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Conserved domains on  [gi|2323918809|ref|XP_051333388|]
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uncharacterized protein NEMIN01_1486 [Nematocida minor]

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 ...
 3-357 6.54e-15

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 cd10230:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 353  Bit Score: 76.77  E-value: 6.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809   3 ILSIDLGS-YKTVVASSDTSAGEIILTKTGSRSTKMAIDYRNKIREFGNvnvtckerekvaedirkeiEELAEQMKNrga 81
Cdd:cd10230     2 VLGIDLGSeFIKVALVKPGVPFEIVLNEESKRKTPSAVAFRNGERLFGD-------------------DALALATRF--- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809  82 ervkimPtSHVYGLLNNLINnYT----------QAKGISSNELEIE-----IVVPSTYTQLHKNIL--------IKILNL 138
Cdd:cd10230    60 ------P-ENTFSYLKDLLG-YSveelvamileYAKSLAESFAGEPikdavITVPPFFTQAQRQALldaaeiagLNVLSL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 139 INpkvqvecitDSMALSSYY-LSRR-TPSSYRMVAFVDIGDAKTTATLAVI-----KDTNINV-INRVTVEA-------G 203
Cdd:cd10230   132 IN---------DNTAAALNYgIDRRfENNEPQNVLFYDMGASSTSATVVEFssvkeKDKGKNKtVPQVEVLGvgwdrtlG 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 204 GRNIT----NHLLEKIYS--GLDKSIPDL---FSK--KEfrVRNIKKIewikgaifgLpSVSTQVDAS----YD----KS 264
Cdd:cd10230   203 GLEFDlrlaDHLADEFNEkhKKDKDVRTNpraMAKllKE--ANRVKEV---------L-SANTEAPASieslYDdidfRT 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 265 VgvcITKADIEEVL-DEFSELKKSLslihkemndESVLERYNLnSEEDIEQeLQITGGSSRM-FIFEDLVHSIFQLKPEV 342
Cdd:cd10230   271 K---ITREEFEELCaDLFERVVAPI---------EEALEKAGL-TLDDIDS-VELIGGGTRVpKVQEALKEALGRKELGK 336

                         410
                  ....*....|....*
gi 2323918809 343 HLNADESIALGGVYR 357
Cdd:cd10230   337 HLNADEAAALGAAFY 351
 
Name Accession Description Interval E-value
ASKHA_NBD_HSP70_HYOU1 cd10230
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ...
 3-357 6.54e-15

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: 76.77  E-value: 6.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809   3 ILSIDLGS-YKTVVASSDTSAGEIILTKTGSRSTKMAIDYRNKIREFGNvnvtckerekvaedirkeiEELAEQMKNrga 81
Cdd:cd10230     2 VLGIDLGSeFIKVALVKPGVPFEIVLNEESKRKTPSAVAFRNGERLFGD-------------------DALALATRF--- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809  82 ervkimPtSHVYGLLNNLINnYT----------QAKGISSNELEIE-----IVVPSTYTQLHKNIL--------IKILNL 138
Cdd:cd10230    60 ------P-ENTFSYLKDLLG-YSveelvamileYAKSLAESFAGEPikdavITVPPFFTQAQRQALldaaeiagLNVLSL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 139 INpkvqvecitDSMALSSYY-LSRR-TPSSYRMVAFVDIGDAKTTATLAVI-----KDTNINV-INRVTVEA-------G 203
Cdd:cd10230   132 IN---------DNTAAALNYgIDRRfENNEPQNVLFYDMGASSTSATVVEFssvkeKDKGKNKtVPQVEVLGvgwdrtlG 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 204 GRNIT----NHLLEKIYS--GLDKSIPDL---FSK--KEfrVRNIKKIewikgaifgLpSVSTQVDAS----YD----KS 264
Cdd:cd10230   203 GLEFDlrlaDHLADEFNEkhKKDKDVRTNpraMAKllKE--ANRVKEV---------L-SANTEAPASieslYDdidfRT 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 265 VgvcITKADIEEVL-DEFSELKKSLslihkemndESVLERYNLnSEEDIEQeLQITGGSSRM-FIFEDLVHSIFQLKPEV 342
Cdd:cd10230   271 K---ITREEFEELCaDLFERVVAPI---------EEALEKAGL-TLDDIDS-VELIGGGTRVpKVQEALKEALGRKELGK 336

                         410
                  ....*....|....*
gi 2323918809 343 HLNADESIALGGVYR 357
Cdd:cd10230   337 HLNADEAAALGAAFY 351
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 251-353 6.75e-05

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 45.97  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 251 PSVSTQVDASYDKSVGVCITKADIEEVLDEFseLKKSLSLIHKemndesVLERYNLnSEEDIeQELQITGGSSRMFIFED 330
Cdd:COG0443   249 DEAEINLPFSGGKHLDVELTRAEFEELIAPL--VERTLDPVRQ------ALADAGL-SPSDI-DAVLLVGGSTRMPAVRE 318

                          90       100
                  ....*....|....*....|...
gi 2323918809 331 LVHSIFQLKPEVHLNADESIALG 353
Cdd:COG0443   319 RVKELFGKEPLKGVDPDEAVALG 341
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 168-353 8.71e-04

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: 42.63  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 168 RMVAFVDIGDAKTTATLAVIKDTNINVINrvT---VEAGGRN----ITNHLLE--KIYSGLDksipdlFSKKEFRVRNIK 238
Cdd:pfam00012 186 RNIAVYDLGGGTFDVSILEIGRGVFEVKA--TngdTHLGGEDfdlrLVDHLAEefKKKYGID------LSKDKRALQRLR 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 239 ------KIEwikgaifgLPSVSTQVDASY------DKSVGVCITKADIEEVLDEFseLKKSLSLIHKEMNDESVlerynl 306
Cdd:pfam00012 258 eaaekaKIE--------LSSNQTNINLPFitamadGKDVSGTLTRAKFEELVADL--FERTLEPVEKALKDAGL------ 321

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2323918809 307 nSEEDIEqELQITGGSSRMFIFEDLVHSIFQLKPEVHLNADESIALG 353
Cdd:pfam00012 322 -SKSEID-EVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIG 366
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
 250-353 1.15e-03

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 42.12  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 250 LPSVSTqvDASYDKSVGVCITKADIEEVLDEFseLKKSLSLIHKEMNDESVlerynlnSEEDIeQELQITGGSSRMFIFE 329
Cdd:PTZ00400  317 LPFITA--DQSGPKHLQIKLSRAKLEELTHDL--LKKTIEPCEKCIKDAGV-------KKDEL-NDVILVGGMTRMPKVS 384

                          90       100
                  ....*....|....*....|....
gi 2323918809 330 DLVHSIFQLKPEVHLNADESIALG 353
Cdd:PTZ00400  385 ETVKKIFGKEPSKGVNPDEAVAMG 408
 
Name Accession Description Interval E-value
ASKHA_NBD_HSP70_HYOU1 cd10230
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ...
 3-357 6.54e-15

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: 76.77  E-value: 6.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809   3 ILSIDLGS-YKTVVASSDTSAGEIILTKTGSRSTKMAIDYRNKIREFGNvnvtckerekvaedirkeiEELAEQMKNrga 81
Cdd:cd10230     2 VLGIDLGSeFIKVALVKPGVPFEIVLNEESKRKTPSAVAFRNGERLFGD-------------------DALALATRF--- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809  82 ervkimPtSHVYGLLNNLINnYT----------QAKGISSNELEIE-----IVVPSTYTQLHKNIL--------IKILNL 138
Cdd:cd10230    60 ------P-ENTFSYLKDLLG-YSveelvamileYAKSLAESFAGEPikdavITVPPFFTQAQRQALldaaeiagLNVLSL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 139 INpkvqvecitDSMALSSYY-LSRR-TPSSYRMVAFVDIGDAKTTATLAVI-----KDTNINV-INRVTVEA-------G 203
Cdd:cd10230   132 IN---------DNTAAALNYgIDRRfENNEPQNVLFYDMGASSTSATVVEFssvkeKDKGKNKtVPQVEVLGvgwdrtlG 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 204 GRNIT----NHLLEKIYS--GLDKSIPDL---FSK--KEfrVRNIKKIewikgaifgLpSVSTQVDAS----YD----KS 264
Cdd:cd10230   203 GLEFDlrlaDHLADEFNEkhKKDKDVRTNpraMAKllKE--ANRVKEV---------L-SANTEAPASieslYDdidfRT 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 265 VgvcITKADIEEVL-DEFSELKKSLslihkemndESVLERYNLnSEEDIEQeLQITGGSSRM-FIFEDLVHSIFQLKPEV 342
Cdd:cd10230   271 K---ITREEFEELCaDLFERVVAPI---------EEALEKAGL-TLDDIDS-VELIGGGTRVpKVQEALKEALGRKELGK 336

                         410
                  ....*....|....*
gi 2323918809 343 HLNADESIALGGVYR 357
Cdd:cd10230   337 HLNADEAAALGAAFY 351
ASKHA_NBD_HSP70_HSP105-110-like cd11732
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ...
 6-353 4.32e-11

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: 65.27  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809   6 IDLGSYKTVVASSDTSAGEIILTKTGSRST-------------------KMAIDYRNKIREFGNV---NVTCKEREKVAE 63
Cdd:cd11732     3 IDFGNQNSVVAAARRGGIDIVLNEVSNRKTptlvgftekerligeaaksQQKSNYKNTIRNFKRLiglKFDDPEVQKEIK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809  64 DIRKEIEELAE-------QMKNrgaERVKIMPTSHVYGLLNNLINNYTQAKGISSNEleIEIVVPSTYTQLHKNIL---- 132
Cdd:cd11732    83 LLPFKLVELEDgkvgievSYNG---EEVVFSPEQVLAMLLGKLKEIAEAANKGEVKD--CVISVPGYYTDAQRRALldaa 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 133 ----IKILNLINPkvqveciTDSMALSsYYLSRR----TPSSYRMVAFVDIGDAKTTATLAVIKDTNINVINRVTVEA-G 203
Cdd:cd11732   158 eiagLNCLRLINE-------TTAAALD-YGIYKSdlleSEEKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNlG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 204 GRN----ITNHLLEKIysgLDKSIPDLFSKKEFRVRNIKKIEWIKGAIFGLPSVSTQVDASY-DKSVGVCITkadieevL 278
Cdd:cd11732   230 GRDfdraLVEHFAEEF---KKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMeDIDFSGQIK-------R 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 279 DEFSELKKSL-----SLIhkemndESVLERYNLNSEE--DIEqelqITGGSSRMFIFEDLVHSIFQLKPEVHLNADESIA 351
Cdd:cd11732   300 EEFEELIQPLlarleAPI------KKALAQAGLTKEDlhSVE----IVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVA 369


                  ..
gi 2323918809 352 LG 353
Cdd:cd11732   370 RG 371
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 100-356 2.16e-07

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: 53.26  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 100 INNYTQAKGISSNELEIEIV--VPSTYTQLHKNILIKILN---LINPKVQVECITDSMALSSYYLSRRTPSSY----RMV 170
Cdd:cd10170    59 AKAELGDRIWELEKAPIEVVitVPAGWSDAAREALREAARaagFGSDSDNVRLVSEPEAAALYALEDKGDLLPlkpgDVV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 171 AFVDIGDAKTTATLAVIKDTNINVINRVTV----EAGGRNIT----NHLLEKI---YSGLDKSIPDLFS--KKEFRvRNI 237
Cdd:cd10170   139 LVCDAGGGTVDLSLYEVTSGSPLLLEEVAPgggaLLGGTDIDeafeKLLREKLgdkGKDLGRSDADALAklLREFE-EAK 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 238 KKIEWIKGAIFGLPSVSTQVDASYDKSVG-VCITKADIEEVLDEFseLKKSLSLIHKEMNDESVlerynlnseEDIeQEL 316
Cdd:cd10170   218 KRFSGGEEDERLVPSLLGGGLPELGLEKGtLLLTEEEIRDLFDPV--IDKILELIEEQLEAKSG---------TPP-DAV 285

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2323918809 317 QITGGSSRMFIFEDLVHSIFQLKPEVHL----NADESIALGGVY 356
Cdd:cd10170   286 VLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARGAAL 329
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
 153-353 7.68e-07

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: 51.81  E-value: 7.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 153 ALSSYYLSRRTPSSYRMVAfvDIGDAKTTATLAVIKDTNINVI-----NRVtveaGGRNITNHLLEKIYSGLDKSIPDLF 227
Cdd:cd24029   150 AALAYGLDKEGKDGTILVY--DLGGGTFDVSILEIENGKFEVLatggdNFL----GGDDFDEAIAELILEKIGIETGILD 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 228 SKKEFRVRN--IKKIEWIKGAIFGLPSVSTQVDASYD-KSVGVCITKADIEEVLDEFseLKKSLSLIHKemndesVLERY 304
Cdd:cd24029   224 DKEDERARArlREAAEEAKIELSSSDSTDILILDDGKgGELEIEITREEFEELIAPL--IERTIDLLEK------ALKDA 295

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2323918809 305 NLNSEeDIEqELQITGGSSRMFIFEDLVHSIFQLKPEVHLNADESIALG 353
Cdd:cd24029   296 KLSPE-DID-RVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKG 342
ASKHA_NBD_HSP70_ScSse cd24094
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ...
 6-368 4.04e-05

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: 46.60  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809   6 IDLGSYKTVVASSDTSAGEIILTKTGSRSTKMAIDYRNKIREFG---------NVNVTCKEREKVA---------EDIRK 67
Cdd:cd24094     3 LDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGeaaktqetsNFKNTVGSLKRLIgrtfsdpevAEEEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809  68 EIE-ELAEQMKNRGAErVKIMPTSHVYGLlNNLINNY-TQAKGISSNEL-----EIEIVVPSTYTQLHKNILI---KILN 137
Cdd:cd24094    83 YFTaKLVDANGEVGAE-VNYLGEKHVFSA-TQLAAMYlGKLKDTTQAELkapvsDVVISVPGWFTDEQRRAILdaaEIAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 138 LiNPkvqVECITDSMALSSYYLSRRT-----PSSYRMVAFVDIGDAKTTATLAVIKDTNINVinRVTV---EAGGRN--- 206
Cdd:cd24094   161 L-NP---LRLMNDTTAAALGYGITKTdlpepEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTV--KGTAydrHFGGRDfdk 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 207 -ITNHLLEKIysgLDKSIPDLFSKKEFRVRNIKKIEWIKGAIFGLPSVSTQVDASY-DKSVGVCITKADIEEVLDEFseL 284
Cdd:cd24094   235 aLTDHFADEF---KEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMnDIDVSSMLKREEFEELIAPL--L 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 285 KKSLSLIhkemndESVLERYNLnSEEDIEQeLQITGGSSRMFIFEDLVHSIFQLKPEVHLNADESIALGGVYRRLMESPF 364
Cdd:cd24094   310 ERVTAPL------EKALAQAGL-TKDEIDF-VELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAILSPV 381


                  ....
gi 2323918809 365 HRFR 368
Cdd:cd24094   382 FRVR 385
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 251-353 6.75e-05

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


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 45.97  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 251 PSVSTQVDASYDKSVGVCITKADIEEVLDEFseLKKSLSLIHKemndesVLERYNLnSEEDIeQELQITGGSSRMFIFED 330
Cdd:COG0443   249 DEAEINLPFSGGKHLDVELTRAEFEELIAPL--VERTLDPVRQ------ALADAGL-SPSDI-DAVLLVGGSTRMPAVRE 318

                          90       100
                  ....*....|....*....|...
gi 2323918809 331 LVHSIFQLKPEVHLNADESIALG 353
Cdd:COG0443   319 RVKELFGKEPLKGVDPDEAVALG 341
ASKHA_NBD_HSP70_AtHsp70-14-like cd24095
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ...
 170-368 1.28e-04

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: 44.99  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 170 VAFVDIGDAKTTATLAVIKDTNINVI----NRvtvEAGGRNITNHLLEKIYSGL-DKSIPDLFSKKEFRVRNIKKIEWIK 244
Cdd:cd24095   196 VVFVDVGHSSTQVCVVAFKKGQLKVLshafDR---NLGGRDFDEVLFDHFAAEFkEKYKIDVKSNKKASLRLRAACEKVK 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 245 GAIFGLPSVSTQVDASY-DKSVGVCITKADIEEVLDEFseLKKSLSLIHKEMNDESVlerynlnSEEDIeQELQITGGSS 323
Cdd:cd24095   273 KILSANPEAPLNIECLMeDKDVKGMITREEFEELAAPL--LERLLEPLEKALADSGL-------TVDQI-HSVEVVGSGS 342

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2323918809 324 RMFIFEDLVHSIFQLKPEVHLNADESIALGGVYRRLMESPFHRFR 368
Cdd:cd24095   343 RIPAILKILTKFFGKEPSRTMNASECVARGCALQCAMLSPTFKVR 387
ASKHA_NBD_HSP70_HSPA4_like cd10228
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ...
 279-353 1.40e-04

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: 44.57  E-value: 1.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2323918809 279 DEFSELKKSL-SLIHKEMNdeSVLERYNLnSEEDIEqELQITGGSSRMFIFEDLVHSIFQLKPEVHLNADESIALG 353
Cdd:cd10228   301 AEFEELCAPLfARVEVPLR--SALADSKL-KPEDIH-SVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARG 372
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 168-353 8.71e-04

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: 42.63  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 168 RMVAFVDIGDAKTTATLAVIKDTNINVINrvT---VEAGGRN----ITNHLLE--KIYSGLDksipdlFSKKEFRVRNIK 238
Cdd:pfam00012 186 RNIAVYDLGGGTFDVSILEIGRGVFEVKA--TngdTHLGGEDfdlrLVDHLAEefKKKYGID------LSKDKRALQRLR 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 239 ------KIEwikgaifgLPSVSTQVDASY------DKSVGVCITKADIEEVLDEFseLKKSLSLIHKEMNDESVlerynl 306
Cdd:pfam00012 258 eaaekaKIE--------LSSNQTNINLPFitamadGKDVSGTLTRAKFEELVADL--FERTLEPVEKALKDAGL------ 321

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2323918809 307 nSEEDIEqELQITGGSSRMFIFEDLVHSIFQLKPEVHLNADESIALG 353
Cdd:pfam00012 322 -SKSEID-EVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIG 366
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
 250-353 1.15e-03

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 42.12  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 250 LPSVSTqvDASYDKSVGVCITKADIEEVLDEFseLKKSLSLIHKEMNDESVlerynlnSEEDIeQELQITGGSSRMFIFE 329
Cdd:PTZ00400  317 LPFITA--DQSGPKHLQIKLSRAKLEELTHDL--LKKTIEPCEKCIKDAGV-------KKDEL-NDVILVGGMTRMPKVS 384

                          90       100
                  ....*....|....*....|....
gi 2323918809 330 DLVHSIFQLKPEVHLNADESIALG 353
Cdd:PTZ00400  385 ETVKKIFGKEPSKGVNPDEAVAMG 408
ASKHA_NBD_HSP70_Ssc1_3 cd11734
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ...
 203-353 1.72e-03

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: 41.28  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 203 GGRNITNHLLEKIYSGLDKSIPDLFSKKEFRVRNIKkiEWIKGAIFGLPS-VSTQV-------DASYDKSVGVCITKADI 274
Cdd:cd11734   222 GGEDFDIALVRHIVSEFKKESGIDLSKDRMAIQRIR--EAAEKAKIELSStLQTDInlpfitaDASGPKHINMKLTRAQF 299

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2323918809 275 EEVLDEFseLKKSLSLIHKEMNDESVlerynlnSEEDIeQELQITGGSSRMFIFEDLVHSIFQLKPEVHLNADESIALG 353
Cdd:cd11734   300 ESLVKPL--VDRTVEPCKKALKDAGV-------KTSEI-NEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIG 368
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
 128-339 7.23e-03

nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 39.18  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 128 HKNILIKILNLI-NPKVQVECIT-DSMALSSYYLSRRTPSSYRMVAFVDIGDAKTtaTLAVIKDTNInVINRvTVEAGGR 205
Cdd:cd24049   134 PKEIVESYLELLkEAGLKPVAIDvESFALARALEYLLPDEEEETVALLDIGASST--TLVIVKNGKL-LFTR-SIPVGGN 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 206 NITNHLlekiysgldksipdlfsKKEFRVrNIKKIEWIKgAIFGLPSVSTQVDASYDKSVgvcitkadIEEVLDEF-SEL 284
Cdd:cd24049   210 DITEAI-----------------AKALGL-SFEEAEELK-REYGLLLEGEEGELKKVAEA--------LRPVLERLvSEI 262

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2323918809 285 KKSLSLIHKEMNDESVlerynlnseedieQELQITGGSSRMFIFEDLVHSIFQLK 339
Cdd:cd24049   263 RRSLDYYRSQNGGEPI-------------DKIYLTGGGSLLPGLDEYLSERLGIP 304
ASKHA_NBD_HSP70_HSPA9 cd11733
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ...
 257-353 7.97e-03

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: 39.17  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 257 VDASYDKSVGVCITKADIEEVLDEFseLKKSLSLIHKEMNDESVlerynlnSEEDIeQELQITGGSSRMFIFEDLVHSIF 336
Cdd:cd11733   282 ADASGPKHLNMKLTRAKFESLVGDL--IKRTVEPCKKCLKDAGV-------SKSDI-GEVLLVGGMTRMPKVQETVQEIF 351

                          90
                  ....*....|....*..
gi 2323918809 337 QLKPEVHLNADESIALG 353
Cdd:cd11733   352 GKAPSKGVNPDEAVAMG 368
ASKHA_NBD_HSP70_HSPA1-like cd24028
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ...
 205-353 9.07e-03

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: 39.03  E-value: 9.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323918809 205 RNITNHLLEKIYSGLDKSIPDlfSKKE-FRVRniKKIEWIKGAIFGLPSVSTQVDASYD-KSVGVCITKADIEEVLDEFs 282
Cdd:cd24028   231 NRLVEYLVEEFKKKHGKDLRE--NPRAmRRLR--SACERAKRTLSTSTSATIEIDSLYDgIDFETTITRAKFEELCEDL- 305

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2323918809 283 eLKKSLSLIhkemndESVLERYNLnSEEDIEqELQITGGSSRMFIFEDLVHSIFQLKP-EVHLNADESIALG 353
Cdd:cd24028   306 -FKKCLEPV------EKVLKDAKL-SKDDID-EVVLVGGSTRIPKIQELLSEFFGGKElCKSINPDEAVAYG 368
 
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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