TYW4_CANAL
ID TYW4_CANAL Reviewed; 689 AA.
AC Q5A931; A0A1D8PCE0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=tRNA wybutosine-synthesizing protein 4;
DE Short=tRNA-yW synthesizing protein 4;
DE EC=2.1.1.290;
DE EC=2.3.1.231;
DE AltName: Full=Leucine carboxyl methyltransferase 2;
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase;
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase;
GN Name=PPM2; Synonyms=TYW4; OrderedLocusNames=CAALFM_C101150CA;
GN ORFNames=CaO19.10813, CaO19.3303;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 (By similarity). {ECO:0000250}.
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 -!- 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 -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000305}.
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DR EMBL; CP017623; AOW25810.1; -; Genomic_DNA.
DR RefSeq; XP_718126.1; XM_713033.1.
DR AlphaFoldDB; Q5A931; -.
DR SMR; Q5A931; -.
DR STRING; 237561.Q5A931; -.
DR GeneID; 3640203; -.
DR KEGG; cal:CAALFM_C101150CA; -.
DR CGD; CAL0000175964; orf19.10813.
DR VEuPathDB; FungiDB:C1_01150C_A; -.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_002761_0_0_1; -.
DR InParanoid; Q5A931; -.
DR OMA; WEVDFPD; -.
DR OrthoDB; 1094856at2759; -.
DR UniPathway; UPA00375; -.
DR PRO; PR:Q5A931; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0031591; P:wybutosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF04072; LCM; 1.
DR SMART; SM00612; Kelch; 1.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..689
FT /note="tRNA wybutosine-synthesizing protein 4"
FT /id="PRO_0000226139"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 183..184
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 689 AA; 78835 MW; 2C5A85C9C94E1104 CRC64;
MTSTSKLDAN QLARQRKKLE KDRRKKVYDD QQVQGTNNSS IVSKRSVEKL YTQVLQPELG
EWFQYFVPKG KRRSPAINRG YWIRMESIRQ MVIRIIKANS PNVRINVVNL GCGFDPLAFQ
LLSLFKNQYN LNFIDIDYPD LVKNKYNMIQ QSDEIKQLIG DQGSKSSDLY VMETDNYQLV
GCDLKNLAYY KEILPKLVSR NVDPHPTSIN IFIAEVSLAY MKPQFANPVI EISSQVNNSH
FLILEQIMPD GATNAFATKM LYHFQHLRSP IQCVETYPTE KLQLQRFKRY YKHAEIKNLY
GNWKFLIDYQ MQKNISTIEE FDEWEEFIIF CQHYVIVHAT HMDQLIYDDE SSEEQKNEKA
FSEMSLDSSV AISHDDRFND EQLQLKFPAI ASFKDKIYVN GGLKQTRNDE NLEIDLQTGV
ITKLDQTENL PTARMCHTLT NLGENLVLIG GRSRPGVFFK DVYMFDTAKK WTRLADLPVG
RSRHATVKIS DHEVLIFGGL DASSSTTGDE LFLLCNTNTN SYTPVKPIGD NDNHPIKNLQ
SACMIFDGKQ GYIFGGMEDI NVPIVNSKLY RFELVGENNI SVTKVFDHSL LKRIGSKAHI
LENGDKLLIV GGVSPDQLFT KSTNIVTLDL NIFTFKSVEI PNVISEKVPP IFVGFELVQI
NNKASYIISG GAVCYSFGSC YNSVYKLEY
