|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
2-638 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1087.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 2 PAIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQ 81
Cdd:PTZ00009 5 PAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 QDMKHWPFTVVNDC-GKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGA 160
Cdd:PTZ00009 85 SDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 161 IAGLNVMRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLA 240
Cdd:PTZ00009 165 IAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDG-IFEVKATAGDTHLGGEDFDNRLVEFCV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 241 EEFKRKYH-KDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERAL 319
Cdd:PTZ00009 244 QDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEKVL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 320 QDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNLSINPDEAVAYGAAVQAAILSGDQSSAIQDVLLVDVAPLSL 399
Cdd:PTZ00009 324 KDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTPLSL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 400 GIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDLD 479
Cdd:PTZ00009 404 GLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDID 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 480 ANGILNVTAKDSSTGRSQNITIRNDKGRLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEE--AGDK 557
Cdd:PTZ00009 484 ANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDekVKGK 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 558 LSEADKARAREECDSVIRWLDSNTLADKEEYEHRLQELQSHVKDAMTKMHpaGAGAGMGASCAPGGC-----------SA 626
Cdd:PTZ00009 564 LSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMY--QAAGGGMPGGMPGGMpggmpggagpaGA 641
|
650
....*....|..
gi 1420818630 627 QARQGPSVEEVD 638
Cdd:PTZ00009 642 GASSGPTVEEVD 653
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
3-606 |
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: 927.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQ 82
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVVNDC-GKPKIQVTFKGErkVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:pfam00012 81 DIKHLPYKVVKLPnGDAGVEVRYLGE--TFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSILEIGRG-VFEVKATNGDTHLGGEDFDLRLVDHLAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLSS-STEANIEIDALY-DGVDFYTKVSRARFEELCADLFRSTLAPVERAL 319
Cdd:pfam00012 237 EFKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMaDGKDVSGTLTRAKFEELVADLFERTLEPVEKAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 320 QDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSGDQssAIQDVLLVDVAPLSL 399
Cdd:pfam00012 317 KDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGTF--DVKDFLLLDVTPLSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 400 GIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDLD 479
Cdd:pfam00012 394 GIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDID 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 480 ANGILNVTAKDSSTGRSQNITIRNDKGrLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAGDKLS 559
Cdd:pfam00012 474 ANGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVP 552
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1420818630 560 EADKararEECDSVIRWLDSNTL-ADKEEYEHRLQELQSHVKDAMTKM 606
Cdd:pfam00012 553 EAEK----SKVESAIEWLKDELEgDDKEEIEAKTEELAQVSQKIGERM 596
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
3-606 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 888.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPKDTVFDAKRLIGRRfdDPKIQ 81
Cdd:PRK00290 4 IIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 QDMKHWPFTVVN-DCGKPKIQVtfKGerKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGA 160
Cdd:PRK00290 82 KDIKLVPYKIVKaDNGDAWVEI--DG--KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 161 IAGLNVMRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLA 240
Cdd:PRK00290 158 IAGLEVLRIINEPTAAALAYGLDK--KGDEKILVYDLGGGTFDVSILEIGDG-VFEVLSTNGDTHLGGDDFDQRIIDYLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 241 EEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDALYDG-VDFYTKVSRARFEELCADLFRSTLAPVE 316
Cdd:PRK00290 235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINlpfITADASGpKHLEIKLTRAKFEELTEDLVERTIEPCK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 317 RALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSGDqssaIQDVLLVDVAP 396
Cdd:PRK00290 315 QALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVLLLDVTP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 397 LSLGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTF 476
Cdd:PRK00290 390 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 477 DLDANGILNVTAKDSSTGRSQNITIRNDKGrLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAGD 556
Cdd:PRK00290 470 DIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGD 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1420818630 557 KLSEADKARAREECDSVIRWLDSNtlaDKEEYEHRLQELQSHVKDAMTKM 606
Cdd:PRK00290 549 KVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAM 595
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
3-378 |
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: 868.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQ 82
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVVNDCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAEE 242
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDG-IFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 243 FKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQDA 322
Cdd:cd10233 240 FKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1420818630 323 KMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNLSINPDEAVAYGAAVQAAIL 378
Cdd:cd10233 320 KLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-608 |
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: 818.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDdpKIQ 81
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 QDMKHWPFTVVNDCGkpkiQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:TIGR02350 80 EEAKRVPYKVVGDGG----DVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSILTIDEGSlFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKS-KKDEKILVFDLGGGTFDVSILEIGDGV-FEVLSTAGDTHLGGDDFDQRIIDWLAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDALYDG-VDFYTKVSRARFEELCADLFRSTLAPVER 317
Cdd:TIGR02350 234 EFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINlpfITADASGpKHLEMTLTRAKFEELTADLVERTKEPVRQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 318 ALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSGDqssaIQDVLLVDVAPL 397
Cdd:TIGR02350 314 ALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 398 SLGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFD 477
Cdd:TIGR02350 389 SLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 478 LDANGILNVTAKDSSTGRSQNITIRNDKGrLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAGDK 557
Cdd:TIGR02350 469 IDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDK 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1420818630 558 LSEADKARAREECDSVIRWLDSNtlaDKEEYEHRLQELQSHVKDAMTKMHP 608
Cdd:TIGR02350 548 LPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
3-378 |
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: 737.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQ 82
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVVND-CGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:cd24028 81 DIKHWPFKVVEDeDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLLSIDNG-VFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQD 321
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1420818630 322 AKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNLSINPDEAVAYGAAVQAAIL 378
Cdd:cd24028 320 AKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
2-378 |
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: 732.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 2 PAIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQ 81
Cdd:cd10241 2 TVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 QDMKHWPFTVVNDCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:cd10241 82 KDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:cd10241 162 AGLNVLRIINEPTAAAIAYGLDKK-GGEKNILVFDLGGGTFDVSLLTIDNG-VFEVLATNGDTHLGGEDFDQRVMDHFIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQD 321
Cdd:cd10241 240 LFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLED 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1420818630 322 AKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNLSINPDEAVAYGAAVQAAIL 378
Cdd:cd10241 320 AGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
4-606 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 699.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDpkIQQ 82
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE--ISE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVVNDcGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:CHL00094 83 EAKQVSYKVKTD-SNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAEE 242
Cdd:CHL00094 162 GLEVLRIINEPTAASLAYGLDK--KNNETILVFDLGGGTFDVSILEVGDG-VFEVLSTSGDTHLGGDDFDKKIVNWLIKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 243 FKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDALYDG-VDFYTKVSRARFEELCADLFRSTLAPVERA 318
Cdd:CHL00094 239 FKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVENA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 319 LQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSGDqssaIQDVLLVDVAPLS 398
Cdd:CHL00094 319 LKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 399 LGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDL 478
Cdd:CHL00094 394 LGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 479 DANGILNVTAKDSSTGRSQNITIRNdKGRLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAGDKL 558
Cdd:CHL00094 474 DANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKI 552
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1420818630 559 SEADKararEECDSVIRWLDSNTlaDKEEYEhRLQELQSHVKDAMTKM 606
Cdd:CHL00094 553 SEEKK----EKIENLIKKLRQAL--QNDNYE-SIKSLLEELQKALMEI 593
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
4-596 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 678.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDpkIQQ 82
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD--TEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVVNdcGKPK-IQVTFKGerKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:PRK13411 83 ERSRVPYTCVK--GRDDtVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNLKgERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:PRK13411 159 AGLEVLRIINEPTAAALAYGLDKQDQ-EQLILVFDLGGGTFDVSILQLGDG-VFEVKATAGNNHLGGDDFDNCIVDWLVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDAlyDGVD---FYTKVSRARFEELCADLFRSTLAPV 315
Cdd:PRK13411 237 NFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINlpfITA--DETGpkhLEMELTRAKFEELTKDLVEATIEPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 316 ERALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNLSINPDEAVAYGAAVQAAILSGDqssaIQDVLLVDVA 395
Cdd:PRK13411 315 QQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDLLLLDVT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 396 PLSLGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVT 475
Cdd:PRK13411 391 PLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 476 FDLDANGILNVTAKDSSTGRSQNITIRNdKGRLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAG 555
Cdd:PRK13411 471 FEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENG 549
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1420818630 556 DKLSEADKARAREECDSVIRWLDSNTLaDKEEYEHRLQELQ 596
Cdd:PRK13411 550 ELISEELKQRAEQKVEQLEAALTDPNI-SLEELKQQLEEFQ 589
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
3-517 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 670.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQ 81
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 qdmkhwpftvVNDcgkpkiqvtfkgerKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:COG0443 81 ----------VGG--------------KRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSILTIDEGSlFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKG-KEEETILVYDLGGGTFDVSILRLGDGV-FEVLATGGDTHLGGDDFDQALADYVAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDaLYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQD 321
Cdd:COG0443 215 EFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALAD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 322 AKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSGDQSSaiqdvllVDVAPLSLGI 401
Cdd:COG0443 294 AGLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 402 ETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDLDAN 481
Cdd:COG0443 366 ETLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDAN 445
|
490 500 510
....*....|....*....|....*....|....*.
gi 1420818630 482 GILNVTAKDSSTGRSQNITIRndkgrlsaDEIQRMV 517
Cdd:COG0443 446 GILSVSAKDLGTGKEQSITIK--------EEIERML 473
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
4-605 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 666.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQ 82
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVVNDcgkPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:PTZ00400 124 EQKILPYKIVRA---SNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSILTIdEGSLFEVRSTAGDTHLGGEDFDSRLVNHLAEE 242
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDKN--DGKTIAVYDLGGGTFDISILEI-LGGVFEVKATNGNTSLGGEDFDQRILNYLIAE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 243 FKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDALYDGVD-FYTKVSRARFEELCADLFRSTLAPVERA 318
Cdd:PTZ00400 278 FKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINlpfITADQSGPKhLQIKLSRAKLEELTHDLLKKTIEPCEKC 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 319 LQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSGDqssaIQDVLLVDVAPLS 398
Cdd:PTZ00400 358 IKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDLLLLDVTPLS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 399 LGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDL 478
Cdd:PTZ00400 433 LGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 479 DANGILNVTAKDSSTGRSQNITIRNDKGrLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAGDKL 558
Cdd:PTZ00400 513 DANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKI 591
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1420818630 559 SEADKARAREECDSVIRWLDSNTLADKEEYEHRLQELQSHVKDAMTK 605
Cdd:PTZ00400 592 SDADKDELKQKITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYK 638
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
4-603 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 655.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDpkIQQ 82
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE--LDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTV-VNDCGKPKIQVTFKgeRKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:PRK13410 83 ESKRVPYTIrRNEQGNVRIKCPRL--EREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLEVGNG-VFEVKATSGDTQLGGNDFDKRIVDWLAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLS--SSTEANIE-IDALYDG-VDFYTKVSRARFEELCADLFRSTLAPVER 317
Cdd:PRK13410 238 QFLEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpKHIETRLDRKQFESLCGDLLDRLLRPVKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 318 ALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSGDqssaIQDVLLVDVAPL 397
Cdd:PRK13410 318 ALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 398 SLGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFD 477
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 478 LDANGILNVTAKDSSTGRSQNITIRNdKGRLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAGDK 557
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAALE 551
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1420818630 558 LSEADKARAREECDSVIRwlDSNTLADKEEyEHRLQELQSHVKDAM 603
Cdd:PRK13410 552 FGPYFAERQRRAVESAMR--DVQDSLEQDD-DRELDLAVADLQEAL 594
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
4-565 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 613.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDpkIQQ 82
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVV-NDCGKPKIQVTFKGerKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:PLN03184 120 ESKQVSYRVVrDENGNVKLDCPAIG--KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEK--KSNETILVFDLGGGTFDVSVLEVGDG-VFEVLSTSGDTHLGGDDFDKRIVDWLAS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDALYDG---VDfyTKVSRARFEELCADLFRSTLAPV 315
Cdd:PLN03184 275 NFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 316 ERALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFfNGKSLNLSINPDEAVAYGAAVQAAILSGDQSsaiqDVLLVDVA 395
Cdd:PLN03184 353 ENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGEVS----DIVLLDVT 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 396 PLSLGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVT 475
Cdd:PLN03184 428 PLSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVK 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 476 FDLDANGILNVTAKDSSTGRSQNITIrNDKGRLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAG 555
Cdd:PLN03184 508 FDIDANGILSVSATDKGTGKKQDITI-TGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELG 586
|
570
....*....|
gi 1420818630 556 DKLSEADKAR 565
Cdd:PLN03184 587 DKVPADVKEK 596
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
3-378 |
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: 610.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQhGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQ 82
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVVNDCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLD-KNLKGERNVLIFDLGGGTFDVSILTIdEGSLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGaGKSEKERHVLIFDLGGGTFDVSLLHI-AGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQD 321
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1420818630 322 AKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNLSINPDEAVAYGAAVQAAIL 378
Cdd:cd24093 319 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
4-567 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 592.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQD 83
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 84 MKHWPFTVV-NDCGKPKIQvtfKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:PTZ00186 110 IKNVPYKIVrAGNGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSILTIdEGSLFEVRSTAGDTHLGGEDFDSRLVNHLAEE 242
Cdd:PTZ00186 187 GLNVIRVVNEPTAAALAYGMDKT--KDSLIAVYDLGGGTFDISVLEI-AGGVFEVKATNGDTHLGGEDFDLALSDYILEE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 243 FKRKYHKDLRSNPRALRRLRTAAERAKRTLSSS--TEANIE-IDALYDGVD-FYTKVSRARFEELCADLFRSTLAPVERA 318
Cdd:PTZ00186 264 FRKTSGIDLSKERMALQRVREAAEKAKCELSSAmeTEVNLPfITANADGAQhIQMHISRSKFEGITQRLIERSIAPCKQC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 319 LQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSGDqssaIQDVLLVDVAPLS 398
Cdd:PTZ00186 344 MKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVTPLS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 399 LGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDL 478
Cdd:PTZ00186 419 LGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDI 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 479 DANGILNVTAKDSSTGRSQNITIRNDKGrLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEaGDKL 558
Cdd:PTZ00186 499 DANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGE-WKYV 576
|
....*....
gi 1420818630 559 SEADKARAR 567
Cdd:PTZ00186 577 SDAEKENVK 585
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
4-379 |
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: 552.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQ 82
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFtvvndCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd10234 82 KQVPYPV-----VSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAEE 242
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDK--KKDEKILVYDLGGGTFDVSILEIGDG-VFEVLSTNGDTHLGGDDFDQRIIDYLADE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 243 FKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDALYDG-VDFYTKVSRARFEELCADLFRSTLAPVERA 318
Cdd:cd10234 234 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpKHLEMKLTRAKFEELTEDLVERTIEPVEQA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1420818630 319 LQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILS 379
Cdd:cd10234 314 LKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
3-564 |
2.86e-178 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 519.35 E-value: 2.86e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDpkIQQ 82
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFT-VVNDCGKPKIQvTFKGERkvfAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:PRK05183 99 RYPHLPYQfVASENGMPLIR-TAQGLK---SPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDSG--QEGVIAVYDLGGGTFDISILRLSKG-VFEVLATGGDSALGGDDFDHLLADWILE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 efkrKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIdALYDGvdfytKVSRARFEELCADLFRSTLAPVERALQD 321
Cdd:PRK05183 252 ----QAGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV-ALWQG-----EITREQFNALIAPLVKRTLLACRRALRD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 322 AKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNlSINPDEAVAYGAAVQAAILSGDQSSAiqDVLLVDVAPLSLGI 401
Cdd:PRK05183 322 AGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLT-SIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 402 ETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDLDAN 481
Cdd:PRK05183 399 ETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDAD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 482 GILNVTAKDSSTGRSQNITIRNDKGrLSADEIQRMVDEAERYKEEDDKQR----ERVAARNQLEsyvfSIKQAVEEAGDK 557
Cdd:PRK05183 479 GLLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLE----ALQAALAADGDL 553
|
....*..
gi 1420818630 558 LSEADKA 564
Cdd:PRK05183 554 LSAAERA 560
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
3-564 |
3.41e-176 |
|
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: 513.74 E-value: 3.41e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQ 81
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 qdmKHWPFTVVNDCGKpkiQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:TIGR01991 81 ---SILPYRFVDGPGE---MVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHlae 241
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDKA--SEGIYAVYDLGGGTFDVSILKLTKG-VFEVLATGGDSALGGDDFDHALAKW--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 eFKRKYHKDLRSNPRALRRLRTAAERAKRTLSssTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQD 321
Cdd:TIGR01991 229 -ILKQLGISADLNPEDQRLLLQAARAAKEALT--DAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 322 AKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNlSINPDEAVAYGAAVQAAILSGDQSSaiQDVLLVDVAPLSLGI 401
Cdd:TIGR01991 306 AGLSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLT-DIDPDQVVALGAAIQADLLAGNRIG--NDLLLLDVTPLSLGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 402 ETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDLDAN 481
Cdd:TIGR01991 383 ETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDAD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 482 GILNVTAKDSSTGRSQNITIRNDKGrLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAGDKLSEA 561
Cdd:TIGR01991 463 GLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSED 541
|
...
gi 1420818630 562 DKA 564
Cdd:TIGR01991 542 ERA 544
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
4-378 |
3.52e-169 |
|
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: 487.16 E-value: 3.52e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQ 82
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMKHWPFTVVNdcgKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd11733 84 DIKMVPYKIVK---ASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAEE 242
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDK--KDDKIIAVYDLGGGTFDISILEIQKG-VFEVKATNGDTFLGGEDFDNALLNYLVAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 243 FKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDALYDG-VDFYTKVSRARFEELCADLFRSTLAPVERA 318
Cdd:cd11733 238 FKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINlpfITADASGpKHLNMKLTRAKFESLVGDLIKRTVEPCKKC 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 319 LQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAIL 378
Cdd:cd11733 318 LKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
2-380 |
9.88e-154 |
|
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: 448.05 E-value: 9.88e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 2 PAIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKI 80
Cdd:cd11734 2 PVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 QQDMKHWPFTVV----NDCgkpkiQVTFKGERkvFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATK 156
Cdd:cd11734 82 QRDIKEVPYKIVkhsnGDA-----WVEARGQK--YSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 157 DAGAIAGLNVMRIINEPTAAALAYGLDKNlkGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLV 236
Cdd:cd11734 155 DAGQIAGLNVLRVINEPTAAALAYGLDKS--GDKVIAVYDLGGGTFDISILEIQKG-VFEVKSTNGDTHLGGEDFDIALV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 237 NHLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIE---IDALYDGVDFY-TKVSRARFEELCADLFRSTL 312
Cdd:cd11734 232 RHIVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINlpfITADASGPKHInMKLTRAQFESLVKPLVDRTV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1420818630 313 APVERALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSG 380
Cdd:cd11734 312 EPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
4-380 |
4.20e-147 |
|
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: 432.15 E-value: 4.20e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQH--GKVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKI 80
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 QQDMKHWPFTVVND-CGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAG 159
Cdd:cd10237 105 EEEAKRYPFKVVNDnIGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 160 AIAGLNVMRIINEPTAAALAYGLDKNlKGERNVLIFDLGGGTFDVSILTIdEGSLFEVRSTAGDTHLGGEDFDSRLVNHL 239
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKK-SDVNNVLVVDLGGGTLDVSLLNV-QGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 240 AEEFKRKYHKDLrSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDG-----VDFYTKVSRARFEELCADLFRSTLAP 314
Cdd:cd10237 263 IDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLpsafkVKFKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1420818630 315 VERALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILSG 380
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
4-376 |
7.59e-146 |
|
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: 427.75 E-value: 7.59e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQD 83
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 84 MKHWPFTVVN-DCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGL---DKNLKGE--RNVLIFDLGGGTFDVSILTIDEGSLfEVRSTAGDTHLGGEDFDSRLVN 237
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIyksDLLESEEkpRIVAFVDMGHSSTQVSIAAFTKGKL-KVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 238 HLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVER 317
Cdd:cd11732 240 HFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1420818630 318 ALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAA 376
Cdd:cd11732 320 ALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
2-378 |
1.58e-145 |
|
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: 427.04 E-value: 1.58e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 2 PAIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQ 81
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 QDMKHWPFTVVNDCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNLKGE-RNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLA 240
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPTEnSNVLVYRLGGTSLDVTVLSVNNG-MYRVLATRTDDNLGGDDFTEALAEHLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 241 EEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQ 320
Cdd:cd10238 240 SEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1420818630 321 DAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNLSINPDEAVAYGAAVQAAIL 378
Cdd:cd10238 320 SAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
3-380 |
1.96e-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: 413.54 E-value: 1.96e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLI-GDAAKNQVAMNPKDTVFDAKRLIGRRFDDpkIQ 81
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 QDMKHWPFTVVNDcgkPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:cd10236 82 EELPLLPYRLVGD---ENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKnlKGERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQ--KKEGTIAVYDLGGGTFDISILRLSDG-VFEVLATGGDTALGGDDFDHLLADWILK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKrkyhKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDAlyDGVDFYTKVSRARFEELCADLFRSTLAPVERALQD 321
Cdd:cd10236 236 QIG----IDARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRALKD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1420818630 322 AKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNlSINPDEAVAYGAAVQAAILSG 380
Cdd:cd10236 310 AGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLT-SINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
4-379 |
3.73e-140 |
|
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: 412.35 E-value: 3.73e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVW-QHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFddpkiq 81
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 82 qdmkhWPFTVVNDcgkpkiqvtfkgerKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAI 161
Cdd:cd24029 75 -----KDKEEIGG--------------KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNLKGErNVLIFDLGGGTFDVSILTIDEGSlFEVRSTAGDTHLGGEDFDSRLVNHLAE 241
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDG-TILVYDLGGGTFDVSILEIENGK-FEVLATGGDNFLGGDDFDEAIAELILE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 EFKRKYHK-DLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQ 320
Cdd:cd24029 214 KIGIETGIlDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1420818630 321 DAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNlSINPDEAVAYGAAVQAAILS 379
Cdd:cd24029 294 DAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPIS-SVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
1-379 |
4.09e-137 |
|
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: 405.93 E-value: 4.09e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 1 MPAIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKI 80
Cdd:cd24095 1 MSVVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 QQDMKHWPFTVVN-DCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAG 159
Cdd:cd24095 81 QRDLKLFPFKVTEgPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 160 AIAGLNVMRIINEPTAAALAYGLDKNLKGE---RNVLIFDLGGGTFDVSILTIDEGSLfEVRSTAGDTHLGGEDFDSRLV 236
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIYKTDLPEtdpTNVVFVDVGHSSTQVCVVAFKKGQL-KVLSHAFDRNLGGRDFDEVLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 237 NHLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVE 316
Cdd:cd24095 240 DHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1420818630 317 RALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILS 379
Cdd:cd24095 320 KALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
4-376 |
1.76e-136 |
|
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: 403.96 E-value: 1.76e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQD 83
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 84 MKHWPFTVVN-DCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKN-LKGE----RNVLIFDLGGGTFDVSILTIDEGSLfEVRSTAGDTHLGGEDFDSRLVN 237
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQdLPAEeekpRNVVFVDMGHSSLQVSVCAFNKGKL-KVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 238 HLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSS-STEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVE 316
Cdd:cd10228 240 HFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLR 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 317 RALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAA 376
Cdd:cd10228 320 SALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
4-379 |
8.69e-124 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and similar proteins; The subgroup includes two Saccharomyces cerevisiae heat shock protein homologs, Sse1 and Sse2. They may have calcium-dependent calmodulin-binding activities. Both Sse1 and Sse2 belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466944 [Multi-domain] Cd Length: 385 Bit Score: 371.71 E-value: 8.69e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQD 83
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 84 MKHWPFTVVNDCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIAG 163
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 164 LNVMRIINEPTAAALAYGLDKN-LKGE----RNVLIFDLGGGTFDVSILTIDEGSLfEVRSTAGDTHLGGEDFDSRLVNH 238
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTdLPEPeekpRIVAFVDIGHSSYTVSIVAFKKGQL-TVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 239 LAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVERA 318
Cdd:cd24094 240 FADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1420818630 319 LQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILS 379
Cdd:cd24094 320 LAQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
4-377 |
3.08e-122 |
|
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: 366.18 E-value: 3.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPKDTVFDAKRligrrfddpkiqq 82
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 DMkhwpftvvndcGKPKiQVTFKGerKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd10235 68 FM-----------GTDK-QYRLGN--HTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKNLKgERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNHLAEE 242
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKRED-ETRFLVFDLGGGTFDVSVLELFEG-VIEVHASAGDNFLGGEDFTHALADYFLKK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 243 FKRKYHKDlrsNPRALRRLRTAAERAKRTLSSSTEANIEIdaLYDGVDFYTKVSRARFEELCADLFRSTLAPVERALQDA 322
Cdd:cd10235 212 HRLDFTSL---SPSELAALRKRAEQAKRQLSSQDSAEIRL--TYRGEELEIELTREEFEELCAPLLERLRQPIERALRDA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1420818630 323 KMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAI 377
Cdd:cd10235 287 GLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
4-376 |
1.83e-118 |
|
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, 170 kDa glucose-regulated protein/GRP170; HSP12A; 150 kDa oxygen-regulated protein/ORP150; GRP-170; ORP-150) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (also known as BiP, Grp78 or HspA5) and may also act as a HSPA5-independent chaperone. S. cerevisiae Lhs1p, does not have a detectable endogenous ATPase activity like canonical HSP70s, but functions as a NEF for Kar2p; it's interaction with Kar2p is stimulated by nucleotide-binding. In addition, Lhs1p has a nucleotide-independent holdase activity that prevents heat-induced aggregation of proteins in vitro. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466828 [Multi-domain] Cd Length: 353 Bit Score: 356.81 E-value: 1.83e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGK-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGrrfddpkiqq 82
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 83 dmkhwpftvvndcgkpkiqvtfkgerkvFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLD--KNLKGERNVLIFDLGGGTFDVSILTID-----------EGSLFEVRSTAGDTHLGGE 229
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDrrFENNEPQNVLFYDMGASSTSATVVEFSsvkekdkgknkTVPQVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 230 DFDSRLVNHLAEEFKRKYHK--DLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADL 307
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1420818630 308 FRSTLAPVERALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNLSINPDEAVAYGAAVQAA 376
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
3-563 |
5.18e-108 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 337.98 E-value: 5.18e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 3 AIGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDaaknqvamnpKDTVFDAKRLIGRRFDD----P 78
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTLKEilntP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 79 KIQQDMKHWpftVVNDCGKPKIQVTFKGERkvfaPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDA 158
Cdd:PRK01433 91 ALFSLVKDY---LDVNSSELKLNFANKQLR----IPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 159 GAIAGLNVMRIINEPTAAALAYGLDKNLKGerNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLVNH 238
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNKNQKG--CYLVYDLGGGTFDVSILNIQEG-IFQVIATNGDNMLGGNDIDVVITQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 239 LAEEFkrkyhkDLRSNPRALRrlrtAAERAKRTLSSstEANIEIDALYdgvdfytkVSRARFEELCADLFRSTLAPVERA 318
Cdd:PRK01433 241 LCNKF------DLPNSIDTLQ----LAKKAKETLTY--KDSFNNDNIS--------INKQTLEQLILPLVERTINIAQEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 319 LQDAKMDKgsIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNlSINPDEAVAYGAAVQAAILSgdqsSAIQDVLLVDVAPLS 398
Cdd:PRK01433 301 LEQAGNPN--IDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLI----APHTNSLLIDVVPLS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 399 LGIETAGGVMTKLVERNARIPCKQKQIFTTYSDNQPAVTIQVYEGERAMTKDNNLLGTFNLTGIPPAPRGVPQIEVTFDL 478
Cdd:PRK01433 374 LGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 479 DANGILNVTAKDSSTGRSQNITIRNDKGrLSADEIQRMVDEAERYKEEDDKQRERVAARNQLESYVFSIKQAVEEAGDKL 558
Cdd:PRK01433 454 DADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLL 532
|
....*
gi 1420818630 559 SEADK 563
Cdd:PRK01433 533 SESEI 537
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
4-377 |
2.21e-102 |
|
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: 316.50 E-value: 2.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQD 83
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 84 MKHWPFTVVN-DCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd11737 83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKN-----LKGERNVLIFDLGGGTFDVSILTIDEGSLfEVRSTAGDTHLGGEDFDSRLVN 237
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQdlpapEEKPRNVVFVDMGHSAYQVSVCAFNKGKL-KVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 238 HLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSS-STEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVE 316
Cdd:cd11737 242 HFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1420818630 317 RALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAI 377
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; ... |
4-379 |
5.01e-98 |
|
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: 305.30 E-value: 5.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQD 83
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 84 MKHWPFTVVN-DCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd11738 83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDKN-----LKGERNVLIFDLGGGTFDVSILTIDEGSLfEVRSTAGDTHLGGEDFDSRLVN 237
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQdlpalEEKPRNVVFVDMGHSAYQVSICAFNKGKL-KVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 238 HLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSS-STEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVE 316
Cdd:cd11738 242 YFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLK 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1420818630 317 RALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAAILS 379
Cdd:cd11738 322 AVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
2-378 |
5.45e-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: 5.45e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 2 PAIGIDLGTTYSCVG-VWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRrfddpki 80
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGT------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 qqdmkhwpftvvndcgkpkiqvtfkgerKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGA 160
Cdd:cd10232 74 ----------------------------TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 161 IAGLNVMRIINEPTAAALAYGLDKNLKG----ERNVLIFDLGGGTFDVSILTIDEGsLFEVRSTAGDTHLGGEDFDSRLV 236
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGdtikDKTVVVADLGGTRSDVTVVAVRGG-LYTILATVHDYELGGVALDDVLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 237 NHLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVE 316
Cdd:cd10232 205 GHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVT 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420818630 317 RALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKS---LNLSINPDEAVAYGAAVQAAIL 378
Cdd:cd10232 285 DAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTiirAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
4-376 |
4.31e-95 |
|
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: 297.54 E-value: 4.31e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPKDTVFDAKRLIGRRFDDPKIQQD 83
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 84 MKHWPFTVVN-DCGKPKIQVTFKGERKVFAPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIA 162
Cdd:cd11739 83 KENLSYDLVPlKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 163 GLNVMRIINEPTAAALAYGLDK-NLKGE----RNVLIFDLGGGTFDVSILTIDEGSlFEVRSTAGDTHLGGEDFDSRLVN 237
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKqDLPAPdekpRIVVFVDMGHSAFQVSACAFNKGK-LKVLGTAFDPYLGGRNFDEKLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 238 HLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSS-STEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLAPVE 316
Cdd:cd11739 242 HFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLY 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 317 RALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGAAVQAA 376
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 ... |
4-373 |
1.12e-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: 205.42 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIandqgnrttpsyvaftdterligdaaknqvamnpkdTVFDAKRLIGRRFDDPKIqqd 83
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPP------------------------------------LVVLQLPWPGGDGGSSKV--- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 84 mkhwPfTVVndcgkpkiqvtfkgerkvfapeEISSMVLTKMKETAEAYLGKSVR-------DAVVTVPAYFNDSQRQATK 156
Cdd:cd10170 42 ----P-SVL----------------------EVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 157 DAGAIAGL----NVMRIINEPTAAALAYGLDK----NLKGERNVLIFDLGGGTFDVSILTIDEGS--LFEVRSTAGDTHL 226
Cdd:cd10170 95 EAARAAGFgsdsDNVRLVSEPEAAALYALEDKgdllPLKPGDVVLVCDAGGGTVDLSLYEVTSGSplLLEEVAPGGGALL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 227 GGEDFDSRLVNHLAEEFKRKYHKDLRSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDGVD---FYTKVSRARFEEL 303
Cdd:cd10170 175 GGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEEE 254
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420818630 304 CADLFRSTLAPVERALQDA--KMDKGSIHDVVLVGGSTRIPKIQSMLQTFFNGKSLNL---SINPDEAVAYGAAV 373
Cdd:cd10170 255 IRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIvlrSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
4-352 |
5.42e-39 |
|
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: 148.58 E-value: 5.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGKVEIIANDQGNRTTPSYVAFTDTE------RLIGDAAKNQVAMNPKDtvfdakrliGRRFDD 77
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEE---------GRLIKS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 78 PKiqqdmkhwpftvvNDCGKPKIQVTFKGERKVFaPEEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQAT-- 155
Cdd:cd10231 72 VK-------------SFLGSSLFDETTIFGRRYP-FEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaq 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 156 -----KDAGAIAGLNVMRIINEPTAAALAYglDKNLKGERNVLIFDLGGGTFDVSILTIDEGSL---FEVRSTAGDtHLG 227
Cdd:cd10231 138 aesrlRDAARRAGFRNVEFQYEPIAAALDY--EQRLDREELVLVVDFGGGTSDFSVLRLGPNRTdrrADILATSGV-GIG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 228 GEDFDSRLVNHLA-----------------------------------------EEFKRKYHKDLRSNPRALR------- 259
Cdd:cd10231 215 GDDFDRELALKKVmphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktLRLLLDLRRDAADPEKIERllslved 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 260 ----RLRTAAERAKRTLSSSTEANIEIDALYDGVDfyTKVSRARFEELCADLFRSTLAPVERALQDAKMDKGSIHDVVLV 335
Cdd:cd10231 295 qlghRLFRAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLT 372
|
410
....*....|....*..
gi 1420818630 336 GGSTRIPKIQSMLQTFF 352
Cdd:cd10231 373 GGSSQSPAVRQALASLF 389
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-372 |
1.06e-23 |
|
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: 103.13 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVG---VWQHGKVEIIANDQG------NRTTPSYVAFTDTERLIG---DAAKNQVAMNPKDTVFDakrli 71
Cdd:cd10229 3 VAIDFGTTYSGYAysfITDPGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDEEHQW----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 72 gRRFDDPKIQQDMKHWPF--TVVNDCGKPKIQVTfkgerKVFAP--EEISSMVLTKMKETAEAYLgkSVRDA--VVTVPA 145
Cdd:cd10229 78 -LYFFKFKMMLLSEKELTrdTKVKAVNGKSMPAL-----EVFAEalRYLKDHALKELRDRSGSSL--DEDDIrwVLTVPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 146 YFNDSQ----RQATKDAGAIAGLNVMR--IINEPTAAALAY------GLDKNLKGERNVLIFDLGGGTFDVSILTIDEGS 213
Cdd:cd10229 150 IWSDAAkqfmREAAVKAGLISEENSEQliIALEPEAAALYCqkllaeGEEKELKPGDKYLVVDCGGGTVDITVHEVLEDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 214 LFE--VRSTAGdtHLGGEDFDSRLVNHLAEEFKRKYHKDLRSN-PRALRRLRTAAERAKRTLSssteanIEIdalydgvd 290
Cdd:cd10229 230 KLEelLKASGG--PWGSTSVDEEFEELLEEIFGDDFMEAFKQKyPSDYLDLLQAFERKKRSFK------LRL-------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 291 fytkvSRARFEELCADLFRSTLAPVERALQDAKMDKgsIHDVVLVGGSTRIPKIQSMLQTFFnGKSLNLSI--NPDEAVA 368
Cdd:cd10229 294 -----SPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAF-STKVKIIIppEPGLAVV 365
|
....
gi 1420818630 369 YGAA 372
Cdd:cd10229 366 KGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
4-373 |
4.52e-12 |
|
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: 67.50 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnpkdtvfDAKRLIGRRFDDPKI 80
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 QQDMKHwpfTVVNDCgkpkiqvtfkgerkvfapeeissmvltkmkETAEAYL----GKSVR-------DAVVTVPAYFND 149
Cdd:cd10225 58 IRPLRD---GVIADF------------------------------EATEAMLryfiRKAHRrrgflrpRVVIGVPSGITE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 150 SQRQATKDAGAIAGLNVMRIINEPTAAALAYGLD-KNLKGernVLIFDLGGGTFDVSILTIdeGSLFEVRStagdTHLGG 228
Cdd:cd10225 105 VERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPiEEPRG---SMVVDIGGGTTEIAVISL--GGIVTSRS----VRVAG 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 229 EDFDSRLVNHLaeefKRKYHkdlrsnpraLRRLRTAAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARfeELCADLF 308
Cdd:cd10225 176 DEMDEAIINYV----RRKYN---------LLIGERTAERIKIEIGSAYPLDEELSMEVRGRDLVTGLPRTI--EITSEEV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 309 RSTLAP--------VERALQDAK-------MDKGsihdVVLVGGSTRIPKIQSMLQtffngKSLNLSI----NPDEAVAY 369
Cdd:cd10225 241 REALEEpvnaiveaVRSTLERTPpelaadiVDRG----IVLTGGGALLRGLDELLR-----EETGLPVhvadDPLTCVAK 311
|
....
gi 1420818630 370 GAAV 373
Cdd:cd10225 312 GAGK 315
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
118-353 |
3.88e-11 |
|
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: 64.24 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 118 SMVLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKdagaiAGLNVMRIINEPTAAAlaYGLDKNLKGERNVLIFDL 197
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAA--NLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 198 GGGTFDVSIltIDEGSLFEVRStagdTHLGGEDFDSRLVNHLAEEFKrkyhkdlrsnpralrrlrtAAERAKRTLSSST- 276
Cdd:cd24004 122 GAGTTDIAL--IRNGGIEAYRM----VPLGGDDFTKAIAEGFLISFE-------------------EAEKIKRTYGIFLl 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1420818630 277 -EANIEIDALYDGVDFYTKVSRArFEELCADLFRSTLapveraLQDAKMdkGSIHDVVLVGGSTRIPKIQSMLQTFFN 353
Cdd:cd24004 177 iEAKDQLGFTINKKEVYDIIKPV-LEELASGIANAIE------EYNGKF--KLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
114-350 |
4.34e-11 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 65.27 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 114 EEISSMVLTKMKETAEAYLGKSVRDAVVTVPAYFN-----DSQRQAT---KDAGAIAGLNVMRIINEPTAAALAYglDKN 185
Cdd:PRK11678 127 EDLVCAMMLHIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDF--EAT 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 186 LKGERNVLIFDLGGGTFDVSILTIdeGSLFEVRSTAGDTHL-------GGEDFD---------------SRLVNHLA--- 240
Cdd:PRK11678 205 LTEEKRVLVVDIGGGTTDCSMLLM--GPSWRGRADRSASLLghsgqriGGNDLDialafkqlmpllgmgSETEKGIAlps 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 241 ----------------EEFKRKYHKDLR------SNPRALRRLRT------------AAERAKRTLSSSTEANIEIDALY 286
Cdd:PRK11678 283 lpfwnavaindvpaqsDFYSLANGRLLNdlirdaREPEKVARLLKvwrqrlsyrlvrSAEEAKIALSDQAETRASLDFIS 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420818630 287 DGVDfyTKVSRARFEELCADLFRSTLAPVERALQDAkmdkGSIHDVV-LVGGSTRIPKIQSMLQT 350
Cdd:PRK11678 363 DGLA--TEISQQGLEEAISQPLARILELVQLALDQA----QVKPDVIyLTGGSARSPLIRAALAQ 421
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
4-372 |
4.43e-09 |
|
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: 58.55 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVwqHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDAAK--------NQVAMNP-KDTV---FD-A 67
Cdd:COG1077 10 IGIDLGTANTLVYV--KGK-GIVLNE------PSVVAIdKKTGKVLavGEEAKemlgrtpgNIVAIRPlKDGViadFEvT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 68 KRLIgRRFddpkIQQDMKHWPFtvvndcGKPKIqvtfkgerkvfapeeissmvltkmketaeaylgksvrdaVVTVPAYF 147
Cdd:COG1077 81 EAML-KYF----IKKVHGRRSF------FRPRV---------------------------------------VICVPSGI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 148 NDSQRQATKDAGAIAGLNVMRIINEPTAAALAYGLDknLKGERNVLIFDLGGGTFDVSILtidegSLFEV---RStagdT 224
Cdd:COG1077 111 TEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLP--IEEPTGNMVVDIGGGTTEVAVI-----SLGGIvvsRS----I 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 225 HLGGEDFDSRLVNHLaeefKRKYHkdlrsnpralrrL----RTaAERAKRTLSSSTEANIEIDALYDGVDFYTKVSRARf 300
Cdd:COG1077 180 RVAGDELDEAIIQYV----RKKYN------------LligeRT-AEEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTI- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 301 eELCADLFRSTLAP--------VERALQDAK-------MDKGsihdVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDE 365
Cdd:COG1077 242 -TITSEEIREALEEplnaiveaIKSVLEKTPpelaadiVDRG----IVLTGGGALLRGLDKLLSEET-GLPVHVAEDPLT 315
|
....*..
gi 1420818630 366 AVAYGAA 372
Cdd:COG1077 316 CVARGTG 322
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
120-251 |
7.11e-07 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 50.98 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 120 VLTKMKETAEAYLGKSVRDAVVTVPAyfndsqrqAT--KDAGAI------AGLNVMRIINEPTAAALAYGLDknlkgerN 191
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGID-------N 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1420818630 192 VLIFDLGGGTFDVSIL-------TIDEgslfevrSTAGdTHLG-------GEDFDSrlvnhlAEEFKR--KYHKDL 251
Cdd:PRK15080 137 GAVVDIGGGTTGISILkdgkvvySADE-------PTGG-THMSlvlagayGISFEE------AEQYKRdpKHHKEI 198
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
4-371 |
7.95e-07 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 51.40 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnpkdtvfDAKRLIGRRFDDPKI 80
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGN---------------EAKKMLGRTPGNIVA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 QQDMKHwpfTVVNDcgkpkIQVTfkgerkvfapeeiSSMVLTKMKETAEAYLGKSVRdAVVTVPAYFNDSQRQATKDAGA 160
Cdd:pfam06723 60 VRPLKD---GVIAD-----FEVT-------------EAMLKYFIKKVHGRRSFSKPR-VVICVPSGITEVERRAVKEAAK 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 161 IAGLNVMRIINEPTAAALAYGLdkNLKGERNVLIFDLGGGTFDVSILTIdeGSLFEVRStagdTHLGGEDFDSRLVNHLa 240
Cdd:pfam06723 118 NAGAREVFLIEEPMAAAIGAGL--PVEEPTGNMVVDIGGGTTEVAVISL--GGIVTSKS----VRVAGDEFDEAIIKYI- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 241 eefKRKYHKDLRSnpralrrlRTaAERAKRTLSS--STEANIEIDALydGVDFYT------KVSRARFEELCADLFRSTL 312
Cdd:pfam06723 189 ---RKKYNLLIGE--------RT-AERIKIEIGSayPTEEEEKMEIR--GRDLVTglpktiEISSEEVREALKEPVSAIV 254
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1420818630 313 APVERALQDAK-------MDKGsihdVVLVGGSTRIPKIQSMLQTFFnGKSLNLSINPDEAVAYGA 371
Cdd:pfam06723 255 EAVKEVLEKTPpelaadiVDRG----IVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
162-376 |
8.50e-07 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 51.67 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYgLDKNLKgERNVLIFDLGGGTFDVSILTidEGSLfevRSTAGDThLGGEDfdsrLVNHLAe 241
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTEDEK-ELGVALVDIGGGTTDIAVFK--DGAL---RHTAVIP-VGGDH----ITNDIA- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 efkrkyhkdlrsnpRALRRLRTAAERAKRT----LSSSTEANIEIDALYDGVDFYTKVSR--------ARFEELcadlfr 309
Cdd:COG0849 241 --------------IGLRTPLEEAERLKIKygsaLASLADEDETIEVPGIGGRPPREISRkelaeiieARVEEI------ 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1420818630 310 stLAPVERALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFN-----GKSLNLSINPDE------AVAYGAAVQAA 376
Cdd:COG0849 301 --FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILGlpvriGRPDGIGGLPEAvrdpayATAVGLLLYAA 376
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
120-246 |
9.07e-07 |
|
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: 50.34 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 120 VLTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIAGLNVMRIINEPTAAALAYGLdknlkgeRNVLIFDLGG 199
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI-------RDGAVVDIGG 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1420818630 200 GTFDVSIL-------TIDEGSlfevrstaGDTHLG-------GEDFDSrlvnhlAEEFKRK 246
Cdd:cd24047 121 GTTGIAVLkdgkvvyTADEPT--------GGTHLSlvlagnyGISFEE------AEIIKRD 167
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
162-373 |
1.16e-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: 50.99 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYgLDKNLKgERNVLIFDLGGGTFDVSILTidEGSLfevRSTAGdTHLGGEDFDSRLVnhlae 241
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEK-ELGVALIDIGGGTTDIAVFK--NGSL---RYTAV-IPVGGNHITNDIA----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 242 efkrkyhkdlrsnpRALRRLRTAAERAKRT----LSSSTEANIEIDALYDGVDFYTKVSR--------ARFEELCADlfr 309
Cdd:cd24048 239 --------------IGLNTPFEEAERLKIKygsaLSEEADEDEIIEIPGVGGREPREVSRrelaeiieARVEEILEL--- 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1420818630 310 stlapVERALQDAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFN-----GKSLNLSINPDEAVAYGAAV 373
Cdd:cd24048 302 -----VKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvriGRPKNIGGLPEEVNDPAYAT 365
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
162-353 |
1.58e-06 |
|
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: 50.74 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 162 AGLNVMRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSIltIDEGSLFEVRSTAgdthLGGEDFDSRLVNHL-- 239
Cdd:cd24049 148 AGLKPVAIDVESFALARALEYLLPDEEEETVALLDIGASSTTLVI--VKNGKLLFTRSIP----VGGNDITEAIAKALgl 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 240 ----AEEFKRKYHKDLRSNPRALRRLRTAAERAkrtlsssteanieidalydgvdfytkvsrarFEELCADlfrstlapV 315
Cdd:cd24049 222 sfeeAEELKREYGLLLEGEEGELKKVAEALRPV-------------------------------LERLVSE--------I 262
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1420818630 316 ERALQ--DAKMDKGSIHDVVLVGGSTRIPKIQSMLQTFFN 353
Cdd:cd24049 263 RRSLDyyRSQNGGEPIDKIYLTGGGSLLPGLDEYLSERLG 302
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
121-352 |
2.65e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 49.96 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 121 LTKMKETAEAYLGKSVRDAVVTVPAYFNDSQRQATKDAGAIAGL------NVMRIINEPTAAAL-AYGLDKnlkgernVL 193
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR-------YI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 194 IFDLGGGTFDVSILTIDE--GSLFEVRSTAGDTHLG-GED--FDSRLVNHLAEEFKRKYHkdlRSNPRALRRLRTAAERA 268
Cdd:cd11736 198 VADCGGGTVDLTVHQIEQpqGTLKELYKASGGPYGAvGVDlaFEKLLCQIFGEDFIATFK---AKRPAAWVDLTIAFEAR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 269 KRT--LSSSTEANIEidalydgvdfytkvsrarfeelcadLFRSTLAPVERALQD--AKMDKGSIHDVVLVGGSTRIPKI 344
Cdd:cd11736 275 KRTaaLRMSSEAMNE-------------------------LFQPTISQIIQHIDDlmKKPEVKGIKFLFLVGGFAESPML 329
|
....*...
gi 1420818630 345 QSMLQTFF 352
Cdd:cd11736 330 QRAVQAAF 337
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
140-356 |
3.34e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 50.00 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 140 VVTVPAYFNDSQRQATKDAGAIAGLNV------MRIINEPTAAALaYGLDKNLKGERNVLIFDLGGGTFDVSI--LTIDE 211
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASI-YCRKLRLHQMDRYVVVDCGGGTVDLTVhqIRLPE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 212 GSLFEVRSTAGDTH--LGGE-DFDSRLVNHLAEEFKRKYHKdlrSNPRALRRLRTAAERAKRTLSSSTEANIEIDALYDG 288
Cdd:cd11735 223 GHLKELYKASGGPYgsLGVDyEFEKLLCKIFGEDFIDQFKI---KRPAAWVDLMIAFESRKRAAAPDRTNPLNITLPFSF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 289 VDFYTKV-----------SRARFEELCAD------------LFRSTLAPVERALQD--AKMDKGSIHDVVLVGGSTRIPK 343
Cdd:cd11735 300 IDYYKKFrghsvehalrkSNVDFVKWSSQgmlrmspdamnaLFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAESPL 379
|
250
....*....|...
gi 1420818630 344 IQSMLQTFFNGKS 356
Cdd:cd11735 380 LQQAVQNAFGDQC 392
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
4-372 |
3.81e-06 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 49.36 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVwqHGKvEIIANDqgnrttPSYVAF-TDTERL--IGDaaknqvamnpkdtvfDAKRLIGRRFDDPKI 80
Cdd:PRK13930 11 IGIDLGTANTLVYV--KGK-GIVLNE------PSVVAIdTKTGKVlaVGE---------------EAKEMLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 QQDMKHwpfTVVNDcgkpkIQVTfkgerkvfapEEISSMVLTKmketaeAYLGKSVR--DAVVTVPAYFNDSQRQATKDA 158
Cdd:PRK13930 67 IRPLKD---GVIAD-----FEAT----------EAMLRYFIKK------ARGRRFFRkpRIVICVPSGITEVERRAVREA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 159 GAIAGLNVMRIINEPTAAALAYGLDknlkgernV------LIFDLGGGTFDVSILtidegSLFEVrSTAGDTHLGGEDFD 232
Cdd:PRK13930 123 AEHAGAREVYLIEEPMAAAIGAGLP--------VtepvgnMVVDIGGGTTEVAVI-----SLGGI-VYSESIRVAGDEMD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 233 SRLVNHLaeefKRKYHkdlrsnpralrrL----RTaAERAKRTLSSST----EANIEIdalyDGVDFYTkvSRARFEELC 304
Cdd:PRK13930 189 EAIVQYV----RRKYN------------LligeRT-AEEIKIEIGSAYpldeEESMEV----RGRDLVT--GLPKTIEIS 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 305 ADLFRSTLAP--------VERALQDAK-------MDKGsihdVVLVGGSTRIPKIQSMLQtffngKSLNLSI----NPDE 365
Cdd:PRK13930 246 SEEVREALAEplqqiveaVKSVLEKTPpelaadiIDRG----IVLTGGGALLRGLDKLLS-----EETGLPVhiaeDPLT 316
|
....*..
gi 1420818630 366 AVAYGAA 372
Cdd:PRK13930 317 CVARGTG 323
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
168-253 |
4.50e-06 |
|
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: 48.67 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 168 RIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTfdVSILTIDEGSLFEVRStagDTHLGGEDFDSRLVNHLAEEFKRKY 247
Cdd:cd10227 141 KVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENGKPIEESS---DTLPGGEEALEKYADDILNELLKKL 215
|
....*.
gi 1420818630 248 HKDLRS 253
Cdd:cd10227 216 GDELDS 221
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
140-244 |
1.93e-05 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 47.20 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 140 VVTVPAYFNDSQRQATKDAGAIAGLNVMRIINEPTAAALAYGLDknLKGERNVLIFDLGGGTFDVSILTIdeGSLFEVRS 219
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLD--ISQPSGNMVVDIGGGTTDIAVLSL--GGIVTSSS 174
|
90 100
....*....|....*....|....*
gi 1420818630 220 tagdTHLGGEDFDSRLVNHLAEEFK 244
Cdd:PRK13928 175 ----IKVAGDKFDEAIIRYIRKKYK 195
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
4-370 |
2.32e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 46.82 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCVGVWQHGkveIIANDqgnrttPSYVAFTDTER---LIGDAAKNQVAMNPkdtvfdAKRLIGRRFDDpki 80
Cdd:PRK13929 7 IGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKavlAIGTEAKNMIGKTP------GKIVAVRPMKD--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 qqdmkhwpftvvndcgkpkiqvtfkgerKVFAPEEISSMVLTKMKETAEAYLGKSVR--DAVVTVPAYFNDSQRQATKDA 158
Cdd:PRK13929 69 ----------------------------GVIADYDMTTDLLKQIMKKAGKNIGMTFRkpNVVVCTPSGSTAVERRAISDA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 159 GAIAGLNVMRIINEPTAAALayGLDKNLKGERNVLIFDLGGGTFDVSILTIdeGSLFEVRStagdTHLGGEDFDSRLVNH 238
Cdd:PRK13929 121 VKNCGAKNVHLIEEPVAAAI--GADLPVDEPVANVVVDIGGGTTEVAIISF--GGVVSCHS----IRIGGDQLDEDIVSF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 239 L------------AEEFKRKY-HKDLRSNPRALrrlrtaaERAKRTLSSSTEANIEIDAlydgvdfyTKVSRARFEELCA 305
Cdd:PRK13929 193 VrkkynlligertAEQVKMEIgYALIEHEPETM-------EVRGRDLVTGLPKTITLES--------KEIQGAMRESLLH 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1420818630 306 DL--FRSTLAPVERALQDAKMDKGsihdVVLVGGSTRIPKIQSMLQTFFNgKSLNLSINPDEAVAYG 370
Cdd:PRK13929 258 ILeaIRATLEDCPPELSGDIVDRG----VILTGGGALLNGIKEWLSEEIV-VPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
4-244 |
2.83e-04 |
|
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: 43.35 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 4 IGIDLGTTYSCvgvwqhgkveiIANDQGNR-TTPSYVAFtdterligdaaknqvamnPKDTVfdAKRLIGRR--FDDPKI 80
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGY------------------PKDII--ARKLLGKEvlFGDEAL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 81 QQDMK---HWPFT--VVNDCGKPKIQVTfkgerkvfapeeisSMVLTKMKETAEAYLGKSVRdAVVTVPAYFNDSQRQAT 155
Cdd:cd24009 53 ENRLAldlRRPLEdgVIKEGDDRDLEAA--------------RELLQHLIELALPGPDDEIY-AVIGVPARASAENKQAL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 156 KDAGAIAGLNVMrIINEPTAAAlaYGLDKnlkgERNVLIFDLGGGTFDVSILtidEGSLFEVRSTAGDTHlGGEDFDSRL 235
Cdd:cd24009 118 LEIARELVDGVM-VVSEPFAVA--YGLDR----LDNSLIVDIGAGTTDLCRM---KGTIPTEEDQITLPK-AGDYIDEEL 186
|
....*....
gi 1420818630 236 VNHLAEEFK 244
Cdd:cd24009 187 VDLIKERYP 195
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
138-201 |
4.21e-04 |
|
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: 40.91 E-value: 4.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420818630 138 DAVVTVPAYFNDSQRQAT-----------KDAGAIAGLNVMRIINEPTAAALAYGLDknlKGERNVLIFDLGGGT 201
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLT---LGPEGLLVVDLGGGT 86
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
192-370 |
4.64e-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: 41.16 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 192 VLIfDLGGGTFDVSIltIDEGSLFEVRSTAgdthLGGEDFDSRLVNHL------AEEFKRKYhKDLRSNPRALRRLRTAA 265
Cdd:pfam14450 1 ALI-DIGGGTTDIAV--FEDGALRHTRVIP----VGGNGITKDIAIGLrtaveeAERLKIKY-GSALASLADEDEVPGVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 266 ERAKRTLSSSTEANIeidalydgvdfytkvSRARFEELCaDLFRSTLAPVERALQDAKMDKGSIHDVVLVGGSTRIPKIQ 345
Cdd:pfam14450 73 GREPREISRKELAEI---------------IEARVEEIL-ELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPGLV 136
|
170 180 190
....*....|....*....|....*....|.
gi 1420818630 346 SMLQTFFN-----GKSLNLS-INPDEAVAYG 370
Cdd:pfam14450 137 ELAERALGlpvriGSPDGIGgRNPAYATALG 167
|
|
| ASKHA_NBD_PPX_GppA |
cd24006 |
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
120-318 |
3.03e-03 |
|
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs 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: 466856 [Multi-domain] Cd Length: 294 Bit Score: 40.21 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 120 VLTKMKETAEAYLGKSVRdAVVTvpayfndsqrQATKDAG----------AIAGLNVmRIINEPTAAALAY-GLDKNLK- 187
Cdd:cd24006 56 ALRRFKKLADEYGVKRIR-AVAT----------SAVREASngdeflerikRETGIDV-EIISGEEEARLIYlAVRSGLPl 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420818630 188 GERNVLIFDLGGGTFDVSILtiDEGSLFEVRStagdTHLGGedfdSRLvnhlaeefKRKYHKDLRSNPRALRRLRTAAER 267
Cdd:cd24006 124 GDGNALIVDIGGGSTELTLG--DNGEILFSES----LPLGA----VRL--------TERFLKDDPPSELLEEYLRSFVRS 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420818630 268 AKRTL--------------SSSTEANIEIDALYDGVDFYTKVSRARFEELCADLFRSTLApvERA 318
Cdd:cd24006 186 VLRPLpkrrkikfdvaigsGGTILALAAMALARKGKPHGYEISREELKALYDELLRLSLE--ERR 248
|
|
| |
