ID A0A1B7P991_9EURO Unreviewed; 972 AA.
AC A0A1B7P991;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=ACJ72_00172 {ECO:0000313|EMBL:OAX85447.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX85447.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX85447.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX85447.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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:OAX85447.1}.
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DR EMBL; LGUA01000008; OAX85447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7P991; -.
DR STRING; 1658172.A0A1B7P991; -.
DR OrthoDB; 9938at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000091918; 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; PF13854; Kelch_5; 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:UP000091918};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 771..928
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
SQ SEQUENCE 972 AA; 107933 MW; 18FB27C3A59B8648 CRC64;
MAPTDSKAER GATLVMETNS ASIVSKRSVE RIYYPEPHFF RHFVKKPQRR SPLINRGYWL
RMRAVESCVR KFLEEPSEHQ KLIVNLGCVD GEKRDIITQC TALNDLLSDV QLTPETGSIL
VRSKEYVGIG CDLGDIPKLE AALNDVIGLA KVSILCIAEV SITYMEVNLA DALIRFMPTL
SNDVNFCLLE QYFPDGPHHP FAIIMMQNFI KLQCPLHSIH KYPSLRQQEQ RFRESGWANA
KATNLWDLWS DPAFLGDDQR LSLNSAEPFD EWEEFALFAS HHFLLVATTR KAETESNPPS
EIGESQIEPS FLTLAYLCPP KLTSKRRFGA IAPTAAKAFG LHGGIGQHTR LSSTDEYVAS
KIDAAPGAVP PIDMEARMCH TITQFHGQDC LVVGGRAAPN KALADCWLRC SGQWRRTDNL
PTPLYRHCAT TVKFKEGDTN VLIYGGRNSN GDVSSTWLLW NVLEGWKEVD VGNRSLPARF
GASIVNIDGQ SGVLFGGMTR YGVVLNDFWT WKLTTSGDGQ LHVDLNDLTE NLRMSEPLFK
WLGRFGASVT TTARGSFIIG GVARNGCVPQ DYEIILLNHS ALKGLVLSPG TPVVTFIGLS
VVFNGPRPIL VGHSCCKVGD DDVLIIGGSA ESKATNQWML CEPSTNGGVA DLPDNVSEQM
HNQSIAGLPT IETIPRMSIS TTREFQIIVD NARPVILSGL DIGSCQKSWT KEYLEKAIGR
DRKVVVHEAK SANMDFQSKN FSYVTKEFGT FIDEIYNGSR QYLRSISSIN PSERPANLAQ
DFPELQDDFR LPPELSLVSE NAHSSPLRLS GPVILWLHYD VMANVLCQIQ GDKRLILYPP
SDAIRLAFAP GASSSSINLF PDLSDTSPLS PPNTHPHEAR LKPGDIIFIP PLWLHTANPT
DGVSVAVNVF FRNLEKGYAS GRDVYGNRDL QAYERGRVEV DKIARSFDGI PRDMARFYIE
RLADELRRKA HS
//
