ID A0A0L1IVE5_ASPNO Unreviewed; 415 AA.
AC A0A0L1IVE5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ANOM_008469 {ECO:0000313|EMBL:KNG83449.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG83449.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG83449.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG83449.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG83449.1}.
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DR EMBL; JNOM01000267; KNG83449.1; -; Genomic_DNA.
DR RefSeq; XP_015404372.1; XM_015553725.1.
DR AlphaFoldDB; A0A0L1IVE5; -.
DR STRING; 1509407.A0A0L1IVE5; -.
DR GeneID; 26810273; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000037505; 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 Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036959}.
FT DOMAIN 42..242
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT DOMAIN 246..368
FT /note="mRNA capping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03919"
FT REGION 377..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 64
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036959-1"
SQ SEQUENCE 415 AA; 48403 MW; A70BC54ACB0C12AC CRC64;
MSNSVPDLDA VGIKAEPELA DQFRREVATL LGRNNLNFPG AQPVSFSSKH LLELQRQDYY
VCEKTDGIRC LMYFARGDPE SETPEIHYLI DRKNDYRYVP GLHFPLPNDE SFQSYHVDTL
VDGELVNDTY EDGTQQLKYL VFDCLVLDGQ SLMHRTLDKR LAYFKEKVLK PYNALYHRFP
EEKQHRVFAV EDKSTQFSYG IEMMFREIIP KVKKIHGNDG LIFTCRSTPY RIGTDEHILK
WKPPAENTID FRMRLEFPVL EPDTDDEADG ISEPYTDYDA MPIFHLFVML NSNEYRHFAE
MFVTPSEWEE LKALGLPLDD SIVECSKDEH NRWRYHRLRD DKADANHIST VEKVLESIQD
RVTEEDLIQA APAIKASWKK RQAQMASEDE ERKRRARQAP PHANGNGVKR KFEDS
//
