|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
4-641 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1174.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 4 AKGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDP 83
Cdd:PTZ00009 2 TKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 84 VVQADMKLWPFQVINEG-GKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKD 162
Cdd:PTZ00009 82 VVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 163 AGVIAGLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:PTZ00009 162 AGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 FVEEFKRKHK-KDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 321
Cdd:PTZ00009 242 CVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 322 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKVQDLLLLDVAPL 401
Cdd:PTZ00009 322 VLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 402 SLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFD 481
Cdd:PTZ00009 402 SLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 482 IDANGILNVTAMDKSTGKVNKITITNDKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGLK 561
Cdd:PTZ00009 482 IDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKVK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 562 GKISESDKNKILDKCNELLSWLEVNQLAEKDEFDHKRKELEQMCNPIITKLYQ-----------GGCTGPACGTGYVPGR 630
Cdd:PTZ00009 562 GKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQaagggmpggmpGGMPGGMPGGAGPAGA 641
|
650
....*....|..
gi 1159610792 631 PA-TGPTIEEVD 641
Cdd:PTZ00009 642 GAsSGPTVEEVD 653
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
8-614 |
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: 946.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 8 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 87
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMKLWPFQVIN-EGGKPKVLVSYKGENkaFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 166
Cdd:pfam00012 81 DIKHLPYKVVKlPNGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYGLDKGgQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYE-GIDFYTSITRARFEELCADLFRGTLEPVEKALR 324
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 325 DAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksEKVQDLLLLDVAPLSLG 404
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 405 LETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDA 484
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 485 NGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGlkGKI 564
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEG--DKV 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1159610792 565 SESDKNKIldkcNELLSWLEVNQL-AEKDEFDHKRKELEQMCNPIITKLYQ 614
Cdd:pfam00012 552 PEAEKSKV----ESAIEWLKDELEgDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
8-382 |
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: 900.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 8 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 87
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEF 247
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 248 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDAK 327
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1159610792 328 MDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
5-625 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 870.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 5 KGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKfnDP 83
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 84 VVQADMKLWPFQVIN-EGGKPKVLVsykgENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKD 162
Cdd:PRK00290 79 EVQKDIKLVPYKIVKaDNGDAWVEI----DGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 163 AGVIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:PRK00290 155 AGKIAGLEVLRIINEPTAAALAYGLDK--KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAnlEIDSLYEGID------FYTSITRARFEELCADLFRGTL 316
Cdd:PRK00290 233 LADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EINLPFITADasgpkhLEIKLTRAKFEELTEDLVERTI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 317 EPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLL 396
Cdd:PRK00290 311 EPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVLLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 397 DVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQI 476
Cdd:PRK00290 386 DVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQI 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 477 EVTFDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVS 556
Cdd:PRK00290 466 EVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLK 544
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159610792 557 DegLKGKISESDKNKILDKCNELLSWLEVNqlaEKDEFDHKRKELEQMCNPIITKLYQGGCTGPACGTG 625
Cdd:PRK00290 545 E--LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGA 608
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
8-614 |
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: 800.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 8 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvVQ 86
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 87 ADMKLWPFQVINEGGKPKVlvsyKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 166
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRV----KVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYGLDKGGQGERhVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAnlEIDSLYEGID------FYTSITRARFEELCADLFRGTLEPVE 320
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLST--EINLPFITADasgpkhLEMTLTRAKFEELTADLVERTKEPVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 321 KALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVAP 400
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 401 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTF 480
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 481 DIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDegL 560
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--A 544
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1159610792 561 KGKISESDKNKILDKCNELLSWLEVNqlaEKDEFDHKRKELEQMCNPIITKLYQ 614
Cdd:TIGR02350 545 GDKLPAEEKEKIEKAVAELKEALKGE---DVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
8-382 |
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: 754.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 8 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 87
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 166
Cdd:cd24028 81 DIKHWPFKVVEdEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 326
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1159610792 327 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
6-382 |
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: 748.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 6 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVV 85
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 86 QADMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGV 165
Cdd:cd10241 81 QKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 166 IAGLNVLRIINEPTAAAIAYGLDKGGqGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVE 245
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKKG-GEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 246 EFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRD 325
Cdd:cd10241 240 LFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLED 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1159610792 326 AKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd10241 320 AGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
6-636 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 708.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 6 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpv 84
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 85 VQADMKLWPFQVInEGGKPKVLVSYKGENkaFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAG 164
Cdd:PRK13411 80 TEEERSRVPYTCV-KGRDDTVNVQIRGRN--YTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 165 VIAGLNVLRIINEPTAAAIAYGLDKGGQgERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFV 244
Cdd:PRK13411 157 TIAGLEVLRIINEPTAAALAYGLDKQDQ-EQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 245 EEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS--STQANLE-IDSLYEGID-FYTSITRARFEELCADLFRGTLEPVE 320
Cdd:PRK13411 236 ENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSmlTTSINLPfITADETGPKhLEMELTRAKFEELTKDLVEATIEPMQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 321 KALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVAP 400
Cdd:PRK13411 316 QALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDLLLLDVTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 401 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTF 480
Cdd:PRK13411 392 LSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 481 DIDANGILNVTAMDKSTGKVNKITITNdKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGl 560
Cdd:PRK13411 472 EIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENG- 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159610792 561 kGKISESDKNKILDKCNELLSWLEvNQLAEKDEFDHKRKELEQMCNPIITKLYQGGCTGPACGTGYVPGRPATGPT 636
Cdd:PRK13411 550 -ELISEELKQRAEQKVEQLEAALT-DPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDTVEPTSDTLITATM 623
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
9-604 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 703.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvVQA 87
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE--ISE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMKLWPFQVINEG-GKPKVLVSYKgeNKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 166
Cdd:CHL00094 83 EAKQVSYKVKTDSnGNIKIECPAL--NKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDK--KNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLE---IDSLYEG-IDFYTSITRARFEELCADLFRGTLEPVEKA 322
Cdd:CHL00094 239 FKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVENA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 323 LRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDyFNGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVAPLS 402
Cdd:CHL00094 319 LKDAKLDKSDIDEVVLVGGSTRIPAIQELVKK-LLGKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 403 LGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDI 482
Cdd:CHL00094 394 LGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 483 DANGILNVTAMDKSTGKVNKITITNdKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDegLKG 562
Cdd:CHL00094 474 DANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE--LKD 550
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1159610792 563 KISESDKNKIldkcNELLSwlEVNQLAEKDEFDHKRKELEQM 604
Cdd:CHL00094 551 KISEEKKEKI----ENLIK--KLRQALQNDNYESIKSLLEEL 586
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
1-619 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 690.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 1 MATAKGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRK 79
Cdd:PTZ00400 36 FAKATGDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 80 FNDPVVQADMKLWPFQVI-NEGGKPKVlvsyKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQ 158
Cdd:PTZ00400 116 YDEDATKKEQKILPYKIVrASNGDAWI----EAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 159 ATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQgeRHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNR 238
Cdd:PTZ00400 192 ATKDAGKIAGLDVLRIINEPTAAALAFGMDKNDG--KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 239 LVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAnlEIDSLYEGID------FYTSITRARFEELCADLF 312
Cdd:PTZ00400 270 ILNYLIAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADqsgpkhLQIKLSRAKLEELTHDLL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 313 RGTLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQD 392
Cdd:PTZ00400 348 KKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 393 LLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRG 472
Cdd:PTZ00400 423 LLLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRG 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 473 VPQIEVTFDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMK 552
Cdd:PTZ00400 503 VPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVE 581
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159610792 553 SVVSDegLKGKISESDKNKILDKCNELLSWLEVNQLaekDEFDHKRKELEQMCNPIITKLYQGGCTG 619
Cdd:PTZ00400 582 KQLSD--LKDKISDADKDELKQKITKLRSTLSSEDV---DSIKDKTKQLQEASWKISQQAYKQGNSD 643
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
8-521 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 689.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 8 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQ 86
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDgEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 87 ADmklwpfqvineggkpkvlvsykgeNKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 166
Cdd:COG0443 81 VG------------------------GKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYGLDKGGQGERhVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKGKEEET-ILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDsLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 326
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 327 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSEkvqdlllLDVAPLSLGLE 406
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 407 TAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDANG 486
Cdd:COG0443 367 TLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANG 446
|
490 500 510
....*....|....*....|....*....|....*
gi 1159610792 487 ILNVTAMDKSTGKVNKITItndkgrlsKEEIERMV 521
Cdd:COG0443 447 ILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
6-592 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 672.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 6 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpv 84
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 85 VQADMKLWPFQV-INEGGKPKVLVSYKgeNKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDA 163
Cdd:PRK13410 80 LDPESKRVPYTIrRNEQGNVRIKCPRL--EREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 164 GVIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 243
Cdd:PRK13410 158 GRIAGLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 244 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLS--SSTQANLE-IDSLYEG---IDfyTSITRARFEELCADLFRGTLE 317
Cdd:PRK13410 236 AEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpkhIE--TRLDRKQFESLCGDLLDRLLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 318 PVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDyFNGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLD 397
Cdd:PRK13410 314 PVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRT-LIPREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 398 VAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIE 477
Cdd:PRK13410 389 VTPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 478 VTFDIDANGILNVTAMDKSTGKVNKITITNdKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFN----MKS 553
Cdd:PRK13410 469 VAFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQaerrLRD 547
|
570 580 590
....*....|....*....|....*....|....*....
gi 1159610792 554 VVSDEGLKGkiSESDKNKILDKCNELLSWLEVNQLAEKD 592
Cdd:PRK13410 548 AALEFGPYF--AERQRRAVESAMRDVQDSLEQDDDRELD 584
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
8-382 |
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: 630.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 8 AIGIDLGTTYSCVGVFQhGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 87
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKG-GQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGAGkSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 326
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1159610792 327 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
9-636 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 628.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvVQA 87
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMKLWPFQVI-NEGGKPKVLVSYKGenKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 166
Cdd:PLN03184 120 ESKQVSYRVVrDENGNVKLDCPAIG--KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEK--KSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLE---IDSLYEG---IDfyTSITRARFEELCADLFRGTLEPVE 320
Cdd:PLN03184 276 FKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 321 KALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDyFNGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVAP 400
Cdd:PLN03184 354 NALRDAKLSFKDIDEVILVGGSTRIPAVQELVKK-LTGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTP 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 401 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTF 480
Cdd:PLN03184 429 LSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKF 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 481 DIDANGILNVTAMDKSTGKVNKITITNdKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDegL 560
Cdd:PLN03184 509 DIDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--L 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159610792 561 KGKISESDKNKILDKCNELLSWLEVNQLAE-KDEFDHKRKELEQMCNpiitKLYQGGCTGPAcGTGYVPGRPATGPT 636
Cdd:PLN03184 586 GDKVPADVKEKVEAKLKELKDAIASGSTQKmKDAMAALNQEVMQIGQ----SLYNQPGAGGA-GPAPGGEAGSSSSS 657
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
5-603 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 609.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 5 KGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPV 84
Cdd:PTZ00186 26 QGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 85 VQADMKLWPFQVINEG-GKPKVlvsYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDA 163
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGnGDAWV---QDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 164 GVIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 243
Cdd:PTZ00186 183 GTIAGLNVIRVVNEPTAAALAYGMDK--TKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 244 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSS--TQANLE-IDSLYEGID-FYTSITRARFEELCADLFRGTLEPV 319
Cdd:PTZ00186 261 LEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAmeTEVNLPfITANADGAQhIQMHISRSKFEGITQRLIERSIAPC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 320 EKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDksekVQDLLLLDVA 399
Cdd:PTZ00186 341 KQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVT 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 400 PLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVT 479
Cdd:PTZ00186 416 PLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVT 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 480 FDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEG 559
Cdd:PTZ00186 496 FDIDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWK 574
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1159610792 560 LkgkISESDKNKILDKCNELLSWLEvNQLAEKDEFDHKRKELEQ 603
Cdd:PTZ00186 575 Y---VSDAEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQK 614
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-546 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 560.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 5 KGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpv 84
Cdd:PRK05183 18 RRLAVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 85 VQADMKLWPFQ-VINEGGKPKV-----LVSykgenkafyPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQ 158
Cdd:PRK05183 96 IQQRYPHLPYQfVASENGMPLIrtaqgLKS---------PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 159 ATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQGerHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNR 238
Cdd:PRK05183 167 ATKDAARLAGLNVLRLLNEPTAAAIAYGLDSGQEG--VIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 239 LVSHFVEEFKRKHKKDISQnkraVRRLRTACERAKRTLSSSTQANLEIdSLYEGIdfytsITRARFEELCADLFRGTLEP 318
Cdd:PRK05183 245 LADWILEQAGLSPRLDPED----QRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 319 VEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKvqDLLLLDV 398
Cdd:PRK05183 315 CRRALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 399 APLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEV 478
Cdd:PRK05183 392 IPLSLGLETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159610792 479 TFDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQR----EKIAAKNALES 546
Cdd:PRK05183 472 TFQVDADGLLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEA 542
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
9-383 |
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: 555.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 87
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMKLWPFqVINEGGKPKVLVsykgENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd10234 82 KQVPYPV-VSAGNGDAWVEI----GGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEF 247
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDK--KKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 248 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLE---IDSLYEG---IDfyTSITRARFEELCADLFRGTLEPVEK 321
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpkhLE--MKLTRAKFEELTEDLVERTIEPVEQ 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159610792 322 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILM 383
Cdd:cd10234 313 ALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
8-545 |
0e+00 |
|
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK. [Protein fate, Protein folding and stabilization]
Pssm-ID: 273915 [Multi-domain] Cd Length: 599 Bit Score: 535.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 8 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvvq 86
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIED---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 87 admklwpfqVINEGGKPKVLVSYKGENKAFY-------PEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQA 159
Cdd:TIGR01991 77 ---------IKTFSILPYRFVDGPGEMVRLRtvqgtvtPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 160 TKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQGerHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 239
Cdd:TIGR01991 148 TKDAARLAGLNVLRLLNEPTAAAVAYGLDKASEG--IYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 240 VSHFVEEFKRKHKKDISQNKRAVRRLRTACERAkrtlssSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPV 319
Cdd:TIGR01991 226 AKWILKQLGISADLNPEDQRLLLQAARAAKEAL------TDAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSIC 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 320 EKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKvqDLLLLDVA 399
Cdd:TIGR01991 300 RRALRDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 400 PLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVT 479
Cdd:TIGR01991 377 PLSLGIETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVT 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159610792 480 FDIDANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAED-----------EVQREKIAAKNALE 545
Cdd:TIGR01991 457 FQVDADGLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDmyaralaeqkvEAERILEALQAALA 532
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
6-382 |
2.96e-174 |
|
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466839 [Multi-domain] Cd Length: 377 Bit Score: 500.25 E-value: 2.96e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 6 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPV 84
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 85 VQADMKLWPFQVIN-EGGKPKVlvsyKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDA 163
Cdd:cd11733 81 VQKDIKMVPYKIVKaSNGDAWV----EAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 164 GVIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 243
Cdd:cd11733 157 GQIAGLNVLRIINEPTAAALAYGLDK--KDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 244 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAnlEIDSLYEGID------FYTSITRARFEELCADLFRGTLE 317
Cdd:cd11733 235 VAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159610792 318 PVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd11733 313 PCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
6-384 |
1.96e-157 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins; This subgroup includes Saccharomyces cerevisiae Stress-Seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space.
Pssm-ID: 466840 [Multi-domain] Cd Length: 378 Bit Score: 457.68 E-value: 1.96e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 6 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPV 84
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 85 VQADMKLWPFQVINEGGKpKVLVSYKGENkaFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAG 164
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNG-DAWVEARGQK--YSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 165 VIAGLNVLRIINEPTAAAIAYGLDKggQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFV 244
Cdd:cd11734 158 QIAGLNVLRVINEPTAAALAYGLDK--SGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 245 EEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGID----FYTSITRARFEELCADLFRGTLEPVE 320
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKLTRAQFESLVKPLVDRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159610792 321 KALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMG 384
Cdd:cd11734 316 KALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
9-384 |
2.15e-149 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187.
Pssm-ID: 466835 [Multi-domain] Cd Length: 409 Bit Score: 438.31 E-value: 2.15e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQH--GKVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVV 85
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 86 QADMKLWPFQVINEG-GKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAG 164
Cdd:cd10237 105 EEEAKRYPFKVVNDNiGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 165 VIAGLNVLRIINEPTAAAIAYGLDKgGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFV 244
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHK-KSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 245 EEFKRKHKKDISqNKRAVRRLRTACERAKRTLSS--STQANLEIDSLYEGID---FYTSITRARFEELCADLFRGTLEPV 319
Cdd:cd10237 264 DRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNhnSASLSLPLQISLPSAFkvkFKEEITRDLFETLNEDLFQRVLEPI 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159610792 320 EKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMG 384
Cdd:cd10237 343 RQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
9-382 |
4.21e-148 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466879 [Multi-domain] Cd Length: 351 Bit Score: 432.77 E-value: 4.21e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVF-QHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDpvvq 86
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 87 admklwpfqvineggkpkvlvSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVI 166
Cdd:cd24029 77 ---------------------KEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYGLDKGGQGERhVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDGT-ILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKH-KKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRD 325
Cdd:cd24029 215 IGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1159610792 326 AKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
8-382 |
7.35e-148 |
|
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: 433.21 E-value: 7.35e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 8 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQA 87
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd10238 82 LKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKGGQGE-RHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEE 246
Cdd:cd10238 162 GFNVLRVISEPSAAALAYGIGQDDPTEnSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLASE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 247 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 326
Cdd:cd10238 242 FKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNSA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1159610792 327 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd10238 322 GLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
5-384 |
1.61e-147 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.
Pssm-ID: 466834 [Multi-domain] Cd Length: 367 Bit Score: 431.64 E-value: 1.61e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 5 KGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLI-GDAAKNQVAMNPQNTVFDAKRLIGRKFNDp 83
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 84 vVQADMKLWPFQVINEggkPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDA 163
Cdd:cd10236 80 -VKEELPLLPYRLVGD---ENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 164 GVIAGLNVLRIINEPTAAAIAYGLDKGGQGErhVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 243
Cdd:cd10236 156 ARLAGLNVLRLLNEPTAAALAYGLDQKKEGT--IAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 244 VEEFkrkhKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSlyEGIDFYTSITRARFEELCADLFRGTLEPVEKAL 323
Cdd:cd10236 234 LKQI----GIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRAL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159610792 324 RDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAILMG 384
Cdd:cd10236 308 KDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
9-380 |
1.12e-145 |
|
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466838 [Multi-domain] Cd Length: 377 Bit Score: 427.36 E-value: 1.12e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 88
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 89 MKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKGGQGE-----RHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLEseekpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKA 322
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1159610792 323 LRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAA 380
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 ... |
6-382 |
2.74e-139 |
|
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: 411.70 E-value: 2.74e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 6 GIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVV 85
Cdd:cd24095 1 MSVVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 86 QADMKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAG 164
Cdd:cd24095 81 QRDLKLFPFKVTEgPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 165 VIAGLNVLRIINEPTAAAIAYGLDKGGQGE---RHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVS 241
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIYKTDLPEtdpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 242 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 321
Cdd:cd24095 241 HFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159610792 322 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd24095 321 ALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
9-380 |
5.99e-132 |
|
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25). They belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466826 [Multi-domain] Cd Length: 378 Bit Score: 392.41 E-value: 5.99e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 88
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 89 MKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYG-----LDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGiykqdLPAEEEKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 321
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1159610792 322 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAA 380
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
9-381 |
1.37e-130 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar proteins; Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. Members in this subfamily belong to the heat shock protein 70 (Hsp70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, Hsp70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Two genes in the vicinity of the HscC gene code for potential cochaperones: J-domain containing proteins, DjlB/YbeS and DjlC/YbeV. HscC and its co-chaperone partners may play a role in the SOS DNA damage response. HscC does not appear to require a NEF.
Pssm-ID: 466833 [Multi-domain] Cd Length: 343 Bit Score: 387.37 E-value: 1.37e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPQNTVFDAKRligrkfndpvvqa 87
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 DMklwpfqvinegGKPKVlvsYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd10235 68 FM-----------GTDKQ---YRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKGGQgERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEef 247
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKRED-ETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLK-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 248 krKHKKDISQNKRAVR-RLRTACERAKRTLSSSTQAnlEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDA 326
Cdd:cd10235 211 --KHRLDFTSLSPSELaALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1159610792 327 KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAI 381
Cdd:cd10235 287 GLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
9-382 |
4.77e-125 |
|
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: 374.79 E-value: 4.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 88
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 89 MKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIAG 168
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 169 LNVLRIINEPTAAAIAYGLDK-----GGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHF 243
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKtdlpePEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 244 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKAL 323
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1159610792 324 RDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
9-380 |
7.19e-118 |
|
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, 170 kDa glucose-regulated protein/GRP170; HSP12A; 150 kDa oxygen-regulated protein/ORP150; GRP-170; ORP-150) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (also known as BiP, Grp78 or HspA5) and may also act as a HSPA5-independent chaperone. S. cerevisiae Lhs1p, does not have a detectable endogenous ATPase activity like canonical HSP70s, but functions as a NEF for Kar2p; it's interaction with Kar2p is stimulated by nucleotide-binding. In addition, Lhs1p has a nucleotide-independent holdase activity that prevents heat-induced aggregation of proteins in vitro. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466828 [Multi-domain] Cd Length: 353 Bit Score: 355.26 E-value: 7.19e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGK-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGrkfndpvvqa 87
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 88 dmklwpfqvineggkpkvlvsykgenkaFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKGGQGE--RHVLIFDLGGGTFDVSILTI------DDGI------FEVKATAGDTHLGGE 233
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRRFENNepQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 234 DFDNRLVSHFVEEFKRKHKK--DISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADL 311
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159610792 312 FRGTLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAA 380
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
7-615 |
7.79e-112 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 348.00 E-value: 7.79e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 7 IAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDaaknqvamnpQNTVFDAKRLIGRK----FND 82
Cdd:PRK01433 20 IAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTlkeiLNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 83 PVVQADMKlwPFQVINEGgkpkvLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKD 162
Cdd:PRK01433 90 PALFSLVK--DYLDVNSS-----ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 163 AGVIAGLNVLRIINEPTAAAIAYGLDKGGQGerHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:PRK01433 163 AAKIAGFEVLRLIAEPTAAAYAYGLNKNQKG--CYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 FVEEFKRKHKKDISQnkravrrlrtACERAKRTLSSstQANLEIDSLyegidfytSITRARFEELCADLFRGTLEPVEKA 322
Cdd:PRK01433 241 LCNKFDLPNSIDTLQ----------LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 323 LRDAKmdKAKIHDIVLVGGSTRIPKVQRLLQDYFNgRDLNKSINPDEAVAYGAAVQAAILMGDKsekvQDLLLLDVAPLS 402
Cdd:PRK01433 301 LEQAG--NPNIDGVILVGGATRIPLIKDELYKAFK-VDILSDIDPDKAVVWGAALQAENLIAPH----TNSLLIDVVPLS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 403 LGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDI 482
Cdd:PRK01433 374 LGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 483 DANGILNVTAMDKSTGKVNKITITNDKGrLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDegLKG 562
Cdd:PRK01433 454 DADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAE--LTT 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1159610792 563 KISESDKNKI---LDKCNELLS---WLEVNQlAEKDEFDHKRKELEQMCNPIITKLYQG 615
Cdd:PRK01433 531 LLSESEISIInslLDNIKEAVHardIILINN-SIKEFKSKIKKSMDTKLNIIINDLLKG 588
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
9-381 |
3.93e-102 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; HSPA4, also called HSP70RY, , HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466843 [Multi-domain] Cd Length: 381 Bit Score: 315.73 E-value: 3.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 88
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 89 MKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd11737 83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKGG-----QGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQDlpapeEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 321
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 322 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAI 381
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
7-382 |
3.40e-101 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex subunit Ssz1 and similar proteins; Ssz1, also called DnaK-related protein Ssz1, heat shock protein 70 homolog Ssz1, or pleiotropic drug resistance protein 13 (PDR13), is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones Ssb1/Ssb2 that bind to the nascent polypeptide chain. Ssz1 is required for Zuo1 to function efficiently as a J-protein for Ssb1/Ssb2. It is also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466830 [Multi-domain] Cd Length: 349 Bit Score: 312.37 E-value: 3.40e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 7 IAIGIDLGTTYSCVG-VFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKfndpvv 85
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGTT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 86 qadmklwpfqvineggkpkvlvsykgenkAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGV 165
Cdd:cd10232 75 -----------------------------TLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 166 IAGLNVLRIINEPTAAAIAYGLDKGGQG----ERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVS 241
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGdtikDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 242 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 321
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159610792 322 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNK----SINPDEAVAYGAAVQAAIL 382
Cdd:cd10232 286 AIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLF-PESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
9-382 |
4.15e-98 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466844 [Multi-domain] Cd Length: 383 Bit Score: 305.30 E-value: 4.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 88
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 89 MKLWPFQVIN-EGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd11738 83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKGG-----QGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQDlpaleEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 321
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159610792 322 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAAIL 382
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
9-380 |
1.51e-97 |
|
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar proteins; HSPH1, also called heat shock protein 105 kDa, antigen NY-CO-25, heat shock 110 kDa protein, acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. It prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. It inhibits HSPA8/HSC70 ATPase and chaperone activities. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466845 [Multi-domain] Cd Length: 380 Bit Score: 304.09 E-value: 1.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQAD 88
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 89 MKLWPFQ-VINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIA 167
Cdd:cd11739 83 KENLSYDlVPLKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 168 GLNVLRIINEPTAAAIAYGLDKGG-----QGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQDlpapdEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEK 321
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1159610792 322 ALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAAVQAA 380
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 ... |
9-377 |
1.15e-61 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 208.11 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVgvfqhgkveiiandqgnrttpsyvAFTDTERligdaaknqvamnpqntvfdakrligrkfNDPVVQAD 88
Cdd:cd10170 1 VGIDFGTTYSGV------------------------AYALLGP-----------------------------GEPPLVVL 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 89 MKLWPFqviNEGGKPKVlvsykgenkafyPE--EISSMVLTKLKETAEAFLGH-------PVTNAVITVPAYFNDSQRQA 159
Cdd:cd10170 28 QLPWPG---GDGGSSKV------------PSvlEVVADFLRALLEHAKAELGDriwelekAPIEVVITVPAGWSDAAREA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 160 TKDAGVIAGL----NVLRIINEPTAAAIAYGLDKGG----QGERHVLIFDLGGGTFDVSILTIDDGIFEVK---ATAGDT 228
Cdd:cd10170 93 LREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDllplKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 229 HLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGID---FYTSITRARFE 305
Cdd:cd10170 173 LLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTE 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159610792 306 ELCADLFRGTLEPVEKALRDA--KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLN---KSINPDEAVAYGAAV 377
Cdd:cd10170 253 EEIRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
9-356 |
5.29e-37 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.
Pssm-ID: 466829 [Multi-domain] Cd Length: 409 Bit Score: 142.80 E-value: 5.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTE------RLIGDAAKNQVAMNPQNTVF--DAKRLIGRKF 80
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 81 NDPVVQADmKLWPFqvineggkpkvlvsykgenkafypEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQAT 160
Cdd:cd10231 81 FDETTIFG-RRYPF------------------------EDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 161 -------KDAGVIAGLNVLRIINEPTAAAIAYglDKGGQGERHVLIFDLGGGTFDVSILTID----DGIFEVKATAGDtH 229
Cdd:cd10231 136 aqaesrlRDAARRAGFRNVEFQYEPIAAALDY--EQRLDREELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-G 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 230 LGGEDFDNRLVSHFV-----------------------------------------EEFKRKHKKDiSQNKRAVRRLRT- 267
Cdd:cd10231 213 IGGDDFDRELALKKVmphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktLRLLLDLRRD-AADPEKIERLLSl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 268 -----------ACERAKRTLSSSTQANLEIDSLYEGIDfyTSITRARFEELCADLFRGTLEPVEKALRDAKMDKAKIHDI 336
Cdd:cd10231 292 vedqlghrlfrAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420
....*....|....*....|
gi 1159610792 337 VLVGGSTRIPKVQRLLQDYF 356
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLF 389
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
9-376 |
4.39e-21 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 95.42 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVG-VFQH--GKVEIIANDQG------NRTTPSYVAFTDTERLIG---DAAKNQVAMNPQNTV---FDAK 73
Cdd:cd10229 3 VAIDFGTTYSGYAySFITdpGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDEEHqwlYFFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 74 RLIGRKFNDPVVQADMKlwpfQVINEGGKP--KVLvsykgenkAFYPEEISSMVLTKLKETaeafLGHPVTNA----VIT 147
Cdd:cd10229 83 FKMMLLSEKELTRDTKV----KAVNGKSMPalEVF--------AEALRYLKDHALKELRDR----SGSSLDEDdirwVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 148 VPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAIAYGLDKGGQ-------GERhVLIFDLGGGTFDVSILTI 214
Cdd:cd10229 147 VPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKLLAEGeekelkpGDK-YLVVDCGGGTVDITVHEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 215 -DDGIFE--VKATAGdtHLGGEDFDNRLVS--------HFVEEFKRKHKKDISQNKRAVrrlrtacERAKRTlssstqan 283
Cdd:cd10229 226 lEDGKLEelLKASGG--PWGSTSVDEEFEElleeifgdDFMEAFKQKYPSDYLDLLQAF-------ERKKRS-------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 284 leiDSLYegidfytsITRARFEELCADLFRGTLEPVEKALRDAKMDkaKIHDIVLVGGSTRIPKVQRLLQDYFNGRdlNK 363
Cdd:cd10229 289 ---FKLR--------LSPELMKSLFDPVVKKIIEHIKELLEKPELK--GVDYIFLVGGFAESPYLQKAVKEAFSTK--VK 353
|
410
....*....|....*.
gi 1159610792 364 SI---NPDEAVAYGAA 376
Cdd:cd10229 354 IIippEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
9-377 |
1.33e-14 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 75.20 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVgvFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVAMNPQNTVfdakrlIGRKFNDPVV 85
Cdd:cd10225 2 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAVdKNTGKVLavGEEAKKMLGRTPGNIV------AIRPLRDGVI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 86 qADmklwpFQVINeggkpKVLvsykgenKAFypeeISSMVLTKlketaeaFLGHPvtNAVITVPAYFNDSQRQATKDAGV 165
Cdd:cd10225 67 -AD-----FEATE-----AML-------RYF----IRKAHRRR-------GFLRP--RVVIGVPSGITEVERRAVKEAAE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 166 IAGLNVLRIINEPTAAAIAYGLD----KGgqgerhVLIFDLGGGTFDVSILTIdDGIFEVKAtagdTHLGGEDFDNRLVS 241
Cdd:cd10225 116 HAGAREVYLIEEPMAAAIGAGLPieepRG------SMVVDIGGGTTEIAVISL-GGIVTSRS----VRVAGDEMDEAIIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 242 HfveeFKRKHKKDISqnkravrrLRTAcERAKRTLSS--STQANLEIDslYEGIDFYTSITRARfeELCADLFRGTLEP- 318
Cdd:cd10225 185 Y----VRRKYNLLIG--------ERTA-ERIKIEIGSayPLDEELSME--VRGRDLVTGLPRTI--EITSEEVREALEEp 247
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159610792 319 ---VEKALRDAkMDK------AKIHD--IVLVGGSTRIPKVQRLLQDYFngrDLNKSI--NPDEAVAYGAAV 377
Cdd:cd10225 248 vnaIVEAVRST-LERtppelaADIVDrgIVLTGGGALLRGLDELLREET---GLPVHVadDPLTCVAKGAGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
9-376 |
1.76e-11 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 65.92 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYscVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERL--IGDAAKNQVAMNPQNTVfdAKRligrkfndPV- 84
Cdd:PRK13930 11 IGIDLGTAN--TLVYVKGK-GIVLNE------PSVVAIdTKTGKVlaVGEEAKEMLGRTPGNIE--AIR--------PLk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 85 --VQADmklwpFQVIneggkpKVLVSYkgenkaFYpeeisSMVLTKLketaeaFLGHPvtNAVITVPAYFNDSQRQATKD 162
Cdd:PRK13930 72 dgVIAD-----FEAT------EAMLRY------FI-----KKARGRR------FFRKP--RIVICVPSGITEVERRAVRE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 163 AGVIAGLNVLRIINEPTAAAIAYGLD----KGGqgerhvLIFDLGGGTFDVSILTIdDGIfevkATAGDTHLGGEDFDNR 238
Cdd:PRK13930 122 AAEHAGAREVYLIEEPMAAAIGAGLPvtepVGN------MVVDIGGGTTEVAVISL-GGI----VYSESIRVAGDEMDEA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 239 LVSHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQAN----LEIdslyEGIDFYTSITRARfeELCADLFRG 314
Cdd:PRK13930 191 IVQY----VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLDeeesMEV----RGRDLVTGLPKTI--EISSEEVRE 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159610792 315 TLEP--------VEKALRDAKMD-KAKIHD--IVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYGAA 376
Cdd:PRK13930 252 ALAEplqqiveaVKSVLEKTPPElAADIIDrgIVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVARGTG 323
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
9-376 |
2.61e-11 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 65.48 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVAMNPQNTVfdAKRligrkfndPV- 84
Cdd:COG1077 10 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIdKKTGKVLavGEEAKEMLGRTPGNIV--AIR--------PLk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 85 --VQADmklwpFQVIneggkpKVLVSYkgenkafypeeissmVLTKLKEtaEAFLGHPvtNAVITVPAYFNDSQRQATKD 162
Cdd:COG1077 71 dgVIAD-----FEVT------EAMLKY---------------FIKKVHG--RRSFFRP--RVVICVPSGITEVERRAVRD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 163 AGVIAGLNVLRIINEPTAAAIAYGLD----KGgqgerhVLIFDLGGGTFDVSILTIdDGIfeVKATAgdTHLGGEDFDNR 238
Cdd:COG1077 121 AAEQAGAREVYLIEEPMAAAIGAGLPieepTG------NMVVDIGGGTTEVAVISL-GGI--VVSRS--IRVAGDELDEA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 239 LVSHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARF---EELcADLFRGT 315
Cdd:COG1077 190 IIQY----VRKKYNLLIGE--------RTA-EEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTITitsEEI-REALEEP 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159610792 316 LEPVEKALRDAkMDK------AKIHD--IVLVGGSTRIPKVQRLLQDYFNgrdLNKSI--NPDEAVAYGAA 376
Cdd:COG1077 256 LNAIVEAIKSV-LEKtppelaADIVDrgIVLTGGGALLRGLDKLLSEETG---LPVHVaeDPLTCVARGTG 322
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
125-230 |
1.53e-09 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 58.82 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 125 VLTKLKETAEAFLGHPVTNAVITVPAyfNDSQRQATKDAGVI--AGLNVLRIINEPTAAAIAYGLDKGGqgerhvlIFDL 202
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPP--GTGERDARAIRNVLegAGLEVSNVVDEPTAANAVLGIRDGA-------VVDI 118
|
90 100 110
....*....|....*....|....*....|..
gi 1159610792 203 GGGTFDVSIltIDDGifEVKATA----GDTHL 230
Cdd:cd24047 119 GGGTTGIAV--LKDG--KVVYTAdeptGGTHL 146
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
9-375 |
5.94e-09 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 57.95 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVAMNPQNTVfdakrlIGRKFNDPVV 85
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGNEAKKMLGRTPGNIV------AVRPLKDGVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 86 qADMklwpfqvineggkpkvlvsykgenkafypeeissmvltklkETAEAFLGH-----------PVTNAVITVPAYFND 154
Cdd:pfam06723 69 -ADF-----------------------------------------EVTEAMLKYfikkvhgrrsfSKPRVVICVPSGITE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 155 SQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD-KGGQGErhvLIFDLGGGTFDVSILTIdDGIfevkATAGDTHLGGE 233
Cdd:pfam06723 107 VERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPvEEPTGN---MVVDIGGGTTEVAVISL-GGI----VTSKSVRVAGD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 234 DFDNRLVSHfveeFKRKHKKDISQnkravrrlRTAcERAKrtlssstqanLEIDSLYEGIDFYTSITRAR---------- 303
Cdd:pfam06723 179 EFDEAIIKY----IRKKYNLLIGE--------RTA-ERIK----------IEIGSAYPTEEEEKMEIRGRdlvtglpkti 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 304 ------FEELCADLFRGTLEPVEKALRDAKMDKAK-IHD--IVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAVAYG 374
Cdd:pfam06723 236 eisseeVREALKEPVSAIVEAVKEVLEKTPPELAAdIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALG 314
|
.
gi 1159610792 375 A 375
Cdd:pfam06723 315 T 315
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
125-230 |
7.41e-08 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 54.07 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 125 VLTKLKETAEAFLGHPVTNAVITVPAyfndsqrqAT--KDAGVI------AGLNVLRIINEPTAAAIAYGLDKGGqgerh 196
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGIDNGA----- 138
|
90 100 110
....*....|....*....|....*....|....*...
gi 1159610792 197 vlIFDLGGGTFDVSILtiDDGifEVKATA----GDTHL 230
Cdd:PRK15080 139 --VVDIGGGTTGISIL--KDG--KVVYSAdeptGGTHM 170
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
126-359 |
1.94e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 50.35 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 126 LTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAI-AYGLDKggqgerhVL 198
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR-------YI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 199 IFDLGGGTFDVSILTIDD--GIFE--VKATAGDTHLGGED--FDNRLVSHFVEEFKRKHKkdiSQNKRAVRRLRTACERA 272
Cdd:cd11736 198 VADCGGGTVDLTVHQIEQpqGTLKelYKASGGPYGAVGVDlaFEKLLCQIFGEDFIATFK---AKRPAAWVDLTIAFEAR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 273 KRTlssstqANLEIDSlyegidfytsitrarfeELCADLFRGTLEPVEKALRD--AKMDKAKIHDIVLVGGSTRIPKVQR 350
Cdd:cd11736 275 KRT------AALRMSS-----------------EAMNELFQPTISQIIQHIDDlmKKPEVKGIKFLFLVGGFAESPMLQR 331
|
....*....
gi 1159610792 351 LLQDYFNGR 359
Cdd:cd11736 332 AVQAAFGNI 340
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
9-375 |
3.12e-06 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 49.52 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCvgvfqhgkveiIANDQGNR-TTPSYVAFTD---------TERLIGDAA-KNQVAMNpqntvfdakrlig 77
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGYPKdiiarkllgKEVLFGDEAlENRLALD------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 78 rkfndpvvqadMKlWPFQ--VINEGGKpkvlvsykgENKafypeEISSMVLTKLKETAEAFLGHPVTnAVITVPAYFNDS 155
Cdd:cd24009 60 -----------LR-RPLEdgVIKEGDD---------RDL-----EAARELLQHLIELALPGPDDEIY-AVIGVPARASAE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 156 QRQATKDA--GVIAGLnvlRIINEPTAaaIAYGLDKggqgERHVLIFDLGGGTFDV-----SILTIDDGIFEVKAtagdt 228
Cdd:cd24009 113 NKQALLEIarELVDGV---MVVSEPFA--VAYGLDR----LDNSLIVDIGAGTTDLcrmkgTIPTEEDQITLPKA----- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 229 hlgGEDFDNRLvshfVEEFKRKHkKDISQNKRAVRRLR-------TACERAKRTLSsstqanleIDSLYEGIDFyTSITR 301
Cdd:cd24009 179 ---GDYIDEEL----VDLIKERY-PEVQLTLNMARRWKekygfvgDASEPVKVELP--------VDGKPVTYDI-TEELR 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159610792 302 ARFEELCADLFRGTLEPVEKAlrDAKMDKAKIHDIVLVGGSTRI----PKVQRLLQDYFNGRdLNKSINPDEAVAYGA 375
Cdd:cd24009 242 IACESLVPDIVEGIKKLIASF--DPEFQEELRNNIVLAGGGSRIrgldTYIEKALKEYGGGK-VTCVDDPVFAGAEGA 316
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
123-357 |
3.23e-06 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 49.21 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 123 SMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKdagviAGLNVLRIINEPTAAaiAYGLDKGGQGERHVLIFDL 202
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAA--ANLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 203 GGGTFDVSIltIDDGifEVKATaGDTHLGGEDFDNRLVSHFveefkrkhkkDISQNKravrrlrtaCERAKRTLSSST-- 280
Cdd:cd24004 122 GAGTTDIAL--IRNG--GIEAY-RMVPLGGDDFTKAIAEGF----------LISFEE---------AEKIKRTYGIFLli 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159610792 281 QANLEIDSLYEGIDFYTSITRArFEELcadlfrgtLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFN 357
Cdd:cd24004 178 EAKDQLGFTINKKEVYDIIKPV-LEEL--------ASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
145-359 |
6.36e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 48.85 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 145 VITVPAYFNDSQRQATKDAGVIAGLNV------LRIINEPTAAAIAYGLDKGGQGERHVLIfDLGGGTFDVSI--LTIDD 216
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIYCRKLRLHQMDRYVVV-DCGGGTVDLTVhqIRLPE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 217 GIFE--VKATAGDTHLGGEDFD-NRLV-----SHFVEEFKRKHKKdisqnkrAVRRLRTACERAKRTLSSSTQANLEIDS 288
Cdd:cd11735 223 GHLKelYKASGGPYGSLGVDYEfEKLLckifgEDFIDQFKIKRPA-------AWVDLMIAFESRKRAAAPDRTNPLNITL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 289 LYEGIDFYTSITRARFE-------------------ELCAD----LFRGTLEPVEKALRD--AKMDKAKIHDIVLVGGST 343
Cdd:cd11735 296 PFSFIDYYKKFRGHSVEhalrksnvdfvkwssqgmlRMSPDamnaLFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFA 375
|
250
....*....|....*.
gi 1159610792 344 RIPKVQRLLQDYFNGR 359
Cdd:cd11735 376 ESPLLQQAVQNAFGDQ 391
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
115-353 |
7.55e-06 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 48.71 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 115 AFYpEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFN-----DSQRQAT---KDAGVIAGLNVLRIINEPTAAAIAY- 185
Cdd:PRK11678 124 ALF-EDLVCAMMLHIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFe 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 186 -GLDKggqgERHVLIFDLGGGTFDVSILTIddgifevkataGDTH-----------------LGGEDFD-----NRLVSH 242
Cdd:PRK11678 203 aTLTE----EKRVLVVDIGGGTTDCSMLLM-----------GPSWrgradrsasllghsgqrIGGNDLDialafKQLMPL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 243 F-------------------------VEE----FKRKHKKDISQNKR------AVRRL-------------RTAcERAKR 274
Cdd:PRK11678 268 LgmgsetekgialpslpfwnavaindVPAqsdfYSLANGRLLNDLIRdarepeKVARLlkvwrqrlsyrlvRSA-EEAKI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 275 TLSSSTQANLEIDSLYEGIDfyTSITRARFEELCADLFRGTLEPVEKALRDA--KMDKakihdIVLVGGSTRIPKVQRLL 352
Cdd:PRK11678 347 ALSDQAETRASLDFISDGLA--TEISQQGLEEAISQPLARILELVQLALDQAqvKPDV-----IYLTGGSARSPLIRAAL 419
|
.
gi 1159610792 353 Q 353
Cdd:PRK11678 420 A 420
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
309-384 |
1.58e-05 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 47.90 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 309 ADLFRGTLEPVEKALRDAkMD-----KAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSiNPDEAVAYGAAVQAAILM 383
Cdd:COG1070 368 AHLARAVLEGVAFALRDG-LEaleeaGVKIDRIRATGGGARSPLWRQILADVL-GRPVEVP-EAEEGGALGAALLAAVGL 444
|
.
gi 1159610792 384 G 384
Cdd:COG1070 445 G 445
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
145-252 |
2.29e-05 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 46.82 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 145 VITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD----KGGqgerhvLIFDLGGGTFDVSILTIDDGIfe 220
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDisqpSGN------MVVDIGGGTTDIAVLSLGGIV-- 170
|
90 100 110
....*....|....*....|....*....|..
gi 1159610792 221 vkaTAGDTHLGGEDFDNRLVSHfveeFKRKHK 252
Cdd:PRK13928 171 ---TSSSIKVAGDKFDEAIIRY----IRKKYK 195
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
167-374 |
7.86e-05 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 45.21 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYgLDkggQGERH--VLIFDLGGGTFDVSILTidDGIFEvkatagDTH---LGGEDFDNRLVS 241
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LT---EDEKElgVALIDIGGGTTDIAVFK--NGSLR------YTAvipVGGNHITNDIAI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 242 HF------VEEFKRKHKKDISQN--KRAVRRLRTACERAKRTLSSSTqanleidsLYEgidfytsITRARFEELcadlfr 313
Cdd:cd24048 240 GLntpfeeAERLKIKYGSALSEEadEDEIIEIPGVGGREPREVSRRE--------LAE-------IIEARVEEI------ 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159610792 314 gtLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFN-----------GRDLNKSINPDEAVAYG 374
Cdd:cd24048 299 --LELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvrigrpkniGGLPEEVNDPAYATAVG 368
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
9-242 |
2.32e-04 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 43.74 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 9 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAFTDTER---LIGDAAKNQVAMNPQNTVfdakrlIGRKFNDPVV 85
Cdd:PRK13929 7 IGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV------AVRPMKDGVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 86 qADMklwpfqvineggkpkvlvsykgenkafypeEISSMVLTKLKETAEAFLGHPV--TNAVITVPAYFNDSQRQATKDA 163
Cdd:PRK13929 72 -ADY------------------------------DMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAISDA 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159610792 164 GVIAGLNVLRIINEPTAAAIayGLDKGGQGERHVLIFDLGGGTFDVSILTiddgiFEVKATAGDTHLGGEDFDNRLVSH 242
Cdd:PRK13929 121 VKNCGAKNVHLIEEPVAAAI--GADLPVDEPVANVVVDIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSF 192
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
125-389 |
3.51e-04 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins; Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp9 forms a stable heterodimer with Arp7 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.
Pssm-ID: 466814 Cd Length: 356 Bit Score: 43.06 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 125 VLTKLKETAEAFLGHPVtnaVITVPAYFNDSQRQ-ATKDagVIAGLNV--LRIINEPTAAAIAYGLDKGgqgerhvLIFD 201
Cdd:cd10208 57 ILFSLLSIPRPTNNSPV---LLSVPPSWSKSDLElLTQL--FFERLNVpaFAILEAPLAALYAAGATSG-------IVVD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 202 LGGGTFDVSIltIDDGIFEVKATAgDTHLGGEDFDNrlvsHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRtlssSTQ 281
Cdd:cd10208 125 IGHEKTDITP--IVDSQVVPHALV-SIPIGGQDCTA----HLAQLLKSDEPELKSQAESGEEATLDLAEALKK----SPI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 282 ANLEIDS--LYEGIDFytSITRARFEeLCADLFRGTLEPVEKALRDAKMDKAKIH------------DIVLVGGSTRI-- 345
Cdd:cd10208 194 CEVLSDGadLASGTEI--TVGKERFR-ACEPLFKPSSLRVDLLIAAIAGALVLNAsdepdkrpalweNIIIVGGGSRIrg 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 346 ------------------------PKVQRLLQ--DYFNGRdlnKSINPDEAVAYGAAVQAAILMGDKSEK 389
Cdd:cd10208 271 lkeallselqqfhlisetsaspqqPRIIRLAKipDYFPEW---KKSGYEEAAFLGASIVAKLVFNDPSSK 337
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
167-357 |
4.99e-04 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 42.81 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 167 AGLNVLRIINEPTAAAIAYgLDKGgqgERH--VLIFDLGGGTFDVSILTidDGIfeVKATAGDThLGGEDFDNrlvshfv 244
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTED---EKElgVALVDIGGGTTDIAVFK--DGA--LRHTAVIP-VGGDHITN------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 245 eefkrkhkkDISqnkravRRLRT---ACERAKRTLSS------STQANLEIDSLyeGIDFYTSITR--------ARFEEL 307
Cdd:COG0849 238 ---------DIA------IGLRTpleEAERLKIKYGSalaslaDEDETIEVPGI--GGRPPREISRkelaeiieARVEEI 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1159610792 308 cadlfrgtLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFN 357
Cdd:COG0849 301 --------FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
169-257 |
5.40e-04 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 42.12 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 169 LNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTfdVSILTIDDGIFEVKatAGDTHLGGEDFDNRLVSHFVEEFK 248
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENGKPIEE--SSDTLPGGEEALEKYADDILNELL 212
|
....*....
gi 1159610792 249 RKHKKDISQ 257
Cdd:cd10227 213 KKLGDELDS 221
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
145-278 |
5.45e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 42.38 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 145 VITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD----KGgqgerhVLIFDLGGGTFDVSILTIdDGIfe 220
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPvtepTG------SMVVDIGGGTTEVAVISL-GGI-- 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1159610792 221 vkATAGDTHLGGEDFDNRLVSHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSS 278
Cdd:PRK13927 171 --VYSKSVRVGGDKFDEAIINY----VRRNYNLLIGE--------RTA-ERIKIEIGS 213
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
309-384 |
1.66e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 41.37 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 309 ADLFRGTLEPVEKALRDA----KMDKAKIHDIVLVGGSTRIPKVQRLLQDYFnGRDLNKSINPDEAvAYGAAVQAAILMG 384
Cdd:cd07808 365 AHLARAVLEGVAFSLRDSlevlKELGIKVKEIRLIGGGAKSPLWRQILADVL-GVPVVVPAEEEGS-AYGAALLAAVGAG 442
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
144-206 |
3.41e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 38.22 E-value: 3.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159610792 144 AVITVPAYFNDSQRQAT-----------KDAGVIAGLNVLRIINEPTAAAIAYGLDKggqGERHVLIFDLGGGT 206
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTL---GPEGLLVVDLGGGT 86
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
298-380 |
4.17e-03 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 39.84 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159610792 298 SITRARFEELC-ADLFRGTLEPVEKALRDAkMDK-----AKIHDIVLVGGSTRIPKVQRLLQDYFNgrdlnKSI---NPD 368
Cdd:cd07809 354 SLVGLTLSNFTrANLARAALEGATFGLRYG-LDIlrelgVEIDEIRLIGGGSKSPVWRQILADVFG-----VPVvvpETG 427
|
90
....*....|..
gi 1159610792 369 EAVAYGAAVQAA 380
Cdd:cd07809 428 EGGALGAALQAA 439
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
309-381 |
8.08e-03 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers 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: 466801 [Multi-domain] Cd Length: 429 Bit Score: 39.13 E-value: 8.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159610792 309 ADLFRGTLEPVEKALRDA--KMDKA---KIHDIVLVGGSTRIPKVQRLLQDYFnGRDLnkSINPDEAVAYGAAVQAAI 381
Cdd:cd07783 353 AEFLRALLEGIAFIERLGyeRLEELgapPVEEVRTAGGGARNDLWNQIRADVL-GVPV--VIAEEEEAALGAALLAAA 427
|
|
| |
