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Conserved domains on  [gi|2045151781|ref|NP_001381945|]
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heat shock 70 kDa protein 12B [Rattus norvegicus]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
61-528 0e+00

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.


The actual alignment was detected with superfamily member cd11736:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 361  Bit Score: 718.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  61 VVVAIDFGTTSSGYAFSFATDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGIFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd11736     1 VVVAIDFGTTSSGYAFSFSSDPEAIHMMRKWEGGDPGVANQKTPTSLLLTPDGAFHSFGYTARDYYHDLDPEEARDWLYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 141 EKFKMKIHSATDLTLKTQLEAVNGKKMLALEVFAHALRFFKEHALQELREQSECMLEKDAVRWVLTVPAIWKQPAKQFMR 220
Cdd:cd11736    81 EKFKMKIHSTSDLTMETELEAVNGKKVQALEVFAHALRFFKEHALQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 221 EAAYLAGLVSREDAEKLLIALEPEAASVYCRKLrlhqlmdlssrtagggrlgerrsidssfrhareqlrrsrhsrtflve 300
Cdd:cd11736   161 EAAYLAGLVSPENPEQLLIALEPEAASIYCRKL----------------------------------------------- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 301 sgvgelwsemqegDRYMVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIAKFKRQR 380
Cdd:cd11736   194 -------------DRYIVADCGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDLAFEKLLCQIFGEDFIATFKAKR 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 381 PAAWVDLTIAFEARKRTAGphragalnislpfsfidfyrkqrghnvetalrrssvnfvkwssqgmLRMSCEAMNELFQPT 460
Cdd:cd11736   261 PAAWVDLTIAFEARKRTAA----------------------------------------------LRMSSEAMNELFQPT 294
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045151781 461 VSGIIQHIEMLLAKPEVQGVKLLFLVGGFAESAVLQHAVQEALGNRgLRVVVPHDVGLTILKGAVLFG 528
Cdd:cd11736   295 ISQIIQHIDDLMKKPEVKGIKFLFLVGGFAESPMLQRAVQAAFGNI-CRVIIPQDVGLTILKGAVLFG 361
 
Name Accession Description Interval E-value
ASKHA_NBD_HSP70_HSPA12B cd11736
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ...
61-528 0e+00

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: 718.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  61 VVVAIDFGTTSSGYAFSFATDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGIFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd11736     1 VVVAIDFGTTSSGYAFSFSSDPEAIHMMRKWEGGDPGVANQKTPTSLLLTPDGAFHSFGYTARDYYHDLDPEEARDWLYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 141 EKFKMKIHSATDLTLKTQLEAVNGKKMLALEVFAHALRFFKEHALQELREQSECMLEKDAVRWVLTVPAIWKQPAKQFMR 220
Cdd:cd11736    81 EKFKMKIHSTSDLTMETELEAVNGKKVQALEVFAHALRFFKEHALQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 221 EAAYLAGLVSREDAEKLLIALEPEAASVYCRKLrlhqlmdlssrtagggrlgerrsidssfrhareqlrrsrhsrtflve 300
Cdd:cd11736   161 EAAYLAGLVSPENPEQLLIALEPEAASIYCRKL----------------------------------------------- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 301 sgvgelwsemqegDRYMVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIAKFKRQR 380
Cdd:cd11736   194 -------------DRYIVADCGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDLAFEKLLCQIFGEDFIATFKAKR 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 381 PAAWVDLTIAFEARKRTAGphragalnislpfsfidfyrkqrghnvetalrrssvnfvkwssqgmLRMSCEAMNELFQPT 460
Cdd:cd11736   261 PAAWVDLTIAFEARKRTAA----------------------------------------------LRMSSEAMNELFQPT 294
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045151781 461 VSGIIQHIEMLLAKPEVQGVKLLFLVGGFAESAVLQHAVQEALGNRgLRVVVPHDVGLTILKGAVLFG 528
Cdd:cd11736   295 ISQIIQHIDDLMKKPEVKGIKFLFLVGGFAESPMLQRAVQAAFGNI-CRVIIPQDVGLTILKGAVLFG 361
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
62-681 3.88e-14

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 75.24  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  62 VVAIDFGTTSSGYAFsfatdpeaihmmrkWEGGDPGV---AHQK--TPTCLLLTPEGIfHSFGYTARDYYHDlDPEEard 136
Cdd:COG0443     1 AIGIDLGTTNSVVAV--------------VEGGEPQVipnAEGRrtLPSVVAFPKDGE-VLVGEAAKRQAVT-NPGR--- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 137 wlYFEKFKMKIHSAtdltLKTQLEAVNGKKMLALEVFAHALRFFKEHALQELREQSEcmlekDAVrwvLTVPAIWKQPAK 216
Cdd:COG0443    62 --TIRSIKRLLGRS----LFDEATEVGGKRYSPEEISALILRKLKADAEAYLGEPVT-----RAV---ITVPAYFDDAQR 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 217 QFMREAAYLAGLvsredaEKLLIALEPEAASVycrklrlhqlmdlssrtagggrlgerrsidsSFRHAREqlrrsrhsrt 296
Cdd:COG0443   128 QATKDAARIAGL------EVLRLLNEPTAAAL-------------------------------AYGLDKG---------- 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 297 flvesgvgelwsemQEGDRYMVADCGGGTVDLTVHQLEQphGTLKELykASGGpYGAVG---VDLAFEQLLCRIFGEDFI 373
Cdd:COG0443   161 --------------KEEETILVYDLGGGTFDVSILRLGD--GVFEVL--ATGG-DTHLGgddFDQALADYVAPEFGKEEG 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 374 AKFkRQRPAAWVDLTIAFEARKRTAGphRAGALNISLPFSfidfyrkqRGHNVETALRRssvnfvkwssqgmlrmscEAM 453
Cdd:COG0443   222 IDL-RLDPAALQRLREAAEKAKIELS--SADEAEINLPFS--------GGKHLDVELTR------------------AEF 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 454 NELFQPTVSGIIQHIEMLL--AKPEVQGVKLLFLVGGFAESAVLQHAVQEALGNRGLRVVVPHDV---GLTILkGAVLFG 528
Cdd:COG0443   273 EELIAPLVERTLDPVRQALadAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAvalGAAIQ-AGVLAG 351
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 529 QapgVVRVRRSPLTYGVGVLNRFVpghhppEKLLvrdgRRWCTdvferfvaaeqsvaLGEEVRRSYCPARPGQRRVLINL 608
Cdd:COG0443   352 D---VKDLDVTPLSLGIETLGGVF------TKLI----PRNTT--------------IPTAKSQVFSTAADNQTAVEIHV 404
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045151781 609 YCCAAEDARfitdpGVRKCGALSLELEPEGSPENTgtspsRREIRAAMqfgDTE--IKVTAVDVSTNRSVRAAID 681
Cdd:COG0443   405 LQGERELAA-----DNRSLGRFELTGIPPAPRGVP-----QIEVTFDI---DANgiLSVSAKDLGTGKEQSITIK 466
 
Name Accession Description Interval E-value
ASKHA_NBD_HSP70_HSPA12B cd11736
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ...
61-528 0e+00

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: 718.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  61 VVVAIDFGTTSSGYAFSFATDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGIFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd11736     1 VVVAIDFGTTSSGYAFSFSSDPEAIHMMRKWEGGDPGVANQKTPTSLLLTPDGAFHSFGYTARDYYHDLDPEEARDWLYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 141 EKFKMKIHSATDLTLKTQLEAVNGKKMLALEVFAHALRFFKEHALQELREQSECMLEKDAVRWVLTVPAIWKQPAKQFMR 220
Cdd:cd11736    81 EKFKMKIHSTSDLTMETELEAVNGKKVQALEVFAHALRFFKEHALQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 221 EAAYLAGLVSREDAEKLLIALEPEAASVYCRKLrlhqlmdlssrtagggrlgerrsidssfrhareqlrrsrhsrtflve 300
Cdd:cd11736   161 EAAYLAGLVSPENPEQLLIALEPEAASIYCRKL----------------------------------------------- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 301 sgvgelwsemqegDRYMVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIAKFKRQR 380
Cdd:cd11736   194 -------------DRYIVADCGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDLAFEKLLCQIFGEDFIATFKAKR 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 381 PAAWVDLTIAFEARKRTAGphragalnislpfsfidfyrkqrghnvetalrrssvnfvkwssqgmLRMSCEAMNELFQPT 460
Cdd:cd11736   261 PAAWVDLTIAFEARKRTAA----------------------------------------------LRMSSEAMNELFQPT 294
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045151781 461 VSGIIQHIEMLLAKPEVQGVKLLFLVGGFAESAVLQHAVQEALGNRgLRVVVPHDVGLTILKGAVLFG 528
Cdd:cd11736   295 ISQIIQHIDDLMKKPEVKGIKFLFLVGGFAESPMLQRAVQAAFGNI-CRVIIPQDVGLTILKGAVLFG 361
ASKHA_NBD_HSP70_HSPA12A cd11735
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ...
61-528 0e+00

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: 686.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  61 VVVAIDFGTTSSGYAFSFATDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGIFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd11735     1 VVVAIDFGTTSSGYAYSFTKEPECIHVMRRWEGGDPGVSNQKTPTTILLTPERKFHSFGYAARDFYHDLDPNESKQWLYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 141 EKFKMKIHSATDLTLKTQLEAVNGKKMLALEVFAHALRFFKEHALQELREQSECMLEKDAVRWVLTVPAIWKQPAKQFMR 220
Cdd:cd11735    81 EKFKMKLHTTGNLTMETDLTAANGKKVKALEIFAYALQFFKEQALKELSDQAGSEFDNSDVRWVITVPAIWKQPAKQFMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 221 EAAYLAGLVSREDAEKLLIALEPEAASVYCRKLRLHQLmdlssrtagggrlgerrsidssfrhareqlrrsrhsrtflve 300
Cdd:cd11735   161 QAAYKAGLASPENPEQLIIALEPEAASIYCRKLRLHQM------------------------------------------ 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 301 sgvgelwsemqegDRYMVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIAKFKRQR 380
Cdd:cd11735   199 -------------DRYVVVDCGGGTVDLTVHQIRLPEGHLKELYKASGGPYGSLGVDYEFEKLLCKIFGEDFIDQFKIKR 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 381 PAAWVDLTIAFEARKRTAGPHRAGALNISLPFSFIDFYRKQRGHNVETALRRSSVNFVKWSSQGMLRMSCEAMNELFQPT 460
Cdd:cd11735   266 PAAWVDLMIAFESRKRAAAPDRTNPLNITLPFSFIDYYKKFRGHSVEHALRKSNVDFVKWSSQGMLRMSPDAMNALFKPT 345
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045151781 461 VSGIIQHIEMLLAKPEVQGVKLLFLVGGFAESAVLQHAVQEALGNRgLRVVVPHDVGLTILKGAVLFG 528
Cdd:cd11735   346 IDHIIQHLTDLFQKPEVSGVKFLFLVGGFAESPLLQQAVQNAFGDQ-CRVIIPHDVGLTILKGAVLFG 412
ASKHA_NBD_HSP70_HSPA12 cd10229
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ...
61-528 0e+00

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: 526.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  61 VVVAIDFGTTSSGYAFSFATDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGIFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd10229     1 VVVAIDFGTTYSGYAYSFITDPGDIHTMYNWWGAPTGVSSPKTPTCLLLNPDGEFHSFGYEAREKYSDLAEDEEHQWLYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 141 EKFKMKIHSATDLTLKTQLEAVNGKKMLALEVFAHALRFFKEHALQELREQSECMLEKDAVRWVLTVPAIWKQPAKQFMR 220
Cdd:cd10229    81 FKFKMMLLSEKELTRDTKVKAVNGKSMPALEVFAEALRYLKDHALKELRDRSGSSLDEDDIRWVLTVPAIWSDAAKQFMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 221 EAAYLAGLVSREDAEKLLIALEPEAASVYCRKLRLHQLMDlssrtagggrlgerrsidssfrhareqlrrsrhsrtflve 300
Cdd:cd10229   161 EAAVKAGLISEENSEQLIIALEPEAAALYCQKLLAEGEEK---------------------------------------- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 301 sgvgelwsEMQEGDRYMVADCGGGTVDLTVHQLEQPhGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIAKFKRQR 380
Cdd:cd10229   201 --------ELKPGDKYLVVDCGGGTVDITVHEVLED-GKLEELLKASGGPWGSTSVDEEFEELLEEIFGDDFMEAFKQKY 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 381 PAAWVDLTIAFEARKRTAGphragalnislpfsfidfyrkqrghnvetalrrssvnfvkwssqgmLRMSCEAMNELFQPT 460
Cdd:cd10229   272 PSDYLDLLQAFERKKRSFK----------------------------------------------LRLSPELMKSLFDPV 305
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045151781 461 VSGIIQHIEMLLAKPEVQGVKLLFLVGGFAESAVLQHAVQEALGNRGlRVVVPHDVGLTILKGAVLFG 528
Cdd:cd10229   306 VKKIIEHIKELLEKPELKGVDYIFLVGGFAESPYLQKAVKEAFSTKV-KIIIPPEPGLAVVKGAVLFG 372
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
63-526 2.14e-52

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: 183.85  E-value: 2.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  63 VAIDFGTTSSGYAFSFATDPEAIHMMRKWEGGDPGVAHQKTPTcllltpegifhsfgytardyyhdldpeeardwlyfek 142
Cdd:cd10170     1 VGIDFGTTYSGVAYALLGPGEPPLVVLQLPWPGGDGGSSKVPS------------------------------------- 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 143 fkmkihsatdltlktqleavngkkmlALEVFAHALRFFKEHALQELREQSEcMLEKDAVRWVLTVPAIWKQPAKQFMREA 222
Cdd:cd10170    44 --------------------------VLEVVADFLRALLEHAKAELGDRIW-ELEKAPIEVVITVPAGWSDAAREALREA 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 223 AYLAGLVSreDAEKLLIALEPEAASVYCrklrlhqlmdlssrtagggrlgerrsidssfrhareqLRRSRHSRTFlvesg 302
Cdd:cd10170    97 ARAAGFGS--DSDNVRLVSEPEAAALYA-------------------------------------LEDKGDLLPL----- 132
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 303 vgelwsemQEGDRYMVADCGGGTVDLTVHQLEQPHGTL-KELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIaKFKRQRP 381
Cdd:cd10170   133 --------KPGDVVLVCDAGGGTVDLSLYEVTSGSPLLlEEVAPGGGALLGGTDIDEAFEKLLREKLGDKGK-DLGRSDA 203
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 382 AAWVDLTIAFEARKRTagphragalnislpfsfiDFYRKQRGHNVETALRRSSVNfvKWSSQGMLRMSCEAMNELFQPTV 461
Cdd:cd10170   204 DALAKLLREFEEAKKR------------------FSGGEEDERLVPSLLGGGLPE--LGLEKGTLLLTEEEIRDLFDPVI 263
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045151781 462 SGIIQHIEMLLAKPEVQGVKLLFLVGGFAESAVLQHAVQEALGNRGLRVV-VPHDVGLTILKGAVL 526
Cdd:cd10170   264 DKILELIEEQLEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlRSDDPDTAVARGAAL 329
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
62-681 3.88e-14

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 75.24  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  62 VVAIDFGTTSSGYAFsfatdpeaihmmrkWEGGDPGV---AHQK--TPTCLLLTPEGIfHSFGYTARDYYHDlDPEEard 136
Cdd:COG0443     1 AIGIDLGTTNSVVAV--------------VEGGEPQVipnAEGRrtLPSVVAFPKDGE-VLVGEAAKRQAVT-NPGR--- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 137 wlYFEKFKMKIHSAtdltLKTQLEAVNGKKMLALEVFAHALRFFKEHALQELREQSEcmlekDAVrwvLTVPAIWKQPAK 216
Cdd:COG0443    62 --TIRSIKRLLGRS----LFDEATEVGGKRYSPEEISALILRKLKADAEAYLGEPVT-----RAV---ITVPAYFDDAQR 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 217 QFMREAAYLAGLvsredaEKLLIALEPEAASVycrklrlhqlmdlssrtagggrlgerrsidsSFRHAREqlrrsrhsrt 296
Cdd:COG0443   128 QATKDAARIAGL------EVLRLLNEPTAAAL-------------------------------AYGLDKG---------- 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 297 flvesgvgelwsemQEGDRYMVADCGGGTVDLTVHQLEQphGTLKELykASGGpYGAVG---VDLAFEQLLCRIFGEDFI 373
Cdd:COG0443   161 --------------KEEETILVYDLGGGTFDVSILRLGD--GVFEVL--ATGG-DTHLGgddFDQALADYVAPEFGKEEG 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 374 AKFkRQRPAAWVDLTIAFEARKRTAGphRAGALNISLPFSfidfyrkqRGHNVETALRRssvnfvkwssqgmlrmscEAM 453
Cdd:COG0443   222 IDL-RLDPAALQRLREAAEKAKIELS--SADEAEINLPFS--------GGKHLDVELTR------------------AEF 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 454 NELFQPTVSGIIQHIEMLL--AKPEVQGVKLLFLVGGFAESAVLQHAVQEALGNRGLRVVVPHDV---GLTILkGAVLFG 528
Cdd:COG0443   273 EELIAPLVERTLDPVRQALadAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAvalGAAIQ-AGVLAG 351
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 529 QapgVVRVRRSPLTYGVGVLNRFVpghhppEKLLvrdgRRWCTdvferfvaaeqsvaLGEEVRRSYCPARPGQRRVLINL 608
Cdd:COG0443   352 D---VKDLDVTPLSLGIETLGGVF------TKLI----PRNTT--------------IPTAKSQVFSTAADNQTAVEIHV 404
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045151781 609 YCCAAEDARfitdpGVRKCGALSLELEPEGSPENTgtspsRREIRAAMqfgDTE--IKVTAVDVSTNRSVRAAID 681
Cdd:COG0443   405 LQGERELAA-----DNRSLGRFELTGIPPAPRGVP-----QIEVTFDI---DANgiLSVSAKDLGTGKEQSITIK 466
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
63-528 4.74e-13

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: 71.07  E-value: 4.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781  63 VAIDFGTTSSGYAFSFATDPEAIhmMRKWEGGDPgvahqkTPTCLLLTPEGIFHsFGYTARDYYhDLDPEEARDWlyfek 142
Cdd:cd24029     1 VGIDLGTTNSAVAYWDGNGAEVI--IENSEGKRT------TPSVVYFDKDGEVL-VGEEAKNQA-LLDPENTIYS----- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 143 FKMKIHSATdltlkTQLEAVNGKKMLALEVFAHALRFFKEHALQELREQsecmlEKDAVrwvLTVPAIWKQPAKQFMREA 222
Cdd:cd24029    66 VKRLMGRDT-----KDKEEIGGKEYTPEEISAEILKKLKEDAEEQLGGE-----VKGAV---ITVPAYFNDKQRKATKKA 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 223 AYLAGLvsredaEKLLIALEPEAASVYCrklrlhqlmdlssrtagggrlgerrsidssfrhareqlrrsrhsrtflvesg 302
Cdd:cd24029   133 AELAGL------NVLRLINEPTAAALAY---------------------------------------------------- 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 303 vgeLWSEMQEGDRYMVADCGGGTVDLTVhqLEQPHGTLKELykASGG-PY-GAVGVDLAFEQLLCRIFGEDFIAKFKRQR 380
Cdd:cd24029   155 ---GLDKEGKDGTILVYDLGGGTFDVSI--LEIENGKFEVL--ATGGdNFlGGDDFDEAIAELILEKIGIETGILDDKED 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 381 PAAWVDLTIAFEARKrtagphragalnISLpfsfidFYRKQrghnvetalRRSSVNFVKWSSQGMLRMSCEAMNELFQPT 460
Cdd:cd24029   228 ERARARLREAAEEAK------------IEL------SSSDS---------TDILILDDGKGGELEIEITREEFEELIAPL 280
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151781 461 VSGIIQHIEMLLAKPEVQGVKL--LFLVGGFAESAVLQHAVQEALGNRGLRvvvPHDVGLTILKGAVLFG 528
Cdd:cd24029   281 IERTIDLLEKALKDAKLSPEDIdrVLLVGGSSRIPLVREMLEEYFGREPIS---SVDPDEAVAKGAAIYA 347
ASKHA_NBD_HSP70_HscA cd10236
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ...
185-248 1.75e-03

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: 41.05  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045151781 185 LQELREQSECMLEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvsredaEKLLIALEPEAASV 248
Cdd:cd10236   118 LKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAGL------NVLRLLNEPTAAAL 175
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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