ID F0W0R4_9STRA Unreviewed; 854 AA.
AC F0W0R4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|ARBA:ARBA00031315};
DE EC=2.1.1.282 {ECO:0000256|ARBA:ARBA00012750};
DE EC=2.5.1.114 {ECO:0000256|ARBA:ARBA00012265};
GN Name=AlNc14C5G699 {ECO:0000313|EMBL:CCA14638.1};
GN ORFNames=ALNC14_007810 {ECO:0000313|EMBL:CCA14638.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA14638.1};
RN [1] {ECO:0000313|EMBL:CCA14638.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA14638.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a
CC component of the wybutosine biosynthesis pathway. Wybutosine is a hyper
CC modified guanosine with a tricyclic base found at the 3'-position
CC adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes
CC the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-
CC adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14)
CC to produce wybutosine-86. {ECO:0000256|ARBA:ARBA00037786}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in
CC tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-
CC carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-
CC COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282;
CC Evidence={ECO:0000256|ARBA:ARBA00001168};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine =
CC 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) +
CC H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-
CC COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC ChEBI:CHEBI:73550; EC=2.5.1.114;
CC Evidence={ECO:0000256|ARBA:ARBA00036405};
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004797}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR824050; CCA14638.1; -; Genomic_DNA.
DR AlphaFoldDB; F0W0R4; -.
DR EnsemblProtists; CCA14638; CCA14638; ALNC14_007810.
DR HOGENOM; CLU_006768_0_0_1; -.
DR UniPathway; UPA00375; -.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR Gene3D; 3.30.1960.10; tRNA wybutosine-synthesizing-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR003827; tRNA_yW-synthesising.
DR InterPro; IPR036602; tRNA_yW-synthesising-like_sf.
DR PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23245:SF25; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF02475; Met_10; 1.
DR Pfam; PF02676; TYW3; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF111278; SSo0622-like; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 562..848
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
SQ SEQUENCE 854 AA; 95136 MW; 62BC06A3774EA3B8 CRC64;
MCAVRSTSNT LEVPLAKCSR ILVDENYLSW IVEIANERFR RNEERVNQLR IAFRQQFGQG
VPIPVKAPSN ILYVRPMVDV SLSLRRVGHT IVYHKGHLIV FGGEGYTEND NVRRLSSVQL
LKLSENEKDQ PIIDEQKIAN DDIVRARMYH SSSIDVKSEQ MIVFGGRASP SKAYGDTLAL
CLSTFTWTQI LPDSGGVLTP VIPAARWNHV ACIAGSKLYI HGGRDSSTVF HDLWVLDVAA
PKGKLAWRLL SSELVYAAFD HVGMYVSRQN KLLFWGGLAT LSGIEVARGN ANACYLFDLE
TETWEEKSIG NTKLGPRTTR FGATISALGN ECDVVLIVGG TSASISRVSR AEEPFYALNT
TDLQWQSARI ICEHDSSSLV HSASTWAPQP YNAIYITGGG FQCYGFAYHY ASSVCCVLDA
PMILSTKNVA VNYTQHKQEL STGSLGVLTA RQRVKWMKTL LEKVSVYDKT RRVHEVAGEE
VSAGVYLLPV TSDIHTALST YDELADCVSS TDIVEDSNAL KNKCGKSSGM TRDERIRTII
TRFAHSRDVS ESEIFKSISG GFEYIGDIIL LNSTCCAEKE SWGSFEQEMW ACICEQVVPC
LTRVAREARI DNGEMRRSRV SLIYVNQDRW KQQAVHQEVC NIPNTTESPG WVEVRENGIV
YGLDITKTMF SSGNITEKAR MAGISCKGEI IVDLFCGIGY YVLPFLVHGG ASMVHACDWN
PDAITALQYN LLRNRVSERC TIHEGDNQVS ARKIGPISDR VNLGLLPKSD KAWPLAVQVL
KSSGGWLHVH ENVPKQELKA WIEHVECSIE TLAKEIDRNW IVTCHHVEKV KSYAPRIYHY
VADIHCVAVD STCK
//
