TYW4_ASPFU
ID TYW4_ASPFU Reviewed; 1047 AA.
AC Q4WVD1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
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=AFUA_5G11670;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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=EAL91445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000003; EAL91445.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_753483.1; XM_748390.1.
DR AlphaFoldDB; Q4WVD1; -.
DR SMR; Q4WVD1; -.
DR STRING; 746128.CADAFUBP00005797; -.
DR GeneID; 3511201; -.
DR KEGG; afm:AFUA_5G11670; -.
DR eggNOG; KOG2132; Eukaryota.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_002761_1_0_1; -.
DR InParanoid; Q4WVD1; -.
DR OrthoDB; 1094856at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000002530; Chromosome 5.
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; 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 Pfam; PF13621; Cupin_8; 1.
DR Pfam; PF04072; LCM; 1.
DR SUPFAM; SSF50965; SSF50965; 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..1047
FT /note="tRNA wybutosine-synthesizing protein 4"
FT /id="PRO_0000226137"
FT DOMAIN 814..1003
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
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 1047 AA; 116731 MW; 0BFEB53A6487A2AA CRC64;
MGAAKKPAAA GVSTKAEREA DLVMETNNSS IVSKRSVELL YYPKPHFFRY FVKRPPRRSP
LINRGYWLRM HAMAESVRQF MKQPSDKPKF VLNLGCGFDP LPFILLSTDK SLCSTTRFVD
IDYEKLMVNK KTAIRRTDEI TRLLENVEFL SDESPIQIRS EQYLAIGCDL KNLKKLDDVL
KTELLPSDCS ILFLAEVSLT YMDVKSANAV LAWASKLNND SQFCILEQFF PDGPNHPFAS
TMMKHFNKLG APLYSIHEYR SLSEQEQRFR NAGWAHAQAR SLWDLWSDNE FVGSSLRAWL
DTVEPFDEWE EFALFASHYF LLVASTKPQT MVQELQKTPA LTTEPDISSQ YVLLAGNNPR
GGQRRFGALI PDSENSMGHH SGLGRQTRDV STDLYSTCKG MTTPQLPFPP REVSARMCHT
VTSLRGGDCL LVGGRASPAN AFQDCWLRQG KQWQSTKSLP APRFRHSAVK ITLETDSESV
LVYGGKSSDG SIFDTWLLWQ THSNGWQEVE IQGARPPARF GACLESINQT TGVLFGGIGS
DGIIIEDFWI WKIRHRSDGT VFLELTDHTE HLQQTPLSQY IYRFGSTVTR TSRGLVIVGG
IIPRQIVPYE CEIMLLDVGE LLEYVENESS WGHRILSAIG LGGILQGARP LLVGHVACAI
DPDQVLILGG GAVCFSFGTF WTEGGWVLKP AGSTAQNNWT LVPEAMHTPE PVASPKTPQI
STALKLSSIR RIRVDTSEQF QQILADGKPV IIEGSDIGPC TELWTKEYLT DVVGSDRKVV
VHESQSENMN FQAKNFSYVT KAFGDFLDEV HAGGRQYLRS ISAELPSKLP ANLAADFPGL
KDDFKLPQAL SLVTENAHSS PLRISGPVTM WLHYDVSSNT KQEGWKLRVA DRYAQVMANV
LCQIRGERRL VLFPPADVQY LQVPPGASSS TIDIFQNIKD GSIVSIPHTS PQEAVLNSGD
ILFIPPMWLH TASPTGGVSV AVNVFFRSLP KGYAAGRDVY GNRDLQAYEK ARIDIQKMVR
SFDGLPSDIS RFYLLRLAQE LKDNAGV
