|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
68-705 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1177.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 68 AKGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDP 147
Cdd:PTZ00009 2 TKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 148 VVQADMKLWPFQVINEG-GKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKD 226
Cdd:PTZ00009 82 VVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 227 AGVIAGLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:PTZ00009 162 AGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 FVEEFKRKHK-KDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 385
Cdd:PTZ00009 242 CVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 386 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKVQDLLLLDVAPL 465
Cdd:PTZ00009 322 VLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 466 SLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFD 545
Cdd:PTZ00009 402 SLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 546 IDANGILNVTAMDKSTGKVNKITITNDKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGLK 625
Cdd:PTZ00009 482 IDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKVK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 626 GKISESDKNKILDKCNELLSWLEVNQLAEKDEFDHKRKELEQMCNPIITKLYQ-----------GGCTGPACGTGYVPGR 694
Cdd:PTZ00009 562 GKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQaagggmpggmpGGMPGGMPGGAGPAGA 641
|
650
....*....|..
gi 119623932 695 PA-TGPTIEEVD 705
Cdd:PTZ00009 642 GAsSGPTVEEVD 653
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
72-678 |
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: 950.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 72 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 151
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMKLWPFQVIN-EGGKPKVLVSYKGENkaFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 230
Cdd:pfam00012 81 DIKHLPYKVVKlPNGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYGLDKGgQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYE-GIDFYTSITRARFEELCADLFRGTLEPVEKALR 388
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 389 DAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksEKVQDLLLLDVAPLSLG 468
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 469 LETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDA 548
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 549 NGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGlkGKI 628
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEG--DKV 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 119623932 629 SESDKNKIldkcNELLSWLEVNQL-AEKDEFDHKRKELEQMCNPIITKLYQ 678
Cdd:pfam00012 552 PEAEKSKV----ESAIEWLKDELEgDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
72-446 |
0e+00 |
|
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: 902.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 72 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 151
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEF 311
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 312 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDAK 391
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 119623932 392 MDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
69-689 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 874.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 69 KGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKfnDP 147
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 148 VVQADMKLWPFQVIN-EGGKPKVLVsykgENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKD 226
Cdd:PRK00290 79 EVQKDIKLVPYKIVKaDNGDAWVEI----DGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 227 AGVIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:PRK00290 155 AGKIAGLEVLRIINEPTAAALAYGLDK--KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAnlEIDSLYEGID------FYTSITRARFEELCADLFRGTL 380
Cdd:PRK00290 233 LADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EINLPFITADasgpkhLEIKLTRAKFEELTEDLVERTI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 381 EPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLL 460
Cdd:PRK00290 311 EPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVLLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 461 DVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQI 540
Cdd:PRK00290 386 DVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQI 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 541 EVTFDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVS 620
Cdd:PRK00290 466 EVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLK 544
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119623932 621 DegLKGKISESDKNKILDKCNELLSWLEVNqlaEKDEFDHKRKELEQMCNPIITKLYQGGCTGPACGTG 689
Cdd:PRK00290 545 E--LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGA 608
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
72-678 |
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: 804.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 72 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvVQ 150
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 151 ADMKLWPFQVINEGGKPKVlvsyKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 230
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRV----KVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYGLDKGGQGERhVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAnlEIDSLYEGID------FYTSITRARFEELCADLFRGTLEPVE 384
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLST--EINLPFITADasgpkhLEMTLTRAKFEELTADLVERTKEPVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 385 KALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVAP 464
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 465 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTF 544
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 545 DIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDegL 624
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--A 544
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 119623932 625 KGKISESDKNKILDKCNELLSWLEVNqlaEKDEFDHKRKELEQMCNPIITKLYQ 678
Cdd:TIGR02350 545 GDKLPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
72-446 |
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: 756.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 72 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 151
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 230
Cdd:cd24028 81 DIKHWPFKVVEdEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 390
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 119623932 391 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
70-446 |
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: 750.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 70 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVV 149
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 150 QADMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGV 229
Cdd:cd10241 81 QKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 230 IAGLNVLRIINEPTAAAIAYGLDKGGqGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVE 309
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKKG-GEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 310 EFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRD 389
Cdd:cd10241 240 LFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLED 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 119623932 390 AKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd10241 320 AGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
70-700 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 711.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 70 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpv 148
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 149 VQADMKLWPFQVInEGGKPKVLVSYKGENkaFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAG 228
Cdd:PRK13411 80 TEEERSRVPYTCV-KGRDDTVNVQIRGRN--YTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 229 VIAGLNVLRIINEPTAAAIAYGLDKGGQgERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFV 308
Cdd:PRK13411 157 TIAGLEVLRIINEPTAAALAYGLDKQDQ-EQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 309 EEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS--STQANLE-IDSLYEGID-FYTSITRARFEELCADLFRGTLEPVE 384
Cdd:PRK13411 236 ENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSmlTTSINLPfITADETGPKhLEMELTRAKFEELTKDLVEATIEPMQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 385 KALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVAP 464
Cdd:PRK13411 316 QALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDLLLLDVTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 465 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTF 544
Cdd:PRK13411 392 LSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 545 DIDANGILNVTAMDKSTGKVNKITITNdKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGl 624
Cdd:PRK13411 472 EIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENG- 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119623932 625 kGKISESDKNKILDKCNELLSWLEvNQLAEKDEFDHKRKELEQMCNPIITKLYQGGCTGPACGTGYVPGRPATGPT 700
Cdd:PRK13411 550 -ELISEELKQRAEQKVEQLEAALT-DPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDTVEPTSDTLITATM 623
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
73-668 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 706.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvVQA 151
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE--ISE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMKLWPFQVINEG-GKPKVLVSYKgeNKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 230
Cdd:CHL00094 83 EAKQVSYKVKTDSnGNIKIECPAL--NKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDK--KNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLE---IDSLYEG-IDFYTSITRARFEELCADLFRGTLEPVEKA 386
Cdd:CHL00094 239 FKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVENA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 387 LRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDyFNGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVAPLS 466
Cdd:CHL00094 319 LKDAKLDKSDIDEVVLVGGSTRIPAIQELVKK-LLGKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 467 LGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDI 546
Cdd:CHL00094 394 LGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 547 DANGILNVTAMDKSTGKVNKITITNdKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDegLKG 626
Cdd:CHL00094 474 DANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE--LKD 550
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 119623932 627 KISESDKNKIldkcNELLSwlEVNQLAEKDEFDHKRKELEQM 668
Cdd:CHL00094 551 KISEEKKEKI----ENLIK--KLRQALQNDNYESIKSLLEEL 586
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
65-683 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 693.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 65 MATAKGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRK 143
Cdd:PTZ00400 36 FAKATGDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 144 FNDPVVQADMKLWPFQVI-NEGGKPKVlvsyKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQ 222
Cdd:PTZ00400 116 YDEDATKKEQKILPYKIVrASNGDAWI----EAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 223 ATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQgeRHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNR 302
Cdd:PTZ00400 192 ATKDAGKIAGLDVLRIINEPTAAALAFGMDKNDG--KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 303 LVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAnlEIDSLYEGID------FYTSITRARFEELCADLF 376
Cdd:PTZ00400 270 ILNYLIAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADqsgpkhLQIKLSRAKLEELTHDLL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 377 RGTLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQD 456
Cdd:PTZ00400 348 KKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 457 LLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRG 536
Cdd:PTZ00400 423 LLLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRG 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 537 VPQIEVTFDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMK 616
Cdd:PTZ00400 503 VPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVE 581
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119623932 617 SVVSDegLKGKISESDKNKILDKCNELLSWLEVNQLaekDEFDHKRKELEQMCNPIITKLYQGGCTG 683
Cdd:PTZ00400 582 KQLSD--LKDKISDADKDELKQKITKLRSTLSSEDV---DSIKDKTKQLQEASWKISQQAYKQGNSD 643
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
72-585 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 691.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 72 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQ 150
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 151 ADmklwpfqvineggkpkvlvsykgeNKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 230
Cdd:COG0443 81 VG------------------------GKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYGLDKGGQGERhVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKGKEEET-ILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDsLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 390
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 391 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSEkvqdlllLDVAPLSLGLE 470
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 471 TAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDANG 550
Cdd:COG0443 367 TLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANG 446
|
490 500 510
....*....|....*....|....*....|....*
gi 119623932 551 ILNVTAMDKSTGKVNKITItndkgrlsKEEIERMV 585
Cdd:COG0443 447 ILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
70-656 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 672.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 70 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpv 148
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 149 VQADMKLWPFQV-INEGGKPKVLVSYKgeNKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDA 227
Cdd:PRK13410 80 LDPESKRVPYTIrRNEQGNVRIKCPRL--EREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 228 GVIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 307
Cdd:PRK13410 158 GRIAGLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 308 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLS--SSTQANLE-IDSLYEG---IDfyTSITRARFEELCADLFRGTLE 381
Cdd:PRK13410 236 AEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpkhIE--TRLDRKQFESLCGDLLDRLLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 382 PVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDyFNGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLD 461
Cdd:PRK13410 314 PVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRT-LIPREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 462 VAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIE 541
Cdd:PRK13410 389 VTPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 542 VTFDIDANGILNVTAMDKSTGKVNKITITNdKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFN----MKS 617
Cdd:PRK13410 469 VAFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQaerrLRD 547
|
570 580 590
....*....|....*....|....*....|....*....
gi 119623932 618 VVSDEGLKGkiSESDKNKILDKCNELLSWLEVNQLAEKD 656
Cdd:PRK13410 548 AALEFGPYF--AERQRRAVESAMRDVQDSLEQDDDRELD 584
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
72-446 |
0e+00 |
|
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: 632.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 72 AIGIDLGTTYSCVGVFQhGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 151
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKG-GQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGAGkSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 390
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 119623932 391 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
73-700 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 631.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvVQA 151
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMKLWPFQVI-NEGGKPKVLVSYKGenKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 230
Cdd:PLN03184 120 ESKQVSYRVVrDENGNVKLDCPAIG--KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEK--KSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLE---IDSLYEG---IDfyTSITRARFEELCADLFRGTLEPVE 384
Cdd:PLN03184 276 FKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 385 KALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDyFNGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVAP 464
Cdd:PLN03184 354 NALRDAKLSFKDIDEVILVGGSTRIPAVQELVKK-LTGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTP 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 465 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTF 544
Cdd:PLN03184 429 LSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKF 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 545 DIDANGILNVTAMDKSTGKVNKITITNdKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDegL 624
Cdd:PLN03184 509 DIDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--L 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119623932 625 KGKISESDKNKILDKCNELLSWLEVNQLAE-KDEFDHKRKELEQMCNpiitKLYQGGCTGPAcGTGYVPGRPATGPT 700
Cdd:PLN03184 586 GDKVPADVKEKVEAKLKELKDAIASGSTQKmKDAMAALNQEVMQIGQ----SLYNQPGAGGA-GPAPGGEAGSSSSS 657
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
69-667 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 611.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 69 KGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPV 148
Cdd:PTZ00186 26 QGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 149 VQADMKLWPFQVINEG-GKPKVlvsYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDA 227
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGnGDAWV---QDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 228 GVIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 307
Cdd:PTZ00186 183 GTIAGLNVIRVVNEPTAAALAYGMDK--TKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 308 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSS--TQANLE-IDSLYEGID-FYTSITRARFEELCADLFRGTLEPV 383
Cdd:PTZ00186 261 LEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAmeTEVNLPfITANADGAQhIQMHISRSKFEGITQRLIERSIAPC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 384 EKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVA 463
Cdd:PTZ00186 341 KQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVT 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 464 PLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVT 543
Cdd:PTZ00186 416 PLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVT 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 544 FDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEG 623
Cdd:PTZ00186 496 FDIDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWK 574
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 119623932 624 LkgkISESDKNKILDKCNELLSWLEvNQLAEKDEFDHKRKELEQ 667
Cdd:PTZ00186 575 Y---VSDAEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQK 614
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
69-610 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 561.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 69 KGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpv 148
Cdd:PRK05183 18 RRLAVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 149 VQADMKLWPFQ-VINEGGKPKV-----LVSykgenkafyPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQ 222
Cdd:PRK05183 96 IQQRYPHLPYQfVASENGMPLIrtaqgLKS---------PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 223 ATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQGerHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNR 302
Cdd:PRK05183 167 ATKDAARLAGLNVLRLLNEPTAAAIAYGLDSGQEG--VIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 303 LVSHFVEEFKRKHKKDISQnkraVRRLRTACERAKRTLSSSTQANLEIdSLYEGIdfytsITRARFEELCADLFRGTLEP 382
Cdd:PRK05183 245 LADWILEQAGLSPRLDPED----QRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 383 VEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKvqDLLLLDV 462
Cdd:PRK05183 315 CRRALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 463 APLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEV 542
Cdd:PRK05183 392 IPLSLGLETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119623932 543 TFDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQR----EKIAAKNALES 610
Cdd:PRK05183 472 TFQVDADGLLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEA 542
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
73-447 |
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: 557.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 151
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMKLWPFqVINEGGKPKVLVsykgENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd10234 82 KQVPYPV-VSAGNGDAWVEI----GGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEF 311
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDK--KKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 312 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLE---IDSLYEG---IDfyTSITRARFEELCADLFRGTLEPVEK 385
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpkhLE--MKLTRAKFEELTEDLVERTIEPVEQ 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119623932 386 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILM 447
Cdd:cd10234 313 ALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
72-609 |
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: 536.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 72 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvvq 150
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIED---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 151 admklwpfqVINEGGKPKVLVSYKGENKAFY-------PEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQA 223
Cdd:TIGR01991 77 ---------IKTFSILPYRFVDGPGEMVRLRtvqgtvtPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 224 TKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQGerHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 303
Cdd:TIGR01991 148 TKDAARLAGLNVLRLLNEPTAAAVAYGLDKASEG--IYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 304 VSHFVEEFKRKHKKDISQNKRAVRRLRTACERAkrtlssSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPV 383
Cdd:TIGR01991 226 AKWILKQLGISADLNPEDQRLLLQAARAAKEAL------TDAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSIC 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 384 EKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKvqDLLLLDVA 463
Cdd:TIGR01991 300 RRALRDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 464 PLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVT 543
Cdd:TIGR01991 377 PLSLGIETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVT 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119623932 544 FDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAED-----------EVQREKIAAKNALE 609
Cdd:TIGR01991 457 FQVDADGLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDmyaralaeqkvEAERILEALQAALA 532
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
70-446 |
7.97e-174 |
|
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: 501.41 E-value: 7.97e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 70 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPV 148
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 149 VQADMKLWPFQVIN-EGGKPKVlvsyKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDA 227
Cdd:cd11733 81 VQKDIKMVPYKIVKaSNGDAWV----EAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 228 GVIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 307
Cdd:cd11733 157 GQIAGLNVLRIINEPTAAALAYGLDK--KDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 308 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAnlEIDSLYEGID------FYTSITRARFEELCADLFRGTLE 381
Cdd:cd11733 235 VAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119623932 382 PVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd11733 313 PCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
70-448 |
2.21e-157 |
|
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: 459.60 E-value: 2.21e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 70 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPV 148
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 149 VQADMKLWPFQVINEGGKpKVLVSYKGENkaFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAG 228
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNG-DAWVEARGQK--YSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 229 VIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFV 308
Cdd:cd11734 158 QIAGLNVLRVINEPTAAALAYGLDK--SGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 309 EEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGID----FYTSITRARFEELCADLFRGTLEPVE 384
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKLTRAQFESLVKPLVDRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119623932 385 KALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMG 448
Cdd:cd11734 316 KALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
73-448 |
4.36e-149 |
|
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: 439.47 E-value: 4.36e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQH--GKVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVV 149
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 150 QADMKLWPFQVINEG-GKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAG 228
Cdd:cd10237 105 EEEAKRYPFKVVNDNiGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 229 VIAGLNVLRIINEPTAAAIAYGLDKgGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFV 308
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHK-KSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 309 EEFKRKHKKDISqNKRAVRRLRTACERAKRTLSS--STQANLEIDSLYEGID---FYTSITRARFEELCADLFRGTLEPV 383
Cdd:cd10237 264 DRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNhnSASLSLPLQISLPSAFkvkFKEEITRDLFETLNEDLFQRVLEPI 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119623932 384 EKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMG 448
Cdd:cd10237 343 RQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
73-446 |
4.74e-148 |
|
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: 434.70 E-value: 4.74e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVF-QHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvvq 150
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 151 admklwpfqvineggkpkvlvSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 230
Cdd:cd24029 77 ---------------------KEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYGLDKGGQGERhVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDGT-ILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKH-KKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRD 389
Cdd:cd24029 215 IGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 119623932 390 AKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
72-446 |
1.69e-147 |
|
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: 434.36 E-value: 1.69e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 72 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 151
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd10238 82 LKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKGGQGE-RHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 310
Cdd:cd10238 162 GFNVLRVISEPSAAALAYGIGQDDPTEnSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLASE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 311 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 390
Cdd:cd10238 242 FKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNSA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 119623932 391 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd10238 322 GLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
69-448 |
4.00e-147 |
|
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: 432.80 E-value: 4.00e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 69 KGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLI-GDAAKNQVAMNPQNTVFDAKRLIGRKFNDp 147
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 148 vVQADMKLWPFQVINEggkPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDA 227
Cdd:cd10236 80 -VKEELPLLPYRLVGD---ENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 228 GVIAGLNVLRIINEPTAAAIAYGLDKGGQGErhVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 307
Cdd:cd10236 156 ARLAGLNVLRLLNEPTAAALAYGLDQKKEGT--IAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 308 VEEFkrkhKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSlyEGIDFYTSITRARFEELCADLFRGTLEPVEKAL 387
Cdd:cd10236 234 LKQI----GIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRAL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119623932 388 RDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMG 448
Cdd:cd10236 308 KDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
73-444 |
3.00e-145 |
|
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: 428.52 E-value: 3.00e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 152
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 153 MKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKGGQGE-----RHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLEseekpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKA 386
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 119623932 387 LRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAA 444
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
70-446 |
1.08e-138 |
|
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: 412.09 E-value: 1.08e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 70 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVV 149
Cdd:cd24095 1 MSVVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 150 QADMKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAG 228
Cdd:cd24095 81 QRDLKLFPFKVTEgPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 229 VIAGLNVLRIINEPTAAAIAYGLDKGGQGE---RHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVS 305
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIYKTDLPEtdpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 306 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 385
Cdd:cd24095 241 HFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119623932 386 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd24095 321 ALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
73-444 |
2.32e-131 |
|
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: 392.79 E-value: 2.32e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 152
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 153 MKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYG-----LDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGiykqdLPAEEEKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 385
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 119623932 386 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAA 444
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
73-445 |
7.89e-130 |
|
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: 387.76 E-value: 7.89e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPQNTVFDAKRligrkfndpvvqa 151
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 DMklwpfqvinegGKPKVlvsYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd10235 68 FM-----------GTDKQ---YRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKGGQgERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEef 311
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKRED-ETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLK-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 312 krKHKKDISQNKRAVR-RLRTACERAKRTLSSSTQAnlEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 390
Cdd:cd10235 211 --KHRLDFTSLSPSELaALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 119623932 391 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAI 445
Cdd:cd10235 287 GLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
73-446 |
1.32e-124 |
|
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: 375.94 E-value: 1.32e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 152
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 153 MKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIAG 232
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 233 LNVLRIINEPTAAAIAYGLDK-----GGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 307
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKtdlpePEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 308 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKAL 387
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 119623932 388 RDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
73-444 |
2.29e-117 |
|
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: 356.03 E-value: 2.29e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGK-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGrkfndpvvqa 151
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 152 dmklwpfqvineggkpkvlvsykgenkaFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKGGQGE--RHVLIFDLGGGTFDVSILTI------DDGI------FEVKATAGDTHLGGE 297
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRRFENNepQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 298 DFDNRLVSHFVEEFKRKHKK--DISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADL 375
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119623932 376 FRGTLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAA 444
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
71-679 |
1.16e-111 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 349.92 E-value: 1.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 71 IAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDaaknqvamnpQNTVFDAKRLIGRK----FND 146
Cdd:PRK01433 20 IAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTlkeiLNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 147 PVVQADMKlwPFQVINEGgkpkvLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKD 226
Cdd:PRK01433 90 PALFSLVK--DYLDVNSS-----ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 227 AGVIAGLNVLRIINEPTAAAIAYGLDKGGQGerHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:PRK01433 163 AAKIAGFEVLRLIAEPTAAAYAYGLNKNQKG--CYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 FVEEFKRKHKKDISQnkravrrlrtACERAKRTLSSstQANLEIDSLyegidfytSITRARFEELCADLFRGTLEPVEKA 386
Cdd:PRK01433 241 LCNKFDLPNSIDTLQ----------LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 387 LRDAKmdKAKIHDIVLVGGSTRIPKVQRLLQDYFNgRDLNKSINPDEAVAYGAAVQAAILMGDKsekvQDLLLLDVAPLS 466
Cdd:PRK01433 301 LEQAG--NPNIDGVILVGGATRIPLIKDELYKAFK-VDILSDIDPDKAVVWGAALQAENLIAPH----TNSLLIDVVPLS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 467 LGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDI 546
Cdd:PRK01433 374 LGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 547 DANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDegLKG 626
Cdd:PRK01433 454 DADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAE--LTT 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 119623932 627 KISESDKNKI---LDKCNELLS---WLEVNQlAEKDEFDHKRKELEQMCNPIITKLYQG 679
Cdd:PRK01433 531 LLSESEISIInslLDNIKEAVHardIILINN-SIKEFKSKIKKSMDTKLNIIINDLLKG 588
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
73-445 |
2.09e-101 |
|
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: 315.73 E-value: 2.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 152
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 153 MKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd11737 83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKGG-----QGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQDlpapeEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 385
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 386 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAI 445
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
71-446 |
5.28e-101 |
|
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: 313.53 E-value: 5.28e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 71 IAIGIDLGTTYSCVG-VFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKfndpvv 149
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGTT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 150 qadmklwpfqvineggkpkvlvsykgenkAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGV 229
Cdd:cd10232 75 -----------------------------TLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 230 IAGLNVLRIINEPTAAAIAYGLDKGGQG----ERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVS 305
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGdtikDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 306 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 385
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119623932 386 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNK----SINPDEAVAYGAAVQAAIL 446
Cdd:cd10232 286 AIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLF-PESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
73-446 |
1.18e-97 |
|
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: 306.07 E-value: 1.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 152
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 153 MKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd11738 83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKGG-----QGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQDlpaleEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 385
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119623932 386 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 446
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
73-444 |
4.09e-97 |
|
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: 304.48 E-value: 4.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 152
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 153 MKLWPFQ-VINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 231
Cdd:cd11739 83 KENLSYDlVPLKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 232 GLNVLRIINEPTAAAIAYGLDKGG-----QGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQDlpapdEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 385
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 119623932 386 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAA 444
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
73-441 |
1.90e-61 |
|
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: 208.88 E-value: 1.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVgvfqhgkveiiandqgnrttpsyvAFTDTERligdaaknqvamnpqntvfdakrligrkfNDPVVQAD 152
Cdd:cd10170 1 VGIDFGTTYSGV------------------------AYALLGP-----------------------------GEPPLVVL 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 153 MKLWPFqviNEGGKPKVlvsykgenkafyPE--EISSMVLTKLKETAEAFLGH-------PVTNAVITVPAYFNDSQRQA 223
Cdd:cd10170 28 QLPWPG---GDGGSSKV------------PSvlEVVADFLRALLEHAKAELGDriwelekAPIEVVITVPAGWSDAAREA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 224 TKDAGVIAGL----NVLRIINEPTAAAIAYGLDKGG----QGERHVLIFDLGGGTFDVSILTIDDGIFEVK---ATAGDT 292
Cdd:cd10170 93 LREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDllplKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 293 HLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGID---FYTSITRARFE 369
Cdd:cd10170 173 LLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTE 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119623932 370 ELCADLFRGTLEPVEKALRDA--KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLN---KSINPDEAVAYGAAV 441
Cdd:cd10170 253 EEIRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
73-420 |
8.49e-37 |
|
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: 142.80 E-value: 8.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTE------RLIGDAAKNQVAMNPQNTVF--DAKRLIGRKF 144
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 145 NDPVVQADmKLWPFqvineggkpkvlvsykgenkafypEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQAT 224
Cdd:cd10231 81 FDETTIFG-RRYPF------------------------EDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 225 -------KDAGVIAGLNVLRIINEPTAAAIAYglDKGGQGERHVLIFDLGGGTFDVSILTID----DGIFEVKATAGDtH 293
Cdd:cd10231 136 aqaesrlRDAARRAGFRNVEFQYEPIAAALDY--EQRLDREELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-G 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 294 LGGEDFDNRLVSHFV-----------------------------------------EEFKRKHKKDiSQNKRAVRRLRT- 331
Cdd:cd10231 213 IGGDDFDRELALKKVmphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktLRLLLDLRRD-AADPEKIERLLSl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 332 -----------ACERAKRTLSSSTQANLEIDSLYEGIDfyTSITRARFEELCADLFRGTLEPVEKALRDAKMDKAKIHDI 400
Cdd:cd10231 292 vedqlghrlfrAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420
....*....|....*....|
gi 119623932 401 VLVGGSTRIPKVQRLLQDYF 420
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLF 389
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
73-440 |
5.07e-21 |
|
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: 95.42 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVG-VFQH--GKVEIIANDQG------NRTTPSYVAFTDTERLIG---DAAKNQVAMNPQNTV---FDAK 137
Cdd:cd10229 3 VAIDFGTTYSGYAySFITdpGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDEEHqwlYFFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 138 RLIGRKFNDPVVQADMKlwpfQVINEGGKP--KVLvsykgenkAFYPEEISSMVLTKLKETaeafLGHPVTNA----VIT 211
Cdd:cd10229 83 FKMMLLSEKELTRDTKV----KAVNGKSMPalEVF--------AEALRYLKDHALKELRDR----SGSSLDEDdirwVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 212 VPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAIAYGLDKGGQ-------GERhVLIFDLGGGTFDVSILTI 278
Cdd:cd10229 147 VPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKLLAEGeekelkpGDK-YLVVDCGGGTVDITVHEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 279 -DDGIFE--VKATAGdtHLGGEDFDNRLVS--------HFVEEFKRKHKKDISQNKRAVrrlrtacERAKRTlssstqan 347
Cdd:cd10229 226 lEDGKLEelLKASGG--PWGSTSVDEEFEElleeifgdDFMEAFKQKYPSDYLDLLQAF-------ERKKRS-------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 348 leiDSLYegidfytsITRARFEELCADLFRGTLEPVEKALRDAKMDkaKIHDIVLVGGSTRIPKVQRLLQDYFNGRdlNK 427
Cdd:cd10229 289 ---FKLR--------LSPELMKSLFDPVVKKIIEHIKELLEKPELK--GVDYIFLVGGFAESPYLQKAVKEAFSTK--VK 353
|
410
....*....|....*.
gi 119623932 428 SI---NPDEAVAYGAA 440
Cdd:cd10229 354 IIippEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
73-441 |
5.87e-15 |
|
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: 76.36 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVgvFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVAMNPQNTVfdakrlIGRKFNDPVV 149
Cdd:cd10225 2 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAVdKNTGKVLavGEEAKKMLGRTPGNIV------AIRPLRDGVI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 150 qADmklwpFQVINeggkpKVLvsykgenKAFypeeISSMVLTKlketaeaFLGHPvtNAVITVPAYFNDSQRQATKDAGV 229
Cdd:cd10225 67 -AD-----FEATE-----AML-------RYF----IRKAHRRR-------GFLRP--RVVIGVPSGITEVERRAVKEAAE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 230 IAGLNVLRIINEPTAAAIAYGLD----KGgqgerhVLIFDLGGGTFDVSILTIdDGIFEVKAtagdTHLGGEDFDNRLVS 305
Cdd:cd10225 116 HAGAREVYLIEEPMAAAIGAGLPieepRG------SMVVDIGGGTTEIAVISL-GGIVTSRS----VRVAGDEMDEAIIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 306 HfveeFKRKHKKDISqnkravrrLRTAcERAKRTLSS--STQANLEIDslYEGIDFYTSITRARfeELCADLFRGTLEP- 382
Cdd:cd10225 185 Y----VRRKYNLLIG--------ERTA-ERIKIEIGSayPLDEELSME--VRGRDLVTGLPRTI--EITSEEVREALEEp 247
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119623932 383 ---VEKALRDAkMDK------AKIHD--IVLVGGSTRIPKVQRLLQDYFngrDLNKSI--NPDEAVAYGAAV 441
Cdd:cd10225 248 vnaIVEAVRST-LERtppelaADIVDrgIVLTGGGALLRGLDELLREET---GLPVHVadDPLTCVAKGAGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
73-440 |
7.83e-12 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 67.08 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYscVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERL--IGDAAKNQVAMNPQNTVfdAKRligrkfndPV- 148
Cdd:PRK13930 11 IGIDLGTAN--TLVYVKGK-GIVLNE------PSVVAIdTKTGKVlaVGEEAKEMLGRTPGNIE--AIR--------PLk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 149 --VQADmklwpFQVIneggkpKVLVSYkgenkaFYpeeisSMVLTKLketaeaFLGHPvtNAVITVPAYFNDSQRQATKD 226
Cdd:PRK13930 72 dgVIAD-----FEAT------EAMLRY------FI-----KKARGRR------FFRKP--RIVICVPSGITEVERRAVRE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 227 AGVIAGLNVLRIINEPTAAAIAYGLD----KGGqgerhvLIFDLGGGTFDVSILTIdDGIfevkATAGDTHLGGEDFDNR 302
Cdd:PRK13930 122 AAEHAGAREVYLIEEPMAAAIGAGLPvtepVGN------MVVDIGGGTTEVAVISL-GGI----VYSESIRVAGDEMDEA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 303 LVSHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQAN----LEIdslyEGIDFYTSITRARfeELCADLFRG 378
Cdd:PRK13930 191 IVQY----VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLDeeesMEV----RGRDLVTGLPKTI--EISSEEVRE 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119623932 379 TLEP--------VEKALRDAKMD-KAKIHD--IVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAA 440
Cdd:PRK13930 252 ALAEplqqiveaVKSVLEKTPPElAADIIDrgIVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVARGTG 323
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
73-440 |
1.50e-11 |
|
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: 66.25 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVAMNPQNTVfdAKRligrkfndPV- 148
Cdd:COG1077 10 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIdKKTGKVLavGEEAKEMLGRTPGNIV--AIR--------PLk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 149 --VQADmklwpFQVIneggkpKVLVSYkgenkafypeeissmVLTKLKEtaEAFLGHPvtNAVITVPAYFNDSQRQATKD 226
Cdd:COG1077 71 dgVIAD-----FEVT------EAMLKY---------------FIKKVHG--RRSFFRP--RVVICVPSGITEVERRAVRD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 227 AGVIAGLNVLRIINEPTAAAIAYGLD----KGgqgerhVLIFDLGGGTFDVSILTIdDGIfeVKATAgdTHLGGEDFDNR 302
Cdd:COG1077 121 AAEQAGAREVYLIEEPMAAAIGAGLPieepTG------NMVVDIGGGTTEVAVISL-GGI--VVSRS--IRVAGDELDEA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 303 LVSHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARF---EELcADLFRGT 379
Cdd:COG1077 190 IIQY----VRKKYNLLIGE--------RTA-EEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTITitsEEI-REALEEP 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119623932 380 LEPVEKALRDAkMDK------AKIHD--IVLVGGSTRIPKVQRLLQDYFNgrdLNKSI--NPDEAVAYGAA 440
Cdd:COG1077 256 LNAIVEAIKSV-LEKtppelaADIVDrgIVLTGGGALLRGLDKLLSEETG---LPVHVaeDPLTCVARGTG 322
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
189-294 |
1.27e-09 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 59.20 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 189 VLTKLKETAEAFLGHPVTNAVITVPAyfNDSQRQATKDAGVI--AGLNVLRIINEPTAAAIAYGLDKGGqgerhvlIFDL 266
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPP--GTGERDARAIRNVLegAGLEVSNVVDEPTAANAVLGIRDGA-------VVDI 118
|
90 100 110
....*....|....*....|....*....|..
gi 119623932 267 GGGTFDVSIltIDDGifEVKATA----GDTHL 294
Cdd:cd24047 119 GGGTTGIAV--LKDG--KVVYTAdeptGGTHL 146
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
73-439 |
2.76e-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: 59.11 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVAMNPQNTVfdakrlIGRKFNDPVV 149
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGNEAKKMLGRTPGNIV------AVRPLKDGVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 150 qADMklwpfqvineggkpkvlvsykgenkafypeeissmvltklkETAEAFLGH-----------PVTNAVITVPAYFND 218
Cdd:pfam06723 69 -ADF-----------------------------------------EVTEAMLKYfikkvhgrrsfSKPRVVICVPSGITE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 219 SQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD-KGGQGErhvLIFDLGGGTFDVSILTIdDGIfevkATAGDTHLGGE 297
Cdd:pfam06723 107 VERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPvEEPTGN---MVVDIGGGTTEVAVISL-GGI----VTSKSVRVAGD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 298 DFDNRLVSHfveeFKRKHKKDISQnkravrrlRTAcERAKrtlssstqanLEIDSLYEGIDFYTSITRAR---------- 367
Cdd:pfam06723 179 EFDEAIIKY----IRKKYNLLIGE--------RTA-ERIK----------IEIGSAYPTEEEEKMEIRGRdlvtglpkti 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 368 ------FEELCADLFRGTLEPVEKALRDAKMDKAK-IHD--IVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYG 438
Cdd:pfam06723 236 eisseeVREALKEPVSAIVEAVKEVLEKTPPELAAdIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALG 314
|
.
gi 119623932 439 A 439
Cdd:pfam06723 315 T 315
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
189-294 |
5.46e-08 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 54.84 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 189 VLTKLKETAEAFLGHPVTNAVITVPAyfndsqrqAT--KDAGVI------AGLNVLRIINEPTAAAIAYGLDKGGqgerh 260
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGIDNGA----- 138
|
90 100 110
....*....|....*....|....*....|....*...
gi 119623932 261 vlIFDLGGGTFDVSILtiDDGifEVKATA----GDTHL 294
Cdd:PRK15080 139 --VVDIGGGTTGISIL--KDG--KVVYSAdeptGGTHM 170
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
190-423 |
2.21e-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: 50.35 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 190 LTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAI-AYGLDKggqgerhVL 262
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR-------YI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 263 IFDLGGGTFDVSILTIDD--GIFE--VKATAGDTHLGGED--FDNRLVSHFVEEFKRKHKkdiSQNKRAVRRLRTACERA 336
Cdd:cd11736 198 VADCGGGTVDLTVHQIEQpqGTLKelYKASGGPYGAVGVDlaFEKLLCQIFGEDFIATFK---AKRPAAWVDLTIAFEAR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 337 KRTlssstqANLEIDSlyegidfytsitrarfeELCADLFRGTLEPVEKALRD--AKMDKAKIHDIVLVGGSTRIPKVQR 414
Cdd:cd11736 275 KRT------AALRMSS-----------------EAMNELFQPTISQIIQHIDDlmKKPEVKGIKFLFLVGGFAESPMLQR 331
|
....*....
gi 119623932 415 LLQDYFNGR 423
Cdd:cd11736 332 AVQAAFGNI 340
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
73-439 |
2.26e-06 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK 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: 466859 [Multi-domain] Cd Length: 328 Bit Score: 50.29 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCvgvfqhgkveiIANDQGNR-TTPSYVAFTD---------TERLIGDAA-KNQVAMNpqntvfdakrlig 141
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGYPKdiiarkllgKEVLFGDEAlENRLALD------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 142 rkfndpvvqadMKlWPFQ--VINEGGKpkvlvsykgENKafypeEISSMVLTKLKETAEAFLGHPVTnAVITVPAYFNDS 219
Cdd:cd24009 60 -----------LR-RPLEdgVIKEGDD---------RDL-----EAARELLQHLIELALPGPDDEIY-AVIGVPARASAE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 220 QRQATKDA--GVIAGLnvlRIINEPTAaaIAYGLDKggqgERHVLIFDLGGGTFDV-----SILTIDDGIFEVKAtagdt 292
Cdd:cd24009 113 NKQALLEIarELVDGV---MVVSEPFA--VAYGLDR----LDNSLIVDIGAGTTDLcrmkgTIPTEEDQITLPKA----- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 293 hlgGEDFDNRLvshfVEEFKRKHkKDISQNKRAVRRLR-------TACERAKRTLSsstqanleIDSLYEGIDFyTSITR 365
Cdd:cd24009 179 ---GDYIDEEL----VDLIKERY-PEVQLTLNMARRWKekygfvgDASEPVKVELP--------VDGKPVTYDI-TEELR 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119623932 366 ARFEELCADLFRGTLEPVEKAlrDAKMDKAKIHDIVLVGGSTRI----PKVQRLLQDYFNGRdLNKSINPDEAVAYGA 439
Cdd:cd24009 242 IACESLVPDIVEGIKKLIASF--DPEFQEELRNNIVLAGGGSRIrgldTYIEKALKEYGGGK-VTCVDDPVFAGAEGA 316
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
187-421 |
2.66e-06 |
|
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: 49.60 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 187 SMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKdagviAGLNVLRIINEPTAAaiAYGLDKGGQGERHVLIFDL 266
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAA--ANLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 267 GGGTFDVSIltIDDGifEVKATaGDTHLGGEDFDNRLVSHFveefkrkhkkDISQNKravrrlrtaCERAKRTLSSST-- 344
Cdd:cd24004 122 GAGTTDIAL--IRNG--GIEAY-RMVPLGGDDFTKAIAEGF----------LISFEE---------AEKIKRTYGIFLli 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119623932 345 QANLEIDSLYEGIDFYTSITRArFEELcadlfrgtLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFN 421
Cdd:cd24004 178 EAKDQLGFTINKKEVYDIIKPV-LEEL--------ASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
209-423 |
7.24e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 48.85 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 209 VITVPAYFNDSQRQATKDAGVIAGLNV------LRIINEPTAAAIAYGLDKGGQGERHVLIfDLGGGTFDVSI--LTIDD 280
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIYCRKLRLHQMDRYVVV-DCGGGTVDLTVhqIRLPE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 281 GIFE--VKATAGDTHLGGEDFD-NRLV-----SHFVEEFKRKHKKdisqnkrAVRRLRTACERAKRTLSSSTQANLEIDS 352
Cdd:cd11735 223 GHLKelYKASGGPYGSLGVDYEfEKLLckifgEDFIDQFKIKRPA-------AWVDLMIAFESRKRAAAPDRTNPLNITL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 353 LYEGIDFYTSITRARFE-------------------ELCAD----LFRGTLEPVEKALRD--AKMDKAKIHDIVLVGGST 407
Cdd:cd11735 296 PFSFIDYYKKFRGHSVEhalrksnvdfvkwssqgmlRMSPDamnaLFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFA 375
|
250
....*....|....*.
gi 119623932 408 RIPKVQRLLQDYFNGR 423
Cdd:cd11735 376 ESPLLQQAVQNAFGDQ 391
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
179-417 |
9.13e-06 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 48.71 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 179 AFYpEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFN-----DSQRQAT---KDAGVIAGLNVLRIINEPTAAAIAY- 249
Cdd:PRK11678 124 ALF-EDLVCAMMLHIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFe 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 250 -GLDKggqgERHVLIFDLGGGTFDVSILTIddgifevkataGDTH-----------------LGGEDFD-----NRLVSH 306
Cdd:PRK11678 203 aTLTE----EKRVLVVDIGGGTTDCSMLLM-----------GPSWrgradrsasllghsgqrIGGNDLDialafKQLMPL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 307 F-------------------------VEE----FKRKHKKDISQNKR------AVRRL-------------RTAcERAKR 338
Cdd:PRK11678 268 LgmgsetekgialpslpfwnavaindVPAqsdfYSLANGRLLNDLIRdarepeKVARLlkvwrqrlsyrlvRSA-EEAKI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 339 TLSSSTQANLEIDSLYEGIDfyTSITRARFEELCADLFRGTLEPVEKALRDA--KMDKakihdIVLVGGSTRIPKVQRLL 416
Cdd:PRK11678 347 ALSDQAETRASLDFISDGLA--TEISQQGLEEAISQPLARILELVQLALDQAqvKPDV-----IYLTGGSARSPLIRAAL 419
|
.
gi 119623932 417 Q 417
Cdd:PRK11678 420 A 420
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
373-448 |
1.80e-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: 47.90 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 373 ADLFRGTLEPVEKALRDAkMD-----KAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSiNPDEAVAYGAAVQAAILM 447
Cdd:COG1070 368 AHLARAVLEGVAFALRDG-LEaleeaGVKIDRIRATGGGARSPLWRQILADVL-GRPVEVP-EAEEGGALGAALLAAVGL 444
|
.
gi 119623932 448 G 448
Cdd:COG1070 445 G 445
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
70-316 |
1.91e-05 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 47.20 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 70 GIAIGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVAMNPQNTVfdakrLIgRKFND 146
Cdd:PRK13928 3 GRDIGIDLGT--ANVLVYVKGK-GIVLNE------PSVVAIdKNTNKVLavGEEARRMVGRTPGNIV-----AI-RPLRD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 147 PVVqADmklwpFQVINeggkpKVLvsykgenKAFypeeissmvLTKLkeTAEAFLGHPvtNAVITVPAYFNDSQRQATKD 226
Cdd:PRK13928 68 GVI-AD-----YDVTE-----KML-------KYF---------INKA--CGKRFFSKP--RIMICIPTGITSVEKRAVRE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 227 AGVIAGLNVLRIINEPTAAAIAYGLD----KGGqgerhvLIFDLGGGTFDVSILTIDDGIfevkaTAGDTHLGGEDFDNR 302
Cdd:PRK13928 117 AAEQAGAKKVYLIEEPLAAAIGAGLDisqpSGN------MVVDIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFDEA 185
|
250
....*....|....
gi 119623932 303 LVSHfveeFKRKHK 316
Cdd:PRK13928 186 IIRY----IRKKYK 195
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
231-438 |
5.09e-05 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 45.98 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYgLDkggQGERH--VLIFDLGGGTFDVSILTidDGIFEvkatagDTH---LGGEDFDNRLVS 305
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LT---EDEKElgVALIDIGGGTTDIAVFK--NGSLR------YTAvipVGGNHITNDIAI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 306 HF------VEEFKRKHKKDISQN--KRAVRRLRTACERAKRTLSSSTqanleidsLYEgidfytsITRARFEELcadlfr 377
Cdd:cd24048 240 GLntpfeeAERLKIKYGSALSEEadEDEIIEIPGVGGREPREVSRRE--------LAE-------IIEARVEEI------ 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119623932 378 gtLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFN-----------GRDLNKSINPDEAVAYG 438
Cdd:cd24048 299 --LELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvrigrpkniGGLPEEVNDPAYATAVG 368
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
73-306 |
1.66e-04 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 44.51 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 73 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAFTDTER---LIGDAAKNQVAMNPQNTVfdakrlIGRKFNDPVV 149
Cdd:PRK13929 7 IGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV------AVRPMKDGVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 150 qADMklwpfqvineggkpkvlvsykgenkafypeEISSMVLTKLKETAEAFLGHPV--TNAVITVPAYFNDSQRQATKDA 227
Cdd:PRK13929 72 -ADY------------------------------DMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAISDA 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119623932 228 GVIAGLNVLRIINEPTAAAIayGLDKGGQGERHVLIFDLGGGTFDVSILTiddgiFEVKATAGDTHLGGEDFDNRLVSH 306
Cdd:PRK13929 121 VKNCGAKNVHLIEEPVAAAI--GADLPVDEPVANVVVDIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSF 192
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
231-421 |
3.41e-04 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 43.58 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 231 AGLNVLRIINEPTAAAIAYgLDKGgqgERH--VLIFDLGGGTFDVSILTidDGIfeVKATAGDThLGGEDFDNrlvshfv 308
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTED---EKElgVALVDIGGGTTDIAVFK--DGA--LRHTAVIP-VGGDHITN------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 309 eefkrkhkkDISqnkravRRLRT---ACERAKRTLSS------STQANLEIDSLyeGIDFYTSITR--------ARFEEL 371
Cdd:COG0849 238 ---------DIA------IGLRTpleEAERLKIKYGSalaslaDEDETIEVPGI--GGRPPREISRkelaeiieARVEEI 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 119623932 372 cadlfrgtLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFN 421
Cdd:COG0849 301 --------FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
189-453 |
3.97e-04 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins; Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp9 forms a stable heterodimer with Arp7 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.
Pssm-ID: 466814 Cd Length: 356 Bit Score: 43.06 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 189 VLTKLKETAEAFLGHPVtnaVITVPAYFNDSQRQ-ATKDagVIAGLNV--LRIINEPTAAAIAYGLDKGgqgerhvLIFD 265
Cdd:cd10208 57 ILFSLLSIPRPTNNSPV---LLSVPPSWSKSDLElLTQL--FFERLNVpaFAILEAPLAALYAAGATSG-------IVVD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 266 LGGGTFDVSIltIDDGIFEVKATAgDTHLGGEDFDNrlvsHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRtlssSTQ 345
Cdd:cd10208 125 IGHEKTDITP--IVDSQVVPHALV-SIPIGGQDCTA----HLAQLLKSDEPELKSQAESGEEATLDLAEALKK----SPI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 346 ANLEIDS--LYEGIDFytSITRARFEeLCADLFRGTLEPVEKALRDAKMDKAKIH------------DIVLVGGSTRI-- 409
Cdd:cd10208 194 CEVLSDGadLASGTEI--TVGKERFR-ACEPLFKPSSLRVDLLIAAIAGALVLNAsdepdkrpalweNIIIVGGGSRIrg 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 410 ------------------------PKVQRLLQ--DYFNGRdlnKSINPDEAVAYGAAVQAAILMGDKSEK 453
Cdd:cd10208 271 lkeallselqqfhlisetsaspqqPRIIRLAKipDYFPEW---KKSGYEEAAFLGASIVAKLVFNDPSSK 337
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
209-342 |
4.69e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 42.77 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 209 VITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD----KGgqgerhVLIFDLGGGTFDVSILTIdDGIfe 284
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPvtepTG------SMVVDIGGGTTEVAVISL-GGI-- 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 119623932 285 vkATAGDTHLGGEDFDNRLVSHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSS 342
Cdd:PRK13927 171 --VYSKSVRVGGDKFDEAIINY----VRRNYNLLIGE--------RTA-ERIKIEIGS 213
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
233-321 |
5.36e-04 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 42.51 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 233 LNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTfdVSILTIDDGIFEVKatAGDTHLGGEDFDNRLVSHFVEEFK 312
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENGKPIEE--SSDTLPGGEEALEKYADDILNELL 212
|
....*....
gi 119623932 313 RKHKKDISQ 321
Cdd:cd10227 213 KKLGDELDS 221
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
373-448 |
1.88e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 41.37 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 373 ADLFRGTLEPVEKALRDA----KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAvAYGAAVQAAILMG 448
Cdd:cd07808 365 AHLARAVLEGVAFSLRDSlevlKELGIKVKEIRLIGGGAKSPLWRQILADVL-GVPVVVPAEEEGS-AYGAALLAAVGAG 442
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
208-270 |
3.19e-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: 38.60 E-value: 3.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119623932 208 AVITVPAYFNDSQRQAT-----------KDAGVIAGLNVLRIINEPTAAAIAYGLDKggqGERHVLIFDLGGGT 270
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTL---GPEGLLVVDLGGGT 86
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
362-444 |
4.70e-03 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 39.84 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623932 362 SITRARFEELC-ADLFRGTLEPVEKALRDAkMDK-----AKIHDIVLVGGSTRIPKVQRLLQDYFNgrdlnKSI---NPD 432
Cdd:cd07809 354 SLVGLTLSNFTrANLARAALEGATFGLRYG-LDIlrelgVEIDEIRLIGGGSKSPVWRQILADVFG-----VPVvvpETG 427
|
90
....*....|..
gi 119623932 433 EAVAYGAAVQAA 444
Cdd:cd07809 428 EGGALGAALQAA 439
|
|
| |
