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Database: UniProt
Entry: A7TQH5_VANPO
LinkDB: A7TQH5_VANPO
Original site: A7TQH5_VANPO 
ID   A7TQH5_VANPO            Unreviewed;       651 AA.
AC   A7TQH5;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Heat shock protein SSC1, mitochondrial {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Kpol_472p7 {ECO:0000313|EMBL:EDO15476.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO15476.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; DS480458; EDO15476.1; -; Genomic_DNA.
DR   RefSeq; XP_001643334.1; XM_001643284.1.
DR   AlphaFoldDB; A7TQH5; -.
DR   STRING; 436907.A7TQH5; -.
DR   GeneID; 5543558; -.
DR   KEGG; vpo:Kpol_472p7; -.
DR   eggNOG; KOG0102; Eukaryota.
DR   HOGENOM; CLU_005965_2_1_1; -.
DR   InParanoid; A7TQH5; -.
DR   OMA; AAEKCKI; -.
DR   OrthoDB; 143at2759; -.
DR   PhylomeDB; A7TQH5; -.
DR   Proteomes; UP000000267; 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; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF197; IRON-SULFUR CLUSTER BIOGENESIS CHAPERONE, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267}.
SQ   SEQUENCE   651 AA;  72024 MW;  DE94463870D8D58F CRC64;
     MLFFNRSVKR PGSRFIPSNL SKYLSTKVIG IDLGTTNSAV AYIKDSDNKK SSTIIENSDG
     ERTIPSVVAV DRSGSFLVGN KAKHQASINA ENTFFATKRL IGRSFDSTEI QKDIKSMSYK
     IVPSPQNGQA YLSAKNGKVF SPSEISSVIL KELKKTAEDY LDETIDKAVI TVPAYFNDSQ
     RQATKDAGRL AGLNVLRVVN EPTAAALCYG LDDKDKSGIV AVYDLGGGTF DISILDIEDG
     VFEVRSTNGD THLGGEDFDN VVVKHIIDSF INENSTLDEK PITENREIMQ RIREAAEKAK
     IALSHVSETF VDIPFITKTK HIHLKLTEEE LDNMTMHLMN RTIDPVRKAI KDADIEFSDI
     DDVILVGGMT RMPRIRKLVE ETFSKKPNTS VNPDESVALG AAIQGGILSG EIKSVLLLDV
     TPLTLGIETY GGAFSPLIPR NSTVPVKKTE VFSTGVDGQT AVDIKVYQGE RGLVSDNKLI
     GDFKLTGIEP MLKGKPQIFV TFDIDADGIL NVSASEKSSG KEQSITVIAN SGLTEEEINR
     MIEEGNKNKE KDNIVRQRVE LITKADIMIS DTERAFEQYK KVISLEQSYK PILEELKQVR
     LLINKFKGNE SSEELNVNDI KRSTDALQNK ALKLFQNATK RQSKENQRQK Q
//
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