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Database: UniProt
Entry: H1VPE8_COLHI
LinkDB: H1VPE8_COLHI
Original site: H1VPE8_COLHI 
ID   H1VPE8_COLHI            Unreviewed;       735 AA.
AC   H1VPE8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=CH063_12190 {ECO:0000313|EMBL:CCF42103.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF42103.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; CACQ02005144; CCF42103.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1VPE8; -.
DR   STRING; 759273.H1VPE8; -.
DR   EnsemblFungi; CCF42103; CCF42103; CH063_12190.
DR   VEuPathDB; FungiDB:CH63R_12820; -.
DR   eggNOG; KOG2132; Eukaryota.
DR   eggNOG; KOG2918; Eukaryota.
DR   HOGENOM; CLU_002761_1_0_1; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000007174; 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; 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   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:CCF42103.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          536..690
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
SQ   SEQUENCE   735 AA;  80077 MW;  570C32CA0F84AA43 CRC64;
     MTAAERRALD TVEAFDEWEE FALFASHYFV IVASTPHPEI KGRVSRSLGE LDVQSCRTPM
     STSGYEAGRG HRRFGAAMLV EAPDGQKFIS HSFGQGPNGR PSSEDVYQIS DQPVAPSSSR
     EGPSSRVCHT LTDLGSIGVL LAGGRASPST AFNDCWLFKK VFNTWERVQD LPCPVFRHSV
     TRLGSSSLAL LAGGKTNHFQ ASAEYFLFDP TKGWVKCRTQ SAPPSLYGAT FVYTGSHGPR
     NFVGFLMGGN LEDGIINQTV YTWTLDLSDA EPSLSFAQQT SRDDQTPSIL SRFGSIAVQS
     NGYVLLFGGV IKDLQLPSAY DILVLKTTAG GEVDVVTRVD GTDGSTIIRP FIVGSSVVPY
     GNGNLAIVGG GATCFSMGTC WTAGSYSFRF DDGRTVRQSD IALPLSQPET VKYLETVEVT
     TGDKEAVVQS LAPVEMRTIP RVQVETAEEF LKILEAGKPV VIEGSDIGPC KSIWSADYLV
     NNVGPERKVS VHESATEKMD FNAKNFRYVT KDFGDFVREA QEGKRLYLRA LSKDEPSNLP
     TQLAADYPSL AKDFALPPQL GFVDQNAFSS VLRISGPVNM WLHYDVMANV YAQVVGSKRL
     ILFPPSDVSH FAFAPGASSS SVDVFSSLDA GSLRGVHPHE AAVQPGDILF LPPLWLHTAT
     PTSDMSVAVN IFFRNLEKGY SVGRDVYGNR DLAAYEKARQ DIARIGSSFS KLPLDAREFY
     IRRLADELLQ STKSL
//
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