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Database: UniProt
Entry: A0A395NBH9_TRIAR
LinkDB: A0A395NBH9_TRIAR
Original site: A0A395NBH9_TRIAR 
ID   A0A395NBH9_TRIAR        Unreviewed;       210 AA.
AC   A0A395NBH9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   22-FEB-2023, entry version 10.
DE   SubName: Full=Cyclase dehydrase family {ECO:0000313|EMBL:RFU73466.1};
GN   ORFNames=TARUN_8803 {ECO:0000313|EMBL:RFU73466.1};
OS   Trichoderma arundinaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU73466.1, ECO:0000313|Proteomes:UP000266272};
RN   [1] {ECO:0000313|EMBL:RFU73466.1, ECO:0000313|Proteomes:UP000266272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU73466.1,
RC   ECO:0000313|Proteomes:UP000266272};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
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:RFU73466.1}.
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DR   EMBL; PXOA01000650; RFU73466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395NBH9; -.
DR   STRING; 490622.A0A395NBH9; -.
DR   Proteomes; UP000266272; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000266272}.
FT   DOMAIN          51..197
FT                   /note="Coenzyme Q-binding protein COQ10 START"
FT                   /evidence="ECO:0000259|Pfam:PF03364"
SQ   SEQUENCE   210 AA;  22938 MW;  09449967692EB5AA CRC64;
     MAARTIARRL PLQPSAPLLR TQRVACSSSH RAFISLPGGS PQSLVATRTL PYRHEPLYEL
     IADVDSYSAF VPYCSHSQVR KWSAPDPSGR RWPTLADLHV GWGGFDEVFT SRLLCVPGVS
     VEARSGGSAE GGPAQDASAI FKTLETLWYL TPLARPSAAP STEVRLTIKY QFVNPLYAAV
     SAAVSDKIAA LMIEAFEKQV HYKLGARQRL
//
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