ID A0A1Y2DY73_9PEZI Unreviewed; 1056 AA.
AC A0A1Y2DY73;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=tRNA wybutosine-synthesizing protein 4 {ECO:0000256|ARBA:ARBA00018045};
DE EC=2.1.1.290 {ECO:0000256|ARBA:ARBA00012779};
DE EC=2.3.1.231 {ECO:0000256|ARBA:ARBA00012155};
DE AltName: Full=Leucine carboxyl methyltransferase 2 {ECO:0000256|ARBA:ARBA00030231};
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase {ECO:0000256|ARBA:ARBA00030847};
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase {ECO:0000256|ARBA:ARBA00029750};
GN ORFNames=BCR38DRAFT_210575 {ECO:0000313|EMBL:ORY64260.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY64260.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY64260.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY64260.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC that acts as a component of the wybutosine biosynthesis pathway.
CC Wybutosine is a hyper modified guanosine with a tricyclic base found at
CC the 3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC tRNA. May methylate the carboxyl group of leucine residues to form
CC alpha-leucine ester residues. {ECO:0000256|ARBA:ARBA00025588}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in
CC tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-
CC homocysteine + wybutosine(37) in tRNA(Phe); Xref=Rhea:RHEA:37119,
CC Rhea:RHEA-COMP:11844, Rhea:RHEA-COMP:11847, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73544, ChEBI:CHEBI:74275; EC=2.3.1.231;
CC Evidence={ECO:0000256|ARBA:ARBA00000401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-
CC adenosyl-L-methionine = 7-[(3S)-(3-amino-3-
CC methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36903, Rhea:RHEA-COMP:10379, Rhea:RHEA-
CC COMP:11844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73543,
CC ChEBI:CHEBI:74275; EC=2.1.1.290;
CC Evidence={ECO:0000256|ARBA:ARBA00001806};
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004797}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000256|ARBA:ARBA00010703}.
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:ORY64260.1}.
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DR EMBL; MCFJ01000007; ORY64260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DY73; -.
DR STRING; 1141098.A0A1Y2DY73; -.
DR InParanoid; A0A1Y2DY73; -.
DR OrthoDB; 9938at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000193689; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.1470; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR46529; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 4; 1.
DR PANTHER; PTHR46529:SF1; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 4; 1.
DR Pfam; PF13621; Cupin_8; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF04072; LCM; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ORY64260.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ORY64260.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 858..1012
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 117641 MW; B29EA629357BDCAB CRC64;
MAPPAAKQTS KRSQKEQAHD ESVMSTNSSS IVSKRSVERI YYLNEPHFFR FFVKKFQRRS
PLINRGYHLR LHVIDVAVRN FLQRSSEKKK VVINLGCGSD VLPWQCMTRY PDHCNSVKFI
DVDFPDLMEN KSKTVRSTPE LNSMLTGVEE SGHPHLILQS DRYVQIGCDL RDLTEIHDAL
SSVVTIADCE FMFVAEVSIT YMETKAADAV IRWASSLGQA EFCLLEQIIP DGADHPFAET
MLKHFEKLKT PLKSVFAYPD LEAQKDRFAR LGWSYVEAES LWSTWSSPKY LSSDDRKVIN
NVEPFDEWEE FAVFGSHYCV ITSRTGTIVS DHCRRHGVDQ DPRHLGPIRS LVALTEFSDD
GTRGQRRFGA PMMLESHIGD KLLVNMFGFG HTTRLKSLDL FSSHPPARDL KLPSAGPPGR
MCHTIVELGT YGNILMGGRA SPSNPLKDCW LFNKNSQTWQ QLRDLPTPLY RHAATRLGSS
HLALVIGGKT GPSSVFNGSF LYHPETGWVE CRISNRCYTP VFGAVLVSFN PMYSDDTDCS
RSVHFRGILA GGLLEDGTVA KQILRWDLEL PESGQPIINF TSYAGTQSAT AAGGQKELKL
DSIICRFGAS AFVDEHGSLL IVGGIIEDYT IPREQEILVV DITLPKYQVI ATASLIQADE
GKLIPRPLLL GISVAPTADG RLVIMGGGAT CFSMGTYWNK GCYTLSRSPI SAMQIVLANT
VRKPLGTTWK YHQTLEVTDA ANAQMPSRPE MGAQQAVTVQ IPRLRLDSPE AFSDILTASR
PVIIEGSNLG SCLQAWTPEH LVAQVGEAHR VIVHEANAAK MDFNTKNFKY VTKDFGTFIQ
EVQRGGRMYL RALSEVAPTE KPANLSQDFP KLAEEFQLPT EMSFASQNTF SSVLRISGPV
NMWLHYDVQA NVYCQIVGSK RLILFPPADV TQLSFAPGAS SSSLDVFAEL DSSSLAGTHP
HEAILKPGDV LFLPPLWLHT AKPLTGFGVA VNVFFRNLEN GYSSGRDIYG NRDLAVYEKG
REYIARLLNA FSKVPQDMRE FYVHRLADEL SQRLRD
//
