ID A0A178EFI2_9PLEO Unreviewed; 1010 AA.
AC A0A178EFI2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=IQ07DRAFT_583706 {ECO:0000313|EMBL:OAL54415.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54415.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL54415.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54415.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441638; OAL54415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EFI2; -.
DR STRING; 765867.A0A178EFI2; -.
DR InParanoid; A0A178EFI2; -.
DR OrthoDB; 9938at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000077535; 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; 2.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
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 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:UP000077535};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 786..951
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 111945 MW; E33A7172BB267B3B CRC64;
MSAKFKMRPK KSPSKRKGSQ KSTQEKRDVD IMNTNDSSIV SKRSVSKLYL SKEPDFYEPF
VPKFVRRNPL INRGYWLRMH AVEQVVRRFL EEDNGKSKIV VNLGNNLLRD ALLRTHLRTS
QNPVYLRSDQ YMALGCDLRD LDTLERILRA EFNLTASSIL FVAEVSVTYM PVADANALIA
WASTLEDARF CLLEQFLPQG PQHPFAQTML SHFDKLQTTI KAAKLYPSLK EQASRFLDNG
WPKLKIARNL WDLWSDDAFT PPALRRGLDA VEPFDEWEEF ALFGGHYFLL VASNAGEGRA
AETFEEKSVT ADASSMRASN AATISVQSWK DSSAAALTPR RFPAAFSMHR DRVAYHGGQG
TQARLADMDL LECIDAPEPY ISPPLSARMC HTITRMMDDS ALLVGGRASP TQALADCWLI
KSNTWTKVDD LAIPRYRHCA VSVTLDWDGS QTNAVLVFGG KASDGTPLDD CCLWTANNGW
HSIAIDGPLP AARFGAAMAV VESAQNWGLL LGGMGVDGTV VEDVWEWSII ATPTPRLKFT
DRTNDIHSSL PSSAYSRIGA SLVPWENSLL LIGGVSKKEL HSRSEDFLLL SQNNTEIVIS
HPGMHFDSSW PLLVGMGVVA VSQHEILVAG GGAVCFSMGS FWNEGYLALT PTQLGAQGAR
LWRVAPRQVH GAAQAKPTSK PPQKKSSSKA GRHVNHRTIS IPRVQIQSSD DFSNLVAKSK
PAIIEGLNLG PCTDLWSLEY LKEKIGSERE LVVHECSSDR MTFKDKNFKY VKKTVADFLD
GITKGSPEYL RAISSSQPNK LPTKLEDDFP TIAADFELPE IFSAVKNSYH SSPLRISGPV
SLWLHYDVLS NILCQISGSK TLHLYPPSDV KYLDFPPGGS SSNTDVLTSQ DPKLRRTHPH
IASLKPGDIL FLPPMWSHTA TPEEGVSVAV NVFWRDLDRG YAAGKDVYGN RDLQAYENGR
RDVEKIIRAF RDIPSDMAGF YLDRLAGEIG DKADKLRAKK EQTLATQGGQ
//
