ID A1DE23_NEOFI Unreviewed; 1050 AA.
AC A1DE23;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 87.
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=NFIA_075600 {ECO:0000313|EMBL:EAW17630.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW17630.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027696; EAW17630.1; -; Genomic_DNA.
DR RefSeq; XP_001259527.1; XM_001259526.1.
DR AlphaFoldDB; A1DE23; -.
DR STRING; 331117.A1DE23; -.
DR EnsemblFungi; EAW17630; EAW17630; NFIA_075600.
DR GeneID; 4585989; -.
DR KEGG; nfi:NFIA_075600; -.
DR VEuPathDB; FungiDB:NFIA_075600; -.
DR eggNOG; KOG2132; Eukaryota.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_002761_1_0_1; -.
DR OMA; WEVDFPD; -.
DR OrthoDB; 9938at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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; PF13854; Kelch_5; 1.
DR Pfam; PF04072; LCM; 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:EAW17630.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAW17630.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 838..1006
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
SQ SEQUENCE 1050 AA; 116773 MW; E5A4514BDF55E389 CRC64;
MGAAKKPATA GVSTKAEREA DLVMGTNNSS IVSKRSVELL YYPKPHFFRY FVKKPPRRSP
LINRGYWLRM HAMAESVRRF MKQPSDKPKF VLNLGCGFDP LPFILLSTDS SLCSTTRFVD
IDYEKLMVNK KTAIRRTDEI TRLLENVEFL SDESPIQIRS EQYLAIGCDL KNLKKLDDVL
KTEVLPSECS ILFLAEVSLT YMDVKSANAV LDWASKLNND SQFCILEQFF PDGPNHPFAS
TMMKHFNKLG APLYSIHEYP SLSEQEQRFR NAGWAHAQAR SLWDLWSDKE FVGSSLRAWL
DTVEPFDEWE EFALFASHYF LLVASTKPHT LVQESQKPPA FTKEPDVSSQ YVLLAGNDPR
GGQRRFGALI PDSETSMGHH SGLGRQTRDV STDLYSKCKG MTTSQLPFPP REVSARMCHT
VTSLSGGDCL LVGGRASPAN AFQDCWLRQG KQWQSTQSLP APRFRHSAVK ITLETVSDSV
LVYGGKSRDG SIFDTWLLWQ TNSNGWQEVE IQGARPTARF GACLESINQT TGVLFGGIGS
DGIIIGDFWI WKIRHRSDGT VFLELTDHTE HLQQTPLSQY IHRFGSTVTR TSWGMVIVGG
IIPRQIVPYE CEIMLLDVGE LLKCVENESS WGHKILSAIG LGAKLQGPRP LLVGHVACAM
DPDQVLILGG GAVCFSFGTF WTEGSWVLKP AGSTAQNDWT LVPEATHTPK PVASPKVPQI
AGCNTASKLS SIRRIRVDTS EQFQQILADG KPVIIEGSDI GPCTELWTKE YLTDAVGSDR
KVVVHESQSE NMNFQAKNFS YVTKTFGDFL DEVHAGGRQY LRSISAEQPS KLPANLAADF
PGLNDDFKLP QALSLVTENA HSSPLRISGP VTMWLHYDVS PITKQEGWKL RVADRYAQVM
ANVLCQIRGE RRLVLFPPTD VQYLQVPPGA SSSTIDIFHN IKDGSVVSIP HTSPQEAVLN
SGDILFIPPM WLHTASPTGG VSVAVNVFFR SLPKGYAAGR DVYGNRDLQA YEKARTDIQK
MVRSFDGLPS DISRFYLLRL AQELKDSAGV
//