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Conserved domains on  [gi|309747075|ref|NP_001184256|]
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heat shock 70 kDa protein 12B isoform 2 [Homo sapiens]

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 ...
61-527 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: 729.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  61 VVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd11736    1 VVVAIDFGTTSSGYAFSFSSDPEAIHMMRKWEGGDPGVANQKTPTSLLLTPDGAFHSFGYTARDYYHDLDPEEARDWLYF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 141 EKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQ-LREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMR 219
Cdd:cd11736   81 EKFKMKIHSTSDLTMETELEAVNGKKVQALEVFAHALRFFKEHALQeLKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 220 EAAYLAGLVSRENAEQLLIALEPEAASVYCRKLrlhqlldlsgrapgggrlgerrsidssfrqareqlrrsrhsrtflve 299
Cdd:cd11736  161 EAAYLAGLVSPENPEQLLIALEPEAASIYCRKL----------------------------------------------- 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 300 sgvgelwaemqagDRYVVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQR 379
Cdd:cd11736  194 -------------DRYIVADCGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDLAFEKLLCQIFGEDFIATFKAKR 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 380 PAAWVDLTIAFEARKRTAGphragalnislpfsfidfyrkqrghnvetalrrssvnfvkwssqgmLRMSCEAMNELFQPT 459
Cdd:cd11736  261 PAAWVDLTIAFEARKRTAA----------------------------------------------LRMSSEAMNELFQPT 294
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309747075 460 VSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARgLRVVVPHDVGLTILKGAVLFG 527
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 ...
61-527 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: 729.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  61 VVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd11736    1 VVVAIDFGTTSSGYAFSFSSDPEAIHMMRKWEGGDPGVANQKTPTSLLLTPDGAFHSFGYTARDYYHDLDPEEARDWLYF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 141 EKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQ-LREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMR 219
Cdd:cd11736   81 EKFKMKIHSTSDLTMETELEAVNGKKVQALEVFAHALRFFKEHALQeLKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 220 EAAYLAGLVSRENAEQLLIALEPEAASVYCRKLrlhqlldlsgrapgggrlgerrsidssfrqareqlrrsrhsrtflve 299
Cdd:cd11736  161 EAAYLAGLVSPENPEQLLIALEPEAASIYCRKL----------------------------------------------- 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 300 sgvgelwaemqagDRYVVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQR 379
Cdd:cd11736  194 -------------DRYIVADCGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDLAFEKLLCQIFGEDFIATFKAKR 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 380 PAAWVDLTIAFEARKRTAGphragalnislpfsfidfyrkqrghnvetalrrssvnfvkwssqgmLRMSCEAMNELFQPT 459
Cdd:cd11736  261 PAAWVDLTIAFEARKRTAA----------------------------------------------LRMSSEAMNELFQPT 294
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309747075 460 VSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARgLRVVVPHDVGLTILKGAVLFG 527
Cdd:cd11736  295 ISQIIQHIDDLMKKPEVKGIKFLFLVGGFAESPMLQRAVQAAFGNI-CRVIIPQDVGLTILKGAVLFG 361
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
62-681 1.78e-14

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 76.40  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  62 VVAIDFGTTSSGYAFSFASDPEAIhmmrKWEGGDPGvahqkTPTCLLLTPEGAfHSFGYTARDYYHDlDPEEardwlYFE 141
Cdd:COG0443    1 AIGIDLGTTNSVVAVVEGGEPQVI----PNAEGRRT-----LPSVVAFPKDGE-VLVGEAAKRQAVT-NPGR-----TIR 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 142 KFKMKIHSAtdltLKTQLEAVNGKTMPALEVFAHALRFFREHAlqlrEQSpsLPEKDTvRWVLTVPAIWKQPAKQFMREA 221
Cdd:COG0443   65 SIKRLLGRS----LFDEATEVGGKRYSPEEISALILRKLKADA----EAY--LGEPVT-RAVITVPAYFDDAQRQATKDA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 222 AYLAGLvsrenaEQLLIALEPEAASVycrklrlhqlldlsgrapgggrlgerrsidsSFRQAREqlrrsrhsrtflvesg 301
Cdd:COG0443  134 ARIAGL------EVLRLLNEPTAAAL-------------------------------AYGLDKG---------------- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 302 vgelwaemQAGDRYVVADCGGGTVDLTVHQLEQphGTLKELykASGGpYGAVG---VDLAFEQLLCRIFGEDFIATFkRQ 378
Cdd:COG0443  161 --------KEEETILVYDLGGGTFDVSILRLGD--GVFEVL--ATGG-DTHLGgddFDQALADYVAPEFGKEEGIDL-RL 226
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 379 RPAAWVDLTIAFEARKRTAGphRAGALNISLPFSfidfyrkqRGHNVETALRRssvnfvkwssqgmlrmscEAMNELFQP 458
Cdd:COG0443  227 DPAALQRLREAAEKAKIELS--SADEAEINLPFS--------GGKHLDVELTR------------------AEFEELIAP 278
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 459 TVSGIIQHIEALL--ARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARGLRVVVPHDV---GLTILkGAVLFGQapgVV 533
Cdd:COG0443  279 LVERTLDPVRQALadAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAvalGAAIQ-AGVLAGD---VK 354
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 534 RVRRSPLTYGVGVLNRFVpgrhppEKLLvrdgRRWCTdvferfvaaeqsvaLGEEVRRSYCPARPGQRRVLINLYCCAAE 613
Cdd:COG0443  355 DLDVTPLSLGIETLGGVF------TKLI----PRNTT--------------IPTAKSQVFSTAADNQTAVEIHVLQGERE 410
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309747075 614 DARfitdpGVRKCGALSLELEPAdcgqdtagAPPGRREIRAAMQFGDTEI-KVTAVDVSTNRSVRASID 681
Cdd:COG0443  411 LAA-----DNRSLGRFELTGIPP--------APRGVPQIEVTFDIDANGIlSVSAKDLGTGKEQSITIK 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 ...
61-527 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: 729.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  61 VVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd11736    1 VVVAIDFGTTSSGYAFSFSSDPEAIHMMRKWEGGDPGVANQKTPTSLLLTPDGAFHSFGYTARDYYHDLDPEEARDWLYF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 141 EKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQ-LREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMR 219
Cdd:cd11736   81 EKFKMKIHSTSDLTMETELEAVNGKKVQALEVFAHALRFFKEHALQeLKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 220 EAAYLAGLVSRENAEQLLIALEPEAASVYCRKLrlhqlldlsgrapgggrlgerrsidssfrqareqlrrsrhsrtflve 299
Cdd:cd11736  161 EAAYLAGLVSPENPEQLLIALEPEAASIYCRKL----------------------------------------------- 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 300 sgvgelwaemqagDRYVVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQR 379
Cdd:cd11736  194 -------------DRYIVADCGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDLAFEKLLCQIFGEDFIATFKAKR 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 380 PAAWVDLTIAFEARKRTAGphragalnislpfsfidfyrkqrghnvetalrrssvnfvkwssqgmLRMSCEAMNELFQPT 459
Cdd:cd11736  261 PAAWVDLTIAFEARKRTAA----------------------------------------------LRMSSEAMNELFQPT 294
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309747075 460 VSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARgLRVVVPHDVGLTILKGAVLFG 527
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 ...
61-527 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: 682.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  61 VVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd11735    1 VVVAIDFGTTSSGYAYSFTKEPECIHVMRRWEGGDPGVSNQKTPTTILLTPERKFHSFGYAARDFYHDLDPNESKQWLYF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 141 EKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQ-LREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMR 219
Cdd:cd11735   81 EKFKMKLHTTGNLTMETDLTAANGKKVKALEIFAYALQFFKEQALKeLSDQAGSEFDNSDVRWVITVPAIWKQPAKQFMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 220 EAAYLAGLVSRENAEQLLIALEPEAASVYCRKLRLHQLldlsgrapgggrlgerrsidssfrqareqlrrsrhsrtflve 299
Cdd:cd11735  161 QAAYKAGLASPENPEQLIIALEPEAASIYCRKLRLHQM------------------------------------------ 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 300 sgvgelwaemqagDRYVVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQR 379
Cdd:cd11735  199 -------------DRYVVVDCGGGTVDLTVHQIRLPEGHLKELYKASGGPYGSLGVDYEFEKLLCKIFGEDFIDQFKIKR 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 380 PAAWVDLTIAFEARKRTAGPHRAGALNISLPFSFIDFYRKQRGHNVETALRRSSVNFVKWSSQGMLRMSCEAMNELFQPT 459
Cdd:cd11735  266 PAAWVDLMIAFESRKRAAAPDRTNPLNITLPFSFIDYYKKFRGHSVEHALRKSNVDFVKWSSQGMLRMSPDAMNALFKPT 345
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309747075 460 VSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARgLRVVVPHDVGLTILKGAVLFG 527
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 ...
61-527 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: 521.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  61 VVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYF 140
Cdd:cd10229    1 VVVAIDFGTTYSGYAYSFITDPGDIHTMYNWWGAPTGVSSPKTPTCLLLNPDGEFHSFGYEAREKYSDLAEDEEHQWLYF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 141 EKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQ-LREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMR 219
Cdd:cd10229   81 FKFKMMLLSEKELTRDTKVKAVNGKSMPALEVFAEALRYLKDHALKeLRDRSGSSLDEDDIRWVLTVPAIWSDAAKQFMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 220 EAAYLAGLVSRENAEQLLIALEPEAASVYCRKLRLHQlldlsgrapgggrlgerrsidssfrqareqlrrsrhsrtflve 299
Cdd:cd10229  161 EAAVKAGLISEENSEQLIIALEPEAAALYCQKLLAEG------------------------------------------- 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 300 sgvgeLWAEMQAGDRYVVADCGGGTVDLTVHQLEQPhGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQR 379
Cdd:cd10229  198 -----EEKELKPGDKYLVVDCGGGTVDITVHEVLED-GKLEELLKASGGPWGSTSVDEEFEELLEEIFGDDFMEAFKQKY 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 380 PAAWVDLTIAFEARKRTAGphragalnislpfsfidfyrkqrghnvetalrrssvnfvkwssqgmLRMSCEAMNELFQPT 459
Cdd:cd10229  272 PSDYLDLLQAFERKKRSFK----------------------------------------------LRLSPELMKSLFDPV 305
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309747075 460 VSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARGlRVVVPHDVGLTILKGAVLFG 527
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 ...
63-525 6.66e-51

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: 179.99  E-value: 6.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  63 VAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTcllltpegafhsfgytardyyhdldpeeardwlyfek 142
Cdd:cd10170    1 VGIDFGTTYSGVAYALLGPGEPPLVVLQLPWPGGDGGSSKVPS------------------------------------- 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 143 fkmkihsatdltlktqleavngktmpALEVFAHALRFFREHALQLREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMREAA 222
Cdd:cd10170   44 --------------------------VLEVVADFLRALLEHAKAELGDRIWELEKAPIEVVITVPAGWSDAAREALREAA 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 223 YLAGLVSreNAEQLLIALEPEAASVYCrklrlhqlldlsgrapgggrlgerrsidssfrqareqLRRSRHSRTFlvesgv 302
Cdd:cd10170   98 RAAGFGS--DSDNVRLVSEPEAAALYA-------------------------------------LEDKGDLLPL------ 132
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 303 gelwaemQAGDRYVVADCGGGTVDLTVHQLEQPHGTL-KELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIaTFKRQRPA 381
Cdd:cd10170  133 -------KPGDVVLVCDAGGGTVDLSLYEVTSGSPLLlEEVAPGGGALLGGTDIDEAFEKLLREKLGDKGK-DLGRSDAD 204
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 382 AWVDLTIAFEARKRTagphragalnislpfsfiDFYRKQRGHNVETALRRSSVNfvKWSSQGMLRMSCEAMNELFQPTVS 461
Cdd:cd10170  205 ALAKLLREFEEAKKR------------------FSGGEEDERLVPSLLGGGLPE--LGLEKGTLLLTEEEIRDLFDPVID 264
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309747075 462 GIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARGLRVV-VPHDVGLTILKGAVL 525
Cdd:cd10170  265 KILELIEEQLEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlRSDDPDTAVARGAAL 329
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
62-681 1.78e-14

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 76.40  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  62 VVAIDFGTTSSGYAFSFASDPEAIhmmrKWEGGDPGvahqkTPTCLLLTPEGAfHSFGYTARDYYHDlDPEEardwlYFE 141
Cdd:COG0443    1 AIGIDLGTTNSVVAVVEGGEPQVI----PNAEGRRT-----LPSVVAFPKDGE-VLVGEAAKRQAVT-NPGR-----TIR 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 142 KFKMKIHSAtdltLKTQLEAVNGKTMPALEVFAHALRFFREHAlqlrEQSpsLPEKDTvRWVLTVPAIWKQPAKQFMREA 221
Cdd:COG0443   65 SIKRLLGRS----LFDEATEVGGKRYSPEEISALILRKLKADA----EAY--LGEPVT-RAVITVPAYFDDAQRQATKDA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 222 AYLAGLvsrenaEQLLIALEPEAASVycrklrlhqlldlsgrapgggrlgerrsidsSFRQAREqlrrsrhsrtflvesg 301
Cdd:COG0443  134 ARIAGL------EVLRLLNEPTAAAL-------------------------------AYGLDKG---------------- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 302 vgelwaemQAGDRYVVADCGGGTVDLTVHQLEQphGTLKELykASGGpYGAVG---VDLAFEQLLCRIFGEDFIATFkRQ 378
Cdd:COG0443  161 --------KEEETILVYDLGGGTFDVSILRLGD--GVFEVL--ATGG-DTHLGgddFDQALADYVAPEFGKEEGIDL-RL 226
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 379 RPAAWVDLTIAFEARKRTAGphRAGALNISLPFSfidfyrkqRGHNVETALRRssvnfvkwssqgmlrmscEAMNELFQP 458
Cdd:COG0443  227 DPAALQRLREAAEKAKIELS--SADEAEINLPFS--------GGKHLDVELTR------------------AEFEELIAP 278
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 459 TVSGIIQHIEALL--ARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARGLRVVVPHDV---GLTILkGAVLFGQapgVV 533
Cdd:COG0443  279 LVERTLDPVRQALadAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAvalGAAIQ-AGVLAGD---VK 354
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 534 RVRRSPLTYGVGVLNRFVpgrhppEKLLvrdgRRWCTdvferfvaaeqsvaLGEEVRRSYCPARPGQRRVLINLYCCAAE 613
Cdd:COG0443  355 DLDVTPLSLGIETLGGVF------TKLI----PRNTT--------------IPTAKSQVFSTAADNQTAVEIHVLQGERE 410
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309747075 614 DARfitdpGVRKCGALSLELEPAdcgqdtagAPPGRREIRAAMQFGDTEI-KVTAVDVSTNRSVRASID 681
Cdd:COG0443  411 LAA-----DNRSLGRFELTGIPP--------APRGVPQIEVTFDIDANGIlSVSAKDLGTGKEQSITIK 466
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
63-394 1.01e-08

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: 57.59  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075  63 VAIDFGTTSSGYAFSFASDPEAIhmMRKWEGGDPgvahqkTPTCLLLTPEGAFHsFGYTARDYYhDLDPEEARDWlyfek 142
Cdd:cd24029    1 VGIDLGTTNSAVAYWDGNGAEVI--IENSEGKRT------TPSVVYFDKDGEVL-VGEEAKNQA-LLDPENTIYS----- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 143 FKMKIHSATdltlkTQLEAVNGKTMPALEVFAHALRFFREHAlqlREQSPSlPEKDTVrwvLTVPAIWKQPAKQFMREAA 222
Cdd:cd24029   66 VKRLMGRDT-----KDKEEIGGKEYTPEEISAEILKKLKEDA---EEQLGG-EVKGAV---ITVPAYFNDKQRKATKKAA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 223 YLAGLvsrenaEQLLIALEPEAASVYCrklrlhqlldlsgrapgggrlgerrSIDSSFRqareqlrrsrhsrtflvesgv 302
Cdd:cd24029  134 ELAGL------NVLRLINEPTAAALAY-------------------------GLDKEGK--------------------- 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747075 303 gelwaemqaGDRYVVADCGGGTVDLTVhqLEQPHGTLKELykASGG-PY-GAVGVDLAFEQLLCRIFGEDFIATFKRQRP 380
Cdd:cd24029  162 ---------DGTILVYDLGGGTFDVSI--LEIENGKFEVL--ATGGdNFlGGDDFDEAIAELILEKIGIETGILDDKEDE 228
                        330
                 ....*....|....
gi 309747075 381 AAWVDLTIAFEARK 394
Cdd:cd24029  229 RARARLREAAEEAK 242
 
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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