GenomeNet

Database: UniProt
Entry: I7MCH8_TETTS
LinkDB: I7MCH8_TETTS
Original site: I7MCH8_TETTS 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system