ID A0A1U7LVU9_NEOID Unreviewed; 955 AA.
AC A0A1U7LVU9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=NEOLI_000676 {ECO:0000313|EMBL:OLL26749.1};
OS Neolecta irregularis (strain DAH-3).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Neolectales;
OC Neolectaceae; Neolecta.
OX NCBI_TaxID=1198029 {ECO:0000313|EMBL:OLL26749.1, ECO:0000313|Proteomes:UP000186594};
RN [1] {ECO:0000313|EMBL:OLL26749.1, ECO:0000313|Proteomes:UP000186594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAH-3 {ECO:0000313|EMBL:OLL26749.1,
RC ECO:0000313|Proteomes:UP000186594};
RA Cisse O., Nguyen A., Hewitt D.A., Jedd G., Stajich J.E.;
RT "Evolutionary innovation and constraint leading to complex multicellularity
RT in the Ascomycota.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
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}.
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:OLL26749.1}.
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DR EMBL; LXFE01000149; OLL26749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7LVU9; -.
DR STRING; 1198029.A0A1U7LVU9; -.
DR OMA; CTHIPLV; -.
DR OrthoDB; 5487921at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000186594; Unassembled WGS sequence.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.20.20.110; Rad4, beta-hairpin domain BHD1; 1.
DR Gene3D; 3.30.60.290; Rad4, beta-hairpin domain BHD2; 1.
DR Gene3D; 3.30.70.2460; Rad4, beta-hairpin domain BHD3; 1.
DR Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR InterPro; IPR018327; BHD_2.
DR InterPro; IPR004583; DNA_repair_Rad4.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR InterPro; IPR042488; Rad4_BHD3_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR NCBIfam; TIGR01934; MenG_MenH_UbiE; 1.
DR PANTHER; PTHR12135:SF3; DNA REPAIR PROTEIN RAD4; 1.
DR PANTHER; PTHR12135; DNA REPAIR PROTEIN XP-C / RAD4; 1.
DR Pfam; PF10403; BHD_1; 1.
DR Pfam; PF10404; BHD_2; 1.
DR Pfam; PF10405; BHD_3; 1.
DR Pfam; PF03835; Rad4; 1.
DR Pfam; PF01209; Ubie_methyltran; 1.
DR SMART; SM01030; BHD_1; 1.
DR SMART; SM01031; BHD_2; 1.
DR SMART; SM01032; BHD_3; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000186594};
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 DOMAIN 389..446
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 448..501
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 508..583
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 217..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 765
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT BINDING 791
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
FT BINDING 821..822
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191"
SQ SEQUENCE 955 AA; 107422 MW; D3F76D4B8A6F8386 CRC64;
MIEIHSDSES DIEWDDVQLT APVLEPSNST GDKPSEILVP LQPKKLLTKT TGRRGISTAE
KQQRLTIHKL HILCLLSHLL ILNRALNTEE LLANSLGNIG LPDRKDLHPQ KDLIPAQRSV
YFNRGLRSLI DLWRNKFKTT CEGIRKPLWR STSANIDIFK SSRETLTQSF SSLSGSRDIG
AQLLTMLLRA AGVETRLVCS LQVLDIISTE ESVVPHSVPF QNPEQGLRSS ANDLTSDDNE
PKQSTLQPRS RRQKFRVPLN NGSNIEIINT FHDPPFPVYW SEVFDVATQK WLPVDAFATN
TIAKPTKLEP PQSLRELHMC YVIALDYDGF VKDVTRRYTR SFNNKIRKSR ITSIESGRNW
FCYAMAFLKR QWIVDSDQIE DAELLNYELS EKMPTSVQDL KDHPMYAMER HLRRDQLIAP
GSRPCGSITV GRGRTPENVY QRQSILTVKS EERWYREGRQ IKNGELPVKS LPRKSRERDN
RAPETAVHMY TFDQTELYVP PPVVNGRIPR NTYGNCDYYM PWMIPLGGIF VQDAATARAA
ANLLIVDYAD AITGFRFQGR LARPIISGII VAAEYLEAVL AVQQGFVDLA LEERVQAQRK
KTLERWKLFL TGLAICKRHL GLIAALSRCH VSQVLPANAT ILIPLCCLRA PLPAAAASHR
PVFAYLRAHT YAALSLLYLR NPTSPILASV KSPPPSSSRW VFHPADLSLI SLHIVAEVFS
SVASSYDLMN DAMSAGIHRL WKDRFVQKLD PGRGRMNILD VAGGTGDIAF RMLDHAAKVH
NDHDTLVTCV DINPDMLAEG KKRLLSTCYA NTPRVSFKVQ NAELLDEIPS NSVDLYTIAF
GIRNCTHIPL VLQQAHRVLK PGGIFACLEF GKVSPPPLAS LYRQYSFSVI PLIGQLIAGD
RDSYQYLVES IEKFPKQEDF AKLIEDAGFE ISGNGWEDLT FGVAAIHTGL KKKYK
//
