ID A0A3F3Q6U7_9EURO Unreviewed; 1039 AA.
AC A0A3F3Q6U7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BDQ94DRAFT_177701 {ECO:0000313|EMBL:RDH34883.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH34883.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH34883.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH34883.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; KZ852042; RDH34883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3Q6U7; -.
DR STRING; 1341132.A0A3F3Q6U7; -.
DR OrthoDB; 9938at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
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; 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; PF04072; LCM; 1.
DR SMART; SM00558; JmjC; 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 Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 847..995
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
SQ SEQUENCE 1039 AA; 115070 MW; 6D72707AC58A1C3C CRC64;
MTANKEAGAV KAAAKKPAMA GISTKAEKEA DLVMGTNNSS IVSKRSVEML YYPKPHFFRY
FVKKPQRRSP LINRGYWLRM HAMAESVRQF MREPTGKPKF VLNLGCGFDP LPFILLSEDP
SLCRDTQFVD IDYEKLMINK KTAIKRTAEI TQVLKDVEFL SDESAVQIRS AQYLGIGCDL
KNLKKLDDVL RTEVLPAECS VLFLAEVSLT YMDVKSANAV VEWASKLNNE AKFCILEQFF
PDGPDHPFAS TMMKHFKKLG APLYSIHEYP SLNEQEQRFR NAGWQQASAR SLWDLWSDDE
FVSSSLRSSL DAVEPFDEWE EFALFASHYF LLVASTSQGG SDRGAAKTLQ SEQEVDVSNQ
YALLAKYPAG GGQRRFGALI PDGTNSFGYH AGLGRQTRLA TTDLYANTND VTGPTLPVPS
RDVPARMCHT VTQLSGGDCL LVGGRASPAA GLKDCWLRQG TQWRPTHNLP VERFRHSAIR
VTLSSDYVLV YGGKTSNGTT LDTWLLWSRE DGWQTVETVN GSPSARFGAC LASTDNTSGI
LFGGIGADGT IVEDFWTWKL HQRSNGSYYL ELHDGTERLQ KASPTFEYLS RFGATLSCSS
RGLLLLGGII PRQIVPYEKE IMLLNTKALV ECLTSDCASQ SGNILSAVGL GLNFGGPRPL
LVGHAAYAID PNQVLLLGGG AVCFSFGTFW TEGTWLLKNT DTALENEWGR VSEIAEPLKA
EEPSVEPSNV DQQSTKGVTP IPRVKVETAA QFQQILVEGK PVIIEGSDLG PCTERWTKEY
LADAVGRDRK VVVHDAQSDH MSFQAKNFSY TTKEFGSFLD EVHAGGRQYL RSISTEEPTK
QPAKLAVDFP NLKDDFRLPE SFAMVVENEH SSPLRISGPV TLWLHYDVMA NVLCQIRGEK
RLILFPPSDV QYLQVPAGAS SSTLNIFQNS VDGSIASVPY TTPHEAVMRR GDILFIPPLW
LHTASPTGQV SVAVNVFFRN LSKGYAAGRD VYGNRDLQAY EKARIDLQKM AKSFDGLPPD
MARFYLLRLA KELRDKAEA
//
