ID A0A1E4RCG8_9ASCO Unreviewed; 613 AA.
AC A0A1E4RCG8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
DE AltName: Full=Hsp70 chaperone Ssb {ECO:0000256|ARBA:ARBA00042875};
GN ORFNames=HYPBUDRAFT_115363 {ECO:0000313|EMBL:ODV64969.1};
OS Hyphopichia burtonii NRRL Y-1933.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Hyphopichia.
OX NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV64969.1, ECO:0000313|Proteomes:UP000095085};
RN [1] {ECO:0000313|Proteomes:UP000095085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. Ssb-type Hsp70
CC subfamily. {ECO:0000256|ARBA:ARBA00037959}.
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DR EMBL; KV454546; ODV64969.1; -; Genomic_DNA.
DR RefSeq; XP_020074036.1; XM_020219116.1.
DR AlphaFoldDB; A0A1E4RCG8; -.
DR STRING; 984485.A0A1E4RCG8; -.
DR GeneID; 30993666; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000095085; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 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; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF467; RIBOSOME-ASSOCIATED MOLECULAR CHAPERONE SSB1-RELATED; 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; PS00297; HSP70_1; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000095085};
KW Stress response {ECO:0000313|EMBL:ODV64969.1}.
SQ SEQUENCE 613 AA; 66636 MW; A4721A4582366780 CRC64;
MAEGVFPGAI GIDLGTTYSC VATYDSAVEI IANEQGNRVT PSFVAFTSEE RLIGDAAKNQ
AALNPRNTVF DAKRLIGRAF EDESVQKDIK SWPFKVVDSN GNPQIEVQYL DETKTFSPQE
ISSMVLTKMK EIAEAKIGKK VEKAVVTVPA YFNDAQRQAT KDAGAIAGLN VLRIINEPTA
AAIAYGLGAG KSEKERHVLI FDLGGGTFDV SLLNITGGVF TVKATAGDTH LGGQDFDTNL
LDFFKADFQR KTKLDISGDA RALRRLRTAC ERAKRTLSSV TQTTVEVDSL FEGQDFSANI
TRARFEDINA GLFKSTLEPV EQVLKDAKVS KSHVDEVVLV GGSTRIPKVQ KLLSDFFEGK
QLEKSINPDE AVAYGAAVQG AILTGQSTSE DTKDLLLLDV IPLSLGVAMQ GNVFAPVVPR
NTTVPTIKRR TFTTVADHQT TVQFPVYQGE RVNCSENTLL GEFDLKNIPP MQAGEPVLES
IFEVDANGIL KVTALEKSTG RSANITISNS IGRLSSEEIE KMIEDAEKFK SSDDAFAKRH
EQKQKLEAYV ASVESTVTDP VLSAKLKRSA KEKIETALSD ALQALELEES TGDDYRKAEL
TLKRAVTKGM STR
//
