ID A0A509AFX9_PLABA Unreviewed; 1575 AA.
AC A0A509AFX9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=tRNA wybutosine-synthesizing protein, putative {ECO:0000313|EMBL:VUC54440.1};
GN ORFNames=PBANKA_0502800 {ECO:0000313|EMBL:VUC54440.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000313|EMBL:VUC54440.1, ECO:0000313|Proteomes:UP000074855};
RN [1] {ECO:0000313|EMBL:VUC54440.1, ECO:0000313|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANKA {ECO:0000313|EMBL:VUC54440.1,
RC ECO:0000313|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/preaccept-1233682211145405;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
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 -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004797}.
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DR EMBL; LK023120; VUC54440.1; -; Genomic_DNA.
DR STRING; 5823.A0A509AFX9; -.
DR VEuPathDB; PlasmoDB:PBANKA_0502800; -.
DR InParanoid; A0A509AFX9; -.
DR OMA; KCMFCSG; -.
DR OrthoDB; 122704at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000074855; Chromosome 5.
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; 3.30.1960.10; tRNA wybutosine-synthesizing-like; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
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:SF31; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 3 HOMOLOG; 1.
DR Pfam; PF13418; Kelch_4; 2.
DR Pfam; PF02475; Met_10; 1.
DR Pfam; PF02676; TYW3; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000074855};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 1226..1572
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
SQ SEQUENCE 1575 AA; 187728 MW; 2E9EA4CA32BDB38F CRC64;
MYHFLEQKKN VLKIINNESS LFRYVDIYKN CENDVYNIYL NIYKAQKNGI GNDEINNTFK
YSQCCKEIPH DNNKFIEKKV KEIIEKKEII EKENDKSIKK SIDLLIYPCI YEINMNENYF
TSSCCSGRTI IFCEADKSKK ENKKKTISNN NLDTPNSVNG LEVNCKDKQF LSYLKKKYIL
KKFMLTNENE DEKKKYIDIN NYKYFSISEK EPIHRKNVKL FYCSHSHHNL EIDTKNIKKK
LLENWKQDFC YILNQKKYLS KNDENLDTPN KEEFRDIKNK NLIHSFSDNE NIDNYFGLNK
KKIEIKKKKN VYIKFEPFII HVKCIDLFTA LKLLKITQIA GLKQSGILNF NKHVTVAIRG
SMRLEHYLGN LLDIDINKMT ELIDICNNKM SKNIMQLIHF YKCYKEQMYT TNNEFFDINY
KFVCDKNQIN DHANNIGEKK TNNNKPIEIG EMENRCFRKM ENTKNKKTIN MKKRDTNIKQ
INLKKYNVEI LEKGEIININ TESNAVNWSV FPKKNDVHNF FVWGHDMFMD KNKIYLFGGF
TKGVRNNKLK IYDILNKEII INETELPSLA FHVFLKLDDN YAFIFGGRKN PQICSNNVWI
YNIRKNTWNL AKIRYNMSSE HIEKNSKDSE KCENCQYNEV PAPRYRHACV VVKRYKKKGN
NSSVYIFYTY GGVNNSSLIL NDIWKGKITI NEKNDEAYIV WNKKGNYNIQ KNIIPIKNHS
MIYNNKKNII YIIGGNYGKV WEMDKENCII NSSAFEEIEE NNNKQILYNI ENINYIYIYS
IKTNLFHFIK CEGDDKYNFP LCRFSHTCCL IDTNYFVLIG GLNYHRTLND IWIFNMKQNK
WYYLDKFDFN SMYVRSKVVC ENYNIYIIGG GCIIFTFGSF FDLPVHASFR EAIVDIKKCN
SNDMNKGIKK YIYEKKTNIY KNNDIEENKK SSLYVKDIKI KKIEKCKKNG DTSYNSDLYI
IAKDKIFVKE IKNYLENVNN FDKSRKIVFS QFSINNIKKE GFYVPIKRKM DMSTNFLEKI
FLCDNKGIFY MNGKVKNEKT NLKKKLKELF ENFVNNKIKN YLNESGKSLI LRACNKYEII
GNILIFHYMH LKPLIDLCIP YLKESEQNKE GIGLLLLRRR KEKWKKKEKY EKKKKYIDIY
TMMKMKYKYN NLMKLIYIFF VSIKKNFNYY THKKSRNNLK TNLFGGIRRY NKSLFKYLAA
KQNKRKKVIK SFRMYIEEGI ICRNKFLKIH KYGNVKIRMF KHDEICREKI KSIAIYEKIT
GKLRKNKIYL MNGQNLKTIH TENNVMYKLD LSKCMFCSGN GTEKERMKNI FLKKKINIYD
NNNHYMAEDF RENVVDLFCG AGYFTLPLLK FIGDRKINNY YAFDINHHSL SFLKKSIKLN
NIKKKNLYIL KENSFHMSKN DNIIKKCHRI LLGLLPNSKN AWKKGFNLID DKIGGTLHIH
GVAEECYKDN LFFEILNTYE YERYNKTMGI DNTKETNVLE FLKIGKRNRD EKDNNVNKHE
VINKEINHKY SGSNISPRLN FAQYVLIEIF KIAMEDYKIY KTHWEVSISH VEKVKSYAPY
IYHYVVDIEC IPQLK
//
