|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-653 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1162.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 5 GEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDA 84
Cdd:PTZ00009 2 TKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 85 SVQSDRQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKD 164
Cdd:PTZ00009 82 VVQSDMKHWPFKVTTGGDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 165 AGVIAGLNVLRIINEPTAAAIAYGLDKKATsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMV 244
Cdd:PTZ00009 162 AGTIAGLNVLRIINEPTAAAIAYGLDKKGD--GEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 245 NHFVQEFKRKNK-KDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPV 323
Cdd:PTZ00009 240 EFCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 324 EKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVT 403
Cdd:PTZ00009 320 EKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 404 PLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQITVC 483
Cdd:PTZ00009 400 PLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 484 FDIDANGILNVSAEDKTTGKKNKITITNDKGRLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIRDEK 563
Cdd:PTZ00009 480 FDIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 564 IGEKLPAADKKKVEDSIEEAIQWLDGNQLAEADEFEDKMKELESVCNPIIAKMYQGGAGGEAGGP---GAAGMDEDDAP- 639
Cdd:PTZ00009 560 VKGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQAAGGGMPGGMpggMPGGMPGGAGPa 639
|
650
....*....|....
gi 297810343 640 PASGGAGPKIEEVD 653
Cdd:PTZ00009 640 GAGASSGPTVEEVD 653
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
9-618 |
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: 931.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQS 88
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQLWPFKIISGTAEKPMIVVEYKGEekQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:pfam00012 81 DIKHLPYKVVKLPNGDAGVEVRYLGE--TFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKAtsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKTD---KERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTA-QTTIEIDSLF-DGADFYSPITRARFEEMNMDLFRKCMEPVEKC 326
Cdd:pfam00012 236 EEFKKKYGIDLSKDKRALQRLREAAEKAKIELSSNQtNINLPFITAMaDGKDVSGTLTRAKFEELVADLFERTLEPVEKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 327 LRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGegNEKVQDLLLLDVTPLS 406
Cdd:pfam00012 316 LKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSG--TFDVKDFLLLDVTPLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 407 LGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDI 486
Cdd:pfam00012 393 LGIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 487 DANGILNVSAEDKTTGKKNKITITNDKGrLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIRDEkiGE 566
Cdd:pfam00012 473 DANGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE--GD 549
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 297810343 567 KLPAADKKKVEDSIEEAIQWLDGnqlAEADEFEDKMKELESVCNPIIAKMYQ 618
Cdd:pfam00012 550 KVPEAEKSKVESAIEWLKDELEG---DDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
9-386 |
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: 890.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQS 88
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQLWPFKIISGtAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:cd10233 81 DMKHWPFKVVSG-GDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKATsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDKKGK--GERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCLR 328
Cdd:cd10233 238 QEFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 297810343 329 DAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAIL 386
Cdd:cd10233 318 DAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
7-618 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 860.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 7 GPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDS-ERLIGDAAKNQVAMNPVNTVFDAKRLIGRRysDAS 85
Cdd:PRK00290 2 GKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 86 VQSDRQLWPFKIISGTAEKPmiVVEYKGeeKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDA 165
Cdd:PRK00290 80 VQKDIKLVPYKIVKADNGDA--WVEIDG--KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 166 GVIAGLNVLRIINEPTAAAIAYGLDKKatsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVN 245
Cdd:PRK00290 156 GKIAGLEVLRIINEPTAAALAYGLDKK----GDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIID 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 246 HFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIeidSL-FDGADFYSP------ITRARFEEMNMDLFRK 318
Cdd:PRK00290 232 YLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEI---NLpFITADASGPkhleikLTRAKFEELTEDLVER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 319 CMEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGEgnekVQDLL 398
Cdd:PRK00290 309 TIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 399 LLDVTPLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVP 478
Cdd:PRK00290 384 LLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 479 QITVCFDIDANGILNVSAEDKTTGKKNKITITNDKGrLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNT 558
Cdd:PRK00290 464 QIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKT 542
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 559 IRDEkiGEKLPAADKKKVEDSIEEAIQWLDGNqlaEADEFEDKMKELESVCNPIIAKMYQ 618
Cdd:PRK00290 543 LKEL--GDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQ 597
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
9-618 |
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: 783.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDS-ERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDasVQ 87
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 88 SDRQLWPFKIisgtaEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGV 167
Cdd:TIGR02350 80 EEAKRVPYKV-----VGDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 168 IAGLNVLRIINEPTAAAIAYGLDKkatSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHF 247
Cdd:TIGR02350 155 IAGLEVLRIINEPTAAALAYGLDK---SKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 248 VQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTtiEIDSLFDGADFYSP------ITRARFEEMNMDLFRKCME 321
Cdd:TIGR02350 232 ADEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLST--EINLPFITADASGPkhlemtLTRAKFEELTADLVERTKE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 322 PVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGEgnekVQDLLLLD 401
Cdd:TIGR02350 310 PVRQALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 402 VTPLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQIT 481
Cdd:TIGR02350 385 VTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 482 VCFDIDANGILNVSAEDKTTGKKNKITITNDKGrLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIRD 561
Cdd:TIGR02350 465 VTFDIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE 543
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 297810343 562 ekIGEKLPAADKKKVEDSIEEAIQWLDGNqlaEADEFEDKMKELESVCNPIIAKMYQ 618
Cdd:TIGR02350 544 --AGDKLPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
9-386 |
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: 740.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQS 88
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:cd24028 81 DIKHWPFKVVEDEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKatSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKK--SSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCLR 328
Cdd:cd24028 239 EEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 297810343 329 DAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAIL 386
Cdd:cd24028 319 DAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
7-386 |
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: 739.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 7 GPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASV 86
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 87 QSDRQLWPFKIISGTAeKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAG 166
Cdd:cd10241 81 QKDIKLLPFKIVNKNG-KPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 167 VIAGLNVLRIINEPTAAAIAYGLDKKAtsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNH 246
Cdd:cd10241 160 TIAGLNVLRIINEPTAAAIAYGLDKKG---GEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKC 326
Cdd:cd10241 237 FIKLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 327 LRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAIL 386
Cdd:cd10241 317 LEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
7-653 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 683.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 7 GPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDS-ERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDAS 85
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 86 VQSDRQlwPFKIISGTAEkpMIVVEYKGeeKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDA 165
Cdd:PRK13411 82 EERSRV--PYTCVKGRDD--TVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 166 GVIAGLNVLRIINEPTAAAIAYGLDKKATsvgEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVN 245
Cdd:PRK13411 156 GTIAGLEVLRIINEPTAAALAYGLDKQDQ---EQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 246 HFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDslFDGADFYSP------ITRARFEEMNMDLFRKC 319
Cdd:PRK13411 233 WLVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLP--FITADETGPkhlemeLTRAKFEELTKDLVEAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 320 MEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILSGEgnekVQDLLL 399
Cdd:PRK13411 311 IEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDLLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 400 LDVTPLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQ 479
Cdd:PRK13411 387 LDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 480 ITVCFDIDANGILNVSAEDKTTGKKNKITITNdKGRLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTI 559
Cdd:PRK13411 467 IEVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 560 RD--EKIGEKLPAADKKKVEdSIEEAIQwldgNQLAEADEFEDKMKELESVCNPIIAKMYQGGAGGEAGGPGAAGMDEDD 637
Cdd:PRK13411 546 KEngELISEELKQRAEQKVE-QLEAALT----DPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDTVEPTSDTLIT 620
|
650
....*....|....*.
gi 297810343 638 APPASGGAGPKIEEVD 653
Cdd:PRK13411 621 ATMNSSNETTLIDEFN 636
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
3-618 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 681.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 3 GKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFT-DSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRY 81
Cdd:PTZ00400 37 AKATGDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTeDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 82 SDASVQSDRQLWPFKIISgtAEKPMIVVEYKGeeKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQA 161
Cdd:PTZ00400 117 DEDATKKEQKILPYKIVR--ASNGDAWIEAQG--KKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 162 TKDAGVIAGLNVLRIINEPTAAAIAYGLDKkatsVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDN 241
Cdd:PTZ00400 193 TKDAGKIAGLDVLRIINEPTAAALAFGMDK----NDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 242 RMVNHFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTtiEIDSLFDGADFYSP------ITRARFEEMNMDL 315
Cdd:PTZ00400 269 RILNYLIAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADQSGPkhlqikLSRAKLEELTHDL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 316 FRKCMEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGEgnekVQ 395
Cdd:PTZ00400 347 LKKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 396 DLLLLDVTPLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPR 475
Cdd:PTZ00400 422 DLLLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPR 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 476 GVPQITVCFDIDANGILNVSAEDKTTGKKNKITITNDKGrLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNM 555
Cdd:PTZ00400 502 GVPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSV 580
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297810343 556 RNTIRDEKigEKLPAADKKKVEDSIEEAIQWLdgnQLAEADEFEDKMKELESVCNPIIAKMYQ 618
Cdd:PTZ00400 581 EKQLSDLK--DKISDADKDELKQKITKLRSTL---SSEDVDSIKDKTKQLQEASWKISQQAYK 638
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
7-636 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 680.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 7 GPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDS-ERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDAS 85
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 86 vQSDRQLwPFKIIsgTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDA 165
Cdd:CHL00094 82 -EEAKQV-SYKVK--TDSNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 166 GVIAGLNVLRIINEPTAAAIAYGLDKKATsvgeKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVN 245
Cdd:CHL00094 158 GKIAGLEVLRIINEPTAASLAYGLDKKNN----ETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 246 HFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDslFDGADFYSP------ITRARFEEMNMDLFRKC 319
Cdd:CHL00094 234 WLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLP--FITATQTGPkhiektLTRAKFEELCSDLINRC 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 320 MEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGEgnekVQDLLL 399
Cdd:CHL00094 312 RIPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 400 LDVTPLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQ 479
Cdd:CHL00094 387 LDVTPLSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 480 ITVCFDIDANGILNVSAEDKTTGKKNKITITNdKGRLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTI 559
Cdd:CHL00094 467 IEVTFDIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQL 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297810343 560 RDekIGEKLPAADKKKVEDSIEEAIQWLDGNQLaeaDEFEDKMKELESVCNPIIAKMYQGGAGGEAGGPGAAGMDED 636
Cdd:CHL00094 546 KE--LKDKISEEKKEKIENLIKKLRQALQNDNY---ESIKSLLEELQKALMEIGKEVYSSTSTTDPASNDDDVIDTD 617
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
9-525 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 666.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFT-DSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQ 87
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 88 SDrqlwpfkiisgtaekpmivveykgeEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGV 167
Cdd:COG0443 81 VG-------------------------GKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAAR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 168 IAGLNVLRIINEPTAAAIAYGLDKKAtsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHF 247
Cdd:COG0443 136 IAGLEVLRLLNEPTAAALAYGLDKGK---EEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 248 VQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDsLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCL 327
Cdd:COG0443 213 APEFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 328 RDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGEgnekVQDlllLDVTPLSL 407
Cdd:COG0443 292 ADAGLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGD----VKD---LDVTPLSL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 408 GLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDID 487
Cdd:COG0443 364 GIETLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDID 443
|
490 500 510
....*....|....*....|....*....|....*...
gi 297810343 488 ANGILNVSAEDKTTGKKNKITItndkgrlsKEDIEKMV 525
Cdd:COG0443 444 ANGILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
7-605 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 645.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 7 GPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFT-DSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDAS 85
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDELD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 86 VQSDRQlwPFKIISGtaEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDA 165
Cdd:PRK13410 82 PESKRV--PYTIRRN--EQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 166 GVIAGLNVLRIINEPTAAAIAYGLDKKATsvgeKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVN 245
Cdd:PRK13410 158 GRIAGLEVERILNEPTAAALAYGLDRSSS----QTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 246 HFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGAD----FYSPITRARFEEMNMDLFRKCME 321
Cdd:PRK13410 234 WLAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDgpkhIETRLDRKQFESLCGDLLDRLLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 322 PVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGEgnekVQDLLLLD 401
Cdd:PRK13410 314 PVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 402 VTPLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQIT 481
Cdd:PRK13410 389 VTPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 482 VCFDIDANGILNVSAEDKTTGKKNKITITNdKGRLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIRD 561
Cdd:PRK13410 469 VAFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRD 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 297810343 562 EKI--GEKLPAADKKKVEDSIEEAIQWLDGNQLAEAD----EFEDKMKEL 605
Cdd:PRK13410 548 AALefGPYFAERQRRAVESAMRDVQDSLEQDDDRELDlavaDLQEALYGL 597
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
9-386 |
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: 620.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDrVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQS 88
Cdd:cd24093 1 AIGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQLWPFKIISGTAeKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:cd24093 80 DMKTWPFKVIDVNG-NPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKaTSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGAG-KSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCLR 328
Cdd:cd24093 238 AEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLK 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 297810343 329 DAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAIL 386
Cdd:cd24093 318 DAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
10-647 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 613.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDS-ERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQS 88
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSEVDEES 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 dRQLwPFKIISGtaEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:PLN03184 122 -KQV-SYRVVRD--ENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKATsvgeKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKKSN----ETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGAD----FYSPITRARFEEMNMDLFRKCMEPVE 324
Cdd:PLN03184 274 SNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADgpkhIDTTLTRAKFEELCSDLLDRCKTPVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 325 KCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFfNGKELCKSINPDEAVAYGAAVQAAILSGEgnekVQDLLLLDVTP 404
Cdd:PLN03184 354 NALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTP 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 405 LSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCF 484
Cdd:PLN03184 429 LSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKF 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 485 DIDANGILNVSAEDKTTGKKNKITITNdKGRLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIrdEKI 564
Cdd:PLN03184 509 DIDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQL--KEL 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 565 GEKLPAADKKKVEDSIEEAIQWLDGNQLAeadEFEDKMKELESVCNPIIAKMYQGGAGGEaggpgaagmdEDDAPPASGG 644
Cdd:PLN03184 586 GDKVPADVKEKVEAKLKELKDAIASGSTQ---KMKDAMAALNQEVMQIGQSLYNQPGAGG----------AGPAPGGEAG 652
|
...
gi 297810343 645 AGP 647
Cdd:PLN03184 653 SSS 655
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
4-596 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 591.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 4 KGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSD 83
Cdd:PTZ00186 24 KVQGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 84 ASVQSDRQLWPFKIISGTAEKPMIvveYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATK 163
Cdd:PTZ00186 104 EHIQKDIKNVPYKIVRAGNGDAWV---QDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 164 DAGVIAGLNVLRIINEPTAAAIAYGLDKKATSVgeknVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRM 243
Cdd:PTZ00186 181 DAGTIAGLNVIRVVNEPTAAALAYGMDKTKDSL----IAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLAL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 244 VNHFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIE---IDSLFDGADFYS-PITRARFEEMNMDLFRKC 319
Cdd:PTZ00186 257 SDYILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNlpfITANADGAQHIQmHISRSKFEGITQRLIERS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 320 MEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGegneKVQDLLL 399
Cdd:PTZ00186 337 IAPCKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRG----DVKGLVL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 400 LDVTPLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQ 479
Cdd:PTZ00186 412 LDVTPLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQ 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 480 ITVCFDIDANGILNVSAEDKTTGKKNKITITNDKGrLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAynmrnTI 559
Cdd:PTZ00186 492 IEVTFDIDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQL-----TT 565
|
570 580 590
....*....|....*....|....*....|....*....
gi 297810343 560 RDEKIGE--KLPAADKKKVEDSIEEAIQWLDGNQLAEAD 596
Cdd:PTZ00186 566 AERQLGEwkYVSDAEKENVKTLVAELRKAMENPNVAKDD 604
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
10-387 |
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: 528.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDS-ERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQS 88
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQLWPFKiisgtaEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:cd10234 82 KQVPYPVV------SAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKatsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:cd10234 156 AGLEVLRIINEPTAAALAYGLDKK----KDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIeidSL-FDGADFYSP------ITRARFEEMNMDLFRKCME 321
Cdd:cd10234 232 DEFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEI---NLpFITADASGPkhlemkLTRAKFEELTEDLVERTIE 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297810343 322 PVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILS 387
Cdd:cd10234 309 PVEQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
9-549 |
2.37e-180 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 525.51 E-value: 2.37e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDasVQS 88
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQLWPFKIISGTAEKPMIVVEyKGEekqFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:PRK05183 99 RYPHLPYQFVASENGMPLIRTA-QGL---KSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKAtsvgEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDSGQ----EGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWIL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKRKNKKDitgnPRALRRLRTACERAKRTLSSTAQTTIEIdSLFDGAdfyspITRARFEEMNMDLFRKCMEPVEKCLR 328
Cdd:PRK05183 251 EQAGLSPRLD----PEDQRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLACRRALR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 329 DAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGegNEKVQDLLLLDVTPLSLG 408
Cdd:PRK05183 321 DAGVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAG--NKPDSDMLLLDVIPLSLG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 409 LETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDA 488
Cdd:PRK05183 398 LETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDA 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297810343 489 NGILNVSAEDKTTGKKNKITITNDKGrLSKEDIEKMVQEAEKYKSEDEE----HKKKVEAKNALE 549
Cdd:PRK05183 478 DGLLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQaralAEQKVEAERVLE 541
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
9-615 |
1.70e-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: 514.90 E-value: 1.70e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAF-TDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRrySDASVQ 87
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGR--SIEDIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 88 SDRQLwPFKIISGTAEkpMIVVEYKGEEKqfAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGV 167
Cdd:TIGR01991 79 TFSIL-PYRFVDGPGE--MVRLRTVQGTV--TPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 168 IAGLNVLRIINEPTAAAIAYGLDKKAtsvgEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHF 247
Cdd:TIGR01991 154 LAGLNVLRLLNEPTAAAVAYGLDKAS----EGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 248 VQEFKRKNKKditgNPRALRRLRTACERAKRTLSSTAQTTIEIDslFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCL 327
Cdd:TIGR01991 230 LKQLGISADL----NPEDQRLLLQAARAAKEALTDAESVEVDFT--LDGKDFKGKLTRDEFEALIQPLVQKTLSICRRAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 328 RDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSGEGNEKvqDLLLLDVTPLSL 407
Cdd:TIGR01991 304 RDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 408 GLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDID 487
Cdd:TIGR01991 381 GIETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 488 ANGILNVSAEDKTTGKKNKITITNDKGrLSKEDIEKMVQEAEKYKSEDEEHK----KKVEAKNALEnyayNMRNTIRDEk 563
Cdd:TIGR01991 461 ADGLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARalaeQKVEAERILE----ALQAALAAD- 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 297810343 564 iGEKLPAADKKKVEDSIEEAIQWLDGNQlaeADEFEDKMKELESVCNPIIAK 615
Cdd:TIGR01991 535 -GDLLSEDERAAIDAAMEALQKALQGDD---ADAIKAAIEALEEATDNFAAR 582
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
7-386 |
9.14e-172 |
|
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: 494.48 E-value: 9.14e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 7 GPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFT-DSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDAS 85
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 86 VQSDRQLWPFKII---SGTAEkpmivVEYKGeeKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQAT 162
Cdd:cd11733 81 VQKDIKMVPYKIVkasNGDAW-----VEAHG--KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 163 KDAGVIAGLNVLRIINEPTAAAIAYGLDKKatsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNR 242
Cdd:cd11733 154 KDAGQIAGLNVLRIINEPTAAALAYGLDKK----DDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 243 MVNHFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTtiEIDSLFDGADFYSP------ITRARFEEMNMDLF 316
Cdd:cd11733 230 LLNYLVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADASGPkhlnmkLTRAKFESLVGDLI 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 317 RKCMEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAIL 386
Cdd:cd11733 308 KRTVEPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
7-388 |
1.50e-152 |
|
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: 445.35 E-value: 1.50e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 7 GPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFT-DSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDAS 85
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 86 VQSDRQLWPFKIISGTAEKPMivVEYKGeeKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDA 165
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNGDAW--VEARG--QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 166 GVIAGLNVLRIINEPTAAAIAYGLDKKatsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVN 245
Cdd:cd11734 157 GQIAGLNVLRVINEPTAAALAYGLDKS----GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 246 HFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTtiEIDSLFDGADFYSP------ITRARFEEMNMDLFRKC 319
Cdd:cd11734 233 HIVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQT--DINLPFITADASGPkhinmkLTRAQFESLVKPLVDRT 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297810343 320 MEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSG 388
Cdd:cd11734 311 VEPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
10-388 |
2.05e-142 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187.
Pssm-ID: 466835 [Multi-domain] Cd Length: 409 Bit Score: 420.59 E-value: 2.05e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHD--RVEIIANDQGNRTTPSYVAFTDSER-LIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASV 86
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAVtgEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 87 QSDRQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAG 166
Cdd:cd10237 105 EEEAKRYPFKVVNDNIGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 167 VIAGLNVLRIINEPTAAAIAYGLDKKAtsvGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNH 246
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKKS---DVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVQEFKRKNKKDITgNPRALRRLRTACERAKRTLSSTAQTTIEID-----SLFDGADFYSPITRARFEEMNMDLFRKCME 321
Cdd:cd10237 262 LIDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqislPSAFKVKFKEEITRDLFETLNEDLFQRVLE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297810343 322 PVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILSG 388
Cdd:cd10237 341 PIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
9-388 |
2.31e-142 |
|
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: 418.93 E-value: 2.31e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLI-GDAAKNQVAMNPVNTVFDAKRLIGRRYSDasVQ 87
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 88 SDRQLWPFKIISGTAEKPMIVVEykgeEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGV 167
Cdd:cd10236 82 EELPLLPYRLVGDENELPRFRTG----AGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 168 IAGLNVLRIINEPTAAAIAYGLDKKAtsvgEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHF 247
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQKK----EGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 248 VQEfkrkNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDslFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCL 327
Cdd:cd10236 234 LKQ----IGIDARLDPAVQQALLQAARRAKEALSDADSASIEVE--VEGKDWEREITREEFEELIQPLVKRTLEPCRRAL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297810343 328 RDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCkSINPDEAVAYGAAVQAAILSG 388
Cdd:cd10236 308 KDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLT-SINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
8-386 |
1.38e-139 |
|
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: 412.41 E-value: 1.38e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 8 PAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQ 87
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 88 SDRQLWPFKIISgTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGV 167
Cdd:cd10238 81 ELKKESKCKIIE-KDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 168 IAGLNVLRIINEPTAAAIAYGLDKKaTSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHF 247
Cdd:cd10238 160 KAGFNVLRVISEPSAAALAYGIGQD-DPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 248 VQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCL 327
Cdd:cd10238 239 ASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 297810343 328 RDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAIL 386
Cdd:cd10238 319 NSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
10-387 |
3.07e-138 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466879 [Multi-domain] Cd Length: 351 Bit Score: 407.73 E-value: 3.07e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVW-QHDRVEIIANDQGNRTTPSYVAFTDSER-LIGDAAKNQVAMNPVNTVFDAKRLIGRRYsdasvq 87
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDKDGEvLVGEEAKNQALLDPENTIYSVKRLMGRDT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 88 sdrqlWPFKIISGtaekpmivveykgeeKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGV 167
Cdd:cd24029 75 -----KDKEEIGG---------------KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 168 IAGLNVLRIINEPTAAAIAYGLDKKatsVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHF 247
Cdd:cd24029 135 LAGLNVLRLINEPTAAALAYGLDKE---GKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 248 VQEFKRK-NKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKC 326
Cdd:cd24029 212 LEKIGIEtGILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKA 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297810343 327 LRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILS 387
Cdd:cd24029 292 LKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
10-384 |
5.98e-134 |
|
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: 397.70 E-value: 5.98e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQSD 89
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 90 RQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVIA 169
Cdd:cd11732 81 IKLLPFKLVELEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 170 GLNVLRIINEPTAAAIAYGLDKKATSVGE---KNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNH 246
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLESEekpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKC 326
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 297810343 327 LRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAA 384
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
9-387 |
1.11e-129 |
|
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: 387.44 E-value: 1.11e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQS 88
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:cd24095 83 DLKLFPFKVTEGPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKATSVGE-KNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHF 247
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIYKTDLPETDpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 248 VQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCL 327
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKAL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 328 RDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILS 387
Cdd:cd24095 323 ADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
10-384 |
3.27e-123 |
|
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: 370.45 E-value: 3.27e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQSD 89
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 90 RQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVIA 169
Cdd:cd10228 81 LKHLPYKVVKLPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 170 GLNVLRIINEPTAAAIAYGLDKKAT-SVGEK--NVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNH 246
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDLpAEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQT-TIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEK 325
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSANATElPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 297810343 326 CLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAA 384
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
10-385 |
6.17e-121 |
|
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: 363.10 E-value: 6.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAF-TDSERLIGDAAKNQVAMNPVNTVFDAKRLIGrrysdasvqS 88
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMG---------T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQlwpfkiisgtaekpmivveYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:cd10235 72 DKQ-------------------YRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGEL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKATsvgEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:cd10235 133 AGLKVERLINEPTAAALAYGLHKRED---ETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKrknKKDITGNPRALRRLRTACERAKRTLSSTAQTtiEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCLR 328
Cdd:cd10235 210 KKHR---LDFTSLSPSELAALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALR 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 297810343 329 DAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAI 385
Cdd:cd10235 285 DAGLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
10-387 |
5.57e-115 |
|
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: 349.37 E-value: 5.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQSD 89
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 90 RQLWPFKIISGTAEKPmIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVIA 169
Cdd:cd24094 81 EKYFTAKLVDANGEVG-AEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 170 GLNVLRIINEPTAAAIAYGLDKKATSVGE---KNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNH 246
Cdd:cd24094 160 GLNPLRLMNDTTAAALGYGITKTDLPEPEekpRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEKC 326
Cdd:cd24094 240 FADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297810343 327 LRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILS 387
Cdd:cd24094 320 LAQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
10-384 |
6.61e-111 |
|
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: 337.55 E-value: 6.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQ-HDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGrrysdasvqs 88
Cdd:cd10230 3 LGIDLGSEFIKVALVKpGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 drqlwpfkiisgtaekpmivveykgeekqFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:cd10230 73 -----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTI------------EEGIFEVKATAGDTHLGG 236
Cdd:cd10230 124 AGLNVLSLINDNTAAALNYGIDRRFENNEPQNVLFYDMGASSTSATVVEFssvkekdkgknkTVPQVEVLGVGWDRTLGG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 237 EDFDNRMVNHFVQEFKRKNKK--DITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMD 314
Cdd:cd10230 204 LEFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCAD 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 315 LFRKCMEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAA 384
Cdd:cd10230 284 LFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
9-613 |
1.30e-102 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 324.50 E-value: 1.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 9 AIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGdaakNQVAMNPVntvfdaKRLIGRrySDASVQS 88
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG----NNKGLRSI------KRLFGK--TLKEILN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 89 DRQLwpFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVI 168
Cdd:PRK01433 89 TPAL--FSLVKDYLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAYGLDKKATSVgeknVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFV 248
Cdd:PRK01433 167 AGFEVLRLIAEPTAAAYAYGLNKNQKGC----YLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 249 QEFKRKNKKDITgnpralrrlrTACERAKRTLssTAQTTIEIDSLFdgadfyspITRARFEEMNMDLFRKCMEPVEKCLR 328
Cdd:PRK01433 243 NKFDLPNSIDTL----------QLAKKAKETL--TYKDSFNNDNIS--------INKQTLEQLILPLVERTINIAQECLE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 329 DAKMDKstVHDIVLVGGSTRIPKVQQLLQDFFNgKELCKSINPDEAVAYGAAVQAAILSGEGnekvQDLLLLDVTPLSLG 408
Cdd:PRK01433 303 QAGNPN--IDGVILVGGATRIPLIKDELYKAFK-VDILSDIDPDKAVVWGAALQAENLIAPH----TNSLLIDVVPLSLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 409 LETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDA 488
Cdd:PRK01433 376 MELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 489 NGILNVSAEDKTTGKKNKITITNDKGrLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIrdEKIGEKL 568
Cdd:PRK01433 456 DGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAI--AELTTLL 532
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 297810343 569 PAADKKKVE---DSIEEAIQWLDGNQLAEA-DEFEDKMKE-LESVCNPII 613
Cdd:PRK01433 533 SESEISIINsllDNIKEAVHARDIILINNSiKEFKSKIKKsMDTKLNIII 582
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
8-386 |
1.17e-96 |
|
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: 300.82 E-value: 1.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 8 PAIGIDLGTTYSCVG-VWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGrrysdasv 86
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 87 qsdrqlwpfkiisgtaekpmivveykgeEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAG 166
Cdd:cd10232 73 ----------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 167 VIAGLNVLRIINEPTAAAIAYGL--DKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMV 244
Cdd:cd10232 125 AAAGLEVLQLIPEPAAAALAYDLraETSGDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 245 NHFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVE 324
Cdd:cd10232 205 GHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVT 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297810343 325 KCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNG---KELCKSINPDEAVAYGAAVQAAIL 386
Cdd:cd10232 285 DAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEstiIRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
10-385 |
3.64e-95 |
|
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: 298.01 E-value: 3.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQSD 89
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 90 RQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVIA 169
Cdd:cd11737 83 KPSLAYELVQLPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 170 GLNVLRIINEPTAAAIAYGLDKKATSVGE---KNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNH 246
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQDLPAPEekpRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTA-QTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEK 325
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANAsDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 326 CLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAI 385
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
10-387 |
6.35e-88 |
|
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: 279.49 E-value: 6.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQSD 89
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 90 RQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVIA 169
Cdd:cd11738 83 KIKLPYELQKMPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 170 GLNVLRIINEPTAAAIAYGLDKKATSVGE---KNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNH 246
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQDLPALEekpRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQT-TIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEK 325
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANASDlPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297810343 326 CLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAAILS 387
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
10-384 |
1.75e-84 |
|
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: 270.19 E-value: 1.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRYSDASVQSD 89
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 90 RQLWPFKIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVIA 169
Cdd:cd11739 83 KENLSYDLVPLKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 170 GLNVLRIINEPTAAAIAYGLDKKATSVGEKN---VLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNH 246
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQDLPAPDEKpriVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSS-TAQTTIEIDSLFDGADFYSPITRARFEEMNMDLFRKCMEPVEK 325
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 297810343 326 CLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAVAYGAAVQAA 384
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
122-381 |
9.30e-60 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 203.11 E-value: 9.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 122 EISSMVLIKMREIAEAFLGTTVKNA-------VVTVPAYFNDSQRQATKDAGVIAGL----NVLRIINEPTAAAIAYGLD 190
Cdd:cd10170 46 EVVADFLRALLEHAKAELGDRIWELekapievVITVPAGWSDAAREALREAARAAGFgsdsDNVRLVSEPEAAALYALED 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 191 KKATSVGEKN--VLIFDLGGGTFDVSLLTIEEGIFEVK---ATAGDTHLGGEDFDNRMVNHFVQEFKRKNKKDITGNPRA 265
Cdd:cd10170 126 KGDLLPLKPGdvVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 266 LRRLRTACERAKRTLSSTAQTTIEIDSLFDGAD---FYSPITRARFEEMNMDLFRKCMEPVEKCLRDA--KMDKSTVHDI 340
Cdd:cd10170 206 LAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQleAKSGTPPDAV 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 297810343 341 VLVGGSTRIPKVQQLLQDFFNGKEL---CKSINPDEAVAYGAAV 381
Cdd:cd10170 286 VLVGGFSRSPYLRERLRERFGSAGIiivLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
10-360 |
1.23e-33 |
|
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: 133.17 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSE------RLIGDAAKNQVAMNPVNTvfdakRLIgrrysd 83
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEG-----RLI------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 84 asvQSDRQLWPFKIISGTAEKpmivveykgeEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQAT- 162
Cdd:cd10231 70 ---KSVKSFLGSSLFDETTIF----------GRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDa 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 163 ------KDAGVIAGLNVLRIINEPTAAAIAYgldkKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFE----VKATAGDt 232
Cdd:cd10231 137 qaesrlRDAARRAGFRNVEFQYEPIAAALDY----EQRLDREELVLVVDFGGGTSDFSVLRLGPNRTDrradILATSGV- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 233 HLGGEDFDNRMVNHFV-QEFKRKN------------------------------------KKDIT---GNPRALRRLRT- 271
Cdd:cd10231 212 GIGGDDFDRELALKKVmPHLGRGStyvsgdkglpvpawlyadlsnwhaisllytkktlrlLLDLRrdaADPEKIERLLSl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 272 -----------ACERAKRTLSSTAQTTIEIDslFDGADFYSPITRARFEEMNMDLFRKCMEPVEKCLRDAKMDKSTVHDI 340
Cdd:cd10231 292 vedqlghrlfrAVEQAKIALSSADEATLSFD--FIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420
....*....|....*....|
gi 297810343 341 VLVGGSTRIPKVQQLLQDFF 360
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLF 389
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
10-380 |
1.42e-20 |
|
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: 93.88 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGV----WQHDRVEIIANDQG-----NRTTPSYVAFTDSERL--IGDAAKnqvamnpvntvfdakrlig 78
Cdd:cd10229 3 VAIDFGTTYSGYAYsfitDPGDIHTMYNWWGAptgvsSPKTPTCLLLNPDGEFhsFGYEAR------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 79 RRYSDASVQSDRQLW----PFKIISGTAE--KPMIVVEYKGeeKQFAAEEISSMVL--IK---MREIAEAFlGTTVKNA- 146
Cdd:cd10229 64 EKYSDLAEDEEHQWLyffkFKMMLLSEKEltRDTKVKAVNG--KSMPALEVFAEALryLKdhaLKELRDRS-GSSLDEDd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 147 ---VVTVPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAIAY-----GLDKKATSVGEKnVLIFDLGGGTFD 212
Cdd:cd10229 141 irwVLTVPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCqkllaEGEEKELKPGDK-YLVVDCGGGTVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 213 VSLLTIEE-GIFE--VKATAGdtHLGGEDFDNRMVN--------HFVQEFKRKnkkditgNPRALRRLRTACERAKRTls 281
Cdd:cd10229 220 ITVHEVLEdGKLEelLKASGG--PWGSTSVDEEFEElleeifgdDFMEAFKQK-------YPSDYLDLLQAFERKKRS-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 282 staqTTIEIDSlfdgadfyspitrarfEEMnMDLFRKCMEPVEKCLRDAkMDKSTVHD---IVLVGGSTRIPKVQQLLQD 358
Cdd:cd10229 289 ----FKLRLSP----------------ELM-KSLFDPVVKKIIEHIKEL-LEKPELKGvdyIFLVGGFAESPYLQKAVKE 346
|
410 420
....*....|....*....|....*.
gi 297810343 359 FFngkELCKSI----NPDEAVAYGAA 380
Cdd:cd10229 347 AF---STKVKIiippEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
10-381 |
9.20e-10 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 60.56 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVwqhDRVEIIANDqgnrttPSYVAF-TDSERLI--GDaaknqvamnpvntvfDAKRLIGRRYSDASV 86
Cdd:cd10225 2 IGIDLGTANTLVYV---KGKGIVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 87 qsdrqLWPFK---IISGTAEKPMIvveykgeeKQFAAEEISSMVLIKMReiaeaflgttvknAVVTVPAYFNDSQRQATK 163
Cdd:cd10225 58 -----IRPLRdgvIADFEATEAML--------RYFIRKAHRRRGFLRPR-------------VVIGVPSGITEVERRAVK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 164 DAGVIAGLNVLRIINEPTAAAIAYGLDkkatsVGEKN-VLIFDLGGGTFDVSLLTIeEGIFEVKAtagdTHLGGEDFDNR 242
Cdd:cd10225 112 EAAEHAGAREVYLIEEPMAAAIGAGLP-----IEEPRgSMVVDIGGGTTEIAVISL-GGIVTSRS----VRVAGDEMDEA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 243 MVNHFvqefkRKNKKDITGnpralrrLRTAcERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARfeEMNMDLFRKCMEP 322
Cdd:cd10225 182 IINYV-----RRKYNLLIG-------ERTA-ERIKIEIGSAYPLDEELSMEVRGRDLVTGLPRTI--EITSEEVREALEE 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297810343 323 --------VEKCLRDAK-------MDkstvHDIVLVGGSTRIPKVQQLLQDFFNGKELCkSINPDEAVAYGAAV 381
Cdd:cd10225 247 pvnaiveaVRSTLERTPpelaadiVD----RGIVLTGGGALLRGLDELLREETGLPVHV-ADDPLTCVAKGAGK 315
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
10-323 |
2.21e-09 |
|
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also called envB) and the paralogous pair MreB and Mrl of Bacillus subtilis have all been shown to help determine cell shape. This protein is present in a wide variety of bacteria, including spirochetes, but is missing from the Mycoplasmas and from Gram-positive cocci. Most completed bacterial genomes have a single member of this family. In some species it is an essential gene. A close homolog is found in the Archaeon Methanobacterium thermoautotrophicum, and a more distant homolog in Archaeoglobus fulgidus. The family is related to cell division protein FtsA and heat shock protein DnaK. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129982 [Multi-domain] Cd Length: 333 Bit Score: 59.34 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVGVwqhDRVEIIANDqgnrttPSYVAFtdsERLIGDAAKNQVAMNPvntvfDAKRLIGRRysdasvqsd 89
Cdd:TIGR00904 5 IGIDLGTANTLVYV---KGRGIVLNE------PSVVAI---RTDRDAKTKSILAVGH-----EAKEMLGKT--------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 90 rqlwPFKIIsgtAEKPM---IVVEYKGEEKQFAAeeissmvLIKMREIAEAFLGTTVknaVVTVPAYFNDSQRQATKDAG 166
Cdd:TIGR00904 59 ----PGNIV---AIRPMkdgVIADFEVTEKMIKY-------FIKQVHSRKSFFKPRI---VICVPSGITPVERRAVKESA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 167 VIAGLNVLRIINEPTAAAIAYGLDKKaTSVGEknvLIFDLGGGTFDVSLLTIeEGIFEVKAtagdTHLGGEDFDNRMVNH 246
Cdd:TIGR00904 122 LSAGAREVYLIEEPMAAAIGAGLPVE-EPTGS---MVVDIGGGTTEVAVISL-GGIVVSRS----IRVGGDEFDEAIINY 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297810343 247 FvqefkRKNKKDITGNpralrrlRTAcERAKRTLSSTAQTTIEIDSL-FDGADFYSPITRaRFEEMNMDLFRKCMEPV 323
Cdd:TIGR00904 193 I-----RRTYNLLIGE-------QTA-ERIKIEIGSAYPLNDEPRKMeVRGRDLVTGLPR-TIEITSVEVREALQEPV 256
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
116-373 |
3.63e-07 |
|
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: 53.09 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 116 KQFAAEEISSMVLIKMREIAEAFL----GTTVKNA----VVTVPAYFNDSQRQATKDAGVIAGLNV------LRIINEPT 181
Cdd:cd11735 105 KKVKALEIFAYALQFFKEQALKELsdqaGSEFDNSdvrwVITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 182 AAAI------AYGLDKkatsvgeknVLIFDLGGGTFDVSLLTIE--EGIFE--VKATAGDTHLGGEDFDNRMV------N 245
Cdd:cd11735 185 AASIycrklrLHQMDR---------YVVVDCGGGTVDLTVHQIRlpEGHLKelYKASGGPYGSLGVDYEFEKLlckifgE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 246 HFVQEFKRKNkkditgnPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGADFYSPITRARFEE--------------- 310
Cdd:cd11735 256 DFIDQFKIKR-------PAAWVDLMIAFESRKRAAAPDRTNPLNITLPFSFIDYYKKFRGHSVEHalrksnvdfvkwssq 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297810343 311 ----MNMD----LFRKCMEPVEKCLRD--AKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFNGKelCKSINPDE 373
Cdd:cd11735 329 gmlrMSPDamnaLFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAESPLLQQAVQNAFGDQ--CRVIIPHD 399
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
121-358 |
3.99e-07 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 52.94 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 121 EEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFN-----DSQRQAT---KDAGVIAGLNVLRIINEPTAAaiayGLDKK 192
Cdd:PRK11678 127 EDLVCAMMLHIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDFE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 193 ATSVGEKNVLIFDLGGGTFDVSLLTIeegifevkataGDTH-----------------LGGEDFD-----NRMVNHF--- 247
Cdd:PRK11678 203 ATLTEEKRVLVVDIGGGTTDCSMLLM-----------GPSWrgradrsasllghsgqrIGGNDLDialafKQLMPLLgmg 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 248 ----------VQEF----------------KRKNKKDI------TGNPRALRRL-------------RTAcERAKRTLSS 282
Cdd:PRK11678 272 setekgialpSLPFwnavaindvpaqsdfySLANGRLLndlirdAREPEKVARLlkvwrqrlsyrlvRSA-EEAKIALSD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 283 TAQTTIEIDSLFDGADfySPITRARFEEMNMDLFRKCMEPVEKCLRDAkmdkSTVHDIV-LVGGSTRIP----KVQQLLQ 357
Cdd:PRK11678 351 QAETRASLDFISDGLA--TEISQQGLEEAISQPLARILELVQLALDQA----QVKPDVIyLTGGSARSPliraALAQQLP 424
|
.
gi 297810343 358 D 358
Cdd:PRK11678 425 G 425
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
133-380 |
2.46e-06 |
|
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: 50.08 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 133 EIAEAFLGTTVKNA-----------VVTVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDkkatsVGE-KN 200
Cdd:COG1077 78 EVTEAMLKYFIKKVhgrrsffrprvVICVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLP-----IEEpTG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 201 VLIFDLGGGTFDVSLLTIeEGIfeVKATAgdTHLGGEDFDNRMVNHFvqefkRKNKKDITGnpralrrLRTAcERAKRTL 280
Cdd:COG1077 153 NMVVDIGGGTTEVAVISL-GGI--VVSRS--IRVAGDELDEAIIQYV-----RKKYNLLIG-------ERTA-EEIKIEI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 281 SS----TAQTTIEIdslfDGADFYS--PITRarfeEMNMDLFRKCM-EPVEKCLRDAK--------------MDKStvhd 339
Cdd:COG1077 215 GSayplEEELTMEV----RGRDLVTglPKTI----TITSEEIREALeEPLNAIVEAIKsvlektppelaadiVDRG---- 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 297810343 340 IVLVGGSTRIPKVQQLLQDFFNgkelcksI------NPDEAVAYGAA 380
Cdd:COG1077 283 IVLTGGGALLRGLDKLLSEETG-------LpvhvaeDPLTCVARGTG 322
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
145-380 |
4.49e-06 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 48.98 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 145 NAVVTVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDkkatsVGEKN-VLIFDLGGGTFDVSLLTIeEGIf 223
Cdd:PRK13930 102 RIVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLP-----VTEPVgNMVVDIGGGTTEVAVISL-GGI- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 224 evkATAGDTHLGGEDFDNRMVNHFvqefkRKNKKDITGNpralrrlRTAcERAKRTLSSTAQ----TTIEID--SLFDGa 297
Cdd:PRK13930 175 ---VYSESIRVAGDEMDEAIVQYV-----RRKYNLLIGE-------RTA-EEIKIEIGSAYPldeeESMEVRgrDLVTG- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 298 dfyspitRARFEEMNMDLFRKCMEP--------VEKCLRDAKMDKST-VHD--IVLVGGSTRIPKVQQLLQDFFnGKELC 366
Cdd:PRK13930 238 -------LPKTIEISSEEVREALAEplqqiveaVKSVLEKTPPELAAdIIDrgIVLTGGGALLRGLDKLLSEET-GLPVH 309
|
250
....*....|....
gi 297810343 367 KSINPDEAVAYGAA 380
Cdd:PRK13930 310 IAEDPLTCVARGTG 323
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
147-373 |
5.67e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 48.81 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 147 VVTVPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAI-AYGLDKkatsvgeknVLIFDLGGGTFDVSLLTIE 219
Cdd:cd11736 144 VLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR---------YIVADCGGGTVDLTVHQIE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 220 E--GIFE--VKATAGDTHLGGEDFD-NRMVNH-----FVQEFKRKnkkditgNPRALRRLRTACERAKRTLSstaqttie 289
Cdd:cd11736 215 QpqGTLKelYKASGGPYGAVGVDLAfEKLLCQifgedFIATFKAK-------RPAAWVDLTIAFEARKRTAA-------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 290 idslfdgadfyspiTRARFEEMNmDLFRKCMEPVEKCLrDAKMDKSTVHDI---VLVGGSTRIPKVQQLLQDFFNgkELC 366
Cdd:cd11736 280 --------------LRMSSEAMN-ELFQPTISQIIQHI-DDLMKKPEVKGIkflFLVGGFAESPMLQRAVQAAFG--NIC 341
|
....*..
gi 297810343 367 KSINPDE 373
Cdd:cd11736 342 RVIIPQD 348
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
107-234 |
2.21e-05 |
|
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: 46.49 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 107 IVVEYkgeekqFAAEEIssmvLIKMREIAEAFLGTTVKNAVVTVPAyfNDSQRQATKDAGVI--AGLNVLRIINEPTAAA 184
Cdd:cd24047 38 IVVDY------IGAIRI----VRKLKETLEKKLGVELTSAATAFPP--GTGERDARAIRNVLegAGLEVSNVVDEPTAAN 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 297810343 185 IAYGLDKKAtsvgeknvlIFDLGGGTFDVSLltIEEGifEVKATA----GDTHL 234
Cdd:cd24047 106 AVLGIRDGA---------VVDIGGGTTGIAV--LKDG--KVVYTAdeptGGTHL 146
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
147-252 |
4.67e-05 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 46.05 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 147 VVTVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKKATSvgekNVLIFDLGGGTFDVSLLTIeEGIfevk 226
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPS----GNMVVDIGGGTTDIAVLSL-GGI---- 169
|
90 100
....*....|....*....|....*.
gi 297810343 227 ATAGDTHLGGEDFDNRMVNHFVQEFK 252
Cdd:PRK13928 170 VTSSSIKVAGDKFDEAIIRYIRKKYK 195
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
169-361 |
1.49e-04 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 44.74 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 169 AGLNVLRIINEPTAAAIAygldkkATSVGEK--NVLIFDLGGGTFDVSLltIEEGIfeVKATAGDThLGGedfdnrmvNH 246
Cdd:COG0849 174 AGLEVEDLVLSPLASAEA------VLTEDEKelGVALVDIGGGTTDIAV--FKDGA--LRHTAVIP-VGG--------DH 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 247 FVqefkrknkKDITgnpRALRRLRTACERAKRTLSST------AQTTIEIDSLfdGADFYSPITR--------ARFEEMn 312
Cdd:COG0849 235 IT--------NDIA---IGLRTPLEEAERLKIKYGSAlasladEDETIEVPGI--GGRPPREISRkelaeiieARVEEI- 300
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297810343 313 mdlfrkcMEPVEKCLRDAKMDKSTVHDIVLVGGSTRIPKVQQLLQDFFN 361
Cdd:COG0849 301 -------FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
145-290 |
1.56e-04 |
|
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: 44.47 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 145 NAVVTVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDkkatsVGE-KNVLIFDLGGGTFDVSLLTIeEGIf 223
Cdd:pfam06723 95 RVVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLP-----VEEpTGNMVVDIGGGTTEVAVISL-GGI- 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297810343 224 evkATAGDTHLGGEDFDNRMVNHFvqefkRKNKKDITGNpralrrlRTAcERAKRTLSSTAQT----TIEI 290
Cdd:pfam06723 168 ---VTSKSVRVAGDEFDEAIIKYI-----RKKYNLLIGE-------RTA-ERIKIEIGSAYPTeeeeKMEI 222
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
10-251 |
2.51e-04 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 43.74 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTtySCVGVWQHDRvEIIANDqgnrttPSYVAFTDSER---LIGDAAKNQVAMNPVNTVfdakrligrrysdasv 86
Cdd:PRK13929 7 IGIDLGT--ANILVYSKNK-GIILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 87 qsdrqlwpfkiisgtAEKPMivveykgEEKQFAAEEISSMVLIKMREIAEAFLGTTVK--NAVVTVPAYFNDSQRQATKD 164
Cdd:PRK13929 62 ---------------AVRPM-------KDGVIADYDMTTDLLKQIMKKAGKNIGMTFRkpNVVVCTPSGSTAVERRAISD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 165 AGVIAGLNVLRIINEPTAAAIAYGL--DKKATSVgeknvlIFDLGGGTFDVSLLTieegiFEVKATAGDTHLGGEDFDNR 242
Cdd:PRK13929 120 AVKNCGAKNVHLIEEPVAAAIGADLpvDEPVANV------VVDIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDED 188
|
....*....
gi 297810343 243 MVNHFVQEF 251
Cdd:PRK13929 189 IVSFVRKKY 197
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
107-234 |
3.23e-04 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 42.90 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 107 IVVEYKGeekqfaaeeiSSMVLIKMREIAEAFLGTTVKNAVVTVPAyfndsqrqAT--KDAGVI------AGLNVLRIIN 178
Cdd:PRK15080 62 IVVDFIG----------AVTIVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLD 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 179 EPTAAAIAYGLDKKAtsvgeknvlIFDLGGGTFDVSLLtiEEGifEVKATA----GDTHL 234
Cdd:PRK15080 124 EPTAAAAVLGIDNGA---------VVDIGGGTTGISIL--KDG--KVVYSAdeptGGTHM 170
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
314-389 |
9.25e-04 |
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Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 42.13 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 314 DLFRKCMEPVEKCLRDAK--MDKSTVH--DIVLVGGSTRIPKVQQLLQDFFnGKELCKSiNPDEAVAYGAAVQAAILSGE 389
Cdd:COG1070 369 HLARAVLEGVAFALRDGLeaLEEAGVKidRIRATGGGARSPLWRQILADVL-GRPVEVP-EAEEGGALGAALLAAVGLGL 446
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| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
314-388 |
3.19e-03 |
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nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 40.60 E-value: 3.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297810343 314 DLFRKCMEPVEKCLRDA----KMDKSTVHDIVLVGGSTRIPKVQQLLQDFFnGKELCKSINPDEAvAYGAAVQAAILSG 388
Cdd:cd07808 366 HLARAVLEGVAFSLRDSlevlKELGIKVKEIRLIGGGAKSPLWRQILADVL-GVPVVVPAEEEGS-AYGAALLAAVGAG 442
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| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
336-388 |
3.85e-03 |
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nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 40.23 E-value: 3.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 297810343 336 TVHDIVLVGGSTRIPKVQQLLQDFFNGKELCksINPDEAVAYGAAVQAAILSG 388
Cdd:cd07809 393 EIDEIRLIGGGSKSPVWRQILADVFGVPVVV--PETGEGGALGAALQAAWGAG 443
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| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
10-259 |
6.56e-03 |
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nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 39.04 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 10 IGIDLGTTYSCVgVWQHDRVEIIandqgnrttPSYVAFTDSERLIGDAAKNQVAMNPVNTVF----DAKRLIGRRYSDAS 85
Cdd:cd10227 1 IGIDIGNGNTKV-VTGGGKEFKF---------PSAVAEARESSLDDGLLEDDIIVEYNGKRYlvgeLALREGGGGRSTGD 70
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 86 VQSDRQLWPFKIISGTA------EKPMIVV------EYKGEEKQFAAEEISSMVLIKmreiaeaflgttvknavvtvpay 153
Cdd:cd10227 71 DKKKSEDALLLLLAALAllgddeEVDVNLVvglpisEYKEEKKELKKKLLKGLHEFT----------------------- 127
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297810343 154 FNDSQRQATkdagviagLNVLRIINEPTAAAIAYGLDKKATSvgEKNVLIFDLGGGTFDVslLTIEEGIFEVKatAGDTH 233
Cdd:cd10227 128 FNGKERRIT--------INDVKVLPEGAGAYLDYLLDDDELE--DGNVLVIDIGGGTTDI--LTFENGKPIEE--SSDTL 193
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250 260
....*....|....*....|....*.
gi 297810343 234 LGGEDFDNRMVNHFVQEFKRKNKKDI 259
Cdd:cd10227 194 PGGEEALEKYADDILNELLKKLGDEL 219
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| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
146-210 |
7.99e-03 |
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ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.06 E-value: 7.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297810343 146 AVVTVPAYFNDSQRQAT-----------KDAGVIAGLNVLRIINEPTAAAIAYGLDKKATsvgekNVLIFDLGGGT 210
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPE-----GLLVVDLGGGT 86
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