ID Q4QBY5_LEIMA Unreviewed; 1037 AA.
AC Q4QBY5;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000256|ARBA:ARBA00011926};
DE EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926};
GN ORFNames=LMJF_22_0090 {ECO:0000313|EMBL:CAJ03800.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ03800.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ03800.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAJ03800.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56;
CC Evidence={ECO:0000256|ARBA:ARBA00024288};
CC -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC guanylyltransferase family. {ECO:0000256|ARBA:ARBA00008556}.
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DR EMBL; FR796418; CAJ03800.1; -; Genomic_DNA.
DR RefSeq; XP_001683163.1; XM_001683111.1.
DR AlphaFoldDB; Q4QBY5; -.
DR STRING; 5664.Q4QBY5; -.
DR EnsemblProtists; CAJ03800; CAJ03800; LMJF_22_0090.
DR GeneID; 5651765; -.
DR KEGG; lma:LMJF_22_0090; -.
DR VEuPathDB; TriTrypDB:LmjF.22.0090; -.
DR VEuPathDB; TriTrypDB:LMJFC_220006500; -.
DR VEuPathDB; TriTrypDB:LMJLV39_220005900; -.
DR VEuPathDB; TriTrypDB:LMJSD75_220006000; -.
DR eggNOG; KOG1975; Eukaryota.
DR HOGENOM; CLU_293292_0_0_1; -.
DR InParanoid; Q4QBY5; -.
DR OMA; CESECFT; -.
DR Proteomes; UP000000542; Chromosome 22.
DR GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:GeneDB.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0036260; P:RNA capping; ISO:GeneDB.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013846; mRNA_cap_enzyme_C.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189:SF2; MRNA CAP GUANINE-N7 METHYLTRANSFERASE; 1.
DR PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1.
DR Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF03291; mRNA_G-N7_MeTrfase; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CAJ03800.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 712..1031
FT /note="MRNA cap 0 methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51562"
SQ SEQUENCE 1037 AA; 114823 MW; 414B93DF83ACF942 CRC64;
MQLQSLKALS EARKDAPHHR WCCHANDAWY NAVHADGAAG VSDAQMTDVE AALEGMLNDA
SPLCAEMLQC VLRHANVTPN PNDAEFPGPM CTPLCKKDTA RLRQHAYTVT EKSDGIRVVV
VSLWTPRFPA WVADSAADAV SASVNLSHLA SVLALERARR ALRRYAGQGE DAAVRATISL
GGRSCTLELL STLEPCESEC FTLRVATAAD DASPSTMVTL HRHRRGRHFA YAVDRSLDAA
YLFMDDHTTL QYHTFVLDAE LMSVHRSAAA SPAVPRLVLG VFDLFAYAGA ADNVLVNLAK
RSMVERYDAL KAVVHTCALP VSTGECGYVS WYVKDMWALA DIGACLAKLR YSAESQCFLY
DGPHGPTEND GLIFTPDEFP VAVGSSSLQL KWKWQHLLSI DWLLQASDKQ PDMYTVSLFF
VKKNYGHRED VAGHWRLRKP MHILNPHGFE MPVDAAIVAE CAYDEATQRW YIQRLRPDKL
GANSIITAIS VYESLVENIS LPHLLELLQV DAEKAKGQAD TLESAARARV GTASKALETV
SSALDTIEAE NCVTAKLALR AIRESRGNTE LYLITYTNNT NKTVLYPLPF PLRKIRDCIG
LGYHPGIRDG TPVPSLEEAL YIQLANAGGC YAWSDYVVDA FYAGDSGYWE IIHANPRGNN
KEAIFDNVIE HLDWLLRHRT APETATLLER KRDAPLVVSR PHSSEATQQT SRHYSTVAKE
LANEERSDLR RFNNWVKSVL LTTMAAAIRR ALKPPAKLHV LDLCCGRGGD LLKWQHIHPA
FLFMTDASVE CVAEAAARYS TSEGQSVKVA KGKQKGFPAF FAVHDAFHAA SGLREDLLKR
GPFQLASCQF SMHYGCRSQE SMRYFVKAIA DSLVPHGRFV GTTVSDVELL YRAKEHGAEF
GNDVYGVRFG AEAFAQLQSA NFEPAALSFG VPYAATVERS VQDMTEYVVP WDAFVALCAE
HQLKLVLEDN FIHYYGQHKD TEAGKAMTLE QRRKRHNDGD VVDCPLSPSE QAAVGLYRLF
VFEKTKAKQS SCGTAER
//
