|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
4-639 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1094.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:PTZ00009 6 AIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLID-VDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:PTZ00009 86 DMKHWPFKVTTgGDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDKKGKEE-HVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQE 241
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKGDGEkNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 242 FKRKNK-KDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRD 320
Cdd:PTZ00009 246 FKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEKVLKD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 321 AKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGI 400
Cdd:PTZ00009 326 AGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTPLSLGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 401 ETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSN 480
Cdd:PTZ00009 406 ETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDAN 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 481 GILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISE--AGDKLE 558
Cdd:PTZ00009 486 GILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDekVKGKLS 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 559 QADKDAVTKKAEETIAWLDSNTTATKEEFDDQLKELQEVANPIMSKLYQA------GGAPEGAAPGGFPGGAPPAPEA-E 631
Cdd:PTZ00009 566 DSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQAagggmpGGMPGGMPGGMPGGAGPAGAGAsS 645
|
....*...
gi 6323004 632 GPTVEEVD 639
Cdd:PTZ00009 646 GPTVEEVD 653
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
4-607 |
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: 918.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLI-DVDGKPQIQVEFKGETknFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:pfam00012 81 DIKHLPYKVVkLPNGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEF 242
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 KRKNKKDLSTNQRALRRLRTACERAKRTLSS-SAQTSVEIDSLFE-GIDFYTSITRARFEELCADLFRSTLDPVEKVLRD 320
Cdd:pfam00012 239 KKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 321 AKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTGDEssKTQDLLLLDVAPLSLGI 400
Cdd:pfam00012 319 AGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGTF--DVKDFLLLDVTPLSLGI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 401 ETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSN 480
Cdd:pfam00012 396 ETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDAN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 481 GILNVSAVEKGTGKSNKITITNDKGrLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQA 560
Cdd:pfam00012 476 GILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEA 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 6323004 561 DKDAVtkkaEETIAWLDSNTT-ATKEEFDDQLKELQEVANPIMSKLYQ 607
Cdd:pfam00012 555 EKSKV----ESAIEWLKDELEgDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-613 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 869.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 1 MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDT-ERLIGDAAKNQAAMNPANTVFDAKRLIGRNfnDP 79
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 80 EVQGDMKHFPFKLIDVDGKpQIQVEFKGetKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDA 159
Cdd:PRK00290 79 EVQKDIKLVPYKIVKADNG-DAWVEIDG--KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 160 GTIAGLNVLRIINEPTAAAIAYGLDKKGkEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFI 239
Cdd:PRK00290 156 GKIAGLEVLRIINEPTAAALAYGLDKKG-DEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 240 QEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVeidSL-FEGID------FYTSITRARFEELCADLFRSTLD 312
Cdd:PRK00290 235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEI---NLpFITADasgpkhLEIKLTRAKFEELTEDLVERTIE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 313 PVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTGDesskTQDLLLLD 392
Cdd:PRK00290 312 PCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVLLLD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 393 VAPLSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIE 472
Cdd:PRK00290 387 VTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 473 VTFDVDSNGILNVSAVEKGTGKSNKITITNDKGrLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISE 552
Cdd:PRK00290 467 VTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKE 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323004 553 AGDKLEQADKDAVTKKAEETIAWLDSNttaTKEEFDDQLKELQEVANPIMSKLYQAGGAPE 613
Cdd:PRK00290 546 LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQQAQAAQ 603
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
4-377 |
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: 867.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKGKEE-HVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEF 242
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGErNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 KRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAK 322
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 6323004 323 LDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-607 |
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: 794.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 3 KAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDT-ERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNdpEV 81
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 82 QGDMKHFPFKLIDVDGkpqiQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGT 161
Cdd:TIGR02350 79 TEEAKRVPYKVVGDGG----DVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 162 IAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQE 241
Cdd:TIGR02350 155 IAGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 242 FKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTsvEIDSLFEGID------FYTSITRARFEELCADLFRSTLDPVE 315
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLST--EINLPFITADasgpkhLEMTLTRAKFEELTADLVERTKEPVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 316 KVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTGDesskTQDLLLLDVAP 395
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 396 LSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTF 475
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 476 DVDSNGILNVSAVEKGTGKSNKITITNDKGrLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGD 555
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGD 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 6323004 556 KLEQADKDAVTKKAEETIAWLDSNTTatkEEFDDQLKELQEVANPIMSKLYQ 607
Cdd:TIGR02350 547 KLPAEEKEKIEKAVAELKEALKGEDV---EEIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
5-377 |
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: 747.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGD 84
Cdd:cd10241 4 IGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 85 MKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAG 164
Cdd:cd10241 84 IKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 165 LNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKR 244
Cdd:cd10241 164 LNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLFKK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 245 KNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAKLD 324
Cdd:cd10241 244 KTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDAGLK 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 6323004 325 KSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd10241 324 KSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
4-377 |
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: 722.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLI-DVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:cd24028 81 DIKHWPFKVVeDEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDKK-GKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQE 241
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKsSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 242 FKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDA 321
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323004 322 KLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
4-516 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 698.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFT-DTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVq 82
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEAT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 83 gdmkhfpfkliDVDGKPqiqvefkgetknFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:COG0443 80 -----------EVGGKR------------YSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEF 242
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 KRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDsLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAK 322
Cdd:COG0443 217 GKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 323 LDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTGDESSktqdlllLDVAPLSLGIET 402
Cdd:COG0443 296 LSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIET 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 403 AGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGI 482
Cdd:COG0443 368 LGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGI 447
|
490 500 510
....*....|....*....|....*....|....
gi 6323004 483 LNVSAVEKGTGKSNKITItndkgrlsKEDIEKMV 516
Cdd:COG0443 448 LSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-608 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 696.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 1 MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDT-ERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNdp 79
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 80 EVQGDMKHFPFKLIDvDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDA 159
Cdd:CHL00094 79 EISEEAKQVSYKVKT-DSNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 160 GTIAGLNVLRIINEPTAAAIAYGLDKKgKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFI 239
Cdd:CHL00094 158 GKIAGLEVLRIINEPTAASLAYGLDKK-NNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 240 QEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVE---IDSLFEG-IDFYTSITRARFEELCADLFRSTLDPVE 315
Cdd:CHL00094 237 KEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 316 KVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDyFNGKEPNRSINPDEAVAYGAAVQAAILTGDesskTQDLLLLDVAP 395
Cdd:CHL00094 317 NALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKK-LLGKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDVTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 396 LSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTF 475
Cdd:CHL00094 392 LSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 476 DVDSNGILNVSAVEKGTGKSNKITITNdKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGD 555
Cdd:CHL00094 472 DIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKD 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 6323004 556 KLEQADKDAVTKKAEETIAWLDSNTTatkEEFDDQLKELQEVANPIMSKLYQA 608
Cdd:CHL00094 551 KISEEKKEKIENLIKKLRQALQNDNY---ESIKSLLEELQKALMEIGKEVYSS 600
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-610 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 690.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 1 MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDT-ERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDP 79
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 80 EVQgdMKHFPFKLidVDGKPQ-IQVEFKGetKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKD 158
Cdd:PRK13411 81 EEE--RSRVPYTC--VKGRDDtVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 159 AGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHF 238
Cdd:PRK13411 155 AGTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 239 IQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSveIDSLFEGID------FYTSITRARFEELCADLFRSTLD 312
Cdd:PRK13411 235 VENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTS--INLPFITADetgpkhLEMELTRAKFEELTKDLVEATIE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 313 PVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAILTGDesskTQDLLLLD 392
Cdd:PRK13411 313 PMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDLLLLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 393 VAPLSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIE 472
Cdd:PRK13411 389 VTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 473 VTFDVDSNGILNVSAVEKGTGKSNKITITNdKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISE 552
Cdd:PRK13411 469 VSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKE 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323004 553 AGDKLEQADKDAVTKKAEETIAWLDsNTTATKEEFDDQLKELQEVANPIMSKLYQAGG 610
Cdd:PRK13411 548 NGELISEELKQRAEQKVEQLEAALT-DPNISLEELKQQLEEFQQALLAIGAEVYQQGG 604
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
5-610 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 678.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDT-ERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLIDVDGKpQIQVEFKGetKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:PTZ00400 124 EQKILPYKIVRASNG-DAWIEAQG--KKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDK-KGKEehVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEF 242
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDKnDGKT--IAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 KRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTsvEIDSLFEGID------FYTSITRARFEELCADLFRSTLDPVEK 316
Cdd:PTZ00400 279 KKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADqsgpkhLQIKLSRAKLEELTHDLLKKTIEPCEK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 317 VLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTGDesskTQDLLLLDVAPL 396
Cdd:PTZ00400 357 CIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDLLLLDVTPL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 397 SLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFD 476
Cdd:PTZ00400 432 SLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFD 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 477 VDSNGILNVSAVEKGTGKSNKITITNDKGrLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDK 556
Cdd:PTZ00400 512 VDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDK 590
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 6323004 557 LEQADKDAVtkkaEETIAWLDSN-TTATKEEFDDQLKELQEVANPIMSKLYQAGG 610
Cdd:PTZ00400 591 ISDADKDEL----KQKITKLRSTlSSEDVDSIKDKTKQLQEASWKISQQAYKQGN 641
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-537 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 634.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 1 MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFT-DTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNdp 79
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 80 EVQGDMKHFPFKlIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDA 159
Cdd:PRK13410 79 ELDPESKRVPYT-IRRNEQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 160 GTIAGLNVLRIINEPTAAAIAYGLDKkGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFI 239
Cdd:PRK13410 158 GRIAGLEVERILNEPTAAALAYGLDR-SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 240 QEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVE---IDSLFEG---IDfyTSITRARFEELCADLFRSTLDP 313
Cdd:PRK13410 237 EQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISlpfITATEDGpkhIE--TRLDRKQFESLCGDLLDRLLRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 314 VEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDyFNGKEPNRSINPDEAVAYGAAVQAAILTGDesskTQDLLLLDV 393
Cdd:PRK13410 315 VKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRT-LIPREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLDV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 394 APLSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEV 473
Cdd:PRK13410 390 TPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQV 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323004 474 TFDVDSNGILNVSAVEKGTGKSNKITITNdKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKN 537
Cdd:PRK13410 470 AFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRN 532
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
4-377 |
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: 633.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDrVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:cd24093 1 AIGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLD--KKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQE 241
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 242 FKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDA 321
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323004 322 KLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-613 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 623.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 3 KAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDT-ERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNdpEV 81
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMS--EV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 82 QGDMKHFPFKLIDvDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGT 161
Cdd:PLN03184 118 DEESKQVSYRVVR-DENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 162 IAGLNVLRIINEPTAAAIAYGLDKKgKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQE 241
Cdd:PLN03184 197 IAGLEVLRIINEPTAASLAYGFEKK-SNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 242 FKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVE---IDSLFEG---IDfyTSITRARFEELCADLFRSTLDPVE 315
Cdd:PLN03184 276 FKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 316 KVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDyFNGKEPNRSINPDEAVAYGAAVQAAILTGDESsktqDLLLLDVAP 395
Cdd:PLN03184 354 NALRDAKLSFKDIDEVILVGGSTRIPAVQELVKK-LTGKDPNVTVNPDEVVALGAAVQAGVLAGEVS----DIVLLDVTP 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 396 LSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTF 475
Cdd:PLN03184 429 LSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKF 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 476 DVDSNGILNVSAVEKGTGKSNKITITNdKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGD 555
Cdd:PLN03184 509 DIDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGD 587
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323004 556 KLEQADKDAVTKKAEETIAWLDSNTTatkEEFDDQLKELQEVANPIMSKLYQAGGAPE 613
Cdd:PLN03184 588 KVPADVKEKVEAKLKELKDAIASGST---QKMKDAMAALNQEVMQIGQSLYNQPGAGG 642
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
5-611 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 599.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGD 84
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 85 MKHFPFKLIDV-DGKPQIQvefKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:PTZ00186 110 IKNVPYKIVRAgNGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKgKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFK 243
Cdd:PTZ00186 187 GLNVIRVVNEPTAAALAYGMDKT-KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEFR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 244 RKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGID----FYTSITRARFEELCADLFRSTLDPVEKVLR 319
Cdd:PTZ00186 266 KTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAPCKQCMK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 320 DAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTGDesskTQDLLLLDVAPLSLG 399
Cdd:PTZ00186 346 DAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVTPLSLG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 400 IETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDS 479
Cdd:PTZ00186 421 IETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 480 NGILNVSAVEKGTGKSNKITITNDKGrLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEaGDKLEQ 559
Cdd:PTZ00186 501 NGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGE-WKYVSD 578
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 6323004 560 ADKDAVTKKAEETIAWLDsNTTATKEEFDDQLKELQEVANPIMSKLYQAGGA 611
Cdd:PTZ00186 579 AEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQKAVMECGRTEYQQAAA 629
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
4-515 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 557.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDpeVQG 83
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLID-VDGKPQIQVEFkGetkNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:PRK05183 99 RYPHLPYQFVAsENGMPLIRTAQ-G---LKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDKkGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEF 242
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDS-GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 KRKNKKDLSTNqralRRLRTACERAKRTLSSSAQTSVEIdSLFEGIdfytsITRARFEELCADLFRSTLDPVEKVLRDAK 322
Cdd:PRK05183 254 GLSPRLDPEDQ----RLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLACRRALRDAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 323 LDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTGDESSKtqDLLLLDVAPLSLGIET 402
Cdd:PRK05183 324 VEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGLET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 403 AGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGI 482
Cdd:PRK05183 401 MGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGL 480
|
490 500 510
....*....|....*....|....*....|...
gi 6323004 483 LNVSAVEKGTGKSNKITITNDKGrLSKEDIEKM 515
Cdd:PRK05183 481 LSVTAMEKSTGVEASIQVKPSYG-LTDDEIARM 512
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
5-378 |
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: 556.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDT-ERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPfklidVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd10234 82 KQVPYP-----VVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKgKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFK 243
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDKK-KDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 244 RKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVE---IDSLFEG-IDFYTSITRARFEELCADLFRSTLDPVEKVLR 319
Cdd:cd10234 236 KEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpKHLEMKLTRAKFEELTEDLVERTIEPVEQALK 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323004 320 DAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILT 378
Cdd:cd10234 316 DAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
4-604 |
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: 531.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGF-TDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQ 82
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 83 GDMkhfPFKLIDVDGKpqiQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:TIGR01991 81 SIL---PYRFVDGPGE---MVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDkKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEF 242
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLD-KASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 KRKNKKDLSTNQRALRRLRTACERAkrtlssSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAK 322
Cdd:TIGR01991 234 GISADLNPEDQRLLLQAARAAKEAL------TDAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 323 LDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTGDESSKtqDLLLLDVAPLSLGIET 402
Cdd:TIGR01991 308 LSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLGIET 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 403 AGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGI 482
Cdd:TIGR01991 385 MGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 483 LNVSAVEKGTGKSNKITITNDKGrLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADK 562
Cdd:TIGR01991 465 LTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDER 543
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 6323004 563 DAVTK---KAEETIAwlDSNTTATKeefdDQLKELQEVANPIMSK 604
Cdd:TIGR01991 544 AAIDAameALQKALQ--GDDADAIK----AAIEALEEATDNFAAR 582
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
5-377 |
1.91e-176 |
|
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: 506.03 E-value: 1.91e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFT-DTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLIDVDGKpQIQVEFKGetKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd11733 84 DIKMVPYKIVKASNG-DAWVEAHG--KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKGkEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFK 243
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKKD-DKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 244 RKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTsvEIDSLFEGID------FYTSITRARFEELCADLFRSTLDPVEKV 317
Cdd:cd11733 240 KEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTVEPCKKC 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 318 LRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd11733 318 LKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
4-379 |
8.48e-159 |
|
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: 461.15 E-value: 8.48e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFT-DTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQ 82
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAEVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 83 GDMKHFPFKLIDvDGKPQIQVEFKGetKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:cd11734 83 RDIKEVPYKIVK-HSNGDAWVEARG--QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDKKGkEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEF 242
Cdd:cd11734 160 AGLNVLRVINEPTAAALAYGLDKSG-DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 KRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTsvEIDSLFEGID------FYTSITRARFEELCADLFRSTLDPVEK 316
Cdd:cd11734 239 KKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQT--DINLPFITADasgpkhINMKLTRAQFESLVKPLVDRTVEPCKK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323004 317 VLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTG 379
Cdd:cd11734 317 ALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
1-379 |
6.55e-154 |
|
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: 448.20 E-value: 6.55e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 1 MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLI-GDAAKNQAAMNPANTVFDAKRLIGRNFNDp 79
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 80 eVQGDMKHFPFKLIDvdgKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDA 159
Cdd:cd10236 80 -VKEELPLLPYRLVG---DENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 160 GTIAGLNVLRIINEPTAAAIAYGLDKKgKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFI 239
Cdd:cd10236 156 ARLAGLNVLRLLNEPTAAALAYGLDQK-KEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 240 QEfkrkNKKDLSTNQRALRRLRTACERAKRTLSSsaQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLR 319
Cdd:cd10236 235 KQ----IGIDARLDPAVQQALLQAARRAKEALSD--ADSASIEVEVEGKDWEREITREEFEELIQPLVKRTLEPCRRALK 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 320 DAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTG 379
Cdd:cd10236 309 DAGLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-379 |
2.83e-153 |
|
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: 447.94 E-value: 2.83e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 3 KAVGIDLGTTYSCVA--HFSNDRVDIIANDQGNRTTPSFVGFTDTER-LIGDAAKNQAAMNPANTVFDAKRLIGRNFNDP 79
Cdd:cd10237 23 KIVGIDLGTTYSCVGvyHAVTGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 80 EVQGDMKHFPFKLI-DVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKD 158
Cdd:cd10237 103 ELEEEAKRYPFKVVnDNIGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 159 AGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHF 238
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 239 IQEFKRKNKKDLsTNQRALRRLRTACERAKRTLSS--SAQTSVEIDSLFEGID---FYTSITRARFEELCADLFRSTLDP 313
Cdd:cd10237 263 IDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNhnSASLSLPLQISLPSAFkvkFKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323004 314 VEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTG 379
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
4-377 |
8.42e-150 |
|
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: 437.83 E-value: 8.42e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQG 83
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 DMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd10238 82 LKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKGKEE--HVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQE 241
Cdd:cd10238 162 GFNVLRVISEPSAAALAYGIGQDDPTEnsNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLASE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 242 FKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDA 321
Cdd:cd10238 242 FKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNSA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323004 322 KLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd10238 322 GLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
5-377 |
2.64e-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: 433.16 E-value: 2.64e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIA-NDQGNRTTPSFVGFT-DTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEvq 82
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 83 gdmkhfpfkliDVDGKPqiqvefkgetknFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:cd24029 79 -----------EIGGKE------------YTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEF 242
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 KRK-NKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDA 321
Cdd:cd24029 216 GIEtGILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKDA 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323004 322 KLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd24029 296 KLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
5-375 |
2.04e-141 |
|
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: 416.58 E-value: 2.04e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGD 84
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 85 MKHFPFKLIDV-DGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd11732 81 IKLLPFKLVELeDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKG------KEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNH 237
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDlleseeKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 238 FIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKV 317
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323004 318 LRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAA 375
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 ... |
1-377 |
1.46e-140 |
|
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: 414.79 E-value: 1.46e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 1 MSkAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPE 80
Cdd:cd24095 1 MS-VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 81 VQGDMKHFPFKLIDV-DGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDA 159
Cdd:cd24095 80 VQRDLKLFPFKVTEGpDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 160 GTIAGLNVLRIINEPTAAAIAYGLDKKGKEE----HVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLV 235
Cdd:cd24095 160 AQIAGLNCLRLMNETTATALAYGIYKTDLPEtdptNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 236 NHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVE 315
Cdd:cd24095 240 DHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323004 316 KVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd24095 320 KALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
5-379 |
8.98e-133 |
|
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: 393.15 E-value: 8.98e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGF-TDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNdpevqg 83
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMGTDKQ------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 dmkhfpFKLIDvdgkpqiqvefkgetKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd10235 75 ------YRLGN---------------HTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFk 243
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKH- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 244 RKNKKDLSTNQRAlrRLRTACERAKRTLSSSAqtSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAKL 323
Cdd:cd10235 213 RLDFTSLSPSELA--ALRKRAEQAKRQLSSQD--SAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAGL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323004 324 DKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILTG 379
Cdd:cd10235 289 KPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
5-375 |
1.27e-132 |
|
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: 393.95 E-value: 1.27e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGD 84
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 85 MKHFPFKLID-VDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKG------KEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNH 237
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDlpaeeeKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 238 FIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQT-SVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEK 316
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSANATElPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323004 317 VLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAA 375
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
5-378 |
6.38e-127 |
|
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: 379.80 E-value: 6.38e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGD 84
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 85 MKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAG 164
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 165 LNVLRIINEPTAAAIAYGLDK------KGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHF 238
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKtdlpepEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 239 IQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVL 318
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 319 RDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILT 378
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
5-375 |
3.79e-113 |
|
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: 342.94 E-value: 3.79e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAH-FSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGrnfndpevqg 83
Cdd:cd10230 3 LGIDLGSEFIKVALvKPGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 84 dmkhfpfklidvdgkpqiqvefkgetknFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKK---GKEEHVLIFDLGGGTFDVSLLSI------EDGI------FEVKATAGDTHLGGE 228
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRRfenNEPQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 229 DFDNRLVNHFIQEFKRKNKK--DLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADL 306
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323004 307 FRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAA 375
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
4-516 |
4.04e-108 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 338.37 E-value: 4.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDaakNQAamnpantVFDAKRLIGRN----FNDP 79
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN---NKG-------LRSIKRLFGKTlkeiLNTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 80 EVQGDMKhfpfKLIDVDGKpqiQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDA 159
Cdd:PRK01433 91 ALFSLVK----DYLDVNSS---ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 160 GTIAGLNVLRIINEPTAAAIAYGLDKkGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFI 239
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNK-NQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 240 qefkrkNKKDLSTNQRALRrlrtACERAKRTLSSsaQTSVEIDSLfegidfytSITRARFEELCADLFRSTLDPVEKVLR 319
Cdd:PRK01433 243 ------NKFDLPNSIDTLQ----LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQECLE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 320 DAKldKSQVDEIVLVGGSTRIPKVQKLVTDYFNgKEPNRSINPDEAVAYGAAVQAAILTgdesSKTQDLLLLDVAPLSLG 399
Cdd:PRK01433 303 QAG--NPNIDGVILVGGATRIPLIKDELYKAFK-VDILSDIDPDKAVVWGAALQAENLI----APHTNSLLIDVVPLSLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 400 IETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDS 479
Cdd:PRK01433 376 MELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDA 455
|
490 500 510
....*....|....*....|....*....|....*..
gi 6323004 480 NGILNVSAVEKGTGKSNKITITNDKGrLSKEDIEKMV 516
Cdd:PRK01433 456 DGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIML 491
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-377 |
4.46e-100 |
|
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: 309.29 E-value: 4.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 4 AVGIDLGTTYSCVAHFSND-RVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVfdakrligRNFNDpevq 82
Cdd:cd10232 2 VIGISFGNSNSSIAIINKDgRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTV--------ANFRD---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 83 gdmkhfpfklidvdgkpqiqveFKGETKnFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTI 162
Cdd:cd10232 70 ----------------------LLGTTT-LTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYGLDK-----KGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNH 237
Cdd:cd10232 127 AGLEVLQLIPEPAAAALAYDLRAetsgdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 238 FIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKV 317
Cdd:cd10232 207 FAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTDA 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323004 318 LRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNG---KEPNRSINPDEAVAYGAAVQAAIL 377
Cdd:cd10232 287 IEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEstiIRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
5-376 |
3.01e-99 |
|
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: 308.41 E-value: 3.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGD 84
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 85 MKHFPFKLIDV-DGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd11737 83 KPSLAYELVQLpTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKG------KEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNH 237
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQDlpapeeKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 238 FIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSA-QTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEK 316
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANAsDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 317 VLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAI 376
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
5-375 |
3.54e-92 |
|
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: 289.84 E-value: 3.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGD 84
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 85 MKHFPFKLIDV-DGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd11739 83 KENLSYDLVPLkNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKK---GKEEH---VLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNH 237
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQdlpAPDEKpriVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 238 FIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSS-SAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEK 316
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323004 317 VLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAA 375
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
5-378 |
5.84e-92 |
|
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: 289.51 E-value: 5.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGD 84
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 85 MKHFPFKLIDV-DGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIA 163
Cdd:cd11738 83 KIKLPYELQKMpNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 164 GLNVLRIINEPTAAAIAYGLDKKG------KEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNH 237
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQDlpaleeKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 238 FIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQT-SVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEK 316
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANASDlPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323004 317 VLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAVQAAILT 378
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
5-372 |
2.52e-62 |
|
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: 210.04 E-value: 2.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIA---------NDQGNRTTPSFVgftdterligdaaknqaamnpantvfdakrligrn 75
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLvvlqlpwpgGDGGSSKVPSVL----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 76 fndpevqgdmkhfpfklidvdgkpqiqvefkgetknftpeQISSMVLGKMKETAESYLGAKVN-------DAVVTVPAYF 148
Cdd:cd10170 46 ----------------------------------------EVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGW 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 149 NDSQRQATKDAGTIAGL----NVLRIINEPTAAAIAYGLDKKG-----KEEHVLIFDLGGGTFDVSLLSIEDGIFEVK-- 217
Cdd:cd10170 86 SDAAREALREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDllplkPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLee 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 218 -ATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGID---FYTS 293
Cdd:cd10170 166 vAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 294 ITRARFEELCADLFRSTLDPVEKVLRDA--KLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPN---RSINPDEAVAY 368
Cdd:cd10170 246 GTLLLTEEEIRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVAR 325
|
....
gi 6323004 369 GAAV 372
Cdd:cd10170 326 GAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
5-372 |
2.62e-38 |
|
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: 146.65 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTE------RLIGDAAKNQAAMNPANtvfdakrliGRNFND 78
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEE---------GRLIKS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 79 PevqgdmKHF-PFKLIDvdgkpqiqvEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQAT- 156
Cdd:cd10231 72 V------KSFlGSSLFD---------ETTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDa 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 157 ------KDAGTIAGLNVLRIINEPTAAAIAYGLDKKgKEEHVLIFDLGGGTFDVSLL----SIEDGIFEVKATAGDtHLG 226
Cdd:cd10231 137 qaesrlRDAARRAGFRNVEFQYEPIAAALDYEQRLD-REELVLVVDFGGGTSDFSVLrlgpNRTDRRADILATSGV-GIG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 227 GEDFDNRLVNH-FIQEFKRK--------------------------NKKDLSTNQRALRRLRT----------------- 262
Cdd:cd10231 215 GDDFDRELALKkVMPHLGRGstyvsgdkglpvpawlyadlsnwhaiSLLYTKKTLRLLLDLRRdaadpekierllslved 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 263 --------ACERAKRTLSSSAQTSVEIDSLFEGIDfyTSITRARFEELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLV 334
Cdd:cd10231 295 qlghrlfrAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLT 372
|
410 420 430
....*....|....*....|....*....|....*...
gi 6323004 335 GGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGAAV 372
Cdd:cd10231 373 GGSSQSPAVRQALASLF-GQARLVEGDEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
5-371 |
4.71e-26 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 110.45 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVA----HFSNDRVDIIANDQG-----NRTTPSFVGFTDTERLIG---DAAKNQAAMNPANTV---FDAK 69
Cdd:cd10229 3 VAIDFGTTYSGYAysfiTDPGDIHTMYNWWGAptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDEEHqwlYFFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 70 RLIGRNFNDPEvqgdmkHFPFKLIDVDGKpqiqvefkgetkNFTPEQISSMVLGKMKETA------ESYLGAKVNDA--V 141
Cdd:cd10229 83 FKMMLLSEKEL------TRDTKVKAVNGK------------SMPALEVFAEALRYLKDHAlkelrdRSGSSLDEDDIrwV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 142 VTVPAYFNDSQRQATKDAGTIAGL------NVLRIINEPTAAAIAYGLDKKGKEEH-------VLIFDLGGGTFDVSLLS 208
Cdd:cd10229 145 LTVPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKLLAEGEEKelkpgdkYLVVDCGGGTVDITVHE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 209 I-EDGIFE--VKATAGdtHLGGEDFDNRLVN--------HFIQEFKRKNKKDLSTNQRALrrlrtacERAKRTlsssaqt 277
Cdd:cd10229 225 VlEDGKLEelLKASGG--PWGSTSVDEEFEElleeifgdDFMEAFKQKYPSDYLDLLQAF-------ERKKRS------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 278 sveiDSLfegidfytSITRARFEELCADLFRSTLDPVEKVLRDAKLDKsqVDEIVLVGGSTRIPKVQKLVTDYFNGKepN 357
Cdd:cd10229 289 ----FKL--------RLSPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAFSTK--V 352
|
410
....*....|....*..
gi 6323004 358 RSI---NPDEAVAYGAA 371
Cdd:cd10229 353 KIIippEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
5-372 |
1.49e-10 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 62.88 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 5 VGIDLGTTYSCVahFSNDRvDIIANDqgnrttPSFVGF-TDTERLI--GDaaknqaamnpantvfDAKRLIGRNFNDPEV 81
Cdd:cd10225 2 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 82 qgdmkHFPFKlidvDGkpqiqVefkgetknftpeqISSMvlgkmkETAESYLGA---KVN--------DAVVTVPAYFND 150
Cdd:cd10225 58 -----IRPLR----DG-----V-------------IADF------EATEAMLRYfirKAHrrrgflrpRVVIGVPSGITE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 151 SQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLD---KKGkeehVLIFDLGGGTFDVSLLSIeDGIFEVKAtagdTHLGG 227
Cdd:cd10225 105 VERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPieePRG----SMVVDIGGGTTEIAVISL-GGIVTSRS----VRVAG 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 228 EDFDNRLVNHfiqeFKRKNKKDLStnqralrrLRTAcERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARfeELCADLF 307
Cdd:cd10225 176 DEMDEAIINY----VRRKYNLLIG--------ERTA-ERIKIEIGSAYPLDEELSMEVRGRDLVTGLPRTI--EITSEEV 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323004 308 RSTLDP--------VEKVLRDAKLDKSQ--VDE-IVLVGGSTRIPKVQKLVTDYFngKEP-NRSINPDEAVAYGAAV 372
Cdd:cd10225 241 REALEEpvnaiveaVRSTLERTPPELAAdiVDRgIVLTGGGALLRGLDELLREET--GLPvHVADDPLTCVAKGAGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
140-371 |
1.08e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 53.98 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 140 AVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDkkgKEEHV--LIFDLGGGTFDVSLLSIeDGIfevk 217
Cdd:PRK13930 103 IVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLP---VTEPVgnMVVDIGGGTTEVAVISL-GGI---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 218 ATAGDTHLGGEDFDNRLVNHFiqefkrKNKKDLSTNQralrrlRTAcERAKRTLsSSAQTSVEIDSL-FEGIDFYTSITR 296
Cdd:PRK13930 175 VYSESIRVAGDEMDEAIVQYV------RRKYNLLIGE------RTA-EEIKIEI-GSAYPLDEEESMeVRGRDLVTGLPK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 297 ARfeELCADLFRSTL-DPVEKVLRDAK--LDKSQ-------VDE-IVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEA 365
Cdd:PRK13930 241 TI--EISSEEVREALaEPLQQIVEAVKsvLEKTPpelaadiIDRgIVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTC 317
|
....*.
gi 6323004 366 VAYGAA 371
Cdd:PRK13930 318 VARGTG 323
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
114-341 |
1.77e-07 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 54.10 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 114 PEQIS-------SMVLgKMKETAESYLGAKVNDAVVTVPAYFN-----DSQRQAT---KDAGTIAGLNVLRIINEPTAAA 178
Cdd:PRK11678 120 PQQVAlfedlvcAMML-HIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 179 IAY--GLDKkgkEEHVLIFDLGGGTFDVSLLsiedgifevkaTAGDTH-----------------LGGEDFD-----NRL 234
Cdd:PRK11678 199 LDFeaTLTE---EKRVLVVDIGGGTTDCSML-----------LMGPSWrgradrsasllghsgqrIGGNDLDialafKQL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 235 VNHF-------------IQEF----------------KRKNKKDLSTNQR------ALRRL-------------RTAcER 266
Cdd:PRK11678 265 MPLLgmgsetekgialpSLPFwnavaindvpaqsdfySLANGRLLNDLIRdarepeKVARLlkvwrqrlsyrlvRSA-EE 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323004 267 AKRTLSSSAQTSVEIDSLFEGIDfyTSITRARFEELCAdlfrstlDPVEKVLR--DAKLDKSQV--DEIVLVGGSTRIP 341
Cdd:PRK11678 344 AKIALSDQAETRASLDFISDGLA--TEISQQGLEEAIS-------QPLARILElvQLALDQAQVkpDVIYLTGGSARSP 413
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
141-371 |
2.05e-07 |
|
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: 53.16 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 141 VVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKgKEEHVLIFDLGGGTFDVSLLSIeDGIfeVKATA 220
Cdd:COG1077 103 VICVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIE-EPTGNMVVDIGGGTTEVAVISL-GGI--VVSRS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 221 gdTHLGGEDFDNRLVNHFiqefkrKNKKDLSTNQralrrlRTAcERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARfe 300
Cdd:COG1077 179 --IRVAGDELDEAIIQYV------RKKYNLLIGE------RTA-EEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTI-- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 301 ELCADLFRSTL-DPVEKVLRDAK--LDKSQ-------VDE-IVLVGGSTRIPKVQKLVTDYFNgkepnrsI------NPD 363
Cdd:COG1077 242 TITSEEIREALeEPLNAIVEAIKsvLEKTPpelaadiVDRgIVLTGGGALLRGLDKLLSEETG-------LpvhvaeDPL 314
|
....*...
gi 6323004 364 EAVAYGAA 371
Cdd:COG1077 315 TCVARGTG 322
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
140-370 |
1.05e-06 |
|
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: 51.02 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 140 AVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHvLIFDLGGGTFDVSLLSIeDGIfevkAT 219
Cdd:pfam06723 96 VVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGN-MVVDIGGGTTEVAVISL-GGI----VT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 220 AGDTHLGGEDFDNRLVNHFiqefkrKNKKDLSTNQralrrlRTAcERAKRTLSSSAQTSVEIDSLFEGIDFYT------S 293
Cdd:pfam06723 170 SKSVRVAGDEFDEAIIKYI------RKKYNLLIGE------RTA-ERIKIEIGSAYPTEEEEKMEIRGRDLVTglpktiE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 294 ITRARFEELCADLFRSTLDPVEKVLRD--AKLDKSQVDE-IVLVGGSTRIPKVQKLVTDYFnGKEPNRSINPDEAVAYGA 370
Cdd:pfam06723 237 ISSEEVREALKEPVSAIVEAVKEVLEKtpPELAADIVDRgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
141-243 |
1.09e-06 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 51.06 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 141 VVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIfDLGGGTFDVSLLSIEDGIfevkaTA 220
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVV-DIGGGTTDIAVLSLGGIV-----TS 172
|
90 100
....*....|....*....|...
gi 6323004 221 GDTHLGGEDFDNRLVNHFIQEFK 243
Cdd:PRK13928 173 SSIKVAGDKFDEAIIRYIRKKYK 195
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
141-354 |
1.65e-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: 50.77 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 141 VVTVPAYFNDSQRQATKDAGTIAGLNV------LRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSI---ED 211
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIYCRKLRLHQMDRYVVVDCGGGTVDLTVHQIrlpEG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 212 GIFEV-KATAGDTHLGGEDFD-NRLV-----NHFIQEFKRKNKKdlstnqrALRRLRTACERAKRTLSSSAQTSVEIDSL 284
Cdd:cd11735 224 HLKELyKASGGPYGSLGVDYEfEKLLckifgEDFIDQFKIKRPA-------AWVDLMIAFESRKRAAAPDRTNPLNITLP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 285 FEGIDFYTSITRARFE-------------------ELCAD----LFRSTLDPVEKVLRD--AKLDKSQVDEIVLVGGSTR 339
Cdd:cd11735 297 FSFIDYYKKFRGHSVEhalrksnvdfvkwssqgmlRMSPDamnaLFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAE 376
|
250
....*....|....*
gi 6323004 340 IPKVQKLVTDYFNGK 354
Cdd:cd11735 377 SPLLQQAVQNAFGDQ 391
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
124-225 |
7.82e-06 |
|
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: 47.65 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 124 KMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGkeehvlIFDLGGGTFD 203
Cdd:cd24047 51 KLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDGA------VVDIGGGTTG 124
|
90 100
....*....|....*....|....*.
gi 6323004 204 VSLlsIEDGifEVKATA----GDTHL 225
Cdd:cd24047 125 IAV--LKDG--KVVYTAdeptGGTHL 146
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
121-225 |
1.09e-05 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 47.52 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 121 VLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGkeehvlIFDLGGG 200
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNGA------VVDIGGG 145
|
90 100
....*....|....*....|....*....
gi 6323004 201 TFDVSLLsiEDGifEVKATA----GDTHL 225
Cdd:PRK15080 146 TTGISIL--KDG--KVVYSAdeptGGTHM 170
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
163-352 |
1.63e-05 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 47.43 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYgLDKKGKEEHVLIFDLGGGTFDVSLlsIEDGIfeVKATAGDThLGGedfdnrlvNHFIqef 242
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTEDEKELGVALVDIGGGTTDIAV--FKDGA--LRHTAVIP-VGG--------DHIT--- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 243 krknkKDLStnqRALR-RLRTAcERAKRTLSSSAQTSVEIDSLFE----GIDFYTSITR--------ARFEELcadlfrs 309
Cdd:COG0849 237 -----NDIA---IGLRtPLEEA-ERLKIKYGSALASLADEDETIEvpgiGGRPPREISRkelaeiieARVEEI------- 300
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6323004 310 tLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFN 352
Cdd:COG0849 301 -FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
285-383 |
5.52e-05 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 45.98 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 285 FEGIDFYTS---ITRARFEELCADLfRSTLDpvekVLRDAKLdksQVDEIVLVGGSTRIPKVQKLVTDYFNgkepnRSI- 360
Cdd:COG1070 358 FFGLTLSHTrahLARAVLEGVAFAL-RDGLE----ALEEAGV---KIDRIRATGGGARSPLWRQILADVLG-----RPVe 424
|
90 100
....*....|....*....|....*
gi 6323004 361 --NPDEAVAYGAAVQAAILTGDESS 383
Cdd:COG1070 425 vpEAEEGGALGAALLAAVGLGLYDD 449
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
141-351 |
6.95e-05 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 45.34 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 141 VVTVPAYFNDSQRQATKDAGTIAGL------NVLRIINEPTAAAI-AYGLDKkgkeehVLIFDLGGGTFDVSLLSIED-- 211
Cdd:cd11736 144 VLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR------YIVADCGGGTVDLTVHQIEQpq 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 212 GIFE--VKATAGDTHLGGED--FDNRLVN----HFIQEFKRKNKK---DLSTNQRAlrRLRTACERakrtLSSSAQTsve 280
Cdd:cd11736 218 GTLKelYKASGGPYGAVGVDlaFEKLLCQifgeDFIATFKAKRPAawvDLTIAFEA--RKRTAALR----MSSEAMN--- 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323004 281 idslfegidfytsitrarfeelcaDLFRSTLDPVEKVLrDAKLDKSQVDEI---VLVGGSTRIPKVQKLVTDYF 351
Cdd:cd11736 289 ------------------------ELFQPTISQIIQHI-DDLMKKPEVKGIkflFLVGGFAESPMLQRAVQAAF 337
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
163-372 |
1.31e-04 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 44.83 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 163 AGLNVLRIINEPTAAAIAYgLDKKGKEEHVLIFDLGGGTFDVSLLsiEDGIFEvkatagDTH---LGGedfdnrlvNHFI 239
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEKELGVALIDIGGGTTDIAVF--KNGSLR------YTAvipVGG--------NHIT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 240 qefkrknkKDLStnqRALRRLRTACERAKRTLSSSAQTSVEIDSLFE--GIDFYTS----------ITRARFEELcadlf 307
Cdd:cd24048 235 --------NDIA---IGLNTPFEEAERLKIKYGSALSEEADEDEIIEipGVGGREPrevsrrelaeIIEARVEEI----- 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 308 rstLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFN-----GKEPNRSINPDEAVAYGAAV 372
Cdd:cd24048 299 ---LELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvriGRPKNIGGLPEEVNDPAYAT 365
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
327-379 |
1.44e-04 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 44.85 E-value: 1.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 6323004 327 QVDEIVLVGGSTRIPKVQKLVTDYFNgkEPNRSINPDEAVAYGAAVQAAILTG 379
Cdd:cd07809 393 EIDEIRLIGGGSKSPVWRQILADVFG--VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
119-352 |
4.00e-04 |
|
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: 42.67 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 119 SMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKdagtiAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIfDLG 198
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPYDMRDLNIALV-DIG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 199 GGTFDVSLlsIEDGifEVKATaGDTHLGGEDFDNRLVNHFIQEFKrknkkdlstnqralrrlrtACERAKRTLSSS-AQT 277
Cdd:cd24004 123 AGTTDIAL--IRNG--GIEAY-RMVPLGGDDFTKAIAEGFLISFE-------------------EAEKIKRTYGIFlLIE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323004 278 SVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLrdakldksQVDEIVLVGGSTRIPKVQKLVTDYFN 352
Cdd:cd24004 179 AKDQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKFK--------LPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
2-237 |
8.41e-04 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 41.82 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 2 SKAVGIDLGTTYSCVahFSNDRvDIIANDqgnrttPSFVGFTDTER---LIGDAAKNQAAMNPANTVfdAKRligrnfnd 78
Cdd:PRK13929 4 STEIGIDLGTANILV--YSKNK-GIILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV--AVR-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 79 pevqgdmkhfPFKlidvDGkpqIQVEFkgetknftpEQISSMVLGKMKETAESY-LGAKVNDAVVTVPAYFNDSQRQATK 157
Cdd:PRK13929 65 ----------PMK----DG---VIADY---------DMTTDLLKQIMKKAGKNIgMTFRKPNVVVCTPSGSTAVERRAIS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 158 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIfDLGGGTFDVSLLSiedgiFEVKATAGDTHLGGEDFDNRLVNH 237
Cdd:PRK13929 119 DAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVV-DIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSF 192
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| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
141-237 |
1.82e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 40.84 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 141 VVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLD---KKGkeehVLIFDLGGGTFDVSLLSIeDGIfevk 217
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPvtePTG----SMVVDIGGGTTEVAVISL-GGI---- 170
|
90 100
....*....|....*....|
gi 6323004 218 ATAGDTHLGGEDFDNRLVNH 237
Cdd:PRK13927 171 VYSKSVRVGGDKFDEAIINY 190
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
165-250 |
4.98e-03 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 39.43 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323004 165 LNVLRIINEPTAAAIAYGLDKKG-KEEHVLIFDLGGGTFDVslLSIEDGIFEVKatAGDTHLGGEDFDNRLVNHFIQEFK 243
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDDElEDGNVLVIDIGGGTTDI--LTFENGKPIEE--SSDTLPGGEEALEKYADDILNELL 212
|
....*..
gi 6323004 244 RKNKKDL 250
Cdd:cd10227 213 KKLGDEL 219
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
139-201 |
7.36e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.06 E-value: 7.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323004 139 DAVVTVPAYFNDSQRQAT-----------KDAGTIAGLNVLRIINEPTAAAIAYGLDKkgKEEHVLIFDLGGGT 201
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTL--GPEGLLVVDLGGGT 86
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