIVNEPTAAALAYGLDKSH---KDMKIAVFDLGGGT-----FDISILELGDG-------VFEVLSTNGDTHLGGDDFD 227
Cdd:cd10230 128 VLSLINDNTAAALNYGIDRRFennEPQNVLFYDMGASStsatvVEFSSVKEKDKgknktvpQVEVLGVGWDRTLGGLEFD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 228 HVIIDWLAEEF--KNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYImpVDGVpkHLVRTLSRAKFEQLSDR 305
Cdd:cd10230 208 LRLADHLADEFneKHKKDKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESL--YDDI--DFRTKITREEFEELCAD 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080686173 306 YIQACRGPVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREP-SKGVNPDEVVALGAAIQG 373
Cdd:cd10230 284 LFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-376 |
5.69e-83 |
|
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: 264.99 E-value: 5.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVL-EGNEPVVIANSEGKRTTPSVVAFVeNGERKVGDPAKRQAITNPQHTVYSIKRFMGERysavkd 82
Cdd:cd10232 2 VIGISFGNSNSSIAIInKDGRAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLGTT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 83 eahrlpyklvegendtprvdidgrHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLK 162
Cdd:cd10232 75 ------------------------TLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 163 VQRIVNEPTAAALAYGL--DKSH---KDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVIIDWLAEE 237
Cdd:cd10232 131 VLQLIPEPAAAALAYDLraETSGdtiKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAKE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 238 FKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYImpVDGVPKHLvrTLSRAKFEQLSDRYIQACRGPVAQA 317
Cdd:cd10232 211 FKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESL--ADGIDFHS--SINRTRYELLASKVFQQFADLVTDA 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080686173 318 LKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSK----GVNPDEVVALGAAIQGGVL 376
Cdd:cd10232 287 IEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
4-372 |
3.72e-76 |
|
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: 247.93 E-value: 3.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERYS--AVK 81
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPK-NRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSdpFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 82 DEAHRLPYKLVEGENDTPRVDI----DGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd11737 81 AEKPSLAYELVQLPTGTTGIKVmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 158 IAGLKVQRIVNEPTAAALAYGLDKS------HKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVII 231
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIYKQdlpapeEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 232 DWLAEEFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTST-EINLPYIM-PVDgvpkhLVRTLSRAKFEQLSDRYIQA 309
Cdd:cd11737 241 NHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANASDlPLNIECFMnDID-----VSGTMNRGQFEEMCADLLAR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080686173 310 CRGPVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQ 372
Cdd:cd11737 316 VEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
4-372 |
2.60e-75 |
|
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: 245.93 E-value: 2.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFvENGERKVGDPAKRQAITNPQHTVYSIKRFMGERY--SAVK 81
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSF-GSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFndPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 82 DEAHRLPYKLVEGENDTPRVDI----DGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd11739 81 KEKENLSYDLVPLKNGGVGVKVmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 158 IAGLKVQRIVNEPTAAALAYGLDK-----SHKDMKIAVF-DLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVII 231
Cdd:cd11739 161 IVGLNCLRLMNDMTAVALNYGIYKqdlpaPDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 232 DWLAEEFKNDEGVDLRKDPMALQRLKEAAEKAKiELSSSTSTEINLPYIMPVDGvpKHLVRTLSRAKFEQLSDRYIQACR 311
Cdd:cd11739 241 EHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLPLNIECFMND--KDVSGKMNRSQFEELCADLLQRIE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080686173 312 GPVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQ 372
Cdd:cd11739 318 VPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
4-377 |
3.66e-75 |
|
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: 245.60 E-value: 3.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAFVENgERKVGDPAKRQAITNPQHTVYSIKRFMGERY--SAVK 81
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSR-NRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFddPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 82 DEAHRLPYKLVEGENDTPRVDI----DGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd11738 81 AEKIKLPYELQKMPNGSTGVKVryldEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 158 IAGLKVQRIVNEPTAAALAYGLDKS------HKDMKIAVFDLGGGTFDISILELGDGVFEVLSTNGDTHLGGDDFDHVII 231
Cdd:cd11738 161 IAGLNCLRLMNETTAVALAYGIYKQdlpaleEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 232 DWLAEEFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTST-EINLPYIM-PVDGVPKhlvrtLSRAKFEQLSDRYIQA 309
Cdd:cd11738 241 DYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANASDlPLNIECFMnDIDVSSK-----MNRAQFEELCASLLAR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080686173 310 CRGPVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLS 377
Cdd:cd11738 316 VEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
5-371 |
4.19e-54 |
|
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: 187.70 E-value: 4.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVlegnepvviansegkrttpsvvAFVENGERKVGDPakrqaitnpqhtvysikrfmgerysavkdea 84
Cdd:cd10170 1 VGIDFGTTYSGVAY----------------------ALLGPGEPPLVVL------------------------------- 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 85 hrlpyklvegeNDTPRVDIDGRHYTPQ--EISAIILQKMKKTAEDYLGAEV-------TDAVITVPAYFSDAQRQATKEA 155
Cdd:cd10170 28 -----------QLPWPGGDGGSSKVPSvlEVVADFLRALLEHAKAELGDRIwelekapIEVVITVPAGWSDAAREALREA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 156 GEIAGLKVQ----RIVNEPTAAALAYGLDKSH-----KDMKIAVFDLGGGTFDISILELGDG---VFEVLSTNGDTHLGG 223
Cdd:cd10170 97 ARAAGFGSDsdnvRLVSEPEAAALYALEDKGDllplkPGDVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGALLGG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 224 DDFDHVIIDWLAEEFKNDEGVDLRKDPMALQRLKEAAEKAKIELSSSTSTEINLPYIMP---VDGVPKHLVRTLSRAKFE 300
Cdd:cd10170 177 TDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGgglPELGLEKGTLLLTEEEIR 256
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080686173 301 QLSDRYIQAcrgpVAQALKDAGLAPS--DVDEVILVGGSTRIPAVQEMVAKIFGREPSKGV----NPDEVVALGAAI 371
Cdd:cd10170 257 DLFDPVIDK----ILELIEEQLEAKSgtPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
5-370 |
8.88e-52 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.
Pssm-ID: 466829 [Multi-domain] Cd Length: 409 Bit Score: 184.01 E-value: 8.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAF-----VENGERKVGDPAKRQAITNPQHTVY--SIKRFMGEry 77
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFprreeEGAESIYFGNDAIDAYLNDPEEGRLikSVKSFLGS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 78 savkdeahrlpyklvEGENDTPrvdIDGRHYTPQEISAIILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd10231 79 ---------------SLFDETT---IFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDAQAES 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 158 I-------AGLKVQRIVNEPTAAALAY--GLDKSHkdmKIAVFDLGGGTFDISILELG----DGVFEVLSTNGDtHLGGD 224
Cdd:cd10231 141 RlrdaarrAGFRNVEFQYEPIAAALDYeqRLDREE---LVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GIGGD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 225 DFDHVIID------------------------WLAEEFKNDEGVDLRKDPMALQ-------------------------- 254
Cdd:cd10231 217 DFDRELALkkvmphlgrgstyvsgdkglpvpaWLYADLSNWHAISLLYTKKTLRllldlrrdaadpekierllslvedql 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 255 --RLKEAAEKAKIELSSSTSTEINLPYImpvdgvPKHLVRTLSRAKFEQLSDRYIQACRGPVAQALKDAGLAPSDVDEVI 332
Cdd:cd10231 297 ghRLFRAVEQAKIALSSADEATLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVF 370
|
410 420 430
....*....|....*....|....*....|....*...
gi 1080686173 333 LVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAA 370
Cdd:cd10231 371 LTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-378 |
2.51e-16 |
|
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: 81.17 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNS----VVAVLEGNEPVVIANSEGK-----RTTPSVVAFveNGERKV---GDPAKRQAITNP---QHTVYS 68
Cdd:cd10229 2 VVAIDFGTTYSgyaySFITDPGDIHTMYNWWGAPtgvssPKTPTCLLL--NPDGEFhsfGYEAREKYSDLAedeEHQWLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 69 IKRFMGERYSavKDEAHRlpyklvegenDTPRVDIDGRHYTPQEISAIILQKMKKTAEDYL----GAEVTDA----VITV 140
Cdd:cd10229 80 FFKFKMMLLS--EKELTR----------DTKVKAVNGKSMPALEVFAEALRYLKDHALKELrdrsGSSLDEDdirwVLTV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 141 PAYFSDAQRQATKEAGEIAGLKVQ------RIVNEPTAAALAYGLDKSHKDMKIA-------VFDLGGGTFDISILEL-- 205
Cdd:cd10229 148 PAIWSDAAKQFMREAAVKAGLISEenseqlIIALEPEAAALYCQKLLAEGEEKELkpgdkylVVDCGGGTVDITVHEVle 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 206 GDGVFEVLSTNGDtHLGGDDFDHVIIDWLAEEFKNDEGVDLR-KDPMALQRLKEAAEKAKIelssSTSTEInlpyimpvd 284
Cdd:cd10229 228 DGKLEELLKASGG-PWGSTSVDEEFEELLEEIFGDDFMEAFKqKYPSDYLDLLQAFERKKR----SFKLRL--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 285 gvPKHLVRTLsrakFEQLSDRYIQAcrgpVAQALKDAGLapSDVDEVILVGGSTRIPAVQEMVAKIFGREpSKGVNPDEV 364
Cdd:cd10229 294 --SPELMKSL----FDPVVKKIIEH----IKELLEKPEL--KGVDYIFLVGGFAESPYLQKAVKEAFSTK-VKIIIPPEP 360
|
410
....*....|....
gi 1080686173 365 VAlgAAIQGGVLSG 378
Cdd:cd10229 361 GL--AVVKGAVLFG 372
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
5-352 |
1.18e-14 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 76.44 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEGNEPVVIANSEGKRTTPSVVAfvengerkvgdPAKRQAITNPQHTVYSIKRFMGERySAVKDEA 84
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLC-----------APTREAVSEWLYRHLDVPAYDDER-QALLRRA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 85 HRLPYKL-VEGENDTPRVdidGR----HY--TPQE--------------------------ISAIILQKMKKTAEDYLGA 131
Cdd:PRK11678 71 IRYNREEdIDVTAQSVFF---GLaalaQYleDPEEvyfvkspksflgasglkpqqvalfedLVCAMMLHIKQQAEAQLQA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 132 EVTDAVITVPAYFS-----DAQRQAT---KEAGEIAGLKVQRIVNEPTAAALAY--GLDKshkDMKIAVFDLGGGTFDIS 201
Cdd:PRK11678 148 AITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTE---EKRVLVVDIGGGTTDCS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 202 ILELG-------DGVFEVLSTNGdTHLGGDDFDhviidwLAEEFK-----------------------------NDEG-- 243
Cdd:PRK11678 225 MLLMGpswrgraDRSASLLGHSG-QRIGGNDLD------IALAFKqlmpllgmgsetekgialpslpfwnavaiNDVPaq 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 244 ------------VDLRKD---PMALQRLKE------------AAEKAKIELSSSTSTEINLPYImpvdgvPKHLVRTLSR 296
Cdd:PRK11678 298 sdfyslangrllNDLIRDarePEKVARLLKvwrqrlsyrlvrSAEEAKIALSDQAETRASLDFI------SDGLATEISQ 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080686173 297 AKFEQLSDRYIQACRGPVAQALKDAGLAPsdvDEVILVGGSTRIPAVQEMVAKIFG 352
Cdd:PRK11678 372 QGLEEAISQPLARILELVQLALDQAQVKP---DVIYLTGGSARSPLIRAALAQQLP 424
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
5-371 |
3.13e-14 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 74.05 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVlEGNEPVVianSEgkrttPSVVAFvengERKVGDPAkrqaitnpqhtvysikrfmgerysAVKDEA 84
Cdd:cd10225 2 IGIDLGTANTLVYV-KGKGIVL---NE-----PSVVAV----DKNTGKVL------------------------AVGEEA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 85 HRLpyklvegendtprvdiDGRhyTPQEISAI----------------ILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQ 148
Cdd:cd10225 45 KKM----------------LGR--TPGNIVAIrplrdgviadfeateaMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 149 RQATKEAGEIAGLKVQRIVNEPTAAALAYGLDKSHKD--MkiaVFDLGGGTFDISILELGDGVfevlsTNGDTHLGGDDF 226
Cdd:cd10225 107 RRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPIEEPRgsM---VVDIGGGTTEIAVISLGGIV-----TSRSVRVAGDEM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 227 DHVIIDWLAEEFKNDEGvdlrkdpmalqrlKEAAEKAKIELSSSTSTEINLpyIMPV------DGVPKhlVRTLSRAKFE 300
Cdd:cd10225 179 DEAIINYVRRKYNLLIG-------------ERTAERIKIEIGSAYPLDEEL--SMEVrgrdlvTGLPR--TIEITSEEVR 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080686173 301 QLSDRYIQAcrgpVAQALKDA--GLAP---SDVDE--VILVGGSTRIPAVQEMVAKIFGRePSKGV-NPDEVVALGAAI 371
Cdd:cd10225 242 EALEEPVNA----IVEAVRSTleRTPPelaADIVDrgIVLTGGGALLRGLDELLREETGL-PVHVAdDPLTCVAKGAGK 315
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
117-371 |
6.44e-14 |
|
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: 71.91 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 117 ILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLKVQRIVNEPTAAALAYGLDKShkdmkiAVFDLGGG 196
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG------AVVDIGGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 197 TFDISILELGdgvfEVLSTnGDTHLGGDDFDHVIIDWLAEEFknDEGVDLRKDPmalqrlkeaaekakielssSTSTEIn 276
Cdd:cd24047 122 TTGIAVLKDG----KVVYT-ADEPTGGTHLSLVLAGNYGISF--EEAEIIKRDP-------------------ARHKEL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 277 LPYIMPVdgvpkhlvrtlsrakFEQLSDryiqacrgPVAQALKDAglapsDVDEVILVGGSTRIPAVQEMVAKIFGREPS 356
Cdd:cd24047 175 LPVVRPV---------------IEKMAS--------IVKRHIKGY-----KVKDLYLVGGTCCLPGIEEVFEKETGLPVY 226
|
250
....*....|....*
gi 1080686173 357 KGVNPDEVVALGAAI 371
Cdd:cd24047 227 KPSNPLLVTPLGIAL 241
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
117-370 |
3.54e-13 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 70.24 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 117 ILQKMKKTAEDYLGAEVTDAVITVPAYFSDAQRQATKEAGEIAGLKVQRIVNEPTAAALAYGLDKShkdmkiAVFDLGGG 196
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG------AVVDIGGG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 197 TFDISILELGDGVFEVLSTNGDTHLG-------GDDFDHviidwlAEEFKNDEgvdlrkdpmalqrlKEAAEkakielss 269
Cdd:PRK15080 146 TTGISILKDGKVVYSADEPTGGTHMSlvlagayGISFEE------AEQYKRDP--------------KHHKE-------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 270 ststeiNLPYIMPVdgvpkhlvrtlsrakFEQLSDryIqacrgpVAQALKDaglapSDVDEVILVGGSTRIPAVQEMVAK 349
Cdd:PRK15080 198 ------IFPVVKPV---------------VEKMAS--I------VARHIEG-----QDVEDIYLVGGTCCLPGFEEVFEK 243
|
250 260
....*....|....*....|.
gi 1080686173 350 IFGREPSKGVNPDEVVALGAA 370
Cdd:PRK15080 244 QTGLPVHKPQHPLFVTPLGIA 264
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-371 |
2.12e-12 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 68.62 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 1 MGKIIGIDLGTTNSVVA------VLegNEPVVIANsegKRTTPSVVAfvengerkVGDPAKRqaitnpqhtvysikrfMG 74
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYvkgkgiVL--NEPSVVAI---DTKTGKVLA--------VGEEAKE----------------ML 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 75 ERysavkdeahrlpyklvegendtprvdidgrhyTPQEISAI------------ILQKM-----KKTAEDYLGAEVtDAV 137
Cdd:PRK13930 58 GR--------------------------------TPGNIEAIrplkdgviadfeATEAMlryfiKKARGRRFFRKP-RIV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 138 ITVPAYFSDAQRQATKEAGEIAGLKVQRIVNEPTAAALAYGLD--KSHKDMkiaVFDLGGGTFDISILELGDGVfevlsT 215
Cdd:PRK13930 105 ICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPvtEPVGNM---VVDIGGGTTEVAVISLGGIV-----Y 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 216 NGDTHLGGDDFDHVIIDWLAEEFKndegvdlrkdpMAL-QRlkeAAEKAKIELSSSTSTEinLPYIMPVDGvpKHLVRTL 294
Cdd:PRK13930 177 SESIRVAGDEMDEAIVQYVRRKYN-----------LLIgER---TAEEIKIEIGSAYPLD--EEESMEVRG--RDLVTGL 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 295 srAKFEQLSDRYIQ-ACRGPVAQ---ALKDA------GLAPSDVDE-VILVGGSTRIPAVQEMVAKIFGREPSKGVNPDE 363
Cdd:PRK13930 239 --PKTIEISSEEVReALAEPLQQiveAVKSVlektppELAADIIDRgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLT 316
|
....*...
gi 1080686173 364 VVALGAAI 371
Cdd:PRK13930 317 CVARGTGK 324
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-371 |
5.00e-12 |
|
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: 67.41 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 1 MGKIIGIDLGTTNSVVAVleGNEPVVIanSEgkrttPSVVAfVENGERKVgdpakrqaitnpqhtvysikrfmgerySAV 80
Cdd:COG1077 6 FSKDIGIDLGTANTLVYV--KGKGIVL--NE-----PSVVA-IDKKTGKV---------------------------LAV 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 81 KDEAHRLpyklvegendtprvdiDGRhyTPQEISAI------------ILQKM-----KKTAEDYL--GAEVtdaVITVP 141
Cdd:COG1077 49 GEEAKEM----------------LGR--TPGNIVAIrplkdgviadfeVTEAMlkyfiKKVHGRRSffRPRV---VICVP 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 142 AYFSDAQRQATKEAGEIAGLKVQRIVNEPTAAALAYGLDkshkdmkIA------VFDLGGGTFDISILELGdGVfeVLST 215
Cdd:COG1077 108 SGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLP-------IEeptgnmVVDIGGGTTEVAVISLG-GI--VVSR 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 216 NgdTHLGGDDFDHVIIDWLAEEFKndegvdlrkdpmalqrL---KEAAEKAKIELSSSTSTEINLPYIM----PVDGVPK 288
Cdd:COG1077 178 S--IRVAGDELDEAIIQYVRKKYN----------------LligERTAEEIKIEIGSAYPLEEELTMEVrgrdLVTGLPK 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 289 HLVRTLS--RAKFEQLSDRYIQAcrgpVAQALKD--AGLApSDVDE--VILVGGSTRIPAVQEMVAKIFgrepskGV--- 359
Cdd:COG1077 240 TITITSEeiREALEEPLNAIVEA----IKSVLEKtpPELA-ADIVDrgIVLTGGGALLRGLDKLLSEET------GLpvh 308
|
410
....*....|....*
gi 1080686173 360 ---NPDEVVALGAAI 371
Cdd:COG1077 309 vaeDPLTCVARGTGK 323
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
5-371 |
1.29e-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: 62.96 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVlEGNEPVVianSEgkrttPSVVAfVENGERKVgdpakrqaitnpqhtvysikrfmgerySAVKDEA 84
Cdd:pfam06723 4 IGIDLGTANTLVYV-KGKGIVL---NE-----PSVVA-INTKTKKV---------------------------LAVGNEA 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 85 hrlpYKLVegendtprvdidGRhyTPQEISAI------------ILQKMKKtaedYLGAEVTDA--------VITVPAYF 144
Cdd:pfam06723 47 ----KKML------------GR--TPGNIVAVrplkdgviadfeVTEAMLK----YFIKKVHGRrsfskprvVICVPSGI 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 145 SDAQRQATKEAGEIAGLKVQRIVNEPTAAALAYGLD--KSHKDMkiaVFDLGGGTFDISILELGDGVfevlsTNGDTHLG 222
Cdd:pfam06723 105 TEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPveEPTGNM---VVDIGGGTTEVAVISLGGIV-----TSKSVRVA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 223 GDDFDHVIIDWLAEEFKNDEGVdlrkdpmalqrlkEAAEKAKIELSSSTSTEINLPyiMPVDGvpKHLVRTLSRaKFEQL 302
Cdd:pfam06723 177 GDEFDEAIIKYIRKKYNLLIGE-------------RTAERIKIEIGSAYPTEEEEK--MEIRG--RDLVTGLPK-TIEIS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 303 SDRYIQACRGPVAQALKDAG---------LApSDVDE--VILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALGAAI 371
Cdd:pfam06723 239 SEEVREALKEPVSAIVEAVKevlektppeLA-ADIVDrgIVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
137-239 |
1.16e-09 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 60.30 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 137 VITVPAYFSDAQRQATKEAGEIAGLKVQRIVNEPTAAALAYGLD--KSHKDMkiaVFDLGGGTFDISILELGDGVfevls 214
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDisQPSGNM---VVDIGGGTTDIAVLSLGGIV----- 170
|
90 100
....*....|....*....|....*
gi 1080686173 215 TNGDTHLGGDDFDHVIIDWLAEEFK 239
Cdd:PRK13928 171 TSSSIKVAGDKFDEAIIRYIRKKYK 195
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
110-393 |
3.61e-09 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 58.07 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 110 PQEISAIIlQKMKKTAEDYLGAEVTDAVITVP----AYFSDAQRqatkeageiAGLKVQRIVNEPTAAALAYGLDKSHkD 185
Cdd:cd24004 45 ISKVAESI-KELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPFAAANLLIPYDMR-D 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 186 MKIAVFDLGGGTFDISILELGdgvfeVLSTNGDTHLGGDDFdhviIDWLAEEFKNDegvdlrkdpmalqrlKEAAEKAKI 265
Cdd:cd24004 114 LNIALVDIGAGTTDIALIRNG-----GIEAYRMVPLGGDDF----TKAIAEGFLIS---------------FEEAEKIKR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 266 ELSSStstEINLPYIMPVDGVPKHLVRTLSRAKFEQLSDRyiqacrgpVAQALKD--AGLAPSdvDEVILVGGSTRIPAV 343
Cdd:cd24004 170 TYGIF---LLIEAKDQLGFTINKKEVYDIIKPVLEELASG--------IANAIEEynGKFKLP--DAVYLVGGGSKLPGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1080686173 344 QEMVAKIFGREPSKGVNPDEVVALGAAIQGGVLSGDvkdvllLDVTPLSL 393
Cdd:cd24004 237 NEALAEKLGLPVERIAPRNIGAISDITDETSKAKGP------EFVTPLGI 280
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
4-353 |
4.02e-08 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 55.91 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEP-------VVIANSEGkrttpsvvafVENGErkvgdpakrqaITNPQHTVYSIKRfmger 76
Cdd:COG0849 6 IVGLDIGTSKVVALVGEVDPDgklevigVGEAPSRG----------VKKGV-----------IVDIEATVEAIRK----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 77 ysaVKDEAHR-LPYKL-----------VEGENDTPRVDIDGRHYTPQEISAIIlQKMKKTA--EDY-------------- 128
Cdd:COG0849 60 ---AVEEAERmAGVKIesvyvgisgghIKSQNSRGVVAISGREITEEDVDRVL-EAARAVAipPDReilhvlpqefivdg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 129 --------------LGAEVTdaVITVPAyfsdAQRQATKEAGEIAGLKVQRIVNEPTAAALAYgLDKSHKDMKIAVFDLG 194
Cdd:COG0849 136 qegikdpvgmsgvrLEVDVH--IVTGPK----TAVQNLVKCVERAGLEVEDLVLSPLASAEAV-LTEDEKELGVALVDIG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 195 GGTFDISILElgDGVF---EVLStngdthLGGddfDHVIIDwLAEEFKndegVDLrkdpmalqrlkEAAEKAKIELSSST 271
Cdd:COG0849 209 GGTTDIAVFK--DGALrhtAVIP------VGG---DHITND-IAIGLR----TPL-----------EEAERLKIKYGSAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 272 STEINLPYIMPVDGVPKHLVRTLSRAkfeQLSDrYIQAcR-----GPVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEM 346
Cdd:COG0849 262 ASLADEDETIEVPGIGGRPPREISRK---ELAE-IIEA-RveeifELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVEL 336
|
....*..
gi 1080686173 347 VAKIFGR 353
Cdd:COG0849 337 AEEILGL 343
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
317-383 |
1.26e-07 |
|
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: 54.45 E-value: 1.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080686173 317 ALKDAGLAPsdvDEVILVGGSTRIPAVQEMVAKIFGRePSKGVNPDEVVALGAAIQGGVLSGDVKDV 383
Cdd:COG1070 388 ALEEAGVKI---DRIRATGGGARSPLWRQILADVLGR-PVEVPEAEEGGALGAALLAAVGLGLYDDL 450
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
159-353 |
3.57e-07 |
|
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: 52.92 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 159 AGLKVQRIVNEPTAAALAYgLDKSHKDMKIAVFDLGGGTFDISILElgDGVF---EVLStngdthLGGddfDHVIIDwLA 235
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEKELGVALIDIGGGTTDIAVFK--NGSLrytAVIP------VGG---NHITND-IA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 236 eefkndegvdlrkdpMALQRLKEAAEKAKIELSSSTSTEINLPYIMPVDGVPKHLVRTLSRAkfeQLSD----RYIQACR 311
Cdd:cd24048 239 ---------------IGLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRR---ELAEiieaRVEEILE 300
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1080686173 312 GpVAQALKDAGLAPSDVDEVILVGGSTRIPAVQEMVAKIFGR 353
Cdd:cd24048 301 L-VKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGM 341
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
5-238 |
4.46e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 52.40 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVleGNEPVVIanSEgkrttPSVVAfVENGERK---VGDPAKRqaitnpqhtvysikrfMGERysavk 81
Cdd:PRK13927 8 LGIDLGTANTLVYV--KGKGIVL--NE-----PSVVA-IRTDTKKvlaVGEEAKQ----------------MLGR----- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 82 deahrlpyklvegendtprvdidgrhyTPQEISAI------------ILQKM-----KKTAEDYLGA-EVtdaVITVPAY 143
Cdd:PRK13927 57 ---------------------------TPGNIVAIrpmkdgviadfdVTEKMlkyfiKKVHKNFRPSpRV---VICVPSG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 144 FSDAQRQATKEAGEIAGLKVQRIVNEPTAAALAYGLD--KSHKDMkiaVFDLGGGTFDISILELGDGVfevlsTNGDTHL 221
Cdd:PRK13927 107 ITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPvtEPTGSM---VVDIGGGTTEVAVISLGGIV-----YSKSVRV 178
|
250
....*....|....*..
gi 1080686173 222 GGDDFDHVIIDWLAEEF 238
Cdd:PRK13927 179 GGDKFDEAIINYVRRNY 195
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
4-378 |
5.60e-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: 49.23 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 4 IIGIDLGTTNSVVAVLEGNEPVVIansegkrttpSVVAFVENGERKVGDPAKRQAIT-NPQHTVYSIKRFMGERYSAVK- 81
Cdd:cd11735 2 VVAIDFGTTSSGYAYSFTKEPECI----------HVMRRWEGGDPGVSNQKTPTTILlTPERKFHSFGYAARDFYHDLDp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 82 DEAHRLPY------KLVEGENDTPRVDI---DGRHYTPQEISAIILQKMKKTA----EDYLGAEVTDA----VITVPAYF 144
Cdd:cd11735 72 NESKQWLYfekfkmKLHTTGNLTMETDLtaaNGKKVKALEIFAYALQFFKEQAlkelSDQAGSEFDNSdvrwVITVPAIW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 145 SDAQRQATKEAGEIAGLKVQR------IVNEPTAAALAYGLDKSHKDMKIAVFDLGGGTFDISI--LELGDG-VFEVLST 215
Cdd:cd11735 152 KQPAKQFMRQAAYKAGLASPEnpeqliIALEPEAASIYCRKLRLHQMDRYVVVDCGGGTVDLTVhqIRLPEGhLKELYKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 216 NGDTH--LGGD-DFDHVIIDWLAEEFKNDEGVdlrKDPMALQRLKEAAEKAKIELSSSTST--EINLPYIMpVDGVPK-- 288
Cdd:cd11735 232 SGGPYgsLGVDyEFEKLLCKIFGEDFIDQFKI---KRPAAWVDLMIAFESRKRAAAPDRTNplNITLPFSF-IDYYKKfr 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 289 -----HLVRTlSRAKFEQLSDR--------YIQACRGP----VAQALKDAGLAP--SDVDEVILVGGSTRIPAVQEMVAK 349
Cdd:cd11735 308 ghsveHALRK-SNVDFVKWSSQgmlrmspdAMNALFKPtidhIIQHLTDLFQKPevSGVKFLFLVGGFAESPLLQQAVQN 386
|
410 420 430
....*....|....*....|....*....|
gi 1080686173 350 IFGrEPSKGVNPDEVvalGAAI-QGGVLSG 378
Cdd:cd11735 387 AFG-DQCRVIIPHDV---GLTIlKGAVLFG 412
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
5-368 |
2.14e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 46.82 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 5 IGIDLGTTNSVVAVLEG----NEPVVIA-NSEgkrtTPSVVAfvengerkVGDPAKRQAITNPQHTVysikrfmgerysA 79
Cdd:PRK13929 7 IGIDLGTANILVYSKNKgiilNEPSVVAvDTE----TKAVLA--------IGTEAKNMIGKTPGKIV------------A 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 80 VKdeahrlPYKlvegenDTPRVDIDgrhytpqeISAIILQKMKKTAEDYLGAEV--TDAVITVPAYFSDAQRQATKEAGE 157
Cdd:PRK13929 63 VR------PMK------DGVIADYD--------MTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAISDAVK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 158 IAGLKVQRIVNEPTAAALAYGLDKSHKDMKIAVfDLGGGTFDISILELGDgvfeVLSTNgDTHLGGDDFDHVIIDWLAEE 237
Cdd:PRK13929 123 NCGAKNVHLIEEPVAAAIGADLPVDEPVANVVV-DIGGGTTEVAIISFGG----VVSCH-SIRIGGDQLDEDIVSFVRKK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 238 FKNDEGvdlrkdpmalqrlKEAAEKAKIELSSSTSTEINLPYIMP----VDGVPKHLvrTLSRAKFEQLSDRYIQACRGP 313
Cdd:PRK13929 197 YNLLIG-------------ERTAEQVKMEIGYALIEHEPETMEVRgrdlVTGLPKTI--TLESKEIQGAMRESLLHILEA 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080686173 314 VAQALKDA--GLAPSDVDE-VILVGGSTRIPAVQEMVAKIFGREPSKGVNPDEVVALG 368
Cdd:PRK13929 262 IRATLEDCppELSGDIVDRgVILTGGGALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
316-378 |
1.69e-04 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 44.46 E-value: 1.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080686173 316 QALKDAGLAPsdvDEVILVGGSTRIPAVQEMVAKIFGRePSKGVNPDEVVALGAAIQGGVLSG 378
Cdd:cd07809 385 DILRELGVEI---DEIRLIGGGSKSPVWRQILADVFGV-PVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
327-383 |
6.01e-04 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 42.51 E-value: 6.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080686173 327 DVDEVILVGGSTRIPAVQEMVAKIFGREPSKGVNPdEVVALGAAIQGGVLSGDVKDV 383
Cdd:cd07779 354 PIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETS-EATALGAAILAAVGAGIYPDF 409
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
316-383 |
1.05e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 42.14 E-value: 1.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080686173 316 QALKDAGLapsDVDEVILVGGSTRIPAVQEMVAKIFGRePSKGVNPDEVVALGAAIQGGVLSGDVKDV 383
Cdd:cd07808 384 EVLKELGI---KVKEIRLIGGGAKSPLWRQILADVLGV-PVVVPAEEEGSAYGAALLAAVGAGVFDDL 447
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
135-197 |
1.24e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 39.37 E-value: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080686173 135 DAVITVPAYFSDAQRQATKE-----------AGEIAGLKVQRIVNEPTAAALAYGLDKshKDMKIAVFDLGGGT 197
Cdd:cd00012 15 PIVITVAAGDRDANRVATITeailllqtnaaTFALFTGPPVRIVNEAVAAAIGALLTL--GPEGLLVVDLGGGT 86
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
542-633 |
4.27e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 40.36 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 542 KQLKEIGDKMPadKKSQIEAElEKLKEAHKA-----------QDVAAIDS---ALSGLNAIMQQMSQEMYANAGADAGAQ 607
Cdd:pfam13779 685 RRLEELQDELK--ELGGKEPG-QALGDAGRAmrdaeealgqgDLAGAVDAqgrALEALRKGAQQLAEAMQQQQGQGQQPG 761
|
90 100 110
....*....|....*....|....*....|....*.
gi 1080686173 608 PGPDMGAQ----------GGASDQGTKSDDHVTDAD 633
Cdd:pfam13779 762 QGGQGGRQagqdplgrplGGGGDFGDDEAVKVPDEI 797
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
323-375 |
6.40e-03 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 38.46 E-value: 6.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1080686173 323 LAPSDVDEVILVGGSTRIPAVQEMVAKIFGRePSKGVNPDEVVALGAAIQGGV 375
Cdd:pfam02782 144 QEGHPIDTIHVSGGGSRNPLLLQLLADALGL-PVVVPGPDEATALGAALLAAV 195
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
314-383 |
6.75e-03 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 39.46 E-value: 6.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080686173 314 VAQALKDAGlapSDVDEVILVGGSTRIPAVQEMVAKIFGREPSKgVNPDEVVALGAAIQGGVLSGDVKDV 383
Cdd:cd07770 380 IYEALEELA---GPVKEIRASGGFLRSPLWLQILADVLGRPVLV-PEEEEASALGAALLALEALGLISSL 445
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