ID A0A2T4GX80_FUSCU Unreviewed; 1021 AA.
AC A0A2T4GX80;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=FCULG_00006860 {ECO:0000313|EMBL:PTD08166.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD08166.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD08166.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD08166.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTD08166.1}.
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DR EMBL; PVEM01000006; PTD08166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4GX80; -.
DR OMA; WEVDFPD; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000241587; 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; 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; SSF117281; Kelch motif; 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:UP000241587};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 826..980
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
SQ SEQUENCE 1021 AA; 113023 MW; CB44521C1A8DB499 CRC64;
MTKEKPSSTR VVKTQALDDL IMGTNSSSIV SKRSVERLYY PNELHFFRYF VNKFQRRAPL
INRGYWLRLR AIDVIVRQFI TASEPGRRKV VINLGAGSDV LPWQSYHRYG NSCGDALFID
VDYPDLMRKK RAIVLGTPQL SELLGEDPYV SEKETDHLLL RSDKYCQVGC DLRELETLRK
CLESFLPLSE CSVLFVAEVS VTYMDTISAD ALIQWASSIG QAEFCLLEQI LPHGPDHPFA
STMLKHFNKL NTSLKSVHQY PTVDSQRSRF EKRGWNSVDV WDLWEAWNSE VFLNSSERAA
LDDVEPFDEW EEFILFARHY IVLHATSYHR GEKGAGQQML ASPPGKHVKA NMVATKSLGA
PKRRFGSPLV ASSPEGGQYL VHTLGMGINA RLNSCDIYSI QESSTSLEMA PVGPSARICH
TTTDLGQGDF LLVGGRASPS KAFSDCWVLK KSSNSWEKTF DLPVPLFRHS TVNLPGSSLA
LVLGGKTGPS EISSDYFIFH PVRGWLKCAV SGVSPNSTFG AFAIASTSLG SKNGHFEGLL
AGGIDGEGKI NNQAYFWTVD VTTHEPIIHF ESVQNYDQHS WALSVFGAQT ANIESLRFVC
GGVGQDPSLQ GQSMACLTVK GKSLEVHLVD LGEKAGQLPF MVGSATVSSG SQLVIVGGGA
TCFSMGTFWD TGVYKIDLEG VISEMIPGRT IHNKPVVVGY QNSPKLTQPT TDGVHPGPQS
NACITAIPKI KLQSKSDFEK LVQNRKPVII EGLDLGGCVE KWNSEYVIQS VGETKEVVVH
ECQTSTGKMD FNSKNFRYVT ESFSSFMTKA ARGEALYLRA LSEEKPTEAP ANLAEDFPGL
ADDFRLPEEL GSVKDRMFSS VLRISGRANM WLHYDVMANV YTQIQGSKRM VLFPPTDVSH
LAFAPGASSS SLDIFSALDT HRLASTNPHE AFLNPGDLLF IPAMWFHTAS PVTDLSVAVN
VFFRDLESGY STGRDVYGNR DLAAYEKGRQ DISRITKSFD RLPSEIRQFY LRRLADELLH
E
//
