ID   TYW4_EMENI              Reviewed;        1068 AA.
AC   Q5BH52; C8VQJ5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=tRNA wybutosine-synthesizing protein 4;
DE            Short=tRNA-yW synthesizing protein 4;
DE            EC=2.1.1.290;
DE            EC=2.3.1.231;
DE   AltName: Full=Leucine carboxyl methyltransferase 2;
DE   AltName: Full=tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase;
DE   AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase;
GN   Name=ppm2; Synonyms=tyw4; ORFNames=AN0128;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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 (By similarity). {ECO:0000250}.
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   -!- 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   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC       {ECO:0000305}.
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DR   EMBL; AACD01000004; EAA65306.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF90143.1; -; Genomic_DNA.
DR   RefSeq; XP_657732.1; XM_652640.1.
DR   AlphaFoldDB; Q5BH52; -.
DR   SMR; Q5BH52; -.
DR   STRING; 162425.CADANIAP00002618; -.
DR   PRIDE; Q5BH52; -.
DR   EnsemblFungi; CBF90143; CBF90143; ANIA_00128.
DR   EnsemblFungi; EAA65306; EAA65306; AN0128.2.
DR   GeneID; 2875904; -.
DR   KEGG; ani:AN0128.2; -.
DR   VEuPathDB; FungiDB:AN0128; -.
DR   eggNOG; KOG2132; Eukaryota.
DR   eggNOG; KOG2918; Eukaryota.
DR   HOGENOM; CLU_002761_1_0_1; -.
DR   InParanoid; Q5BH52; -.
DR   OMA; WEVDFPD; -.
DR   OrthoDB; 1094856at2759; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0031591; P:wybutosine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 2.120.10.80; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   Pfam; PF13621; Cupin_8; 1.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..1068
FT                   /note="tRNA wybutosine-synthesizing protein 4"
FT                   /id="PRO_0000226141"
FT   DOMAIN          876..1024
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         181..182
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1068 AA;  117417 MW;  9107053B261AABB2 CRC64;
     MCPPEQPAKA MAPSKSNQAA KSAVPTKEEK SADLVMATNN SSIVSKRSVE MLYYPEPHFF
     CHFVKKPQRR APLINRGYWL RMHAMEESVR RFMRESPDKP KFVLNLGCGF DPLPFILLSA
     DRSLCSQTTF VDIDYEKLML NKKAALREAG ALTQILEDVE FGPDESAVQI RSGQYVAVGC
     DLKNLDKLDR VLRAEVLPAE CAVLFLAEVS LTYMDVKSAN AVVSWASRLS NDAQFCILEQ
     YFPDGPSHPF AATMMEHFGK LGAPLHSIHE FPSLSDQERR FTEAGWTHAH ARSLWDLWSD
     DEFVPAVLRT SLDSIESFDE WEEFALFASH YFLLHASTRP GTKGSKSAAA TADVGPSRQA
     VTRSNEFRLI PNTSLPTGQR RFGALVPGGE AVIGIHSGWG RQTRVADTDV YKTSKDNIDS
     HARFPSSNDI SARLCHTITA FSDDGDCLLV GGRTSPASAL QDTWVRKNNV WQAGSSLPLA
     RFRHCATRVT LGSDRSSGSV LIYGGKTSDG TTLDTWLLWN DNGEGWSSVT VRTMNDAPAP
     KARFGACLAS IDSTNGLLFG GIGPDGTILE DFWTWKLYEE ADGSLCMELT DQTGSLRNIA
     LGFDILPRFG ATVSSTAQGL VVSGGIIPRR VVPFDGEILL LDSATLLDCI KNGLPLTTPI
     LSTIGLDAGF TGPRPLLVGH VSHAISTDQV LLLGGGAVCF SFGTFWTRGT WMLCPVGERA
     VNDWALVCEN VEKPTKAKAA AQIPAKTKKQ KASKKYKPEK YKSTTKVTPI RRVTVESADE
     FQQILEDAQP VIIESADIGP CTELWTKEYL VNTVGSDRKV IVHAAETETM SFRTKNFKYE
     SKTFGTFMDE VHAGGRQYLR SISEKQPAKL PANLAADFPS LSSDFRLPEA LKTVVENAHS
     SPLRISGPVT LWLHYDVMAN VLCQIQGEKR LILYPPSDVP HLDVPAGASS SNINVFQNRA
     DGAIALIPHT SPHEARLKRG DILFIPPLWL HTAAPTGKVS VAVNVFFRNL SQGYALGRDV
     YGNRDVQAYE KGRKDLEKLV KSFSGLPPDM ARFYLLRLAD ELQETAEQ