ID G3AK92_SPAPN Unreviewed; 514 AA.
AC G3AK92;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN ORFNames=SPAPADRAFT_60887 {ECO:0000313|EMBL:EGW33551.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW33551.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000256|ARBA:ARBA00001629};
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; GL996501; EGW33551.1; -; Genomic_DNA.
DR RefSeq; XP_007375066.1; XM_007375004.1.
DR AlphaFoldDB; G3AK92; -.
DR STRING; 619300.G3AK92; -.
DR GeneID; 18873618; -.
DR KEGG; spaa:SPAPADRAFT_60887; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; G3AK92; -.
DR OMA; VNHERTI; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT REGION 487..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..153
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 514 AA; 55765 MW; 07839B07640EF01F CRC64;
MKSIAEEYLG KKVTHAVVTV PAYFNDAQRQ ATKDAGTIAG LNVLRIVNEP TAAAIAYGLD
KGDKEKQIIV YDLGGGTFDV SLLSIEGGVF EVMATAGDTH LGGEDFDFKV VRYLAKQFKK
KHGIDITSNQ KAIAKLKREA EKAKRTLSAQ MSTRVEIDSF VDGIDFSETL SRAKFEELNL
AAFKKTLKPV EQVLKDAGVK KSEIHDIVLV GGSTRIPKVQ ELLEAFFDGK KASKGINPDE
AVAYGAAVQA GVLSGEEGVD DIVLLDVNPL TLGIETSGGV MTTLIKRNTA IPTKKSQIFS
TAADNQPTVL IQVYEGERTM AKDNNRLGKF ELTGIPPAPR GVPQIEVTFS LDANGILKVE
AMDKGTGKSE SITITNDKGR LSKDDIDRMV EEAEKYAKQD QELKEKIEAR NSLENYAHVL
RGQVNDKSET GLGSKLSEED KETLDDAIKE TLEFIEDNFD SATAEEFEEQ KQKLMDVANP
ITAKLYGGAE GGAGGAGAKF GDDESDDEFD HDEL
//
