ID B6JYQ9_SCHJY Unreviewed; 415 AA.
AC B6JYQ9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=mRNA-capping enzyme subunit alpha {ECO:0000256|ARBA:ARBA00019171, ECO:0000256|PIRNR:PIRNR036959};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475, ECO:0000256|PIRNR:PIRNR036959};
DE AltName: Full=GTP--RNA guanylyltransferase {ECO:0000256|ARBA:ARBA00029909, ECO:0000256|PIRNR:PIRNR036959};
DE AltName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00030702, ECO:0000256|PIRNR:PIRNR036959};
GN Name=ceg1 {ECO:0000313|JaponicusDB:SJAG_01724};
GN ORFNames=SJAG_01724 {ECO:0000313|EMBL:EEB06677.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB06677.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB06677.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- FUNCTION: Second step of mRNA capping. Transfer of the GMP moiety of
CC GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction
CC intermediate. {ECO:0000256|PIRNR:PIRNR036959}.
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 -!- SUBUNIT: Heterodimer. {ECO:0000256|PIRNR:PIRNR036959}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR036959}.
CC -!- SIMILARITY: Belongs to the eukaryotic GTase family.
CC {ECO:0000256|ARBA:ARBA00010237, ECO:0000256|PIRNR:PIRNR036959}.
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DR EMBL; KE651168; EEB06677.1; -; Genomic_DNA.
DR RefSeq; XP_002172970.1; XM_002172934.1.
DR AlphaFoldDB; B6JYQ9; -.
DR STRING; 402676.B6JYQ9; -.
DR EnsemblFungi; EEB06677; EEB06677; SJAG_01724.
DR GeneID; 7049889; -.
DR JaponicusDB; SJAG_01724; ceg1.
DR VEuPathDB; FungiDB:SJAG_01724; -.
DR eggNOG; KOG2386; Eukaryota.
DR HOGENOM; CLU_021710_0_2_1; -.
DR OMA; KDYYVCE; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IBA:GO_Central.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IEA:EnsemblFungi.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0008033; P:tRNA processing; IEA:EnsemblFungi.
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; IPR017075; mRNA_cap_enzyme_alpha.
DR InterPro; IPR013846; mRNA_cap_enzyme_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR PANTHER; PTHR10367:SF17; MRNA-CAPPING ENZYME; 1.
DR Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR PIRSF; PIRSF036959; mRNA_cap_alpha; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR036959};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042,
KW ECO:0000256|PIRNR:PIRNR036959};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR036959};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036959};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR036959}; Nucleus {ECO:0000256|PIRNR:PIRNR036959};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036959}.
FT DOMAIN 41..237
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT DOMAIN 242..353
FT /note="mRNA capping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03919"
FT REGION 369..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 63
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036959-1"
SQ SEQUENCE 415 AA; 48525 MW; 8285A1E42DE6DB47 CRC64;
MELTPPAIIP GSKIPHKDAN ILRERVSRLL GLRSLNFPGA QPVSFAKKHL QTVKEHDYYV
CEKSDGIRCL MYMTMHHATP KRYAVYLIDR KNDYYLVPKV WFPTTNDPND SRLHTETLID
GELVMDSIQG KSQLKFLVFD CLACNGRLYT NRPLDRRLGV YREFVEKPLR TLVKAKPKVL
AVMPFHVEFK LMQRAHGIEM MFREIIPKLH HGSDGLIFTC IETPYVTGTD ETLLKWKSRE
SNTVDFLLEL RFTAKLDTGD IDYSAMPEMP LSIWEGGKRY SYFADLYLEN EEWEKLKESN
TPLQGRIVEC YLDEQNRWRF MRFRDDKQNG NHRSTVRSVI ESIEDGVTKE ELLHEAYYIR
KSYYERKERR EARHHDNPET HSVREASKEP AASGAEKRKL TPESEESTKR ARAAD
//
