ID A0A1E4TWA7_PACTA Unreviewed; 613 AA.
AC A0A1E4TWA7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=PACTADRAFT_49441 {ECO:0000313|EMBL:ODV96021.1};
OS Pachysolen tannophilus NRRL Y-2460.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX NCBI_TaxID=669874 {ECO:0000313|EMBL:ODV96021.1, ECO:0000313|Proteomes:UP000094236};
RN [1] {ECO:0000313|Proteomes:UP000094236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2460 {ECO:0000313|Proteomes:UP000094236};
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; KV454013; ODV96021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4TWA7; -.
DR STRING; 669874.A0A1E4TWA7; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000094236; 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:UP000094236}.
SQ SEQUENCE 613 AA; 66656 MW; 248F2BBF06E9B73D CRC64;
MADGVFQGAI GIDLGTTYSC VATYDSAVEI IANEQGNRVT PSFVAFTPEE RLIGDAAKNQ
AALNPKNTVF DAKRLIGRAF TDESVQKDIK SWPFKVINSN GNPLIEVEYL EETKTFSPQE
ISAMVLTKMK EIAEAKIGKK VEKAVITVPA YFNDAQRQAT KDAGAISGLN VLRIINEPTA
AAIAYGLGAG KSDKERHVLI FDLGGGTFDV SLLQITGGVF TVKATAGDTH LGGQDFDTNL
LEHFKKEFQK KTGLDISNDP RALRRLRTAC ERAKRTLSSV TQTTVEVDSL FEGEDFSSNI
TRARFEDVNS ALFKSTLDPV EQVLKDAKIS KSNVDEVVLV GGSTRIPKVQ KLLSDFFDGK
QLEKSINPDE AVAYGAAVQG AILTGQSTSE ETKDLLLLDV IPLSLGVAMQ GNVFAPVVPR
NTTVPTIKRR TFTTVEDHQT TVQFPVYQGE RVNCSENTLL GEFDLKNIPP MQAGEPVLEA
IFEVDANGIL KVTAVEKSTG RSANITISNS IGRLTSEDIE KMINDADKFK KADEEFSKRH
EAKQKLEAYV SSIESTVTDP VLSAKLKRGS KDKIEAALSD ALAALEIEES SADDYRKAEL
GLKRVVTKAM ATR
//
