ID   I2GY61_TETBL            Unreviewed;       652 AA.
AC   I2GY61;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Heat shock protein SSC1, mitochondrial {ECO:0008006|Google:ProtNLM};
GN   Name=TBLA0B02210 {ECO:0000313|EMBL:CCH59063.1};
GN   ORFNames=TBLA_0B02210 {ECO:0000313|EMBL:CCH59063.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH59063.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH59063.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; HE806317; CCH59063.1; -; Genomic_DNA.
DR   RefSeq; XP_004178582.1; XM_004178534.1.
DR   AlphaFoldDB; I2GY61; -.
DR   STRING; 1071380.I2GY61; -.
DR   GeneID; 14494527; -.
DR   KEGG; tbl:TBLA_0B02210; -.
DR   eggNOG; KOG0102; Eukaryota.
DR   HOGENOM; CLU_005965_2_1_1; -.
DR   InParanoid; I2GY61; -.
DR   OMA; GREQKMT; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000002866; Chromosome 2.
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:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd11733; HSPA9-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT   REGION          547..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  70417 MW;  2207B07BCD7B1481 CRC64;
     MLAAKNLLRN NNTAISKSLR LATRFQSTKV QGSVIGIDLG TTNSAVAVME GKVPRIIENA
     EGSRTTPSVV AFNKDGERLV GIPAKRQAVV NPENTLFATK RLIGRRFEDA EVQRDIKQVP
     YKIVKHSNGD AWVEALGETY SPAQIGGFVL NKMKETAEAF LGKSAKNAVV TVPAYFNDSQ
     RQATKDAGQI VGLNVLRVVN EPTAAALAYG LEKSDSKVVA VFDLGGGTFD ISILDIDNGV
     FEVKSTNGDT HLGGEDFDIY LLREIVARFK KESGIDLEND RMAIQRIREA AEKAKIELSS
     TVSTDINLPF ITADASGPKH INMKFSRAQF ETLTEPLVKR TVDPVKKALK DAGLSTSDIS
     EVLLVGGMSR MPKVVETVKQ LFGKEPSKAV NPDEAVAIGA AIQGAVLSGE VTDVLLLDVT
     PLSLGIETLG GVFTRLIPRN TTIPTKKSQV FSTAAAGQTS VEIRVFQGER ELVRDNKLIG
     NFTLSGIPPA PKGVPQIEVT FDIDADGIIN VSAKDKASNK DASITVAGSS GLSENEIEQM
     VNDAEKFKSQ DEARKKSIES ANRADQLAND TEASLKEFEA KVDKVEAQKV KDQVTALKEL
     VARVQSGEEV DAETLKTKTE ELQTSSMKLF EQIYKNNNNT SSSSDANNET KE
//