MCE1_NEUCR
ID MCE1_NEUCR Reviewed; 402 AA.
AC Q7SB53; U9W4P3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=mRNA-capping enzyme subunit alpha;
DE AltName: Full=GTP--RNA guanylyltransferase;
DE Short=GTase;
DE AltName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.50 {ECO:0000250|UniProtKB:Q01159};
DE AltName: Full=mRNA processing protein 2;
GN Name=rnp-2; ORFNames=NCU06260;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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:0000250|UniProtKB:Q01159}.
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:0000250|UniProtKB:Q01159};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000250|UniProtKB:Q01159};
CC -!- SUBUNIT: Heterodimer. The mRNA-capping enzyme is composed of two
CC separate chains alpha and beta, respectively a mRNA guanylyltransferase
CC and an mRNA 5'-triphosphate monophosphatase.
CC {ECO:0000250|UniProtKB:Q01159}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic GTase family. {ECO:0000305}.
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DR EMBL; CM002238; ESA43219.1; -; Genomic_DNA.
DR RefSeq; XP_011393903.1; XM_011395601.1.
DR AlphaFoldDB; Q7SB53; -.
DR SMR; Q7SB53; -.
DR STRING; 5141.EFNCRP00000005948; -.
DR EnsemblFungi; ESA43219; ESA43219; NCU06260.
DR GeneID; 3879017; -.
DR KEGG; ncr:NCU06260; -.
DR VEuPathDB; FungiDB:NCU06260; -.
DR HOGENOM; CLU_021710_0_2_1; -.
DR InParanoid; Q7SB53; -.
DR OMA; KDYYVCE; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IEA:InterPro.
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 CDD; cd07895; Adenylation_mRNA_capping; 1.
DR Gene3D; 2.40.50.140; -; 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 Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR PIRSF; PIRSF036959; mRNA_cap_alpha; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 3: Inferred from homology;
KW GTP-binding; mRNA capping; mRNA processing; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..402
FT /note="mRNA-capping enzyme subunit alpha"
FT /id="PRO_0000210103"
FT ACT_SITE 66
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 402 AA; 46572 MW; 9A3862BF446C0F60 CRC64;
MEQPGPITDI AKPGIKAPRD LAISLREEVA RILGRSSIGF PGAQPVSFAR KHLEELRRED
YYVCEKSDGI RYLLYLTVDE EGQEVQYLID RKNDYWFLPR NSMHFPMPND IQAFHRGTII
DGELVMDTVP GTNGRKEPRF LVFDLLALDD KAELLNKPLD KRLGYFSAYI YEPYKKLLQQ
FPQEIPFMAF KVEMKRMELS YGIETMFREV IPALKHDSDG LIFTCRTTPY HFGTDPHILK
WKAPHENTLD FRMRLNFPLV QATEAELDEG FPEQFTDYDS VPQAELYVFC GNDGPGGSKY
ELFPDPLYIA EDEWETLKAL GDPLQDRVVE CCLDAENRWR LFRFRDDKNE ANHTSTVSSV
MASIRDGVSD QELLSAATAI KESWKIRAQK RKEQQQQQQP KH
