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Database: UniProt
Entry: A0A093Y994_9PEZI
LinkDB: A0A093Y994_9PEZI
Original site: A0A093Y994_9PEZI 
ID   A0A093Y994_9PEZI        Unreviewed;       938 AA.
AC   A0A093Y994;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=POLO box domain-containing protein {ECO:0000259|PROSITE:PS50078};
DE   Flags: Fragment;
GN   ORFNames=O988_02630 {ECO:0000313|EMBL:KFY01621.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFY01621.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFY01621.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFY01621.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the UbiH/COQ6 family.
CC       {ECO:0000256|ARBA:ARBA00005349}.
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:KFY01621.1}.
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DR   EMBL; JPJR01000423; KFY01621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093Y994; -.
DR   STRING; 1391699.A0A093Y994; -.
DR   HOGENOM; CLU_312752_0_0_1; -.
DR   Proteomes; UP000029329; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd13118; POLO_box_1; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.1120.30; POLO box domain; 1.
DR   HAMAP; MF_03193; COQ6_monooxygenase; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR018168; Ubi_Hdrlase_CS.
DR   InterPro; IPR010971; UbiH/COQ6.
DR   InterPro; IPR000689; UbQ_mOase_COQ6.
DR   NCBIfam; TIGR01988; Ubi-OHases; 1.
DR   PANTHER; PTHR43876; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43876:SF7; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 2.
DR   PROSITE; PS50078; POLO_BOX; 1.
DR   PROSITE; PS01304; UBIH; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW   Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688}.
FT   DOMAIN          308..328
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFY01621.1"
SQ   SEQUENCE   938 AA;  103258 MW;  D5F04FDCF3A44126 CRC64;
     SDQVSEEEQV PTETRTRPRR EPRETSRSQG KGKAISESAV STEARLGADM VQQLGRSNSE
     TSVKSSSRDP TVASIFSPSE NAEFLHRSKP RHVTKNLQIL YAEIERALNS RSVGPAREAP
     DSEPTIVVKW VDYTNKFGLG YILNDGGVGC IFKSLPASGD SNAQIPPTCV VVRNAEKHLQ
     NRRNPNYADR HQLVPVSGAD IEFFENNGDE GISCVKVNPR AFAASEEYGA AGKLGRGKDE
     WEDRKREKIV LWRKFANYMT VFGRDQDHPY DDALNRMSLD GDSDSSDPNK SNVVTFYQRF
     GDVGCWGFRN GSFQFNFPDH TKLLLSADGT WCDFYHLPLE AARDLALTGN LPSAALDDRQ
     HLSFPLQAFL NFMTKPSTRN GMTSRRRGIQ VDPMIQGIPA ANDFRRKVEF IKSIVGEWIT
     NGGIGRSAME PESRLRWLGN RELVNVKVPF KHVWVTVGAY GGDDRRVACC SHQAPRQRRG
     YATESSPELY DVVCVGGGPA GLSVLAALRA TAATSGLKVA LIESQDLSRT RSWSLPPTQF
     SNRCSSLTPT SVEFLDKIGA WKNIKRDRVQ AYEEMQVWDG VTGSRIEFDW PQGSQGKTIA
     YMNENLNLTS GLLKRIDELS GVSIFDNTKV ENIELGQETE TTDLRSWPIV QLSGGRQIAA
     RLLIGADGAN SPVRAFAGIN SSGWDYNRHG VVATVELEGE GWGGEDHKVA YQRFLPTGPA
     AMLPLPGRLS TLVWSTTPER AALLKTLSTE DFTAMVNAAF RLSPVDLTYM HTLSSGQADE
     YAWRSQHTSS ETNRIPQRVL TVQEGTVASF PLKMRHADTY IGERVALIGD AAHTVHPLAG
     QGLNQGQGDV ESLVKTIEYS VTHGLDIGVS MSLESYNADR YAKNHVLMGV VDKLHKLYAY
     ESGPIVPLRS IGLSAVNALG PLKHFFMGQA AGTGAKIL
//
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