ID A0A2S4PZ37_9PEZI Unreviewed; 1012 AA.
AC A0A2S4PZ37;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=EPUL_000714 {ECO:0000313|EMBL:POS87310.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS87310.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS87310.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS87310.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-2017) 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:POS87310.1}.
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DR EMBL; PEDP01000150; POS87310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4PZ37; -.
DR STRING; 225359.A0A2S4PZ37; -.
DR OrthoDB; 9938at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000237438; 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 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:UP000237438};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 810..965
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
SQ SEQUENCE 1012 AA; 115003 MW; 97F3D1CAF028F4EE CRC64;
MTSQSSQSRK NQEFIIDTNN SSIVSKRSVE RLYFLNETHY FRHFVKKPKR RSPLINRGYW
LRIKAIDDIV HRFLSQSSSK QKTVINLGSG YDPLPWQCLS KYPDACEGAV FIDIDYRDLI
LRKRKLVQDV PDLSSILTNM QTSDDDVLLR SDQYLQVGCD LSEIARLHDI LSQAVDIKDS
SILFIAEVSI TYMDVNAADS LISWASQFLD AQFCLLEQLL PDGIEHPFAQ TMMAHFEKLK
SPLGAVRKYQ TKNAQMNRFK DLGWKQVYAR NLWELWSSDD FLTAEERIAL DGIEPFDEWE
EFSLFGSHYL LLVANSQALH SGVLKSLKSP LIGENKPSDS FRWKQIHSPY HKPHDSRRFG
APLFVKSQYR FKDRIALFGG LGKTTRLNSR DEYSSIDEDV ISSNYCNSAM PSSRMCHTIT
DLGDMGAILI GGRTSPDVGL CDCWIYHKYS DSWERVDDLP WPLYRHQSVR VGSNSVLVSI
GRIDSHRLSD SFLLWNRRTG WVKCIYDGMK PFLVYSPVFF NFKLGDPKSQ SGLLAGGMNS
GVVINKVWRW ILKDILTEHP KIQFTETILC PNLCSNLCRF GSCAVAHHGK LYLLGGITKD
ELLTYADEIC CIEITDENLS ISQVTRPITS HFRYLFIGLS AVSIGEAIVV IGGSAVCFSF
GTFWNPGCLT LLPKKNTGNE EWKFLGTIEV RPSVGDFRPT SIEDSSNPVI PRIKLRSESH
FIEILNAAKP VIFEGLDIGS CTAKWNTEYL KRAIGEEREA RLLIIHEAST KYMDFNTKNF
KYTNMKFGDF ISQIEQGAKL YLRSLSSENP SLVPADISKD FPSICSDFSL PEKLSFVKQN
SHSSPLRISG PVVMWLHYDT LANILCQVKG EKNILLFHPS EFKYFDLKPG KSSSSVNVFE
SMQCQQHQKF PKPYQALLKS GDVIYIPPFW LHTLSSEKGV SIAVNIFFKN LSIGYASGKD
VYGNRDLQAY EKGRQDVAKI LASFDSTPTT ARDFYLQRLV EELKQGALRY SP
//
