ID Q381X9_TRYB2 Unreviewed; 586 AA.
AC Q381X9;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=RNA guanylyltransferase {ECO:0000313|EMBL:EAN80402.1};
GN ORFNames=Tb11.01.6190 {ECO:0000313|EMBL:EAN80402.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000313|EMBL:EAN80402.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:EAN80402.1, ECO:0000313|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN80402.1,
RC ECO:0000313|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
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DR EMBL; CH464491; EAN80402.1; -; Genomic_DNA.
DR RefSeq; XP_829514.1; XM_824421.1.
DR AlphaFoldDB; Q381X9; -.
DR SMR; Q381X9; -.
DR STRING; 185431.Q381X9; -.
DR PaxDb; 5691-EAN80402; -.
DR GeneID; 3665334; -.
DR KEGG; tbr:Tb11.01.6190; -.
DR VEuPathDB; TriTrypDB:Tb927.11.14580; -.
DR eggNOG; ENOG502SHA2; Eukaryota.
DR InParanoid; Q381X9; -.
DR OrthoDB; 169683at2759; -.
DR Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0019002; F:GMP binding; IDA:GeneDB.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IBA:GO_Central.
DR GO; GO:0008192; F:RNA guanylyltransferase activity; IDA:GeneDB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0036260; P:RNA capping; IDA:GeneDB.
DR CDD; cd07895; Adenylation_mRNA_capping; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR PANTHER; PTHR10367:SF17; MRNA-CAPPING ENZYME; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EAN80402.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 282..452
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
SQ SEQUENCE 586 AA; 66942 MW; 136C0575EFF31593 CRC64;
MSATDVASEL RSGAPEYVPT FLRCKQSENV TAFESPVVFL MFGCRGAGKS TQSTLLSKTY
NLLYLSSGDI YKSGKQPFVE LRKILNEHFG DGKERVYNGV VLDRFIANSE FEAFYVQTAL
RSVGLPVPFV FMLAIDQGLA AKRAEERGDN KGGNQRWRAV EQKAQAITAN TVYAPIQCLK
TIRVESDMTI DDVFNEIKTT IANQLPPDLF NLQLPREARR EVEGTVLVED YELYMELAND
VHTVVGNLRG RRDSAPLSNV GAHLDKEYFS FANKRLRSQL TTMHVTLKAD GLRFLVMKHK
TRGYIGFPSA FTHCYELNDL FEGVEMAPKP YTELKKWMND KSCELPADFL LDTEVVVHEK
KPTLYIIDFI YFWGLDGRRM QFEQRLKVLR EYFGDMKPQG QVIAMKDYVP INKIRTLVEE
MKRRTELPVD GLIFQHNGSY RFGSDKFLIK WKPVHLCTVD FRLANGRVEN GVWTFDLFVT
DDFIEENGFR EVAYPGATAL IPASVVEENG LQNGMIIEMA LSEKESVKKT SPNAPSEKTR
WTFRNARNDK PSPNKYSIVT RICELMHVDL DELVSLCEKV PFYRNV
//
