ID I7MCH8_TETTS Unreviewed; 502 AA.
AC I7MCH8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=mRNA capping enzyme {ECO:0000313|EMBL:EAR83973.1};
GN ORFNames=TTHERM_00760200 {ECO:0000313|EMBL:EAR83973.1};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR83973.1, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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; GG662440; EAR83973.1; -; Genomic_DNA.
DR RefSeq; XP_001031636.1; XM_001031636.3.
DR AlphaFoldDB; I7MCH8; -.
DR STRING; 312017.I7MCH8; -.
DR EnsemblProtists; EAR83973; EAR83973; TTHERM_00760200.
DR GeneID; 7825018; -.
DR KEGG; tet:TTHERM_00760200; -.
DR eggNOG; KOG2386; Eukaryota.
DR HOGENOM; CLU_021710_0_2_1; -.
DR InParanoid; I7MCH8; -.
DR OMA; IVCEKTD; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
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 InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR10367:SF25; DUAL SPECIFICITY PHOSPHATASE CATALYTIC DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_1G03540); 1.
DR PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 2.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT DOMAIN 56..186
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT DOMAIN 238..293
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT REGION 475..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 58789 MW; BEA54E833B7FC3B6 CRC64;
MGDFQILLHR PGNEVIMGEE FNYIQGYLNE FKKEMLIENK ITDPRKIERI DFIGAQPVSM
RNSHADRIRE ERDQADISYI VCEKTDGVRY IMVITNNGYC YLTGRNTSTD SENKYKLNQI
NVQLNKQLFI DENDDEEENL QILEIFDGEL VLDKKGDNYY LKYLVFDCLV HFGEKVSNID
YLNRLTNALY FVQYNNSLYE INGEELPKPQ PFCEFKAKAL SQFLETGETD NFEDSENDLV
ISICVKDFFK IKYCNYLFDN YIPSLPHHND GLIFTKNNSI YKPGTDENII KWKPPSMNTI
DFLLVANQDN ILCGIDEKKS DGNYLLQSRV IDLYVMDNNL ERKNYEITFF DFMIVDPDFF
EEVIQKTSEK EGAKGVVAEC KWIDLDQDKG EIIKKIYTSD TDKILVLPEF PDDSNQDDNR
KWIASQKQTY KENKFSKGWG FDRYRLDKNF SNNKKIAKDI VSSIKENLDS KALMQRLMPN
QHQNSNMGNP NLEPSIQKKQ KR
//