TYW4_ASPOR
ID TYW4_ASPOR Reviewed; 1032 AA.
AC Q2U6D4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=AO090120000285;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE62881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007166; BAE62881.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2U6D4; -.
DR SMR; Q2U6D4; -.
DR STRING; 510516.Q2U6D4; -.
DR EnsemblFungi; BAE62881; BAE62881; AO090120000285.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000006564; Chromosome 5.
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; 2.120.10.80; -; 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..1032
FT /note="tRNA wybutosine-synthesizing protein 4"
FT /id="PRO_0000226138"
FT DOMAIN 833..988
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 702..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 169..170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1032 AA; 114725 MW; 888A52CA78557DFD CRC64;
MGPAKKPAMA GVNSKAEREA DLVMGTNNSS IVSKRSVEML YYSKPHFFRY FVKKPQRRSP
LINRGYWLRM HAMAETVRKF MREPSDKPKF VLNLGCGFDP LPYMLLSADN DLCRDTTFVD
IDYEKLMVNK KTAIRKTDEI TQLLEDVEFL PDDSAVQIRS KPYLAIGCDL KNLTKLDTVL
RAEVLPSECA VLFLAEVSLT YMDVKSANAV VSWASGLSND AQFCILEQFF PDGPDHPFAS
TMMKHFKKLG APLYSIHEYP SLNEQEQRFK DAGWNHAHAR SLWDLWSDDE FVDGSLRASL
DAIEPFDEWE EFALFGSHYF LLHASTRPRV SETATRTLTG LDPQTDKSGH FRLLAKCPPG
SGQRRFGAVI PDSDKAVGHH SGLGRQTRLS STELYTKSEG TTKTHEFPPG DIPARMCHTV
TCLSNQDCLL VGGRASPASG FKDCWVRQGN QWRSTQSLPV PRFRHSAVKV TLDSEYVLVY
GGKTSDGTTL NTWLAWSSKK QDWQQVETNS IHIKARFGAC LGSINDTSGV LFGGIGAEGT
ILGDFFTWKL HQRSDGSLFM ELTDHTDDLR RTSSLFNQIH RFGATVNQTA WGLVIVGGIV
PRGIITHDKE IMLLDSTELT KCIASGWPSN HTIISALGLG NRLDGPRPLL VGHVSCAIDS
KEILILGGGA VCFSFGTYWT EGTWLLQDVS STTENDWTLI PESVEPNKSQ SEKATSKPSA
QSQNEPYRAA EVITPIPRVC VQNPAQFQDI LAEGRPVIIE GSDVGPCTEL WTKEYLTSAV
GGDRKIVVHE AQSAHMSFQT KNFSYATKTF GTFMDEVYAG DRQYLRSISA EQPTKLPANL
AVDFPSLSHD FRLPESLSIV TDNTHSSPLR ISGPVTLWLH YDVMANVLCQ IRGEKRLILF
PPSDVQYLQV PPGASSSTIN IFQSNGSVAS IPHTSPQEAV LKRGDILFIP PLWLHTASPT
GDVSVAVNVF FRNLSKGYAA GRDVYGNRDL QAYEKARNDI QKMAKSFDGL PSEMARFYLL
RLAQELKDKA EK
