ID Q4D3H7_TRYCC Unreviewed; 589 AA.
AC Q4D3H7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=RNA guanylyltransferase, putative {ECO:0000313|EMBL:EAN87076.1};
GN ORFNames=Tc00.1047053507511.30 {ECO:0000313|EMBL:EAN87076.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN87076.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN87076.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN87076.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAN87076.1}.
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DR EMBL; AAHK01001093; EAN87076.1; -; Genomic_DNA.
DR RefSeq; XP_808927.1; XM_803834.1.
DR AlphaFoldDB; Q4D3H7; -.
DR SMR; Q4D3H7; -.
DR STRING; 353153.Q4D3H7; -.
DR PaxDb; 353153-Q4D3H7; -.
DR EnsemblProtists; EAN87076; EAN87076; Tc00.1047053507511.30.
DR GeneID; 3539465; -.
DR KEGG; tcr:507511.30; -.
DR eggNOG; ENOG502SHA2; Eukaryota.
DR InParanoid; Q4D3H7; -.
DR OMA; HIIDYVY; -.
DR OrthoDB; 169683at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:InterPro.
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:EAN87076.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 275..456
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
SQ SEQUENCE 589 AA; 66513 MW; F1D09FEAF024A034 CRC64;
MSAFNPDAPA FIPTFLRRTG SNAVGEEELS NEASSPSAKR PLVFLIFGCR GAGKTTQSEL
LAKEYNLLHI SSGNIYRQGK QPFVELRRVL LEEFGEGKKR RYNGLVLDRF VVNSEFDAFY
IQSVLDAVKL PVPFVFMLAI DAKLASKRAE SREDNKTAHQ YWRVVEQKAQ AVTLNTIYAP
IRCLKTIQVT EDATIEDVFG EIKAAIGTQL PANPEGIKLC PAARREAKGM KLIEDYETYM
ELVCCVHAAV GNVSGRKDTA PLSGIGAYLD REYFSFGHKN LRSLLSTFHV TLKADGQRYL
LVKHKRYGYI GFPAAFTHCY DFNKLFDGVE MSCDFPPETQ KFITDKKHDK SVEVLLDTEL
VIHDGNPVFY VLDYLYLGGL EGKKMRFEAR LKILREFFGR LASVTQAVVL KDYVPINMLR
TLLPKWKEAK MPIDGLVFQH NDVYKIGRDR FLVKWKPIEH CTVDFRLANG ILKGDSWTFE
LMVTDDISAN GGFGEIPYEG ALAIIPSTLV QENGLCNGII VELALKDRKE TNEGVSSPQT
TTWWSFRCLR NDKPSPNKHS IVKKIVDLRH LSLEELVDLC EKVPFYGST
//
