MCE1_CANAX
ID MCE1_CANAX Reviewed; 449 AA.
AC P78587;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=CGT1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060 / 2024;
RX PubMed=8828219; DOI=10.1099/00221287-142-9-2515;
RA Yamada-Okabe T., Shimmi O., Doi R., Mizumoto K., Arisawa M.,
RA Yamada-Okabe H.;
RT "Isolation of the mRNA-capping enzyme and ferric-reductase-related genes
RT from Candida albicans.";
RL Microbiology 142:2515-2523(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-395.
RX PubMed=12820968; DOI=10.1016/s1097-2765(03)00187-4;
RA Fabrega C., Shen V., Shuman S., Lima C.D.;
RT "Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-
RT terminal domain of RNA polymerase II.";
RL Mol. Cell 11:1549-1561(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.
CC -!- SIMILARITY: Belongs to the eukaryotic GTase family. {ECO:0000305}.
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DR EMBL; D83180; BAA11833.1; -; Genomic_DNA.
DR PDB; 1P16; X-ray; 2.70 A; A/B=2-395.
DR PDBsum; 1P16; -.
DR AlphaFoldDB; P78587; -.
DR SMR; P78587; -.
DR CGD; CAL0000174743; CGT1.
DR VEuPathDB; FungiDB:C4_05760W_A; -.
DR VEuPathDB; FungiDB:CAWG_03247; -.
DR PhylomeDB; P78587; -.
DR EvolutionaryTrace; P78587; -.
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; IDA:CGD.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IGI:CGD.
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; 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; Transferase.
FT CHAIN 1..449
FT /note="mRNA-capping enzyme subunit alpha"
FT /id="PRO_0000210099"
FT REGION 384..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000255"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:1P16"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 119..130
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 138..149
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 219..229
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1P16"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:1P16"
FT HELIX 367..389
FT /evidence="ECO:0007829|PDB:1P16"
SQ SEQUENCE 449 AA; 52253 MW; D93F44BF112305BB CRC64;
MIQLEEREIP VIPGNKLDEE ETKELRLMVA ELLGRRNTGF PGSQPVSFER RHLEETLMQK
DYFVCEKTDG LRCLLFLIND PDKGEGVFLV TRENDYYFIP NIHFPLSVNE TREKPTYHHG
TLLDGELVLE NRNVSEPVLR YVIFDALAIH GKCIIDRPLP KRLGYITENV MKPFDNFKKH
NPDIVNSPEF PFKVGFKTML TSYHADDVLS KMDKLFHASD GLIYTCAETP YVFGTDQTLL
KWKPAEENTV DFQLEFVFNE VQDPDLDERD PTSTYLDYDA KPNLIKLRVW QGSNVHTDFA
KLDLSDDDWE RLKALEQPLQ GRIAECRQST TKKGYWEMLR FRNDKSNGNH ISVVEKILVS
IKDGVKEKEV IEWCPKISRA WKKRENDRRQ KHFNGVARPA SVSHEEPLRK KIKTESNGNG
HQTPPRQEQQ QQSQQILNDI PTYEDSDDE
