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Database: UniProt
Entry: M3K7H8_CANMX
LinkDB: M3K7H8_CANMX
Original site: M3K7H8_CANMX 
ID   M3K7H8_CANMX            Unreviewed;       209 AA.
AC   M3K7H8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Co-chaperone HscB C-terminal oligomerisation domain-containing protein {ECO:0000259|Pfam:PF07743};
GN   ORFNames=G210_4997 {ECO:0000313|EMBL:EMG51145.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG51145.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG51145.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HscB family.
CC       {ECO:0000256|ARBA:ARBA00010476}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG51145.1}.
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DR   EMBL; AOGT01000001; EMG51145.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3K7H8; -.
DR   STRING; 1245528.M3K7H8; -.
DR   eggNOG; KOG3192; Eukaryota.
DR   HOGENOM; CLU_068529_1_1_1; -.
DR   OMA; TVELKYW; -.
DR   OrthoDB; 1479333at2759; -.
DR   Proteomes; UP000011777; 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   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR004640; HscB.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT   DOMAIN          125..197
FT                   /note="Co-chaperone HscB C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07743"
FT   COILED          133..160
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   209 AA;  24524 MW;  AFDF56747668993D CRC64;
     MLTRLFLKHP TYLTRCYSTQ SFYKLFPKNF PHGGPPKDSF IINDRDLRRE YRSLQSENHP
     DVSSDTAASS NINKAYTTLK NPYTRIAHFI HLYSPNHVDI TEDSVAKKII SEYQRKSTET
     SMDYKDMLMS VLEAHEQLEL AESENQLETL EVENNERIEK TESKIEHVLQ QPNINWDDLI
     MDAIKLKYWV TIQNGIKEWE PGKPVHLTH
//
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