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Database: UniProt
Entry: A0A0D2IQV4_9EURO
LinkDB: A0A0D2IQV4_9EURO
Original site: A0A0D2IQV4_9EURO 
ID   A0A0D2IQV4_9EURO        Unreviewed;      1084 AA.
AC   A0A0D2IQV4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=Z518_03010 {ECO:0000313|EMBL:KIX08354.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX08354.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX08354.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX08354.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; KN847476; KIX08354.1; -; Genomic_DNA.
DR   RefSeq; XP_013275490.1; XM_013420036.1.
DR   AlphaFoldDB; A0A0D2IQV4; -.
DR   STRING; 1442369.A0A0D2IQV4; -.
DR   GeneID; 25291081; -.
DR   VEuPathDB; FungiDB:Z518_03010; -.
DR   HOGENOM; CLU_002761_1_0_1; -.
DR   OrthoDB; 9938at2759; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000053617; 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; 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; 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; PF04072; LCM; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF117281; Kelch motif; 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   Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          841..1007
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
SQ   SEQUENCE   1084 AA;  121798 MW;  DB90DF5C5D89C090 CRC64;
     MTSPITPRSM GSDDEIPMER NAGLIMGTNN SSIVSKRSVE RLYLPQPHFY RYFVRKPQRR
     SPTINRGYWL RMRAIDWVVR QFLERPSDQK KVIINLGCGY DPIPFQWMSQ DRELCSNTRF
     IDVDFEELMI SKREIILNTP KMRDMLSLIG DLPLEKGIIL DTDEYVALGC DLRNLRRLEH
     LLKSVVDIEQ CLVLFIAEVS ITYMATEDSD ALIAWTTSLA PGKSPDRPDN PFTAAMLNHF
     SKLGTPLRSV LTYPGNHTQT LRFQGAGFSI VDIQSLWELW ADPRFLSPSQ RMSLDEVEPF
     DEWEEFALFA SHYCLIIAQT GPEPLIPEQP RSRRASIDSF ASDLSTRTVS PYRGKTQWFA
     YKYSANPDRE GRTHHASAFF IPGQDAIGVH GGVGLKNRLS STSVYASADS KVSAPTLPPE
     DVGARCCHTI TSLANGWNVL VGGRGSPSAP MKDCWLQTES GWERIQDLPE PRFRHRAVAV
     VLPYNEYGVV VFGGKTSATK VALDCLLWDR VNGWQKLRSL RSDPMPRFGA SFVRLGFNHG
     LLFGGMRHDG VICQGLWRWR LIIRDNAVAG ISFKTSTALD TSAGIWPWLA RLGASYSVIR
     NELLVIGGVA KHGCIPKDYE ILSILGSFSA FGEFEKEMEL RVACVVPKKD PDVPRPFLIG
     HSTHRSGKET TLLVGGGATC FSFGAYWNPG CWLLYDREAG ISSHWALIKP APVKALPPPV
     PKDDSPTPQP MSIERIRLCD EKEFTDILRE GIPKVFASLD IGPCISEWTP CKLLSKIPPS
     KSIVVHSAAT RTMNFQRKDF VYTAMPFHEF INQLENNQDA HMYLRSISST NPTQLPANFN
     TDWPELSSDF QLPTPLRFIK QTQHSSPLRI SANVNMWLHY DVMANVLFQV RGRRKLILFP
     SEDIKYLSFP AGATTSTLDI LEAAEHPEKE EDRLKPIPNT HPHITILRPG EALFIPPLWA
     HSGTPMPPQP PSNVDAPSPD NSRINISLNV FFRTIPATMY PAGRDVYGNR DLAAYEDARR
     DLDKIVRRFT AISVKQKVNG DNSSASTTTQ GDVPVDIHES IPKPIAKAYL ERLADELKEK
     AERL
//
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