MCE1_SCHPO
ID MCE1_SCHPO Reviewed; 402 AA.
AC P40997;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 148.
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};
GN Name=ceg1; Synonyms=pce1; ORFNames=SPBC2F12.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7991582; DOI=10.1073/pnas.91.25.12046;
RA Shuman S., Liu Y., Schwer B.;
RT "Covalent catalysis in nucleotidyl transfer reactions: essential motifs in
RT Saccharomyces cerevisiae RNA capping enzyme are conserved in
RT Schizosaccharomyces pombe and viral capping enzymes and among
RT polynucleotide ligases.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12046-12050(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fresco L.D., Woo S., Buratowski S.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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.
CC -!- SIMILARITY: Belongs to the eukaryotic GTase family. {ECO:0000305}.
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DR EMBL; U16143; AAA64996.1; -; Genomic_DNA.
DR EMBL; U18811; AAA58715.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB10156.1; -; Genomic_DNA.
DR PIR; T40133; T40133.
DR RefSeq; NP_595708.1; NM_001021605.2.
DR PDB; 4PZ6; X-ray; 2.41 A; A/B=1-402.
DR PDB; 4PZ7; X-ray; 2.11 A; A/B=1-402.
DR PDB; 4PZ8; X-ray; 3.10 A; A=1-402.
DR PDBsum; 4PZ6; -.
DR PDBsum; 4PZ7; -.
DR PDBsum; 4PZ8; -.
DR AlphaFoldDB; P40997; -.
DR SMR; P40997; -.
DR BioGRID; 276891; 3.
DR STRING; 4896.SPBC2F12.08c.1; -.
DR iPTMnet; P40997; -.
DR MaxQB; P40997; -.
DR PaxDb; P40997; -.
DR PRIDE; P40997; -.
DR EnsemblFungi; SPBC2F12.08c.1; SPBC2F12.08c.1:pep; SPBC2F12.08c.
DR GeneID; 2540362; -.
DR KEGG; spo:SPBC2F12.08c; -.
DR PomBase; SPBC2F12.08c; ceg1.
DR VEuPathDB; FungiDB:SPBC2F12.08c; -.
DR eggNOG; KOG2386; Eukaryota.
DR HOGENOM; CLU_021710_0_2_1; -.
DR InParanoid; P40997; -.
DR OMA; KDYYVCE; -.
DR PhylomeDB; P40997; -.
DR BRENDA; 2.7.7.50; 5613.
DR Reactome; R-SPO-72086; mRNA Capping.
DR Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:P40997; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IPI:PomBase.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISO:PomBase.
DR GO; GO:0009452; P:7-methylguanosine RNA capping; IDA:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; GTP-binding; mRNA capping; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..402
FT /note="mRNA-capping enzyme subunit alpha"
FT /id="PRO_0000210104"
FT REGION 374..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250"
FT MUTAGEN 67
FT /note="K->A: Loss of function."
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:4PZ8"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:4PZ8"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 137..149
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4PZ8"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4PZ6"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:4PZ7"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:4PZ7"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:4PZ7"
SQ SEQUENCE 402 AA; 46875 MW; 76B1E2052DABB974 CRC64;
MAPSEKDIEE VSVPGVLAPR DDVRVLKTRI AKLLGTSPDT FPGSQPVSFS KKHLQALKEK
NYFVCEKSDG IRCLLYMTEH PRYENRPSVY LFDRKMNFYH VEKIFYPVEN DKSGKKYHVD
TLLDGELVLD IYPGGKKQLR YLVFDCLACD GIVYMSRLLD KRLGIFAKSI QKPLDEYTKT
HMRETAIFPF LTSLKKMELG HGILKLFNEV IPRLRHGNDG LIFTCTETPY VSGTDQSLLK
WKPKEMNTID FMLKLEFAQP EEGDIDYSAM PEFQLGVWEG RNMYSFFAFM YVDEKEWEKL
KSFNVPLSER IVECYLDDEN RWRFLRFRDD KRDANHISTV KSVLQSIEDG VSKEDLLKEM
PIIREAYYNR KKPSVTKRKL DETSNDDAPA IKKVAKESEK EI
