|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
1-632 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1065.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 1 MGKIPAIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDD 80
Cdd:PTZ00009 1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 81 KKIQEDLKLWPFKVINE-KGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATK 159
Cdd:PTZ00009 81 SVVQSDMKHWPFKVTTGgDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 160 DAGSIAGLNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLV 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDG-IFEVKATAGDTHLGGEDFDNRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 240 NHFAEEFKRKHKS-DIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPV 318
Cdd:PTZ00009 240 EFCVQDFKRKNRGkDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 319 ERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNLSINPDEAVAYGAAVQAAILTGVGSSQIQDLLLVDVA 398
Cdd:PTZ00009 320 EKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 399 PLSLGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVA 478
Cdd:PTZ00009 400 PLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 479 FDLNADGILNVNAKDNSTGKSEKITISNDKGRLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAVDDAP 558
Cdd:PTZ00009 480 FDIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 559 -SGVLSETERSKVRDKCSSEASWLDKNSLAEKEEFESHLKECQRICTPIMSKIH-------------------GGKKGKS 618
Cdd:PTZ00009 560 vKGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYqaagggmpggmpggmpggmPGGAGPA 639
|
650
....*....|....
gi 54650896 619 SMGKGSHPTVEEVD 632
Cdd:PTZ00009 640 GAGASSGPTVEEVD 653
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
6-610 |
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: 879.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQE 85
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFKVIN-EKGKPKIEVEFKGERkrFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:pfam00012 81 DIKHLPYKVVKlPNGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSILEIGRG-VFEVKATNGDTHLGGEDFDLRLVDHLAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDIKGNARALRRLRTACERAKRTLSS-STEASLEID-ALHEGIDFYSKISRARFEELNMDLFRSTMQPVERAL 322
Cdd:pfam00012 237 EFKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFItAMADGKDVSGTLTRAKFEELVADLFERTLEPVEKAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 323 SDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGgKQLNLSINPDEAVAYGAAVQAAILTGvgSSQIQDLLLVDVAPLSL 402
Cdd:pfam00012 317 KDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFG-KEPSKGVNPDEAVAIGAAVQAGVLSG--TFDVKDFLLLDVTPLSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 403 GIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVAFDLN 482
Cdd:pfam00012 394 GIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDID 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 483 ADGILNVNAKDNSTGKSEKITISNDKGrLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAVDDApSGVL 562
Cdd:pfam00012 474 ANGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE-GDKV 551
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 54650896 563 SETERSKVRDKcsseASWLDKN-SLAEKEEFESHLKECQRICTPIMSKI 610
Cdd:pfam00012 552 PEAEKSKVESA----IEWLKDElEGDDKEEIEAKTEELAQVSQKIGERM 596
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
6-381 |
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: 857.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQE 85
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFKVINEKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAEE 245
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDG-IFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 246 FKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERALSDA 325
Cdd:cd10233 240 FKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 54650896 326 KMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNLSINPDEAVAYGAAVQAAIL 381
Cdd:cd10233 320 KLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-573 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 814.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 1 MGKIpaIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFD 79
Cdd:PRK00290 1 MGKI--IGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRRDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 80 DkkIQEDLKLWPFKVIN-EKGKPKIEVefKGerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQAT 158
Cdd:PRK00290 79 E--VQKDIKLVPYKIVKaDNGDAWVEI--DG--KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 159 KDAGSIAGLNVLRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRL 238
Cdd:PRK00290 153 KDAGKIAGLEVLRIINEPTAAALAYGLDK--KGDEKILVYDLGGGTFDVSILEIGDG-VFEVLSTNGDTHLGGDDFDQRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 239 VNHFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEAslEI-------DA---LHEGIdfysKISRARFEELNM 308
Cdd:PRK00290 230 IDYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EInlpfitaDAsgpKHLEI----KLTRAKFEELTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 309 DLFRSTMQPVERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGgKQLNLSINPDEAVAYGAAVQAAILTGvgssQ 388
Cdd:PRK00290 304 DLVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFG-KEPNKGVNPDEVVAIGAAIQGGVLAG----D 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 389 IQDLLLVDVAPLSLGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPA 468
Cdd:PRK00290 379 VKDVLLLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 469 PRGVPQIEVAFDLNADGILNVNAKDNSTGKSEKITISNDKGrLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIY 548
Cdd:PRK00290 459 PRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIY 537
|
570 580
....*....|....*....|....*
gi 54650896 549 ACRQAVDDApSGVLSETERSKVRDK 573
Cdd:PRK00290 538 QTEKTLKEL-GDKVPADEKEKIEAA 561
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
6-570 |
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: 746.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDdkKIQ 84
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 85 EDLKLWPFKVINEKGkpkiEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:TIGR02350 80 EEAKRVPYKVVGDGG----DVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSVLSIDEGSlFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKS-KKDEKILVFDLGGGTFDVSILEIGDGV-FEVLSTAGDTHLGGDDFDQRIIDWLAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLE---IDALHEG-IDFYSKISRARFEELNMDLFRSTMQPVER 320
Cdd:TIGR02350 234 EFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINlpfITADASGpKHLEMTLTRAKFEELTADLVERTKEPVRQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 321 ALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGgKQLNLSINPDEAVAYGAAVQAAILTGvgssQIQDLLLVDVAPL 400
Cdd:TIGR02350 314 ALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFG-KEPNKSVNPDEVVAIGAAIQGGVLKG----DVKDVLLLDVTPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 401 SLGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVAFD 480
Cdd:TIGR02350 389 SLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 481 LNADGILNVNAKDNSTGKSEKITISNDKGrLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAVDDAPSG 560
Cdd:TIGR02350 469 IDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDK 547
|
570
....*....|
gi 54650896 561 vLSETERSKV 570
Cdd:TIGR02350 548 -LPAEEKEKI 556
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
6-381 |
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: 732.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQE 85
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFKVIN-EKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:cd24028 81 DIKHWPFKVVEdEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLLSIDNG-VFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERALSD 324
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 54650896 325 AKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNLSINPDEAVAYGAAVQAAIL 381
Cdd:cd24028 320 AKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
5-381 |
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: 719.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 5 PAIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQ 84
Cdd:cd10241 2 TVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 85 EDLKLWPFKVINEKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:cd10241 82 KDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:cd10241 162 AGLNVLRIINEPTAAAIAYGLDKK-GGEKNILVFDLGGGTFDVSLLTIDNG-VFEVLATNGDTHLGGEDFDQRVMDHFIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERALSD 324
Cdd:cd10241 240 LFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLED 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 54650896 325 AKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNLSINPDEAVAYGAAVQAAIL 381
Cdd:cd10241 320 AGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-619 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 660.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 1 MGKIpaIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFD 79
Cdd:PRK13411 1 MGKV--IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 80 DKkiQEDLKLWPFKVIneKGKPK-IEVEFKGerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQAT 158
Cdd:PRK13411 79 DT--EEERSRVPYTCV--KGRDDtVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 159 KDAGSIAGLNVLRIINEPTAAALAYGLDKNLKgERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRL 238
Cdd:PRK13411 153 KDAGTIAGLEVLRIINEPTAAALAYGLDKQDQ-EQLILVFDLGGGTFDVSILQLGDG-VFEVKATAGNNHLGGDDFDNCI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 239 VNHFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSS--STEASL------EIDALHEGIDFyskiSRARFEELNMDL 310
Cdd:PRK13411 231 VDWLVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSmlTTSINLpfitadETGPKHLEMEL----TRAKFEELTKDL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 311 FRSTMQPVERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNLSINPDEAVAYGAAVQAAILTGvgssQIQ 390
Cdd:PRK13411 307 VEATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGG----EVK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 391 DLLLVDVAPLSLGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPR 470
Cdd:PRK13411 383 DLLLLDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 471 GVPQIEVAFDLNADGILNVNAKDNSTGKSEKITISNdKGRLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYAC 550
Cdd:PRK13411 463 GVPQIEVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSY 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54650896 551 RQAVDDApSGVLSETERSKVRDKCSSEASWLDKNSLaEKEEFESHLKECQRICTPIMSKIHGGKKGKSS 619
Cdd:PRK13411 542 ESTLKEN-GELISEELKQRAEQKVEQLEAALTDPNI-SLEELKQQLEEFQQALLAIGAEVYQQGGSQTT 608
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-620 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 656.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 1 MGKIpaIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFD 79
Cdd:CHL00094 1 MGKV--VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 80 DkkIQEDLKLWPFKVIN-EKGKPKIEVEFKGerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQAT 158
Cdd:CHL00094 79 E--ISEEAKQVSYKVKTdSNGNIKIECPALN--KDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 159 KDAGSIAGLNVLRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRL 238
Cdd:CHL00094 155 KDAGKIAGLEVLRIINEPTAASLAYGLDK--KNNETILVFDLGGGTFDVSILEVGDG-VFEVLSTSGDTHLGGDDFDKKI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 239 VNHFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLE---IDALHEG-IDFYSKISRARFEELNMDLFRST 314
Cdd:CHL00094 232 VNWLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRC 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 315 MQPVERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGgKQLNLSINPDEAVAYGAAVQAAILTGvgssQIQDLLL 394
Cdd:CHL00094 312 RIPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLG-KKPNQSVNPDEVVAIGAAVQAGVLAG----EVKDILL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 395 VDVAPLSLGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQ 474
Cdd:CHL00094 387 LDVTPLSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 475 IEVAFDLNADGILNVNAKDNSTGKSEKITISNdKGRLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAV 554
Cdd:CHL00094 467 IEVTFDIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQL 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54650896 555 DDApSGVLSETERSKVRDKCSSEASWLDKNSLaekEEFESHLKECQRICTPIMSKIHGGKKGKSSM 620
Cdd:CHL00094 546 KEL-KDKISEEKKEKIENLIKKLRQALQNDNY---ESIKSLLEELQKALMEIGKEVYSSTSTTDPA 607
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
6-520 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 655.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDkkiq 84
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDgEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 85 edlklwpfkvinekgkpkIEVEFKGerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:COG0443 77 ------------------EATEVGG--KRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSVLSIDEGSlFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKG-KEEETILVYDLGGGTFDVSILRLGDGV-FEVLATGGDTHLGGDDFDQALADYVAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDaLHEGIDFYSKISRARFEELNMDLFRSTMQPVERALSD 324
Cdd:COG0443 215 EFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALAD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 325 AKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGgKQLNLSINPDEAVAYGAAVQAAILTGvgssQIQDLllvDVAPLSLGI 404
Cdd:COG0443 294 AGLSPSDIDAVLLVGGSTRMPAVRERVKELFG-KEPLKGVDPDEAVALGAAIQAGVLAG----DVKDL---DVTPLSLGI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 405 ETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVAFDLNAD 484
Cdd:COG0443 366 ETLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDAN 445
|
490 500 510
....*....|....*....|....*....|....*.
gi 54650896 485 GILNVNAKDNSTGKSEKITIsndkgrlsKAEIDRML 520
Cdd:COG0443 446 GILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-557 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 637.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 1 MGKIpaIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFN-ETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFD 79
Cdd:PRK13410 1 MGRI--VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 80 DkkIQEDLKLWPFKV-INEKGKPKIEVEFKgeRKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQAT 158
Cdd:PRK13410 79 E--LDPESKRVPYTIrRNEQGNVRIKCPRL--EREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 159 KDAGSIAGLNVLRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRL 238
Cdd:PRK13410 155 RDAGRIAGLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLEVGNG-VFEVKATSGDTQLGGNDFDKRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 239 VNHFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLS--SSTEASLE-IDALHEG---IDfySKISRARFEELNMDLFR 312
Cdd:PRK13410 232 VDWLAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpkhIE--TRLDRKQFESLCGDLLD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 313 STMQPVERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGgKQLNLSINPDEAVAYGAAVQAAILTGvgssQIQDL 392
Cdd:PRK13410 310 RLLRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIP-REPNQNVNPDEVVAVGAAIQAGILAG----ELKDL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 393 LLVDVAPLSLGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGV 472
Cdd:PRK13410 385 LLLDVTPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 473 PQIEVAFDLNADGILNVNAKDNSTGKSEKITI---SNdkgrLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYA 549
Cdd:PRK13410 465 PQVQVAFDIDANGILQVSATDRTTGREQSVTIqgaST----LSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQ 540
|
....*...
gi 54650896 550 CRQAVDDA 557
Cdd:PRK13410 541 AERRLRDA 548
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
7-630 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 635.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQE 85
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFKVINEK-GKPKIEvefkGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:PTZ00400 124 EQKILPYKIVRASnGDAWIE----AQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSVLSIdEGSLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:PTZ00400 200 AGLDVLRIINEPTAAALAFGMDKN--DGKTIAVYDLGGGTFDISILEI-LGGVFEVKATNGNTSLGGEDFDQRILNYLIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLE---IDALHEGID-FYSKISRARFEELNMDLFRSTMQPVER 320
Cdd:PTZ00400 277 EFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINlpfITADQSGPKhLQIKLSRAKLEELTHDLLKKTIEPCEK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 321 ALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGgKQLNLSINPDEAVAYGAAVQAAILTGvgssQIQDLLLVDVAPL 400
Cdd:PTZ00400 357 CIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFG-KEPSKGVNPDEAVAMGAAIQAGVLKG----EIKDLLLLDVTPL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 401 SLGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVAFD 480
Cdd:PTZ00400 432 SLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFD 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 481 LNADGILNVNAKDNSTGKSEKITISNDKGrLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAVDDApSG 560
Cdd:PTZ00400 512 VDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDL-KD 589
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54650896 561 VLSETERSKVRDKCSSEASWLDKNSLaekEEFESHLKECQRICTPIMSKIH--GGKKGKSSMGKGSHPTVEE 630
Cdd:PTZ00400 590 KISDADKDELKQKITKLRSTLSSEDV---DSIKDKTKQLQEASWKISQQAYkqGNSDNQQSEQSTNSEESEE 658
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
6-381 |
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: 616.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSkVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQE 85
Cdd:cd24093 1 AIGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFKVINEKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLD-KNLKGERNVLIFDLGGGTFDVSVLSIdEGSLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGaGKSEKERHVLIFDLGGGTFDVSLLHI-AGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERALSD 324
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 54650896 325 AKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNLSINPDEAVAYGAAVQAAIL 381
Cdd:cd24093 319 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
7-573 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 572.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDkkIQE 85
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFKVI-NEKGKPKIEVEFKGerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:PLN03184 120 ESKQVSYRVVrDENGNVKLDCPAIG--KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEK--KSNETILVFDLGGGTFDVSVLEVGDG-VFEVLSTSGDTHLGGDDFDKRIVDWLAS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLE---IDALHEG---IDfySKISRARFEELNMDLFRSTMQPV 318
Cdd:PLN03184 275 NFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 319 ERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLfGGKQLNLSINPDEAVAYGAAVQAAILTGvgssQIQDLLLVDVA 398
Cdd:PLN03184 353 ENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAG----EVSDIVLLDVT 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 399 PLSLGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVA 478
Cdd:PLN03184 428 PLSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVK 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 479 FDLNADGILNVNAKDNSTGKSEKITISNdKGRLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAVDDAP 558
Cdd:PLN03184 508 FDIDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELG 586
|
570
....*....|....*
gi 54650896 559 SGVLSETeRSKVRDK 573
Cdd:PLN03184 587 DKVPADV-KEKVEAK 600
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
7-601 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 567.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQED 86
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 87 LKLWPFKVINE-KGKPKIEvefKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:PTZ00186 110 IKNVPYKIVRAgNGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSVLSIdEGSLFEVKATAGDTHLGGEDFDNRLVNHFAEE 245
Cdd:PTZ00186 187 GLNVIRVVNEPTAAALAYGMDKT--KDSLIAVYDLGGGTFDISVLEI-AGGVFEVKATNGDTHLGGEDFDLALSDYILEE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 246 FKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLE---IDALHEGIDFYS-KISRARFEELNMDLFRSTMQPVERA 321
Cdd:PTZ00186 264 FRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNlpfITANADGAQHIQmHISRSKFEGITQRLIERSIAPCKQC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 322 LSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNlSINPDEAVAYGAAVQAAILTGvgssQIQDLLLVDVAPLS 401
Cdd:PTZ00186 344 MKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFR-GVNPDEAVALGAATLGGVLRG----DVKGLVLLDVTPLS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 402 LGIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVAFDL 481
Cdd:PTZ00186 419 LGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDI 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 482 NADGILNVNAKDNSTGKSEKITISNDKGrLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAVDDAPsgV 561
Cdd:PTZ00186 499 DANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWK--Y 575
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 54650896 562 LSETERSKVRD-----KCSSEASWLDKNSL-AEKEEFESHLKECQR 601
Cdd:PTZ00186 576 VSDAEKENVKTlvaelRKAMENPNVAKDDLaAATDKLQKAVMECGR 621
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
7-382 |
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: 534.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQE 85
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFkviNEKGKPKIEVEFKGerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd10234 82 KQVPYPV---VSAGNGDAWVEIGG--KEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAEE 245
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDK--KKDEKILVYDLGGGTFDVSILEIGDG-VFEVLSTNGDTHLGGDDFDQRIIDYLADE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 246 FKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLE---IDALHEG---IDFysKISRARFEELNMDLFRSTMQPVE 319
Cdd:cd10234 234 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpkhLEM--KLTRAKFEELTEDLVERTIEPVE 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54650896 320 RALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAAILT 382
Cdd:cd10234 312 QALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
6-571 |
4.34e-170 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 498.55 E-value: 4.34e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDkkIQE 85
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFK-VINEKGKPKIEVEFkGERkrfAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:PRK05183 99 RYPHLPYQfVASENGMPLIRTAQ-GLK---SPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDSG--QEGVIAVYDLGGGTFDISILRLSKG-VFEVLATGGDSALGGDDFDHLLADWILE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKHKSDikgnARALRRLRTACERAKRTLSSSTEASLEIdALHEGIdfyskISRARFEELNMDLFRSTMQPVERALSD 324
Cdd:PRK05183 252 QAGLSPRLD----PEDQRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLACRRALRD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 325 AKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNlSINPDEAVAYGAAVQAAILtgVGSSQIQDLLLVDVAPLSLGI 404
Cdd:PRK05183 322 AGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLT-SIDPDKVVAIGAAIQADIL--AGNKPDSDMLLLDVIPLSLGL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 405 ETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVAFDLNAD 484
Cdd:PRK05183 399 ETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDAD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 485 GILNVNAKDNSTGKSEKITISNDKGrLSKAEIDRMLSEAEKYKVEDDRQR----ERVQSKNNLEAYiyacrQAVDDAPSG 560
Cdd:PRK05183 479 GLLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEAL-----QAALAADGD 552
|
570
....*....|.
gi 54650896 561 VLSETERSKVR 571
Cdd:PRK05183 553 LLSAAERAAID 563
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
6-571 |
1.48e-169 |
|
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: 496.41 E-value: 1.48e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNE-TERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQ 84
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKdGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 85 EDLklwPFKVINEKGKpkiEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:TIGR01991 81 SIL---PYRFVDGPGE---MVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDKA--SEGIYAVYDLGGGTFDVSILKLTKG-VFEVLATGGDSALGGDDFDHALAKWILK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 efkrkhKSDIKG--NARALRRLRTACERAKRTLSssTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERAL 322
Cdd:TIGR01991 232 ------QLGISAdlNPEDQRLLLQAARAAKEALT--DAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 323 SDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNlSINPDEAVAYGAAVQAAILTGVGSSQiqDLLLVDVAPLSL 402
Cdd:TIGR01991 304 RDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLT-DIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 403 GIETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVAFDLN 482
Cdd:TIGR01991 381 GIETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 483 ADGILNVNAKDNSTGKSEKITISNDKGrLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAVdDAPSGVL 562
Cdd:TIGR01991 461 ADGLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAAL-AADGDLL 538
|
....*....
gi 54650896 563 SETERSKVR 571
Cdd:TIGR01991 539 SEDERAAID 547
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
7-381 |
3.08e-166 |
|
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: 479.45 E-value: 3.08e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAF-NETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQE 85
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFtADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFKVINEKGKPKIeVEFKGerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd11733 84 DIKMVPYKIVKASNGDAW-VEAHG--KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAEE 245
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDK--KDDKIIAVYDLGGGTFDISILEIQKG-VFEVKATNGDTFLGGEDFDNALLNYLVAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 246 FKRKHKSDIKGNARALRRLRTACERAKRTLSSS--TEASLE-IDALHEGID-FYSKISRARFEELNMDLFRSTMQPVERA 321
Cdd:cd11733 238 FKKEQGIDLSKDNLALQRLREAAEKAKIELSSSlqTDINLPfITADASGPKhLNMKLTRAKFESLVGDLIKRTVEPCKKC 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 322 LSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAAIL 381
Cdd:cd11733 318 LKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
5-383 |
2.92e-150 |
|
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: 438.80 E-value: 2.92e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 5 PAIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKI 83
Cdd:cd11734 2 PVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDgERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 84 QEDLKLWPFKVINEKGKPKIeVEFKGerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGS 163
Cdd:cd11734 82 QRDIKEVPYKIVKHSNGDAW-VEARG--QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 164 IAGLNVLRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFA 243
Cdd:cd11734 159 IAGLNVLRVINEPTAAALAYGLDKS--GDKVIAVYDLGGGTFDISILEIQKG-VFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 244 EEFKRKHKSDIKGNARALRRLRTACERAKRTLSSS--TEASLE-IDALHEGIDFYS-KISRARFEELNMDLFRSTMQPVE 319
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTlqTDINLPfITADASGPKHINmKLTRAQFESLVKPLVDRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54650896 320 RALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAAILTG 383
Cdd:cd11734 316 KALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-381 |
1.34e-147 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; HSPA14, also called HSP70-like protein 1 (Hsp70L1), or heat shock protein HSP60, is a component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, HSPA14 binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466836 [Multi-domain] Cd Length: 377 Bit Score: 432.05 E-value: 1.34e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 5 PAIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQ 84
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 85 EDLKLWPFKVINEKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNLK-GERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFA 243
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPtENSNVLVYRLGGTSLDVTVLSVNNG-MYRVLATRTDDNLGGDDFTEALAEHLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 244 EEFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERALS 323
Cdd:cd10238 240 SEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 54650896 324 DAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNLSINPDEAVAYGAAVQAAIL 381
Cdd:cd10238 320 SAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
7-379 |
2.28e-142 |
|
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: 418.89 E-value: 2.28e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQED 86
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 87 LKLWPFKVIN-EKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGL---DKNLKGE--RNVLIFDLGGGTFDVSVLSIDEGSLfEVKATAGDTHLGGEDFDNRLVN 240
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIyksDLLESEEkpRIVAFVDMGHSSTQVSIAAFTKGKL-KVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 241 HFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVER 320
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 54650896 321 ALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAA 379
Cdd:cd11732 320 ALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
7-383 |
5.33e-142 |
|
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: 419.05 E-value: 5.33e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQ--NSKVEIIANDQGNRTTPSYVAFNETER-LIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKI 83
Cdd:cd10237 25 VGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 84 QEDLKLWPFKVINEK-GKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAG 162
Cdd:cd10237 105 EEEAKRYPFKVVNDNiGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 163 SIAGLNVLRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSVLSIdEGSLFEVKATAGDTHLGGEDFDNRLVNHF 242
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKK-SDVNNVLVVDLGGGTLDVSLLNV-QGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 243 AEEFKRKHKSDIKgNARALRRLRTACERAKRTLSSSTEASLEID-----ALHEGIDFYSKISRARFEELNMDLFRSTMQP 317
Cdd:cd10237 263 IDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqislPSAFKVKFKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54650896 318 VERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAAILTG 383
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
6-383 |
6.15e-140 |
|
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: 411.99 E-value: 6.15e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLI-GDPAKNQVAMNAKNTVFDAKRLIGRKFDDkkIQ 84
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 85 EDLKLWPFKVIN-EKGKPKIEVEFKgerkRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGS 163
Cdd:cd10236 82 EELPLLPYRLVGdENELPRFRTGAG----NLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 164 IAGLNVLRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFA 243
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQ--KKEGTIAVYDLGGGTFDISILRLSDG-VFEVLATGGDTALGGDDFDHLLADWIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 244 EEFKRkhksDIKGNARALRRLRTACERAKRTLSSSTEASLEIDAlhEGIDFYSKISRARFEELNMDLFRSTMQPVERALS 323
Cdd:cd10236 235 KQIGI----DARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRALK 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 324 DAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNlSINPDEAVAYGAAVQAAILTG 383
Cdd:cd10236 309 DAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLT-SINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
7-381 |
5.93e-138 |
|
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: 406.58 E-value: 5.93e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIA-NDQGNRTTPSYVAFNE-TERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQ 84
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDKdGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 85 EDlklwpfkvinekgkpkievefkgerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:cd24029 81 GG-------------------------KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNLKGErNVLIFDLGGGTFDVSVLSIDEGSlFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDG-TILVYDLGGGTFDVSILEIENGK-FEVLATGGDNFLGGDDFDEAIAELILE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFKRKH-KSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERALS 323
Cdd:cd24029 214 KIGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 54650896 324 DAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNlSINPDEAVAYGAAVQAAIL 381
Cdd:cd24029 294 DAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPIS-SVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
6-381 |
1.22e-135 |
|
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: 402.07 E-value: 1.22e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQE 85
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLWPFKVIN-EKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:cd24095 83 DLKLFPFKVTEgPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNLKGE---RNVLIFDLGGGTFDVSVLSIDEGSLfEVKATAGDTHLGGEDFDNRLVNH 241
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIYKTDLPEtdpTNVVFVDVGHSSTQVCVVAFKKGQL-KVLSHAFDRNLGGRDFDEVLFDH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 242 FAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERA 321
Cdd:cd24095 242 FAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 322 LSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAAIL 381
Cdd:cd24095 322 LADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
7-379 |
5.28e-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: 392.41 E-value: 5.28e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQED 86
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 87 LKLWPFKVIN-EKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDKN-LKGE----RNVLIFDLGGGTFDVSVLSIDEGSLfEVKATAGDTHLGGEDFDNRLVN 240
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQdLPAEeekpRNVVFVDMGHSSLQVSVCAFNKGKL-KVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 241 HFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSS-STEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVE 319
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLR 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 320 RALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAA 379
Cdd:cd10228 320 SALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
7-384 |
5.86e-126 |
|
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: 377.10 E-value: 5.86e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQED 86
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 87 LKLWPFKVINEKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIAG 166
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 167 LNVLRIINEPTAAALAYGLDKN-LKGE----RNVLIFDLGGGTFDVSVLSIDEGSLfEVKATAGDTHLGGEDFDNRLVNH 241
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTdLPEPeekpRIVAFVDIGHSSYTVSIVAFKKGQL-TVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 242 FAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERA 321
Cdd:cd24094 240 FADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54650896 322 LSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAAILTGV 384
Cdd:cd24094 320 LAQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILSPV 381
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
7-383 |
2.06e-120 |
|
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: 361.18 E-value: 2.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNET-ERLIGDPAKNQVAMNAKNTVFDAKRLIGrkfddkkiqe 85
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDgSILVGRAAKERLVTHPDRTAASFKRFMG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 dlklwpfkviNEKgkpkievEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd10235 71 ----------TDK-------QYRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDKNLKgERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAEE 245
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKRED-ETRFLVFDLGGGTFDVSVLELFEG-VIEVHASAGDNFLGGEDFTHALADYFLKK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 246 FKRKHKSDikgNARALRRLRTACERAKRTLSSSTEAslEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVERALSDA 325
Cdd:cd10235 212 HRLDFTSL---SPSELAALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 54650896 326 KMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNlSINPDEAVAYGAAVQAAILTG 383
Cdd:cd10235 287 GLKPSDIDAVILVGGATRMPLVRQLIARLFGRLPLS-SLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
7-379 |
1.45e-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: 344.09 E-value: 1.45e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQ-NSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGrkfddkkiqe 85
Cdd:cd10230 3 LGIDLGSEFIKVALVKpGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 dlklwpfkvinekgkpkievefkgerkrFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLD--KNLKGERNVLIFDLGGGTFDVSVLSID-----------EGSLFEVKATAGDTHLGGE 232
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDrrFENNEPQNVLFYDMGASSTSATVVEFSsvkekdkgknkTVPQVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 233 DFDNRLVNHFAEEFKRKHKS--DIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDL 310
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54650896 311 FRSTMQPVERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNLSINPDEAVAYGAAVQAA 379
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
6-619 |
3.00e-106 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 333.36 E-value: 3.00e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 6 AIGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDpaknqvamnaKNTVFDAKRLIGRKFddKKIQE 85
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTL--KEILN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKLwpFKVINEK-GKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI 164
Cdd:PRK01433 89 TPAL--FSLVKDYlDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNLKGerNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLVNHFAE 244
Cdd:PRK01433 167 AGFEVLRLIAEPTAAAYAYGLNKNQKG--CYLVYDLGGGTFDVSILNIQEG-IFQVIATNGDNMLGGNDIDVVITQYLCN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 EFkrkhksDIKGNARALRrlrtACERAKRTLSSstEASLEIDALHegidfyskISRARFEELNMDLFRSTMQPVERALSD 324
Cdd:PRK01433 244 KF------DLPNSIDTLQ----LAKKAKETLTY--KDSFNNDNIS--------INKQTLEQLILPLVERTINIAQECLEQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 325 AKMDKkaIHDVVLVGGSTRIPKIQKLLQDLFGGKQLNlSINPDEAVAYGAAVQAAILTgvgsSQIQDLLLVDVAPLSLGI 404
Cdd:PRK01433 304 AGNPN--IDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLI----APHTNSLLIDVVPLSLGM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 405 ETAGGVMTNLVERNARIPCKQQQIFTTYSDNQNAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVAFDLNAD 484
Cdd:PRK01433 377 ELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDAD 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 485 GILNVNAKDNSTGKSEKITISNDKGrLSKAEIDRMLSEAEKYKVEDDRQRERVQSKNNLEAYIYACRQAVDDApSGVLSE 564
Cdd:PRK01433 457 GILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAEL-TTLLSE 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54650896 565 TERS-------KVRDKCSSEASWLDKNSLaekEEFESHLKecQRICTPIMSKIHGGKKGKSS 619
Cdd:PRK01433 535 SEISiinslldNIKEAVHARDIILINNSI---KEFKSKIK--KSMDTKLNIIINDLLKGKNI 591
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
5-381 |
5.26e-98 |
|
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: 303.90 E-value: 5.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 5 PAIGIDLGTTYSCVG-VWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKfddkki 83
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGTT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 84 qedlklwpfkvinekgkpkievefkgerkRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGS 163
Cdd:cd10232 75 -----------------------------TLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 164 IAGLNVLRIINEPTAAALAYGLDKNLKG----ERNVLIFDLGGGTFDVSVLSIDEGsLFEVKATAGDTHLGGEDFDNRLV 239
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGdtikDKTVVVADLGGTRSDVTVVAVRGG-LYTILATVHDYELGGVALDDVLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 240 NHFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSSSTEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVE 319
Cdd:cd10232 205 GHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVT 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54650896 320 RALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFGG---KQLNLSINPDEAVAYGAAVQAAIL 381
Cdd:cd10232 285 DAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEstiIRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
7-380 |
1.79e-96 |
|
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: 301.09 E-value: 1.79e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQED 86
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 87 LKLWPFKVIN-EKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd11737 83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDKN-----LKGERNVLIFDLGGGTFDVSVLSIDEGSLfEVKATAGDTHLGGEDFDNRLVN 240
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQdlpapEEKPRNVVFVDMGHSAYQVSVCAFNKGKL-KVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 241 HFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSS-STEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVE 319
Cdd:cd11737 242 HFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54650896 320 RALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAAI 380
Cdd:cd11737 322 SVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
7-382 |
7.03e-93 |
|
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: 291.82 E-value: 7.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQED 86
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 87 LKLWPFKVIN-EKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd11738 83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDKN-----LKGERNVLIFDLGGGTFDVSVLSIDEGSLfEVKATAGDTHLGGEDFDNRLVN 240
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQdlpalEEKPRNVVFVDMGHSAYQVSICAFNKGKL-KVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 241 HFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSS-STEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVE 319
Cdd:cd11738 242 YFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLK 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54650896 320 RALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAAILT 382
Cdd:cd11738 322 AVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
7-379 |
2.48e-89 |
|
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: 282.52 E-value: 2.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTVFDAKRLIGRKFDDKKIQED 86
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 87 LKLWPFK-VINEKGKPKIEVEFKGERKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIA 165
Cdd:cd11739 83 KENLSYDlVPLKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 166 GLNVLRIINEPTAAALAYGLDK-NLKGE----RNVLIFDLGGGTFDVSVLSIDEGSlFEVKATAGDTHLGGEDFDNRLVN 240
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKqDLPAPdekpRIVVFVDMGHSAFQVSACAFNKGK-LKVLGTAFDPYLGGRNFDEKLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 241 HFAEEFKRKHKSDIKGNARALRRLRTACERAKRTLSS-STEASLEIDALHEGIDFYSKISRARFEELNMDLFRSTMQPVE 319
Cdd:cd11739 242 HFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLY 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 320 RALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYGAAVQAA 379
Cdd:cd11739 322 SLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
118-376 |
6.04e-60 |
|
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: 203.49 E-value: 6.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 118 EISSMVLTKMREIAEVYLGGKVK-------DAVVTVPAYFNDSQRQATKDAGSIAGL----NVLRIINEPTAAALAYGLD 186
Cdd:cd10170 46 EVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALREAARAAGFgsdsDNVRLVSEPEAAALYALED 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 187 K----NLKGERNVLIFDLGGGTFDVSVLSIDEGSLFEVK--ATAGDTHLGGEDFDNRLVNHFAEEFKRKHKSDIKGNARA 260
Cdd:cd10170 126 KgdllPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLEevAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 261 LRRLRTACERAKRTLSSSTEASLEIDALHEGID---FYSKISRARFEELNMDLFRSTMQPVERALSDA--KMDKKAIHDV 335
Cdd:cd10170 206 LAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQleAKSGTPPDAV 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 54650896 336 VLVGGSTRIPKIQKLLQDLFGGKQLNL---SINPDEAVAYGAAV 376
Cdd:cd10170 286 VLVGGFSRSPYLRERLRERFGSAGIIIvlrSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
7-360 |
5.61e-37 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.
Pssm-ID: 466829 [Multi-domain] Cd Length: 409 Bit Score: 142.80 E-value: 5.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVWQNSKVEIIANDQGNRTTPSYVAFneTERLIGDPAKNQVAMNAKNTVFDAkRLIGRKFddKKIQED 86
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYF--PRREEEGAESIYFGNDAIDAYLND-PEEGRLI--KSVKSF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 87 LklwPFKVINEKGKPKievefkgerKRFAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSI-- 164
Cdd:cd10231 76 L---GSSLFDETTIFG---------RRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDAQAESRlr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 -----AGLNVLRIINEPTAAALAYglDKNLKGERNVLIFDLGGGTFDVSVLSIDEGSL---FEVKATAGDtHLGGEDFDN 236
Cdd:cd10231 144 daarrAGFRNVEFQYEPIAAALDY--EQRLDREELVLVVDFGGGTSDFSVLRLGPNRTdrrADILATSGV-GIGGDDFDR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 237 RLVNH-FAEEFKRK--HKSDIKG------------------------NARALRRLRT----------------------- 266
Cdd:cd10231 221 ELALKkVMPHLGRGstYVSGDKGlpvpawlyadlsnwhaisllytkkTLRLLLDLRRdaadpekierllslvedqlghrl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 267 --ACERAKRTLSSSTEASLEIDALHEGIDfySKISRARFEELNMDLFRSTMQPVERALSDAKMDKKAIHDVVLVGGSTRI 344
Cdd:cd10231 301 frAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQS 378
|
410
....*....|....*.
gi 54650896 345 PKIQKLLQDLFGGKQL 360
Cdd:cd10231 379 PAVRQALASLFGQARL 394
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
7-375 |
1.78e-22 |
|
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: 99.66 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGV----WQNSKVEIIANDQG-----NRTTPSYVAFNETERL--IGDPAKNQVAMNAKNTVFDAKRLIG 75
Cdd:cd10229 3 VAIDFGTTYSGYAYsfitDPGDIHTMYNWWGAptgvsSPKTPTCLLLNPDGEFhsFGYEAREKYSDLAEDEEHQWLYFFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 76 RKFDDKKIQEDLKLWPFKVINEKGKPKIEV--EFKGERKRFAPEEISSMVLTKMREIaevylggkvkDA--VVTVPAYFN 151
Cdd:cd10229 83 FKMMLLSEKELTRDTKVKAVNGKSMPALEVfaEALRYLKDHALKELRDRSGSSLDED----------DIrwVLTVPAIWS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 152 DSQRQATKDAGSIAGL------NVLRIINEPTAAALAY------GLDKNLKGERNVLIFDLGGGTFDVSVLSIDEGSLFE 219
Cdd:cd10229 153 DAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCqkllaeGEEKELKPGDKYLVVDCGGGTVDITVHEVLEDGKLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 220 --VKATAGdtHLGGEDFDNRLVN--------HFAEEFKRKHKSDikgnaraLRRLRTACERAKRTlsssteASLEIDalh 289
Cdd:cd10229 233 elLKASGG--PWGSTSVDEEFEElleeifgdDFMEAFKQKYPSD-------YLDLLQAFERKKRS------FKLRLS--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 290 egidfyskisrarfEELNMDLFRSTMQPVERALSDAkMDKKAIHDV---VLVGGSTRIPKIQKLLQDLFGGKqLNLSI-- 364
Cdd:cd10229 295 --------------PELMKSLFDPVVKKIIEHIKEL-LEKPELKGVdyiFLVGGFAESPYLQKAVKEAFSTK-VKIIIpp 358
|
410
....*....|.
gi 54650896 365 NPDEAVAYGAA 375
Cdd:cd10229 359 EPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
7-376 |
1.20e-14 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 75.20 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVGVwqnSKVEIIANDqgnrttPSYVAFN-ETERLI--GDpaknqvamnakntvfDAKRLIGRKFDDKKI 83
Cdd:cd10225 2 IGIDLGTANTLVYV---KGKGIVLNE------PSVVAVDkNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 84 qedlkLWPFK--VInekgkpkievefkgerkrfAPEEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDA 161
Cdd:cd10225 58 -----IRPLRdgVI-------------------ADFEATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 162 GSIAGLNVLRIINEPTAAALAYGLD-KNLKGernVLIFDLGGGTFDVSVLSIdeGSLFEVKAtagdTHLGGEDFDNRLVN 240
Cdd:cd10225 114 AEHAGAREVYLIEEPMAAAIGAGLPiEEPRG---SMVVDIGGGTTEIAVISL--GGIVTSRS----VRVAGDEMDEAIIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 241 HfaeeFKRKHKSDIkGnaralrrLRTAcERAKRTLSS----STEASLEIdalhEGIDFYSKISRARfeELNMDLFRSTMQ 316
Cdd:cd10225 185 Y----VRRKYNLLI-G-------ERTA-ERIKIEIGSayplDEELSMEV----RGRDLVTGLPRTI--EITSEEVREALE 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54650896 317 P--------VERALSDAKMDKKA-IHD--VVLVGGSTRIPKIQKLLQdlfggKQLNLSI----NPDEAVAYGAAV 376
Cdd:cd10225 246 EpvnaiveaVRSTLERTPPELAAdIVDrgIVLTGGGALLRGLDELLR-----EETGLPVhvadDPLTCVAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
7-375 |
1.73e-10 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 62.79 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTyscvgvwqNSKV-----EIIANDqgnrttPSYVAFN-ETERLI--GDpaknqvamnakntvfDAKRLIGRkf 78
Cdd:COG1077 10 IGIDLGTA--------NTLVyvkgkGIVLNE------PSVVAIDkKTGKVLavGE---------------EAKEMLGR-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 79 ddkkiqedlklwpfkvinekgkpkievefkgerkrfAPEEISsmVLTKMR-------EIAEVYLG---GKVKD------- 141
Cdd:COG1077 59 ------------------------------------TPGNIV--AIRPLKdgviadfEVTEAMLKyfiKKVHGrrsffrp 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 142 -AVVTVPAYFNDSQRQATKDAGSIAGLNVLRIINEPTAAALAYGLDknLKGERNVLIFDLGGGTFDVSVLSIdeGSLfeV 220
Cdd:COG1077 101 rVVICVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLP--IEEPTGNMVVDIGGGTTEVAVISL--GGI--V 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 221 KATAgdTHLGGEDFDNRLVNHfaeeFKRKHKSDIkGnaralrrLRTAcERAKRTLSS----STEASLEIdalhEGIDFYS 296
Cdd:COG1077 175 VSRS--IRVAGDELDEAIIQY----VRKKYNLLI-G-------ERTA-EEIKIEIGSayplEEELTMEV----RGRDLVT 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 297 KISRARfeELNMDLFRSTMQPVERALSDakmdkkAIHDV-----------------VLVGGSTRIPKIQKLLQDLFGgkq 359
Cdd:COG1077 236 GLPKTI--TITSEEIREALEEPLNAIVE------AIKSVlektppelaadivdrgiVLTGGGALLRGLDKLLSEETG--- 304
|
410
....*....|....*...
gi 54650896 360 LNLSI--NPDEAVAYGAA 375
Cdd:COG1077 305 LPVHVaeDPLTCVARGTG 322
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
142-375 |
1.96e-10 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 62.46 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 142 AVVTVPAYFNDSQRQATKDAGSIAGLNVLRIINEPTAAALAYGLDknlkgernV------LIFDLGGGTFDVSVLsideg 215
Cdd:PRK13930 103 IVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLP--------VtepvgnMVVDIGGGTTEVAVI----- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 216 SLFEVkATAGDTHLGGEDFDNRLVNHfaeeFKRKHKSDIkGNaralrrlRTAcERAKRTLSSST----EASLEIdalhEG 291
Cdd:PRK13930 170 SLGGI-VYSESIRVAGDEMDEAIVQY----VRRKYNLLI-GE-------RTA-EEIKIEIGSAYpldeEESMEV----RG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 292 IDFYSkiSRARFEELNMDLFRSTMQP--------VERALSDAK----MDkkaIHD--VVLVGGSTRIPKIQKLLQDLFGg 357
Cdd:PRK13930 232 RDLVT--GLPKTIEISSEEVREALAEplqqiveaVKSVLEKTPpelaAD---IIDrgIVLTGGGALLRGLDKLLSEETG- 305
|
250 260
....*....|....*....|
gi 54650896 358 kqLNLSI--NPDEAVAYGAA 375
Cdd:PRK13930 306 --LPVHIaeDPLTCVARGTG 323
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
143-358 |
6.60e-10 |
|
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: 61.56 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 143 VVTVPAYFNDSQRQATKDAGSIAGLNV------LRIINEPTAAALaYGLDKNLKGERNVLIFDLGGGTFDVSV--LSIDE 214
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASI-YCRKLRLHQMDRYVVVDCGGGTVDLTVhqIRLPE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 215 GSLFEV-KATAGDTHLGGED--FDNRLVNHFAEEFKRKHKsdIKGNArALRRLRTACERAKRTLSSSTEASLEIDALHEG 291
Cdd:cd11735 223 GHLKELyKASGGPYGSLGVDyeFEKLLCKIFGEDFIDQFK--IKRPA-AWVDLMIAFESRKRAAAPDRTNPLNITLPFSF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 292 IDFYSKISRARFEE-----------------LNMD------LFRSTMQPVERALSD--AKMDKKAIHDVVLVGGSTRIPK 346
Cdd:cd11735 300 IDYYKKFRGHSVEHalrksnvdfvkwssqgmLRMSpdamnaLFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAESPL 379
|
250
....*....|..
gi 54650896 347 IQKLLQDLFGGK 358
Cdd:cd11735 380 LQQAVQNAFGDQ 391
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
121-356 |
6.71e-09 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 57.30 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 121 SMVLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKdagsiAGLNVLRIINEPTAAAlaYGLDKNLKGERNVLIFDL 200
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAA--NLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 201 GGGTFDVSVlsIDEGSLFevkaTAGDTHLGGEDFDNRLVNHFAEEFKrkhksdikgnaralrrlrtACERAKRTLSSST- 279
Cdd:cd24004 122 GAGTTDIAL--IRNGGIE----AYRMVPLGGDDFTKAIAEGFLISFE-------------------EAEKIKRTYGIFLl 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54650896 280 -EASLEIDALHEGIDFYSKISRArFEELnmdlfrstMQPVERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFG 356
Cdd:cd24004 177 iEAKDQLGFTINKKEVYDIIKPV-LEEL--------ASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
143-356 |
1.15e-08 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 57.28 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 143 VVTVPAYFNDSQRQATKDAGSIAGL------NVLRIINEPTAAAL-AYGLDKnlkgernVLIFDLGGGTFDVSVLSIDE- 214
Cdd:cd11736 144 VLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR-------YIVADCGGGTVDLTVHQIEQp 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 215 -GSLFEV-KATAGDTHLGGED--FDNRLVNHFAEEFKRKHKSDikgNARALRRLRTACERAKRT--LSSSTEASLEidal 288
Cdd:cd11736 217 qGTLKELyKASGGPYGAVGVDlaFEKLLCQIFGEDFIATFKAK---RPAAWVDLTIAFEARKRTaaLRMSSEAMNE---- 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 289 hegidfyskisrarfeelnmdLFRSTMQPVERALSD--AKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFG 356
Cdd:cd11736 290 ---------------------LFQPTISQIIQHIDDlmKKPEVKGIKFLFLVGGFAESPMLQRAVQAAFG 338
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
165-379 |
1.63e-07 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 53.98 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYgLDKNLKgERNVLIFDLGGGTFDVSVlsIDEGSLfevKATAGDThLGGEDFDNrlvnhfae 244
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTEDEK-ELGVALVDIGGGTTDIAV--FKDGAL---RHTAVIP-VGGDHITN-------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 245 efkrkhksDIkgnARALR-RLRTAcERAKRTLSSSTEASLEIDALHE----GIDFYSKISR--------ARFEELnMDLf 311
Cdd:COG0849 238 --------DI---AIGLRtPLEEA-ERLKIKYGSALASLADEDETIEvpgiGGRPPREISRkelaeiieARVEEI-FEL- 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54650896 312 rstmqpVERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFG-----GKQLNLSINPDE------AVAYGAAVQAA 379
Cdd:COG0849 304 ------VRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILGlpvriGRPDGIGGLPEAvrdpayATAVGLLLYAA 376
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
7-374 |
5.78e-07 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 51.83 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCvgvwqnskveiIANDQGNR-TTPSYVAFneterligdpAKNQVAMNakntVFDAKRLIGRKFDDKKIQE 85
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGY----------PKDIIARK----LLGKEVLFGDEALENRLAL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 86 DLKlWPFK--VINEKGKPKIEVefkgerkrfapeeiSSMVLTKMREIAEVYLGGKVKdAVVTVPAYFNDSQRQATKDAGS 163
Cdd:cd24009 59 DLR-RPLEdgVIKEGDDRDLEA--------------ARELLQHLIELALPGPDDEIY-AVIGVPARASAENKQALLEIAR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 164 IAGLNVLrIINEPTAAalAYGLDKnlkgERNVLIFDLGGGTFDVSVLSideGSLFEVKATAGDTHlGGEDFDNRLVN--- 240
Cdd:cd24009 123 ELVDGVM-VVSEPFAV--AYGLDR----LDNSLIVDIGAGTTDLCRMK---GTIPTEEDQITLPK-AGDYIDEELVDlik 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 241 ----------HFAEEFKRKHKSDIKGNARALRRLRtacERAKRTLSSSTEasleidalhegidfyskISRARFEELNMDL 310
Cdd:cd24009 192 erypevqltlNMARRWKEKYGFVGDASEPVKVELP---VDGKPVTYDITE-----------------ELRIACESLVPDI 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 54650896 311 FRSTMQPVERAlsDAKMDKKAIHDVVLVGGSTRIPKIQKLLQ---DLFGGKQLNLSINPDEAVAYGA 374
Cdd:cd24009 252 VEGIKKLIASF--DPEFQEELRNNIVLAGGGSRIRGLDTYIEkalKEYGGGKVTCVDDPVFAGAEGA 316
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
117-357 |
8.07e-07 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 51.79 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 117 EEISSMVLTKMREIAEVYLGGKVKDAVVTVPAYFN-----DSQRQAT---KDAGSIAGLNVLRIINEPTAAALAYglDKN 188
Cdd:PRK11678 127 EDLVCAMMLHIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDF--EAT 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 189 LKGERNVLIFDLGGGTFDVSVLSIdeGSLFEVKATAGDTHL-------GGEDFDNRL----------------------- 238
Cdd:PRK11678 205 LTEEKRVLVVDIGGGTTDCSMLLM--GPSWRGRADRSASLLghsgqriGGNDLDIALafkqlmpllgmgsetekgialps 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 239 --------VNH------FAEEFKRKHKSDIKGNAR---ALRRL-------------RTAcERAKRTLSSSTEASLEIDAL 288
Cdd:PRK11678 283 lpfwnavaINDvpaqsdFYSLANGRLLNDLIRDARepeKVARLlkvwrqrlsyrlvRSA-EEAKIALSDQAETRASLDFI 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 289 HEGIDfySKISRARFEELNMDLFRSTMQPVERALSDAkmDKKAihDVV-LVGGSTRIPKIQKLLQDLFGG 357
Cdd:PRK11678 362 SDGLA--TEISQQGLEEAISQPLARILELVQLALDQA--QVKP--DVIyLTGGSARSPLIRAALAQQLPG 425
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
129-374 |
2.22e-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: 49.86 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 129 EIAE---VYLGGKVKDA--------VVTVPAYFNDSQRQATKDAGSIAGLNVLRIINEPTAAALAYGLdkNLKGERNVLI 197
Cdd:pfam06723 72 EVTEamlKYFIKKVHGRrsfskprvVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGL--PVEEPTGNMV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 198 FDLGGGTFDVSVLSIdeGSLfevkATAGDTHLGGEDFDNRLVNHfaeeFKRKHKSDIkGNaralrrlRTAcERAKRTLSS 277
Cdd:pfam06723 150 VDIGGGTTEVAVISL--GGI----VTSKSVRVAGDEFDEAIIKY----IRKKYNLLI-GE-------RTA-ERIKIEIGS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 278 --STEASLEIDAlhEGIDFYS------KISRARFEELNMDLFRSTMQPVERALSDAKMDKKA-IHD--VVLVGGSTRIPK 346
Cdd:pfam06723 211 ayPTEEEEKMEI--RGRDLVTglpktiEISSEEVREALKEPVSAIVEAVKEVLEKTPPELAAdIVDrgIVLTGGGALLRG 288
|
250 260
....*....|....*....|....*...
gi 54650896 347 IQKLLQDLFGGKQLnLSINPDEAVAYGA 374
Cdd:pfam06723 289 LDKLLSDETGLPVH-IAEDPLTCVALGT 315
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
143-251 |
2.98e-06 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 49.52 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 143 VVTVPAYFNDSQRQATKDAGSIAGLNVLRIINEPTAAALAYGLDknLKGERNVLIFDLGGGTFDVSVLSIdeGSLfevkA 222
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLD--ISQPSGNMVVDIGGGTTDIAVLSL--GGI----V 170
|
90 100
....*....|....*....|....*....
gi 54650896 223 TAGDTHLGGEDFDNRLVNHfaeeFKRKHK 251
Cdd:PRK13928 171 TSSSIKVAGDKFDEAIIRY----IRKKYK 195
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
123-251 |
4.76e-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: 48.42 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 123 VLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIAGLNVLRIINEPTAAALAYGLdknlkgeRNVLIFDLGG 202
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI-------RDGAVVDIGG 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 203 GTFDVSVLSidEGslfEVKATA----GDTHLG-------GEDFDNrlvnhfAEEFKRKHK 251
Cdd:cd24047 121 GTTGIAVLK--DG---KVVYTAdeptGGTHLSlvlagnyGISFEE------AEIIKRDPA 169
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
165-376 |
5.58e-06 |
|
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: 49.07 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYgLDKNLKgERNVLIFDLGGGTFDVSVLSidEGSL--FEVKAtagdthLGGEDFDNRLVNHF 242
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEK-ELGVALIDIGGGTTDIAVFK--NGSLryTAVIP------VGGNHITNDIAIGL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 243 ------AEEFKRKHKSDIKGNARALRRLRTAC--ERAKRTLSSSteaslEIdalhegidfySKISRARFEE-LNMdlfrs 313
Cdd:cd24048 242 ntpfeeAERLKIKYGSALSEEADEDEIIEIPGvgGREPREVSRR-----EL----------AEIIEARVEEiLEL----- 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54650896 314 tmqpVERALSDAKMDKKAIHDVVLVGGSTRIPKIQKLLQDLFG-----GKQLNLSINPDEAVAYGAAV 376
Cdd:cd24048 302 ----VKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvriGRPKNIGGLPEEVNDPAYAT 365
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
165-356 |
1.88e-05 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 47.27 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 165 AGLNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSVlsIDEGSLF---EVKatagdthLGGEDFDNRLVNH 241
Cdd:cd24049 148 AGLKPVAIDVESFALARALEYLLPDEEEETVALLDIGASSTTLVI--VKNGKLLftrSIP-------VGGNDITEAIAKA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 242 F------AEEFKRKHKSDIKGNARALRRLRTACERAkrtlsssteasleIDALHEGIdfyskisrarfeELNMDLFRSTM 315
Cdd:cd24049 219 LglsfeeAEELKREYGLLLEGEEGELKKVAEALRPV-------------LERLVSEI------------RRSLDYYRSQN 273
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 54650896 316 QpveralsdakmdKKAIHDVVLVGGSTRIPKIQKLLQDLFG 356
Cdd:cd24049 274 G------------GEPIDKIYLTGGGSLLPGLDEYLSERLG 302
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
123-254 |
2.62e-05 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 46.36 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 123 VLTKMREIAEVYLGGKVKDAVVTVPAYFNDSQRQATKDAGSIAGLNVLRIINEPTAAALAYGLDknlkgerNVLIFDLGG 202
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGID-------NGAVVDIGG 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54650896 203 GTFDVSVL-------SIDEgslfevkATAGdTHLG-------GEDFDNrlvnhfAEEFKR--KHKSDI 254
Cdd:PRK15080 145 GTTGISILkdgkvvySADE-------PTGG-THMSlvlagayGISFEE------AEQYKRdpKHHKEI 198
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
195-373 |
1.01e-04 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 43.09 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 195 VLIfDLGGGTFDVSVLSidEGSLFEVKATAgdthLGGEDFDNRLVNHF------AEEFKRKHksdikGNARALRrlrtAC 268
Cdd:pfam14450 1 ALI-DIGGGTTDIAVFE--DGALRHTRVIP----VGGNGITKDIAIGLrtaveeAERLKIKY-----GSALASL----AD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 269 ERAKRTLSSSTEASLEIDALHEgidfyskISRARFEELnMDLFRSTMQPVERALSDAKMDKKAIHDVVLVGGSTRIPKIQ 348
Cdd:pfam14450 65 EDEVPGVGGREPREISRKELAE-------IIEARVEEI-LELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPGLV 136
|
170 180 190
....*....|....*....|....*....|.
gi 54650896 349 KLLQDLFG-----GKQLNLS-INPDEAVAYG 373
Cdd:pfam14450 137 ELAERALGlpvriGSPDGIGgRNPAYATALG 167
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
7-254 |
5.56e-04 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 42.12 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTTYSCVgVWQNSKVEII----------ANDQGNRTTPSYVAFNETERLIGDPAKNQVAMNAKNTvfdakrligr 76
Cdd:cd10227 1 IGIDIGNGNTKV-VTGGGKEFKFpsavaearesSLDDGLLEDDIIVEYNGKRYLVGELALREGGGGRSTG---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 77 kfDDKKIQEDLKLWPFKVINEKGKPKIEV----------EFKGERKRFApeeissmvLTKMREIAEVYLGGKVKDAVVtv 146
Cdd:cd10227 70 --DDKKKSEDALLLLLAALALLGDDEEVDvnlvvglpisEYKEEKKELK--------KKLLKGLHEFTFNGKERRITI-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 147 payfndsqrqatkdagsiaglNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTfdVSVLSIDEGSLFEVKataGD 226
Cdd:cd10227 138 ---------------------NDVKVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENGKPIEES---SD 191
|
250 260
....*....|....*....|....*...
gi 54650896 227 THLGGEDFDNRLVNHFAEEFKRKHKSDI 254
Cdd:cd10227 192 TLPGGEEALEKYADDILNELLKKLGDEL 219
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
7-373 |
8.91e-04 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 41.82 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 7 IGIDLGTtySCVGVWQNSKvEIIANDqgnrttPSYVAFNETER---LIGDPAKNQVAMNAKNTVfdakrlIGRKFDDKKI 83
Cdd:PRK13929 7 IGIDLGT--ANILVYSKNK-GIILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV------AVRPMKDGVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 84 QE-DLKLWPFKVINEKGKPKIEVEFkgeRKrfapeeissmvltkmreiaevylggkvKDAVVTVPAYFNDSQRQATKDAG 162
Cdd:PRK13929 72 ADyDMTTDLLKQIMKKAGKNIGMTF---RK---------------------------PNVVVCTPSGSTAVERRAISDAV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 163 SIAGLNVLRIINEPTAAALayGLDKNLKGERNVLIFDLGGGTFDVSVLSidegslFEVKATAGDTHLGGEDFDNRLVNHF 242
Cdd:PRK13929 122 KNCGAKNVHLIEEPVAAAI--GADLPVDEPVANVVVDIGGGTTEVAIIS------FGGVVSCHSIRIGGDQLDEDIVSFV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 243 aeefkRKHKSDIKGNaralrrlRTAcERAK----RTLSSSTEASLEI------DALHEGIDFYSK-ISRARFEEL--NMD 309
Cdd:PRK13929 194 -----RKKYNLLIGE-------RTA-EQVKmeigYALIEHEPETMEVrgrdlvTGLPKTITLESKeIQGAMRESLlhILE 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54650896 310 LFRSTMQPVERALSDAKMDKkaihDVVLVGGSTRIPKIQKLLQDLFgGKQLNLSINPDEAVAYG 373
Cdd:PRK13929 261 AIRATLEDCPPELSGDIVDR----GVILTGGGALLNGIKEWLSEEI-VVPVHVAANPLESVAIG 319
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
141-204 |
1.15e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 39.37 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54650896 141 DAVVTVPAYFNDSQRQAT-----------KDAGSIAGLNVLRIINEPTAAALAYGLDknlKGERNVLIFDLGGGT 204
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLT---LGPEGLLVVDLGGGT 86
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
143-277 |
1.32e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 41.23 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54650896 143 VVTVPAYFNDSQRQATKDAGSIAGLNVLRIINEPTAAALAYGLD-KNLKGernVLIFDLGGGTFDVSVLSIdeGSLfevk 221
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPvTEPTG---SMVVDIGGGTTEVAVISL--GGI---- 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 54650896 222 ATAGDTHLGGEDFDNRLVNHfaeeFKRKHKSDIkGNaralrrlRTAcERAKRTLSS 277
Cdd:PRK13927 171 VYSKSVRVGGDKFDEAIINY----VRRNYNLLI-GE-------RTA-ERIKIEIGS 213
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
331-387 |
3.00e-03 |
|
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: 40.59 E-value: 3.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 54650896 331 AIHDVVLVGGSTRIPKIQKLLQDLFGgkqLNLSI-NPDEAVAYGAAVQAAILTGVGSS 387
Cdd:COG1070 395 KIDRIRATGGGARSPLWRQILADVLG---RPVEVpEAEEGGALGAALLAAVGLGLYDD 449
|
|
| |
