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Database: UniProt
Entry: V5GQV0_KALBG
LinkDB: V5GQV0_KALBG
Original site: V5GQV0_KALBG 
ID   V5GQV0_KALBG            Unreviewed;       173 AA.
AC   V5GQV0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Mitochondrial J-type chaperone {ECO:0000313|EMBL:EST08327.1};
GN   ORFNames=PSEUBRA_SCAF17g04344 {ECO:0000313|EMBL:EST08327.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST08327.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
CC   -!- SIMILARITY: Belongs to the HscB family.
CC       {ECO:0000256|ARBA:ARBA00010476}.
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DR   EMBL; KI545859; EST08327.1; -; Genomic_DNA.
DR   RefSeq; XP_016293316.1; XM_016435278.1.
DR   AlphaFoldDB; V5GQV0; -.
DR   STRING; 1365824.V5GQV0; -.
DR   GeneID; 27417897; -.
DR   eggNOG; KOG3192; Eukaryota.
DR   HOGENOM; CLU_068529_1_1_1; -.
DR   OMA; TVELKYW; -.
DR   OrthoDB; 1479333at2759; -.
DR   Proteomes; UP000019377; 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:UP000019377}.
FT   DOMAIN          87..160
FT                   /note="Co-chaperone HscB C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07743"
FT   COILED          88..124
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   173 AA;  19684 MW;  AD53B3E0FB393BF3 CRC64;
     MNLDFTSIPQ NGWSVDPAAL KRAWRLKMAV THPDRMVGRS DKEQQIGAQQ SALINRAYET
     LLNPLPRAHY LLERHNAPEV SESDSLEDPE LLMEVMELRE RLEEAESEEE AAEVRADNAK
     LLEATVETLA QAFGQSPPDL ETARQAAVQL RYWTNIEKAA REWSPGKRVE LQH
//
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