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Database: UniProt
Entry: A0A2J5I449_9EURO
LinkDB: A0A2J5I449_9EURO
Original site: A0A2J5I449_9EURO 
ID   A0A2J5I449_9EURO        Unreviewed;       256 AA.
AC   A0A2J5I449;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Dehydrase and lipid transport-domain-containing protein {ECO:0000313|EMBL:PLN84584.1};
GN   ORFNames=BDW42DRAFT_191436 {ECO:0000313|EMBL:PLN84584.1};
OS   Aspergillus taichungensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN84584.1, ECO:0000313|Proteomes:UP000235023};
RN   [1] {ECO:0000313|Proteomes:UP000235023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA   Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA   Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA   LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA   Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA   Cantor M.N., Hua S.X.;
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the function of coenzyme Q in the respiratory
CC       chain. May serve as a chaperone or may be involved in the transport of
CC       Q6 from its site of synthesis to the catalytic sites of the respiratory
CC       complexes. {ECO:0000256|ARBA:ARBA00024947}.
CC   -!- SUBUNIT: Interacts with coenzyme Q. {ECO:0000256|ARBA:ARBA00011814}.
CC   -!- SIMILARITY: Belongs to the COQ10 family.
CC       {ECO:0000256|ARBA:ARBA00006885}.
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DR   EMBL; KZ559510; PLN84584.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J5I449; -.
DR   OrthoDB; 2722348at2759; -.
DR   Proteomes; UP000235023; Unassembled WGS sequence.
DR   GO; GO:0048039; F:ubiquinone binding; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:InterPro.
DR   CDD; cd07813; COQ10p_like; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   InterPro; IPR044996; COQ10-like.
DR   InterPro; IPR005031; COQ10_START.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   PANTHER; PTHR12901:SF10; COENZYME Q-BINDING PROTEIN COQ10, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12901; SPERM PROTEIN HOMOLOG; 1.
DR   Pfam; PF03364; Polyketide_cyc; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          84..247
FT                   /note="Coenzyme Q-binding protein COQ10 START"
FT                   /evidence="ECO:0000259|Pfam:PF03364"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   256 AA;  28152 MW;  78E256647C0C1070 CRC64;
     MKLPFPPRQL SRATQRVLRA QRTPSTSLQR TSPTLLSSRT STSTHFHQQT RPFNLSSLAS
     LLPNNNGGNN NDKHRTLTAI RTLPYAPSPL FKVISSVESY SEFLPFLTAS TVTARDPTTN
     LPTRAFLTVG YGPLSETFTS QVDCDRANWT VEARSGARFG VDSKDGQSQA QAQNSLSSVG
     FPGANEGIFE YLSTRWELLP LEEQGSGGRP QTRVQLQIQF EFRNQFHAAV MGAVEGQMAG
     AMIAAFEARI RQLEGV
//
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