|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-609 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1250.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 1 MGKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQV 80
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRRDEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 81 QKEINRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAG 160
Cdd:PRK00290 81 QKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 161 LNVRRIVNEPTAASLAYGLDKtNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFLR 240
Cdd:PRK00290 161 LEVLRIINEPTAAALAYGLDK-KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 241 EEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKD 320
Cdd:PRK00290 240 ENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 321 AGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETMGG 400
Cdd:PRK00290 320 AGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 401 VMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGILNV 480
Cdd:PRK00290 400 VMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 481 SAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTPIE 560
Cdd:PRK00290 480 SAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIE 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2486192116 561 TALNKLKEAHKAQDIAGIDAAMAELNSVFQAASQEMYNAQNAQGGAQPG 609
Cdd:PRK00290 560 AAIKELKEALKGEDKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGA 608
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-597 |
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: 1064.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 3 KIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQVQK 82
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDEVTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVrGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLN 162
Cdd:TIGR02350 81 EAKRVPYKVV-GDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 163 VRRIVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFLREE 242
Cdd:TIGR02350 160 VLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKKEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 243 GVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKDAG 322
Cdd:TIGR02350 240 GIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKDAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 323 LSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETMGGVM 402
Cdd:TIGR02350 320 LSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGVM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 403 TKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGILNVSA 482
Cdd:TIGR02350 400 TKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 483 KDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTPIETA 562
Cdd:TIGR02350 480 KDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKA 559
|
570 580 590
....*....|....*....|....*....|....*
gi 2486192116 563 LNKLKEAHKAQDIAGIDAAMAELNSVFQAASQEMY 597
Cdd:TIGR02350 560 VAELKEALKGEDVEEIKAKTEELQQALQKLAEAMY 594
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
4-597 |
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: 933.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQ 81
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPK-ERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSdpVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 82 KEINRVPYKVVRGDNNTPRVDIE--GRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:pfam00012 80 RDIKHLPYKVVKLPNGDAGVEVRylGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 160 GLNVRRIVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFL 239
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 240 REEGVDLRKDPMALQRLKEAAEKAKIELSSTtSTEINLPYIMpVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLK 319
Cdd:pfam00012 240 KKYGIDLSKDKRALQRLREAAEKAKIELSSN-QTNINLPFIT-AMADGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 320 DAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTG--EVKDVLLLDVTPLSLGIET 397
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIET 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 398 MGGVMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGI 477
Cdd:pfam00012 398 LGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 478 LNVSAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKT 557
Cdd:pfam00012 478 LTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKS 557
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2486192116 558 PIETALNKLKEAHKAQDIAGIDAAMAELNSVFQAASQEMY 597
Cdd:pfam00012 558 KVESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMY 597
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-603 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 913.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 1 MGKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQV 80
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 81 QKEINRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAG 160
Cdd:PRK13411 81 EEERSRVPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 161 LNVRRIVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFLR 240
Cdd:PRK13411 161 LEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 241 EEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKD 320
Cdd:PRK13411 241 QEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 321 AGLSTSDIDEVILVGGSTRIPAVQAIVEKFF-GKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETMG 399
Cdd:PRK13411 321 AGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 400 GVMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGILN 479
Cdd:PRK13411 401 EVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 480 VSAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTPI 559
Cdd:PRK13411 481 VSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRA 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2486192116 560 ETALNKLKEAHKAQDI--AGIDAAMAELNSVFQAASQEMYNAQNAQ 603
Cdd:PRK13411 561 EQKVEQLEAALTDPNIslEELKQQLEEFQQALLAIGAEVYQQGGSQ 606
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-611 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 901.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 1 MGKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQV 80
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 81 QKEINRVPYKVVRGDNNTPRVD--IEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:CHL00094 81 SEEAKQVSYKVKTDSNGNIKIEcpALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDKTNKDmKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDKKNNE-TILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 239 LREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSL 318
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 319 KDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETM 398
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 399 GGVMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGIL 478
Cdd:CHL00094 400 GGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 479 NVSAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTP 558
Cdd:CHL00094 480 SVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEK 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2486192116 559 IETALNKLKEAHKAQDIAGIDAAMAELNSVFQAASQEMYNAQNAQGGAQPGPD 611
Cdd:CHL00094 560 IENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYSSTSTTDPASNDDD 612
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-608 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 855.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 1 MGKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQV 80
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 81 QKEINRVPYKVVRGDNNTPRV--DIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:PRK13410 81 DPESKRVPYTIRRNEQGNVRIkcPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDKTNkDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 239 LREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSL 318
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 319 KDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETM 398
Cdd:PRK13410 320 KDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 399 GGVMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGIL 478
Cdd:PRK13410 400 GGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 479 NVSAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKD----LGDKLPAD 554
Cdd:PRK13410 480 QVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDaaleFGPYFAER 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2486192116 555 KKTPIETALNKLKEAHKAQDIAGIDAAMAELNSVFQAASQEMyNAQNAQGGAQP 608
Cdd:PRK13410 560 QRRAVESAMRDVQDSLEQDDDRELDLAVADLQEALYGLNREV-RAEYKEEDEGP 612
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-626 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 824.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 3 KIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQVQK 82
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSEVDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVRGDNNTPRVDIE--GRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAG 160
Cdd:PLN03184 120 ESKQVSYRVVRDENGNVKLDCPaiGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 161 LNVRRIVNEPTAASLAYGLDKTNKDMkIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFLR 240
Cdd:PLN03184 200 LEVLRIINEPTAASLAYGFEKKSNET-ILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 241 EEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKD 320
Cdd:PLN03184 279 DEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVENALRD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 321 AGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETMGG 400
Cdd:PLN03184 359 AKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLGLETLGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 401 VMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGILNV 480
Cdd:PLN03184 439 VMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSV 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 481 SAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTPIE 560
Cdd:PLN03184 519 SATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVE 598
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486192116 561 TALNKLKEAHKAQDIAGIDAAMAELNSVFQAASQEMYN-AQNAQGGAQPGPDFGQQAGGNAGNNKQD 626
Cdd:PLN03184 599 AKLKELKDAIASGSTQKMKDAMAALNQEVMQIGQSLYNqPGAGGAGPAPGGEAGSSSSSSSGGDGDD 665
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
2-611 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 804.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 2 GKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQ-- 79
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEda 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 80 VQKEINRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:PTZ00400 121 TKKEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 160 GLNVRRIVNEPTAASLAYGLDKtNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFL 239
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDK-NDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEFK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 240 REEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLK 319
Cdd:PTZ00400 280 KQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCEKCIK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 320 DAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETMG 399
Cdd:PTZ00400 360 DAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGIETLG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 400 GVMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGILN 479
Cdd:PTZ00400 440 GVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMN 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 480 VSAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTPI 559
Cdd:PTZ00400 520 ISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDEL 599
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2486192116 560 ETALNKLKEAHKAQDIAGIDAAMAELNSVFQAASQEMYNaQNAQGGAQPGPD 611
Cdd:PTZ00400 600 KQKITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYK-QGNSDNQQSEQS 650
|
|
| 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: 799.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDqvqke 83
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLF----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 84 inrvpykvvrgdnnTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNV 163
Cdd:COG0443 76 --------------DEATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 164 RRIVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFLREEG 243
Cdd:COG0443 142 LRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEEG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 244 VDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYimpvnGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKDAGL 323
Cdd:COG0443 222 IDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 324 STSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDvllLDVTPLSLGIETMGGVMT 403
Cdd:COG0443 297 SPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIETLGGVFT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 404 KLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGILNVSAK 483
Cdd:COG0443 374 KLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAK 453
|
490 500
....*....|....*....|....*..
gi 2486192116 484 DKGTGKVQSIRIeassglsDDEVKRMK 510
Cdd:COG0443 454 DLGTGKEQSITI-------KEEIERML 473
|
|
| 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: 741.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQVQKE 83
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 84 INRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNV 163
Cdd:cd10234 81 RKQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 164 RRIVNEPTAASLAYGLDKtNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFLREEG 243
Cdd:cd10234 161 LRIINEPTAAALAYGLDK-KKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 244 VDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKDAGL 323
Cdd:cd10234 240 IDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAKL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2486192116 324 STSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLT 377
Cdd:cd10234 320 SPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
2-618 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 702.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 2 GKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFvEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--Q 79
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAF-KGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEdeH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 80 VQKEINRVPYKVVRGDNNTPRV-DIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGNGDAWVqDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDKTnKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:PTZ00186 186 AGLNVIRVVNEPTAAALAYGMDKT-KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 239 LREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSL 318
Cdd:PTZ00186 265 RKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPCKQCM 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 319 KDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETM 398
Cdd:PTZ00186 345 KDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLGIETL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 399 GGVMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGIL 478
Cdd:PTZ00186 425 GGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGIC 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 479 NVSAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTp 558
Cdd:PTZ00186 505 HVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSDAEKEN- 583
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 559 IETALNKLKEAHKAQDIAGIDAAMAE---LNSVFQAASQEMYNAQNAQGGA-------QPGPDFGQQAGG 618
Cdd:PTZ00186 584 VKTLVAELRKAMENPNVAKDDLAAATdklQKAVMECGRTEYQQAAAANSGSssnsgeqQQQQQQQQQQNS 653
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-621 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 635.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQ--VQK 82
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDsvVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVRGDNNTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:PTZ00009 86 DMKHWPFKVTTGGDDKPMIEVtyqgEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDKTNK-DMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEE 237
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKGDgEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 238 FLRE-EGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMpvNGVPKHLvkTLTRAKFEQLADSLIQACIEPCRQ 316
Cdd:PTZ00009 246 FKRKnRGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLF--EGIDYNV--TISRARFEELCGDYFRNTLQPVEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 317 SLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFF-GKAPSKGVNPDEVVAVGAAIQGGVLTGE----VKDVLLLDVTPL 391
Cdd:PTZ00009 322 VLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLDVTPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 392 SLGIETMGGVMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFD 471
Cdd:PTZ00009 402 SLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 472 IDANGILNVSAKDKGTGKVQSIRIEASSG-LSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKD--LG 548
Cdd:PTZ00009 482 IDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDekVK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 549 DKLPADKKTPIETA-------LNKLKEAHKAQdiagIDAAMAELNSVFQAASQEMYNAQ--NAQGGAQPGPDFGQQAGGN 619
Cdd:PTZ00009 562 GKLSDSDKATIEKAidealewLEKNQLAEKEE----FEHKQKEVESVCNPIMTKMYQAAggGMPGGMPGGMPGGMPGGAG 637
|
..
gi 2486192116 620 AG 621
Cdd:PTZ00009 638 PA 639
|
|
| 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: 633.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 2 GKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--Q 79
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDdpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 80 VQKEINRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:cd11733 81 VQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 160 GLNVRRIVNEPTAASLAYGLDKTnKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFL 239
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKK-DDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 240 REEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLK 319
Cdd:cd11733 240 KEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2486192116 320 DAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVL 376
Cdd:cd11733 320 DAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-596 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 627.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGeRKVGDPAKRQAITNPEKTIFSIKRFMGETYDQVQKEI 84
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLADIQQRY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 85 NRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNVR 164
Cdd:PRK05183 101 PHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 165 RIVNEPTAASLAYGLDKtNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEflreEGV 244
Cdd:PRK05183 181 RLLNEPTAAAIAYGLDS-GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQ----AGL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 245 DLRKDPMALQRLKEAAEKAKIELSSTTSTEINlpyIMPVNGvpkhlvkTLTRAKFEQLADSLIQACIEPCRQSLKDAGLS 324
Cdd:PRK05183 256 SPRLDPEDQRLLLDAARAAKEALSDADSVEVS---VALWQG-------EITREQFNALIAPLVKRTLLACRRALRDAGVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 325 TSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTG--EVKDVLLLDVTPLSLGIETMGGVM 402
Cdd:PRK05183 326 ADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGnkPDSDMLLLDVIPLSLGLETMGGLV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 403 TKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGILNVSA 482
Cdd:PRK05183 406 EKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVTA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 483 KDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTPIETA 562
Cdd:PRK05183 486 MEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERAAIDAA 565
|
570 580 590
....*....|....*....|....*....|....*
gi 2486192116 563 LNKLKEAHKAQDIAGIDAAMAELNSVFQA-ASQEM 596
Cdd:PRK05183 566 MAALREVAQGDDADAIEAAIKALDKATQEfAARRM 600
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
4-588 |
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: 613.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQVqKE 83
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDI-KT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 84 INRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNV 163
Cdd:TIGR01991 80 FSILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 164 RRIVNEPTAASLAYGLDKtNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWlaeeFLREEG 243
Cdd:TIGR01991 160 LRLLNEPTAAAVAYGLDK-ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKW----ILKQLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 244 VDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPyimpVNGvpKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKDAGL 323
Cdd:TIGR01991 235 ISADLNPEDQRLLLQAARAAKEALTDAESVEVDFT----LDG--KDFKGKLTRDEFEALIQPLVQKTLSICRRALRDAGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 324 STSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEV--KDVLLLDVTPLSLGIETMGGV 401
Cdd:TIGR01991 309 SVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRigNDLLLLDVTPLSLGIETMGGL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 402 MTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGILNVS 481
Cdd:TIGR01991 389 VEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTVS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 482 AKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTPIET 561
Cdd:TIGR01991 469 AQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAIDA 548
|
570 580
....*....|....*....|....*..
gi 2486192116 562 ALNKLKEAHKAQDIAGIDAAMAELNSV 588
Cdd:TIGR01991 549 AMEALQKALQGDDADAIKAAIEALEEA 575
|
|
| 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: 558.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 2 GKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--Q 79
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDdaE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 80 VQKEINRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 160 GLNVRRIVNEPTAASLAYGLDKTNkDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFL 239
Cdd:cd11734 161 GLNVLRVINEPTAAALAYGLDKSG-DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 240 REEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLK 319
Cdd:cd11734 240 KESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486192116 320 DAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTG 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: 531.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQ 81
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDG-ERLVGEAAKNQAASNPENTIFDVKRLIGRKFDdpSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 82 KEINRVPYKVVRGDNNTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd24028 80 SDIKHWPFKVVEDEDGKPKIEVtykgEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 158 IAGLNVRRIVNEPTAASLAYGLDKTNKDMK-IAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAE 236
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDKKSSGERnVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 237 EFLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMpvNGVPKHLvkTLTRAKFEQLADSLIQACIEPCRQ 316
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLY--DGIDFET--TITRAKFEELCEDLFKKCLEPVEK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486192116 317 SLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFF-GKAPSKGVNPDEVVAVGAAIQGGVL 376
Cdd:cd24028 316 VLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
2-376 |
0e+00 |
|
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 518.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 2 GKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--Q 79
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDG-ERLIGDAAKNQATSNPENTVFDVKRLIGRKFDdkE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 80 VQKEINRVPYKVVRgDNNTP--RVDIEG--RLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEA 155
Cdd:cd10241 80 VQKDIKLLPFKIVN-KNGKPyiQVEVKGekKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 156 GEIAGLNVRRIVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLA 235
Cdd:cd10241 159 GTIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 236 EEFLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMpvNGVpkHLVKTLTRAKFEQLADSLIQACIEPCR 315
Cdd:cd10241 239 KLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLF--DGE--DFSETLTRAKFEELNMDLFRKTLKPVQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486192116 316 QSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFF-GKAPSKGVNPDEVVAVGAAIQGGVL 376
Cdd:cd10241 315 KVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
1-378 |
1.30e-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: 502.90 E-value: 1.30e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 1 MGKIIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQV 80
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 81 QKEINRVPYKVVRGDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAG 160
Cdd:cd10236 81 KEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 161 LNVRRIVNEPTAASLAYGLDKtNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWlaeeFLR 240
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQ-KKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADW----ILK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 241 EEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLpyimPVNGVPKHlvKTLTRAKFEQLADSLIQACIEPCRQSLKD 320
Cdd:cd10236 236 QIGIDARLDPAVQQALLQAARRAKEALSDADSASIEV----EVEGKDWE--REITREEFEELIQPLVKRTLEPCRRALKD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2486192116 321 AGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTG 378
Cdd:cd10236 310 AGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
5-376 |
4.21e-162 |
|
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: 467.82 E-value: 4.21e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEP-VVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGetydqvqke 83
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAeVIIENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 84 inrvpykvvrgDNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNV 163
Cdd:cd24029 72 -----------RDTKDKEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 164 RRIVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEFLREEG 243
Cdd:cd24029 141 LRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 244 V-DLRKDPMALQRLKEAAEKAKIELSSTTSTEInlpyIMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKDAG 322
Cdd:cd24029 221 IlDDKEDERARARLREAAEEAKIELSSSDSTDI----LILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKDAK 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2486192116 323 LSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVL 376
Cdd:cd24029 297 LSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
5-376 |
6.66e-160 |
|
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: 463.25 E-value: 6.66e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQK 82
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDdpVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVRGDNnTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd10233 81 DMKHWPFKVVSGGD-KPKIQVeykgETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDK-TNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEE 237
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDKkGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 238 FLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYImpVNGVpkHLVKTLTRAKFEQLADSLIQACIEPCRQS 317
Cdd:cd10233 240 FKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSL--FEGI--DFYTSITRARFEELCADLFRSTLEPVEKV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 318 LKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFF-GKAPSKGVNPDEVVAVGAAIQGGVL 376
Cdd:cd10233 316 LRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
5-376 |
6.94e-141 |
|
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466943 [Multi-domain] Cd Length: 375 Bit Score: 414.77 E-value: 6.94e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVvIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQK 82
Cdd:cd24093 2 IGIDLGTTYSCVATYESSVEI-IANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDdeSVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVrGDNNTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd24093 80 DMKTWPFKVI-DVNGNPVIEVqylgETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLD--KTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAE 236
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 237 EFLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMpvNGvpKHLVKTLTRAKFEQLADSLIQACIEPCRQ 316
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLF--DG--EDFESSITRARFEDLNAALFKSTLEPVEQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486192116 317 SLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFF-GKAPSKGVNPDEVVAVGAAIQGGVL 376
Cdd:cd24093 315 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
5-378 |
8.67e-136 |
|
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: 400.47 E-value: 8.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETydqvqkei 84
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMGTD-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 85 nrvpyKVVRgdnntprvdIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNVR 164
Cdd:cd10235 73 -----KQYR---------LGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 165 RIVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWlaeeFLREEGV 244
Cdd:cd10235 139 RLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADY----FLKKHRL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 245 D-LRKDPMALQRLKEAAEKAKIELSSTTSTEinlpyiMPVNGVPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKDAGL 323
Cdd:cd10235 215 DfTSLSPSELAALRKRAEQAKRQLSSQDSAE------IRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAGL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2486192116 324 STSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTG 378
Cdd:cd10235 289 KPSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
5-598 |
6.94e-126 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 384.21 E-value: 6.94e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGGerkvgdpakrqAITNPEKTIFSIKRFMGETYdqvqKEI 84
Cdd:PRK01433 22 VGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN-----------FTIGNNKGLRSIKRLFGKTL----KEI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 85 NRVP--YKVVRG----DNNTPRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:PRK01433 87 LNTPalFSLVKDyldvNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDKtNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:PRK01433 167 AGFEVLRLIAEPTAAAYAYGLNK-NQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNKF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 239 lreegvDLRKDPMALQrlkeAAEKAKIELSSTTSTEINLPYImpvngvpkhlvktlTRAKFEQLADSLIQACIEPCRQSL 318
Cdd:PRK01433 246 ------DLPNSIDTLQ----LAKKAKETLTYKDSFNNDNISI--------------NKQTLEQLILPLVERTINIAQECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 319 KDAGlsTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTGEVKDVLLLDVTPLSLGIETM 398
Cdd:PRK01433 302 EQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGMELY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 399 GGVMTKLIEANTTIPTKKSETFTTAVDNQPSVEIHVLQGERSLAKDNKSIGRFHLDGIPAAQRGVPQIEVTFDIDANGIL 478
Cdd:PRK01433 380 GGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGIL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 479 NVSAKDKGTGKVQSIRIEASSGLSDDEVKRMKEEAQANAEADKKEKERIDKLNQADSMIFQTEKQLKDLGDKLPADKKTP 558
Cdd:PRK01433 460 SVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISI 539
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2486192116 559 IETALNKLKEAHKAQDIAGIDAAMAELNSVFQAASQEMYN 598
Cdd:PRK01433 540 INSLLDNIKEAVHARDIILINNSIKEFKSKIKKSMDTKLN 579
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-378 |
4.80e-120 |
|
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: 362.43 E-value: 4.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 3 KIIGIDLGTTNSCVAVLEG--NEPVVIANSEGKRTTPSIVAFVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQ- 79
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 80 -VQKEINRVPYKVVRGDNNT----PRVDIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKE 154
Cdd:cd10237 103 eLEEEAKRYPFKVVNDNIGSaffeVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 155 AGEIAGLNVRRIVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWL 234
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 235 AEEFLREEGVDLrKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHLVK-TLTRAKFEQLADSLIQACIEP 313
Cdd:cd10237 263 IDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKFKeEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486192116 314 CRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLTG 378
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-376 |
6.70e-105 |
|
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: 322.27 E-value: 6.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQK 82
Cdd:cd10238 3 FGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDN-EKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDdpAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVRGDNNtPRVDIE----GRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd10238 82 LKKESKCKIIEKDGK-PGYEIEleekKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDKTNKDMK--IAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAE 236
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPTENsnVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 237 EFLREEGVDLRKDPMALQRLKEAAEKAKIELSsTTSTEInlpyimpvngvpkHLVKTL----------TRAKFEQLADSL 306
Cdd:cd10238 241 EFKRQWKQDVRENKRAMAKLMNAAEVCKHVLS-TLNTAT-------------CSVESLydgmdfqcnvSRARFESLCSSL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486192116 307 IQACIEPCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFF-GKAPSKGVNPDEVVAVGAAIQGGVL 376
Cdd:cd10238 307 FQQCLEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
5-372 |
1.94e-103 |
|
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: 318.35 E-value: 1.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQK 82
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEK-ERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDdpEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVRGDNNTP--RVDIEG--RLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd11732 80 EIKLLPFKLVELEDGKVgiEVSYNGeeVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDKTN------KDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIID 232
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSDlleseeKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 233 WLAEEFLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMP---VNGVpkhlvktLTRAKFEQLADSLIQA 309
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEdidFSGQ-------IKREEFEELIQPLLAR 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486192116 310 CIEPCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQ 372
Cdd:cd11732 313 LEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQ 375
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
4-376 |
2.53e-100 |
|
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: 310.78 E-value: 2.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQ 81
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEK-QRFLGEAAAASILMNPKNTISQLKRLIGRKFDdpEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 82 KEINRVPYKVVRGDNNTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd24095 82 RDLKLFPFKVTEGPDGEIGINVnylgEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 158 IAGLNVRRIVNEPTAASLAYGLDKT----NKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDW 233
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGIYKTdlpeTDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 234 LAEEFLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMP---VNGVpkhlvktLTRAKFEQLADSLIQAC 310
Cdd:cd24095 242 FAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEdkdVKGM-------ITREEFEELAAPLLERL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486192116 311 IEPCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVL 376
Cdd:cd24095 315 LEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
5-372 |
1.10e-96 |
|
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: 301.12 E-value: 1.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQK 82
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEK-NRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDdpFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVRGDNNTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEI 158
Cdd:cd10228 80 ELKHLPYKVVKLPNGSVGIKVqylgEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 159 AGLNVRRIVNEPTAASLAYGLDKTN------KDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIID 232
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGIYKQDlpaeeeKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 233 WLAEEFLREEGVDLRKDPMALQRLKEAAEKAKiELSSTTSTEI--NLPYIM---PVNGvpkhlvkTLTRAKFEQLADSLI 307
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATELplNIECFMddkDVSG-------KMKRAEFEELCAPLF 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486192116 308 QACIEPCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQ 372
Cdd:cd10228 312 ARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
5-377 |
1.00e-86 |
|
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: 275.41 E-value: 1.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFVEGgERKVGDPAKRQAITNPEKTIFSIKRFMGETYD--QVQK 82
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPK-SRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSdpEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 EINRVPYKVVRGDNNT-PRVDIEG--RLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIA 159
Cdd:cd24094 80 EEKYFTAKLVDANGEVgAEVNYLGekHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 160 GLNVRRIVNEPTAASLAYGLDKTN------KDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDW 233
Cdd:cd24094 160 GLNPLRLMNDTTAAALGYGITKTDlpepeeKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 234 LAEEFLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVNGVPKHlvktLTRAKFEQLADSLIQACIEP 313
Cdd:cd24094 240 FADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSM----LKREEFEELIAPLLERVTAP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486192116 314 CRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLT 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 |
1.56e-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: 265.90 E-value: 1.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIA-NSEGKRTTPSIVAFvEGGERKVGDPAKRQAITNPEKTIFSIKRFMGetydqvqk 82
Cdd:cd10230 2 VLGIDLGSEFIKVALVKPGVPFEIVlNEESKRKTPSAVAF-RNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 einrvpykvvrgdnntprvdiegrlYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLN 162
Cdd:cd10230 73 -------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 163 VRRIVNEPTAASLAYGLDKT---NKDMKIAVFDLGGGT-----FDISILELGDG-------VFEVKSTNGDTHLGGDDFD 227
Cdd:cd10230 128 VLSLINDNTAAALNYGIDRRfenNEPQNVLFYDMGASStsatvVEFSSVKEKDKgknktvpQVEVLGVGWDRTLGGLEFD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 228 HVIIDWLAEEFLRE--EGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINlpyimpVNGvpkhLVK------TLTRAKF 299
Cdd:cd10230 208 LRLADHLADEFNEKhkKDKDVRTNPRAMAKLLKEANRVKEVLSANTEAPAS------IES----LYDdidfrtKITREEF 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486192116 300 EQLADSLIQACIEPCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAP-SKGVNPDEVVAVGAAIQG 373
Cdd:cd10230 278 EELCADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-376 |
2.78e-78 |
|
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: 252.28 E-value: 2.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVL-EGNEPVVIANSEGKRTTPSIVAFVeGGERKVGDPAKRQAITNPEKTIFSIKRFMGETydqvqk 82
Cdd:cd10232 2 VIGISFGNSNSSIAIInKDGRAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLGTT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 einrvpykvvrgdnntprvdiegrLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLN 162
Cdd:cd10232 75 ------------------------TLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 163 VRRIVNEPTAASLAYGLDK-----TNKDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVIIDWLAEE 237
Cdd:cd10232 131 VLQLIPEPAAAALAYDLRAetsgdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAKE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 238 FLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYImpVNGVPKHLvkTLTRAKFEQLADSLIQACIEPCRQS 317
Cdd:cd10232 211 FKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESL--ADGIDFHS--SINRTRYELLASKVFQQFADLVTDA 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486192116 318 LKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSK----GVNPDEVVAVGAAIQGGVL 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 |
2.13e-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: 248.32 E-value: 2.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFvEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQ--VQ 81
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSF-GPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDpfVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 82 KEINRVPYKVVRGDNNTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd11737 81 AEKPSLAYELVQLPTGTTGIKVmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 158 IAGLNVRRIVNEPTAASLAYGLDKTN------KDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVII 231
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIYKQDlpapeeKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 232 DWLAEEFLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTST-EINLPYIMpvNGVpkHLVKTLTRAKFEQLADSLIQAC 310
Cdd:cd11737 241 NHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANASDlPLNIECFM--NDI--DVSGTMNRGQFEEMCADLLARV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486192116 311 IEPCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQ 372
Cdd:cd11737 317 EPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
4-372 |
1.63e-73 |
|
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: 240.92 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAFvEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQ--VQ 81
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSF-GSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDpfVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 82 KEINRVPYKVVRGDNNTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd11739 81 KEKENLSYDLVPLKNGGVGVKVmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 158 IAGLNVRRIVNEPTAASLAYGLDKTN-----KDMKIAVF-DLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVII 231
Cdd:cd11739 161 IVGLNCLRLMNDMTAVALNYGIYKQDlpapdEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 232 DWLAEEFLREEGVDLRKDPMALQRLKEAAEKAKiELSSTTSTEINLPYIMPVNGvpKHLVKTLTRAKFEQLADSLIQACI 311
Cdd:cd11739 241 EHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLPLNIECFMND--KDVSGKMNRSQFEELCADLLQRIE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486192116 312 EPCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQ 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 |
1.81e-73 |
|
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: 240.97 E-value: 1.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAfVEGGERKVGDPAKRQAITNPEKTIFSIKRFMGETYDQ--VQ 81
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVS-LGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDpfVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 82 KEINRVPYKVVRGDNNTPRVDI----EGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd11738 81 AEKIKLPYELQKMPNGSTGVKVryldEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 158 IAGLNVRRIVNEPTAASLAYGLDKTN------KDMKIAVFDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVII 231
Cdd:cd11738 161 IAGLNCLRLMNETTAVALAYGIYKQDlpaleeKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 232 DWLAEEFLREEGVDLRKDPMALQRLKEAAEKAKiELSSTTSTEINLPYIMPVNGVpkHLVKTLTRAKFEQLADSLIQACI 311
Cdd:cd11738 241 DYFCEEFKTKYKLNVKENIRALLRLYQECEKLK-KLMSANASDLPLNIECFMNDI--DVSSKMNRAQFEELCASLLARVE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486192116 312 EPCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAIQGGVLT 377
Cdd:cd11738 318 PPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
5-371 |
6.56e-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: 186.93 E-value: 6.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSivafvEGGERKVgdPAKRQAITnpektifsikRFMGETYDQVQKEI 84
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVVLQLPWPGG-----DGGSSKV--PSVLEVVA----------DFLRALLEHAKAEL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 85 nrvpykvvrgdnntprvdiegrlytpqeisamvlqkmkKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGL--- 161
Cdd:cd10170 64 --------------------------------------GDRIWELEKAPIEVVITVPAGWSDAAREALREAARAAGFgsd 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 162 -NVRRIVNEPTAASLAYGLDKTN-----KDMKIAVFDLGGGTFDISILELGDGVFEVK---STNGDTHLGGDDFDHVIID 232
Cdd:cd10170 106 sDNVRLVSEPEAAALYALEDKGDllplkPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALLGGTDIDEAFEK 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 233 WLAEEFLREEGVDLRKDPMALQRLKEAAEKAKIELSSTTSTEINLPYIMPvNGVPKHLVKTLTRAKFEQLADSLIQACIE 312
Cdd:cd10170 186 LLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLG-GGLPELGLEKGTLLLTEEEIRDLFDPVID 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486192116 313 PCRQSLKDAGLSTS--DIDEVILVGGSTRIPAVQAIVEKFFGKAPSKGV----NPDEVVAVGAAI 371
Cdd:cd10170 265 KILELIEEQLEAKSgtPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
5-370 |
1.60e-48 |
|
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: 174.77 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVLEGNEPVVIANSEGKRTTPSIVAF----VEGGERKV-GDPAKRQAITNPEKTIF--SIKRFMGEty 77
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFprreEEGAESIYfGNDAIDAYLNDPEEGRLikSVKSFLGS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 78 dqvqkeinrvpykvvRGDNNTPrvdIEGRLYTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd10231 79 ---------------SLFDETT---IFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDAQAES 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 158 I-------AGLNVRRIVNEPTAASLAYglDKTNKDMKIA-VFDLGGGTFDISILELG----DGVFEVKSTNGDtHLGGDD 225
Cdd:cd10231 141 RlrdaarrAGFRNVEFQYEPIAAALDY--EQRLDREELVlVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GIGGDD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 226 FDHVIID------------------------WLAEEFLREEGVDLRKDPMALQ--------------------------- 254
Cdd:cd10231 218 FDRELALkkvmphlgrgstyvsgdkglpvpaWLYADLSNWHAISLLYTKKTLRllldlrrdaadpekierllslvedqlg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 255 -RLKEAAEKAKIELSSTTSTEINLPYImpvngvPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKDAGLSTSDIDEVIL 333
Cdd:cd10231 298 hRLFRAVEQAKIALSSADEATLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFL 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 2486192116 334 VGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAA 370
Cdd:cd10231 372 TGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-378 |
1.09e-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: 82.33 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVL----EGNEPVVIANSEGK-----RTTPSIVAFVEGGE-RKVGDPAKRQAITNPEKTIFSIKRFM 73
Cdd:cd10229 2 VVAIDFGTTYSGYAYSfitdPGDIHTMYNWWGAPtgvssPKTPTCLLLNPDGEfHSFGYEAREKYSDLAEDEEHQWLYFF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 74 GETYDQVQKEINRVPYKVVrgDNNtprvdieGRLYTPQEISAMVLQKMKKTAEDYL----GQEVTEA----VITVPAYFS 145
Cdd:cd10229 82 KFKMMLLSEKELTRDTKVK--AVN-------GKSMPALEVFAEALRYLKDHALKELrdrsGSSLDEDdirwVLTVPAIWS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 146 DAQRQATKEAGEIAGLNVR------RIVNEPTAASLAYGLDKTNKDMKIA-------VFDLGGGTFDISILEL--GDGVF 210
Cdd:cd10229 153 DAAKQFMREAAVKAGLISEenseqlIIALEPEAAALYCQKLLAEGEEKELkpgdkylVVDCGGGTVDITVHEVleDGKLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 211 EV-KSTNGdtHLGGDDFDHVIIDWLaEEFLREEGVDL--RKDPMALQRLKEAAEKAKIelssTTSTEInlpyimpvngvP 287
Cdd:cd10229 233 ELlKASGG--PWGSTSVDEEFEELL-EEIFGDDFMEAfkQKYPSDYLDLLQAFERKKR----SFKLRL-----------S 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 288 KHLVKTLtrakFEQLADSLIQaCIepcRQSLKDAGLstSDIDEVILVGGSTRIPAVQAIVEKFFGKApSKGVNPDEVVAv 367
Cdd:cd10229 295 PELMKSL----FDPVVKKIIE-HI---KELLEKPEL--KGVDYIFLVGGFAESPYLQKAVKEAFSTK-VKIIIPPEPGL- 362
|
410
....*....|.
gi 2486192116 368 gAAIQGGVLTG 378
Cdd:cd10229 363 -AVVKGAVLFG 372
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
117-371 |
1.53e-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: 73.45 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 117 VLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNVRRIVNEPTAASLAYGLDKTnkdmkiAVFDLGGG 196
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG------AVVDIGGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 197 TFDISILELGDGVFEVKSTNGDTHLggddfDHVIIDWLAEEFlrEEGVDLRKDPmalqrlkeaaekakielssTTSTEIn 276
Cdd:cd24047 122 TTGIAVLKDGKVVYTADEPTGGTHL-----SLVLAGNYGISF--EEAEIIKRDP-------------------ARHKEL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 277 LPYIMPVngvpkhlvktltrakFEQLADSLiqaciepcRQSLKDAglstsDIDEVILVGGSTRIPAVQAIVEKFFGKAPS 356
Cdd:cd24047 175 LPVVRPV---------------IEKMASIV--------KRHIKGY-----KVKDLYLVGGTCCLPGIEEVFEKETGLPVY 226
|
250
....*....|....*
gi 2486192116 357 KGVNPDEVVAVGAAI 371
Cdd:cd24047 227 KPSNPLLVTPLGIAL 241
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
117-361 |
1.36e-13 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 71.40 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 117 VLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNVRRIVNEPTAASLAYGLDKTnkdmkiAVFDLGGG 196
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG------AVVDIGGG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 197 TFDISILELGDGVFEVKSTNGDTHlggddFDHVIIDWLAEEFlrEEGVDLRKDPMALQRLkeaaekakielssttstein 276
Cdd:PRK15080 146 TTGISILKDGKVVYSADEPTGGTH-----MSLVLAGAYGISF--EEAEQYKRDPKHHKEI-------------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 277 LPYIMPVngvpkhlvktltrakFEQLAdSLIQACIEpcrqslkdaglsTSDIDEVILVGGSTRIPAVQAIVEKFFGKAPS 356
Cdd:PRK15080 199 FPVVKPV---------------VEKMA-SIVARHIE------------GQDVEDIYLVGGTCCLPGFEEVFEKQTGLPVH 250
|
....*
gi 2486192116 357 KGVNP 361
Cdd:PRK15080 251 KPQHP 255
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
5-371 |
1.91e-13 |
|
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: 71.74 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVlEG-----NEPVVIANsegKRTTPSIVAfveggerkVGDPAKRqaitnpektifsikrFMGETYDQ 79
Cdd:cd10225 2 IGIDLGTANTLVYV-KGkgivlNEPSVVAV---DKNTGKVLA--------VGEEAKK---------------MLGRTPGN 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 80 VqkeinrvpyKVVRgdnntPRVD--IegrlyTPQEISAMVLQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGE 157
Cdd:cd10225 55 I---------VAIR-----PLRDgvI-----ADFEATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 158 IAGLNVRRIVNEPTAASLAYGLDKTNKD--MkiaVFDLGGGTFDISILELGdGVFEVKStngdTHLGGDDFDHVIIDwla 235
Cdd:cd10225 116 HAGAREVYLIEEPMAAAIGAGLPIEEPRgsM---VVDIGGGTTEIAVISLG-GIVTSRS----VRVAGDEMDEAIIN--- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 236 eeFLREE---GVDLRkdpmalqrlkeAAEKAKIELSSTTSTEINLpyIMPV------NGVPKHLvkTLTRAKFEQLADSL 306
Cdd:cd10225 185 --YVRRKynlLIGER-----------TAERIKIEIGSAYPLDEEL--SMEVrgrdlvTGLPRTI--EITSEEVREALEEP 247
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486192116 307 IQACIEPCRQSLKDAG--LStSDIDE--VILVGGSTRIPAV-QAIVEKFfgKAPSKGV-NPDEVVAVGAAI 371
Cdd:cd10225 248 VNAIVEAVRSTLERTPpeLA-ADIVDrgIVLTGGGALLRGLdELLREET--GLPVHVAdDPLTCVAKGAGK 315
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
110-355 |
5.18e-13 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 71.43 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 110 PQEIS-------AMvLQKMKKTAEDYLGQEVTEAVITVPAYFS-----DAQRQAT---KEAGEIAGLNVRRIVNEPTAAs 174
Cdd:PRK11678 120 PQQVAlfedlvcAM-MLHIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 175 layGLD---KTNKDMKIAVFDLGGGTFDISILELGDGvfEVKSTNGDTHL--------GGDDFD----------HVIID- 232
Cdd:PRK11678 198 ---GLDfeaTLTEEKRVLVVDIGGGTTDCSMLLMGPS--WRGRADRSASLlghsgqriGGNDLDialafkqlmpLLGMGs 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 233 -------------WLA---------EEFL----REEGVDLRKD---PMALQRLKE------------AAEKAKIELSSTT 271
Cdd:PRK11678 273 etekgialpslpfWNAvaindvpaqSDFYslanGRLLNDLIRDarePEKVARLLKvwrqrlsyrlvrSAEEAKIALSDQA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 272 STEINLPYImpvngvPKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKDAGLSTsdiDEVILVGGSTRIPAVQAIVEKFF 351
Cdd:PRK11678 353 ETRASLDFI------SDGLATEISQQGLEEAISQPLARILELVQLALDQAQVKP---DVIYLTGGSARSPLIRAALAQQL 423
|
....
gi 2486192116 352 GKAP 355
Cdd:PRK11678 424 PGIP 427
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-371 |
2.19e-10 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 62.40 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 1 MGKIIGIDLGTTNSCVAVleGNEPVVIanSEgkrttPSIVAFVEGGER--KVGDPAKRqaitnpektifsikrfMgetyd 78
Cdd:COG1077 6 FSKDIGIDLGTANTLVYV--KGKGIVL--NE-----PSVVAIDKKTGKvlAVGEEAKE----------------M----- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 79 qvqkeinrvpykvvrgdnntprvdiEGRlyTPQEISAM------VLQkmkktaeDYlgqEVTEA---------------- 136
Cdd:COG1077 56 -------------------------LGR--TPGNIVAIrplkdgVIA-------DF---EVTEAmlkyfikkvhgrrsff 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 137 ----VITVPAYFSDAQRQATKEAGEIAGlnVRRI--VNEPTAASLAYGLDKTNKD--MkiaVFDLGGGTFDISILELGDG 208
Cdd:COG1077 99 rprvVICVPSGITEVERRAVRDAAEQAG--AREVylIEEPMAAAIGAGLPIEEPTgnM---VVDIGGGTTEVAVISLGGI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 209 VFEvKStngdTHLGGDDFDHVIIDWLAEEFlreegvdlrkdpmalqRL---KEAAEKAKIELSSTTSTEINLPyiMPVNG 285
Cdd:COG1077 174 VVS-RS----IRVAGDELDEAIIQYVRKKY----------------NLligERTAEEIKIEIGSAYPLEEELT--MEVRG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 286 vpKHLV----KTLTrakfeqLADSLIQACIEPCRQSLKDAGLST---------SDIDE--VILVGGSTRIPAVQAIVEKF 350
Cdd:COG1077 231 --RDLVtglpKTIT------ITSEEIREALEEPLNAIVEAIKSVlektppelaADIVDrgIVLTGGGALLRGLDKLLSEE 302
|
410 420
....*....|....*....|....*
gi 2486192116 351 FG----KAPskgvNPDEVVAVGAAI 371
Cdd:COG1077 303 TGlpvhVAE----DPLTCVARGTGK 323
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-371 |
6.92e-10 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 60.92 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 1 MGKIIGIDLGTTNSCVA------VLegNEPVVIANsegKRTTPSIVAFVEGGERKVGD---------PAKRQAITNPEKT 65
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYvkgkgiVL--NEPSVVAI---DTKTGKVLAVGEEAKEMLGRtpgnieairPLKDGVIADFEAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 66 IFSIKRFMGetydqvqkeinrvpyKVVRGdnntprvdieGRLYTPqeisamvlqkmkktaedylgqevtEAVITVPAYFS 145
Cdd:PRK13930 82 EAMLRYFIK---------------KARGR----------RFFRKP------------------------RIVICVPSGIT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 146 DAQRQATKEAGEIAGLNVRRIVNEPTAASLAYGLD--KTNKDMkiaVFDLGGGTFDISILELGDGVfevksTNGDTHLGG 223
Cdd:PRK13930 113 EVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPvtEPVGNM---VVDIGGGTTEVAVISLGGIV-----YSESIRVAG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 224 DDFDHVIIDWLAEEFlreegvdlrkdpmalqRL---KEAAEKAKIELSSTTSTEinLPYIMPVNGvpKHLVKTLtrAKFE 300
Cdd:PRK13930 185 DEMDEAIVQYVRRKY----------------NLligERTAEEIKIEIGSAYPLD--EEESMEVRG--RDLVTGL--PKTI 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 301 QLADSLIQACIEPCRQSLKDAGLST---------SDIDE--VILVGGS-------------TRIPAVqaIVEkffgkaps 356
Cdd:PRK13930 243 EISSEEVREALAEPLQQIVEAVKSVlektppelaADIIDrgIVLTGGGallrgldkllseeTGLPVH--IAE-------- 312
|
410
....*....|....*
gi 2486192116 357 kgvNPDEVVAVGAAI 371
Cdd:PRK13930 313 ---DPLTCVARGTGK 324
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
115-352 |
2.34e-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: 58.84 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 115 AMVLQKMKKTAEDYLGQEVTEAVITVP----AYFSDAQRqatkeageiAGLNVRRIVNEPTAASLAYGLDKTnKDMKIAV 190
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPFAAANLLIPYDM-RDLNIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 191 FDLGGGTFDISILELGdGVFEVkstnGDTHLGGDDFdhviIDWLAEEFLreegVDLrkdpmalqrlkEAAEKAKIELSST 270
Cdd:cd24004 119 VDIGAGTTDIALIRNG-GIEAY----RMVPLGGDDF----TKAIAEGFL----ISF-----------EEAEKIKRTYGIF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 271 TSTEINLPYIMPVNgvpKHLVKTLTRAKFEQLADSLIQACIEPCRQSLKdaglstsdIDEVILVGGSTRIPAVQAIVEKF 350
Cdd:cd24004 175 LLIEAKDQLGFTIN---KKEVYDIIKPVLEELASGIANAIEEYNGKFKL--------PDAVYLVGGGSKLPGLNEALAEK 243
|
..
gi 2486192116 351 FG 352
Cdd:cd24004 244 LG 245
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
4-382 |
2.96e-09 |
|
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: 59.08 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLE---GNEPVVIANSegkrTTPSivafvEGgerkvgdpAKRQAITNPEKTIFSIKRFMGETYDQV 80
Cdd:cd24048 3 IVGLDIGTSKICALVGEvseDGELEVIGVG----TVPS-----RG--------IKKGVIVDLEEAVESIRKAIEEAERMA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 81 QKEINRV----PYKVVRGDNNTPRVDIEGRLY-TPQEISAmVLQKMKKTA------------EDYL--GQEVT------- 134
Cdd:cd24048 66 GVKIDSVyvgiSGKHIRSVNSRGVIAISDKDEiTEEDVER-VIEAAKAVAlpedreilhvipQEYIvdGQDGIkdpvgms 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 135 ----EA---VITVPAyfsdAQRQATKEAGEIAGLNVRRIVNEPTAASLAYgLDKTNKDMKIAVFDLGGGTFDISILElgD 207
Cdd:cd24048 145 gsrlEVdvhVITGSS----SAIQNLIKCVERAGLEVDDIVLSPLASAEAV-LTEDEKELGVALIDIGGGTTDIAVFK--N 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 208 GVFEvkstngDTH---LGGddfDHVIIDwLAeeflreegvdlrkdpMALQRLKEAAEKAKIELSSTTSTEINLPYIMPVN 284
Cdd:cd24048 218 GSLR------YTAvipVGG---NHITND-IA---------------IGLNTPFEEAERLKIKYGSALSEEADEDEIIEIP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 285 GVPKHLVKTLTRAkfeQLADsLIQACIEP----CRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGKApskgvn 360
Cdd:cd24048 273 GVGGREPREVSRR---ELAE-IIEARVEEilelVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGMP------ 342
|
410 420
....*....|....*....|..
gi 2486192116 361 pdevVAVGAAIQGGVLTGEVKD 382
Cdd:cd24048 343 ----VRIGRPKNIGGLPEEVND 360
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
4-353 |
3.86e-09 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 58.99 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEP-------VVIANSEGkrttpsivafVEGGErkvgdpakrqaITNPEKTIFSIKRFMGET 76
Cdd:COG0849 6 IVGLDIGTSKVVALVGEVDPDgklevigVGEAPSRG----------VKKGV-----------IVDIEATVEAIRKAVEEA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 77 YDQVQKEINRVpykVV-------RGDNNTPRVDIEGRLYTPQEISAmVLQKMKKTA--EDY------------------- 128
Cdd:COG0849 65 ERMAGVKIESV---YVgisgghiKSQNSRGVVAISGREITEEDVDR-VLEAARAVAipPDReilhvlpqefivdgqegik 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 129 --LGQ-----EVTEAVITVPAyfsdAQRQATKEAGEIAGLNVRRIVNEPTAASLAYgLDKTNKDMKIAVFDLGGGTFDIS 201
Cdd:COG0849 141 dpVGMsgvrlEVDVHIVTGPK----TAVQNLVKCVERAGLEVEDLVLSPLASAEAV-LTEDEKELGVALVDIGGGTTDIA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 202 ILELGD----GVFEVkstngdthlGGddfDHVIIDwLAeeflreegvdlrkdpMALQRLKEAAEKAKIELSSTTSTEINL 277
Cdd:COG0849 216 VFKDGAlrhtAVIPV---------GG---DHITND-IA---------------IGLRTPLEEAERLKIKYGSALASLADE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 278 PYIMPVNGVPKHLVKTLTRAkfeQLADSlIQACIE----PCRQSLKDAGLSTSDIDEVILVGGSTRIPAVQAIVEKFFGK 353
Cdd:COG0849 268 DETIEVPGIGGRPPREISRK---ELAEI-IEARVEeifeLVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILGL 343
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
5-371 |
4.12e-09 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 58.34 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVlEG-----NEPVVIANsegKRTTPSIVAfveggerkVGDPAKRqaitnpektifsikrFMGETYDQ 79
Cdd:pfam06723 4 IGIDLGTANTLVYV-KGkgivlNEPSVVAI---NTKTKKVLA--------VGNEAKK---------------MLGRTPGN 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 80 VqkeinrvpyKVVRGDNNTPRVDIEgrlytpqeisamVLQKMKKtaedYLGQEVTEA--------VITVPAYFSDAQRQA 151
Cdd:pfam06723 57 I---------VAVRPLKDGVIADFE------------VTEAMLK----YFIKKVHGRrsfskprvVICVPSGITEVERRA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 152 TKEAGEIAGLNVRRIVNEPTAASLAYGLD--KTNKDMkiaVFDLGGGTFDISILELGDGVfevksTNGDTHLGGDDFDHV 229
Cdd:pfam06723 112 VKEAAKNAGAREVFLIEEPMAAAIGAGLPveEPTGNM---VVDIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFDEA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 230 IIDWLAEEFLREEGVdlrkdpmalqrlkEAAEKAKIELSSTTSTEINLPYIMP----VNGVPKHLvktltRAKFEQLADS 305
Cdd:pfam06723 184 IIKYIRKKYNLLIGE-------------RTAERIKIEIGSAYPTEEEEKMEIRgrdlVTGLPKTI-----EISSEEVREA 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486192116 306 L---IQACIEPCRQSLKD--AGLStSDIDE--VILVGGSTRIPAVQAIVEKFFGKAPSKGVNPDEVVAVGAAI 371
Cdd:pfam06723 246 LkepVSAIVEAVKEVLEKtpPELA-ADIVDrgIVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
137-238 |
4.51e-08 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 55.29 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 137 VITVPAYFSDAQRQATKEAGEIAGLNVRRIVNEPTAASLAYGLD--KTNKDMkiaVFDLGGGTFDISILELGDGVfevks 214
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDisQPSGNM---VVDIGGGTTDIAVLSLGGIV----- 170
|
90 100
....*....|....*....|....
gi 2486192116 215 TNGDTHLGGDDFDHVIIDWLAEEF 238
Cdd:PRK13928 171 TSSSIKVAGDKFDEAIIRYIRKKY 194
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
4-378 |
1.33e-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: 51.16 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 4 IIGIDLGTTNSCVAVLEGNEPVVIansegkrttpSIVAFVEGGERKVGDPAKRQAIT-NPEKTIFSIKRFMGETYDQVQK 82
Cdd:cd11735 2 VVAIDFGTTSSGYAYSFTKEPECI----------HVMRRWEGGDPGVSNQKTPTTILlTPERKFHSFGYAARDFYHDLDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 83 E-------INRVPYKVVRGDNNTPRVDIE---GRLYTPQEISAMVLQKMKKTA----EDYLGQEVTEA----VITVPAYF 144
Cdd:cd11735 72 NeskqwlyFEKFKMKLHTTGNLTMETDLTaanGKKVKALEIFAYALQFFKEQAlkelSDQAGSEFDNSdvrwVITVPAIW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 145 SDAQRQATKEAGEIAGLNVRR------IVNEPTAASLAYGLDKTNKDMKIAVFDLGGGTFDISI--LELGDGVFE--VKS 214
Cdd:cd11735 152 KQPAKQFMRQAAYKAGLASPEnpeqliIALEPEAASIYCRKLRLHQMDRYVVVDCGGGTVDLTVhqIRLPEGHLKelYKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 215 TNGD-THLGGD-DFDHVIIDWLAEEFLREEGVdlrKDPMALQRLKEAAEKAKIELS--STTSTEINLP--YIMPVNGVPK 288
Cdd:cd11735 232 SGGPyGSLGVDyEFEKLLCKIFGEDFIDQFKI---KRPAAWVDLMIAFESRKRAAApdRTNPLNITLPfsFIDYYKKFRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 289 HLVKTLTR---AKFEQLA------------DSLIQACIEPCRQSLKD--AGLSTSDIDEVILVGGSTRIPAVQAIVEKFF 351
Cdd:cd11735 309 HSVEHALRksnVDFVKWSsqgmlrmspdamNALFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAESPLLQQAVQNAF 388
|
410 420
....*....|....*....|....*...
gi 2486192116 352 GKApSKGVNPDEvvaVGAAI-QGGVLTG 378
Cdd:cd11735 389 GDQ-CRVIIPHD---VGLTIlKGAVLFG 412
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
112-368 |
1.50e-06 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 50.68 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 112 EISAMVLQKMKKTAEDYLGQEVTE--AVITVPAYFSDAQRQATKEAGEIAGLNVRRIVNEPTAASLAYGLdKTNKDMKIA 189
Cdd:PRK13929 75 DMTTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADL-PVDEPVANV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 190 VFDLGGGTFDISILELGdGVFEVKStngdTHLGGDDFDHVIIDWLAEEFLREEGvdlrkdpmalqrlKEAAEKAKIELS- 268
Cdd:PRK13929 154 VVDIGGGTTEVAIISFG-GVVSCHS----IRIGGDQLDEDIVSFVRKKYNLLIG-------------ERTAEQVKMEIGy 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 269 -----STTSTEINLPYImpVNGVPKHLvkTLTRAKFEQ-LADSLIQAcIEPCRQSLKDA--GLSTSDIDE-VILVGGSTR 339
Cdd:PRK13929 216 aliehEPETMEVRGRDL--VTGLPKTI--TLESKEIQGaMRESLLHI-LEAIRATLEDCppELSGDIVDRgVILTGGGAL 290
|
250 260
....*....|....*....|....*....
gi 2486192116 340 IPAVQAIVEKFFGKAPSKGVNPDEVVAVG 368
Cdd:PRK13929 291 LNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
118-378 |
6.32e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 48.81 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 118 LQKMKKTAEDYLGQEVTEAVITVPAYFSDAQRQATKEAGEIAGLNVRR------IVNEPTAASL-AYGLDktnkdmKIAV 190
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLVSPEnpeqllIALEPEAASIyCRKLD------RYIV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 191 FDLGGGTFDISI--LELGDGVFE--VKSTNGDTHLGGDD--FDHVIIDWLAEEFLREEGvdlRKDPMALQRLKEAAEKAK 264
Cdd:cd11736 199 ADCGGGTVDLTVhqIEQPQGTLKelYKASGGPYGAVGVDlaFEKLLCQIFGEDFIATFK---AKRPAAWVDLTIAFEARK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 265 ----IELSSTTSTEINLPYImpvNGVPKHLvktltrakfeqlaDSLIQaciEPCRQSLKdaglstsdidEVILVGGSTRI 340
Cdd:cd11736 276 rtaaLRMSSEAMNELFQPTI---SQIIQHI-------------DDLMK---KPEVKGIK----------FLFLVGGFAES 326
|
250 260 270
....*....|....*....|....*....|....*....
gi 2486192116 341 PAVQAIVEKFFGKApSKGVNPDEvvaVGAAI-QGGVLTG 378
Cdd:cd11736 327 PMLQRAVQAAFGNI-CRVIIPQD---VGLTIlKGAVLFG 361
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
231-383 |
5.95e-05 |
|
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: 45.98 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 231 IDWLAEEFLREEGVDLrkdpmalQRLKEAAEKAKIelssTTSTEINLPYIM----PVN-----GV---------PKHLVk 292
Cdd:COG1070 304 LRWFRDLFADGELDDY-------EELNALAAEVPP----GADGLLFLPYLSgertPHWdpnarGAffgltlshtRAHLA- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 293 tltRAKFE----QLADSLiqaciepcrQSLKDAGLstsDIDEVILVGGSTRIPAVQAIVEKFFGKaPSKGVNPDEVVAVG 368
Cdd:COG1070 372 ---RAVLEgvafALRDGL---------EALEEAGV---KIDRIRATGGGARSPLWRQILADVLGR-PVEVPEAEEGGALG 435
|
170
....*....|....*
gi 2486192116 369 AAIQGGVLTGEVKDV 383
Cdd:COG1070 436 AALLAAVGLGLYDDL 450
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
5-238 |
7.23e-05 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 45.47 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 5 IGIDLGTTNSCVAVlEG-----NEPVVIANsegKRTTPSIVAfveggerkVGDPAKRQAitnpEKTIFSIK--RFMGE-- 75
Cdd:PRK13927 8 LGIDLGTANTLVYV-KGkgivlNEPSVVAI---RTDTKKVLA--------VGEEAKQML----GRTPGNIVaiRPMKDgv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 76 --TYDQVQKEINRVPYKVVRGDNNTPRVdiegrlytpqeisamvlqkmkktaedylgqevteaVITVPAYFSDAQRQATK 153
Cdd:PRK13927 72 iaDFDVTEKMLKYFIKKVHKNFRPSPRV-----------------------------------VICVPSGITEVERRAVR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 154 EAGEIAGLNVRRIVNEPTAASLAYGLDKTNK--DMkiaVFDLGGGTFDISILELGDGVfevksTNGDTHLGGDDFDHVII 231
Cdd:PRK13927 117 ESALGAGAREVYLIEEPMAAAIGAGLPVTEPtgSM---VVDIGGGTTEVAVISLGGIV-----YSKSVRVGGDKFDEAII 188
|
....*..
gi 2486192116 232 DWLAEEF 238
Cdd:PRK13927 189 NYVRRNY 195
|
|
| SerB |
COG0560 |
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ... |
225-385 |
7.83e-03 |
|
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 440326 [Multi-domain] Cd Length: 221 Bit Score: 38.28 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 225 DFDHVII-----DWLAEEFLREEGVDLRKdpmALQRLKEAAEKAKI-ELSSTTSTEINLpyimpvngvpkHLVKTLTRAK 298
Cdd:COG0560 9 DLDGTLIagesiDELARFLGRRGLVDRRE---VLEEVAAITERAMAgELDFEESLRFRV-----------ALLAGLPEEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486192116 299 FEQLADSLI----------QACIEpcrqSLKDAGlstsdiDEVILVGGSTRiPAVQAIVEKFfgkapskGVnpDEVVAVG 368
Cdd:COG0560 75 LEELAERLFeevprlypgaRELIA----EHRAAG------HKVAIVSGGFT-FFVEPIAERL-------GI--DHVIANE 134
|
170
....*....|....*..
gi 2486192116 369 AAIQGGVLTGEVKDVLL 385
Cdd:COG0560 135 LEVEDGRLTGEVVGPIV 151
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
136-197 |
8.22e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.06 E-value: 8.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486192116 136 AVITVPAYFSDAQRQATKE-----------AGEIAGLNVRRIVNEPTAAslAYGLDKTNKDMKIAVFDLGGGT 197
Cdd:cd00012 16 IVITVAAGDRDANRVATITeailllqtnaaTFALFTGPPVRIVNEAVAA--AIGALLTLGPEGLLVVDLGGGT 86
|
|
| |
