ID A0A2G8RSB1_9APHY Unreviewed; 446 AA.
AC A0A2G8RSB1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=GSI_13981 {ECO:0000313|EMBL:PIL24228.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL24228.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL24228.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL24228.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
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:PIL24228.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYKW01000067; PIL24228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8RSB1; -.
DR STRING; 1077348.A0A2G8RSB1; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000230002; 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:0003910; F:DNA ligase (ATP) activity; 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 GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR012310; DNA_ligase_ATP-dep_cent.
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.
DR PROSITE; PS50160; DNA_LIGASE_A3; 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:UP000230002};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036959}.
FT DOMAIN 135..237
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 369..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 63
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036959-1"
SQ SEQUENCE 446 AA; 51344 MW; 095629768487E59B CRC64;
MPRIPDIPGN AVAHNSDQEH WLKRHVASLC HLDHERFPGS QPVSFAARDL DKLEAQDYWV
AEKSDGIRVL LLIHADTNTC DQMVYLIDRH NSYRQLTGLY FPHHGDPRNP LRDTLVDGEL
VIDVHPHTKQ ETLRYLAFDC LVADQQNVMS RPLDKRYGRL QQWVYEPYRK MMRDHPHMAL
QQPFEFKVKE VKFSYRVEDV FNIDIPHLQH GNDGLIYTCV STPYAPGTDP NILKWKPPSE
NSIDFKLVLR FAPTPGKPKV PDFQTKPIFE LHVWCGDDRG VPRYEFYDVM HVADDEWERM
KTSNEQLDDR VVEVHWDPAH EHWRMMRFRD DKPHGNHKSV VDNIIKSIAD GIEKDALLSR
SAAIRNNWKA RAAPGGPPPP PPPQKGGHAP PHSYSHPQKP VPPPPLPLAA QRARPDAPHV
EQRYSRLAPS PWSKVTGPPM VGGMYR
//
