ID C6HG21_AJECH Unreviewed; 1009 AA.
AC C6HG21;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=HCDG_05361 {ECO:0000313|EMBL:EER40772.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER40772.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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; GG692425; EER40772.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HG21; -.
DR STRING; 544712.C6HG21; -.
DR VEuPathDB; FungiDB:HCDG_05361; -.
DR eggNOG; KOG2132; Eukaryota.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_002761_1_0_1; -.
DR OMA; WEVDFPD; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000002624; 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; 2.
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; 2.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF04072; LCM; 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:UP000002624};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 807..965
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
SQ SEQUENCE 1009 AA; 112194 MW; D55B786038605D6A CRC64;
MAPKSTKAER GATAVMETNS ASIVSKRSVE RIYYPEPHFF RYFVKKPLRR SPLVNRGYWL
RMRAVESMVR RFLEGPSGHQ KVVVNLGCGF DPLPFQLLNR DAALCQNAKF IDVDHHKLMV
KKRDIITQCP ALRDLLSDAQ LTPETDSILL RSKEYVGIGC DLGDLSELDA ALSDVIGLDQ
ASILCIAEVS ITYMDVELAD ALIRFMLKLS NAKVNNSTNS WKDVNFCLLE QYFPEGPHHP
FAAVMMKDFL KLQCPLHSVH KYPSLRQQEQ RFRGSGWTNA KATNLWELWN DPTFVTEDER
LSLDSIEAFD EWEEFALFAS HHFLLSASIR KTAAESEPPD GLGKALVEPS PLSLTPLCSP
KLTSKRRFGA ILPTSANTFG LHGGLGQQTR LSSTDEYTVS KSKTASGEMP PLDVEPRMCH
TITQFYGQDC LLVGGRAAPK KVMADCWLRH SGRWNRTDSL PTPLYRHCAT AVNLGGNDAY
VLIYGGKTNN GDVSGKWFLW NVSKGWQEAT VANQSPTARF GASIVNIDGQ SGVVFGGMSR
YAVVLDDFWT WKLVKSSDGR IHVELNNLTE TIGASSPLDK WLGRFGASIT TTARGCFIIG
GIAKHCCIPQ AYEIILLNKN ALDGLVLAPN IPLLTAVDLD LESIGSRPLL VGHSSCKVGD
DDVLIVGGGA LCFSFGIYWN ESTWLLQSAK SKAINGWSLC EPSTNGHGAN PLEEVTTTRV
DDRPNTNSPE MEIIPRINIS TPQEFQRVVD KAKPVILSGL DLGSCVKTWR KEYLEKAIGR
DRKVVVHEAK SENMNFQTKN FSYVTKEFGK FIDEIYDGSR QYLRSVSSVN PMEQPANLAQ
DFPGLQGDFH LPPELSFVMA NVLCQIQGDK RLILYPPSDV LRLGFAPGAS SSSINIFKNM
SDTSPYSPPN THPHEARLRP GDVLFIPPLW PHTANPINGV SIAVNAFFRN IDRGYAAGRD
AYGNRDLQAY ERGRMEVDKI ARSFDGLPRD MARFYMDRLA DELRRKAHT
//