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Database: UniProt
Entry: A0A0D2F5C3_9EURO
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ID   A0A0D2F5C3_9EURO        Unreviewed;       402 AA.
AC   A0A0D2F5C3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   ORFNames=PV04_09951 {ECO:0000313|EMBL:KIW63073.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW63073.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW63073.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW63073.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846962; KIW63073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2F5C3; -.
DR   STRING; 5601.A0A0D2F5C3; -.
DR   HOGENOM; CLU_021710_0_2_1; -.
DR   OrthoDB; 49440at2759; -.
DR   Proteomes; UP000054266; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036959}.
FT   DOMAIN          56..250
FT                   /note="mRNA capping enzyme adenylation"
FT                   /evidence="ECO:0000259|Pfam:PF01331"
FT   DOMAIN          254..374
FT                   /note="mRNA capping enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03919"
FT   ACT_SITE        78
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036959-1"
SQ   SEQUENCE   402 AA;  47570 MW;  C063C05F8F059C34 CRC64;
     MDGHPASEIK GPEANPLLER IGGIWAGRTP GLQEEFQREV AQLLGRGRNL SFPGAQPVSF
     SAEHIQELKT QDYYVCEKTD GLRYLMYLTR EGEHDIHYLI DRKNDYWFVP YLHFPHHEDK
     TFERFHTDTI LDGELVEDRY PDRPPVIKFL VFDCLVLDKQ VLMQRPLDKR LAYFKSHVLG
     PYKEMYKQQP DRPQPFVLED KATEFSYGLE KMFKEIIPKV KQLHGNDGLI FTCRNTPYKT
     GTDEHILKWK PPSENTVDFL LHIEWPKMDP DPDDPDRSPQ PDYYAFPSRF SLYIHHGSNE
     YSYIDDLYVE PQEYEEWKAL GHPLQDIIIE AAKDDEQRWR YHRFRHDKDQ SNHIKVYKSV
     IRSIQSHVTE QDLLDHAGDI RSAWKARDEE RKRLQGGVKR DT
//
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