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Database: UniProt
Entry: A1DE23_NEOFI
LinkDB: A1DE23_NEOFI
Original site: A1DE23_NEOFI 
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}.
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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
//
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