ID   S7MZ92_MYOBR            Unreviewed;       225 AA.
AC   S7MZ92;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Iron-sulfur cluster co-chaperone protein HscB, mitochondrial {ECO:0000313|EMBL:EPQ09894.1};
GN   ORFNames=D623_10027493 {ECO:0000313|EMBL:EPQ09894.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ09894.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
CC   -!- SIMILARITY: Belongs to the HscB family.
CC       {ECO:0000256|ARBA:ARBA00010476}.
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DR   EMBL; KE162863; EPQ09894.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7MZ92; -.
DR   eggNOG; KOG3192; Eukaryota.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR   InterPro; IPR004640; HscB.
DR   InterPro; IPR040682; HscB_4_cys.
DR   InterPro; IPR036386; HscB_C_sf.
DR   InterPro; IPR009073; HscB_oligo_C.
DR   InterPro; IPR036869; J_dom_sf.
DR   NCBIfam; TIGR00714; hscB; 1.
DR   PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR   PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR   Pfam; PF18256; HscB_4_cys; 1.
DR   Pfam; PF07743; HSCB_C; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..225
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004543143"
FT   DOMAIN          39..65
FT                   /note="HscB tetracysteine metal binding motif"
FT                   /evidence="ECO:0000259|Pfam:PF18256"
FT   DOMAIN          157..205
FT                   /note="Co-chaperone HscB C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07743"
SQ   SEQUENCE   225 AA;  25345 MW;  3B471A61F0635A3F CRC64;
     MWGGRAGALP RVWGLWPPGV LGRRPLRCSA ASLAGSSSPQ CWNCGGPGGP IREDGFFCPQ
     CRALQPPDPT RDHFSLMDCK RSFNVDTAKL QHRYQQLQRL VHPDFFGQRS QTEKDFSEKH
     STLVNDAYKT LLAPLSRGLY LLKLHGVEIP EGTDYKMDNQ FLMEIMDINE KLAEAQSEAA
     INEFESIVRA KQEELTDNLS RAFEQGIVFI SSLSQIWKEI VSTET
//