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Entry: A0A317XZ67_9BASI
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ID   A0A317XZ67_9BASI        Unreviewed;       417 AA.
AC   A0A317XZ67;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JUN-2023, entry version 17.
DE   RecName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03191};
DE            EC=2.1.1.201 {ECO:0000256|HAMAP-Rule:MF_03191};
DE   AltName: Full=Ubiquinone biosynthesis methyltransferase COQ5 {ECO:0000256|HAMAP-Rule:MF_03191};
GN   Name=COQ5 {ECO:0000256|HAMAP-Rule:MF_03191};
GN   ORFNames=BCV70DRAFT_197317 {ECO:0000313|EMBL:PWZ03083.1};
OS   Testicularia cyperi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX   NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWZ03083.1, ECO:0000313|Proteomes:UP000246740};
RN   [1] {ECO:0000313|EMBL:PWZ03083.1, ECO:0000313|Proteomes:UP000246740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 3645 {ECO:0000313|EMBL:PWZ03083.1,
RC   ECO:0000313|Proteomes:UP000246740};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- FUNCTION: Methyltransferase required for the conversion of 2-
CC       polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-
CC       6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000256|HAMAP-Rule:MF_03191}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-
CC         adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-
CC         1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03191};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_03191}.
CC   -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC       at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000256|HAMAP-
CC       Rule:MF_03191}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03191}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03191}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03191}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. MenG/UbiE family. {ECO:0000256|HAMAP-Rule:MF_03191}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03191}.
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DR   EMBL; KZ819188; PWZ03083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317XZ67; -.
DR   STRING; 1882483.A0A317XZ67; -.
DR   InParanoid; A0A317XZ67; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000246740; Unassembled WGS sequence.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR   InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR   PANTHER; PTHR43591:SF24; 2-METHOXY-6-POLYPRENYL-1,4-BENZOQUINOL METHYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43591; METHYLTRANSFERASE; 1.
DR   Pfam; PF01209; Ubie_methyltran; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51608; SAM_MT_UBIE; 1.
DR   PROSITE; PS01183; UBIE_1; 1.
DR   PROSITE; PS01184; UBIE_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03191};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_03191}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03191};
KW   Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03191};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246740};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_03191};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03191}; Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03191}.
FT   REGION          14..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..61
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT   BINDING         207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT   BINDING         237..238
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
SQ   SEQUENCE   417 AA;  44914 MW;  77891070011C197F CRC64;
     MVAQRYTLSA LRSTLSAASG ATPRPAVASS SRSFASTPYS RSDRPPSSPF PPPPPGPSTS
     NTAQQPSPFA APSSSTSASD APSSSIHDQS HASATNSSPF GSAAQSGASG FDAKHTHFGF
     KTVREEEKET LVGSVFSSVA SKYDVMNDAM SLGIHRLWKD HFVSKLDPRG GIKVLDVAGG
     TGDIALRILD HARTKHFDRE THVTVLDINP HMLKEGQKRF KQTMYWGGPQ ITFQLGNAEQ
     LDSTMPVPAD PVRGPNSKQP LLPPLISQPI PDESIDLYTI AFGIRNCTHI DEVLRQAYRV
     LKPGGVFSCL EFGKVNVPFL AEAYKQYSFN VIPPLGQMLA GDRDSYQYLV ESIERFPTQP
     NFARMMRDAG FHLTGSPTAT SLGFGAESGA KPGDEDVAGA WEDLTFGVAT IWTGIKL
//
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