ID A0A2J6PZC9_9HELO Unreviewed; 425 AA.
AC A0A2J6PZC9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=NA56DRAFT_575334 {ECO:0000313|EMBL:PMD19381.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD19381.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD19381.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD19381.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) 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; KZ613489; PMD19381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6PZC9; -.
DR STRING; 1745343.A0A2J6PZC9; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000235672; 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:UP000235672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036959}.
FT DOMAIN 42..237
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT DOMAIN 241..364
FT /note="mRNA capping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03919"
FT REGION 381..425
FT /note="Disordered"
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 425 AA; 48971 MW; B6AA7BB57E112EAB CRC64;
MTGPVASIEA PGIKIDGELL QNMRKEVAHL LGRNNTTFPG AQPVSFARRH LEELTKQDFY
VCEKSDGFRY LLYLTQDDQR GEIHYLIDRK NDYWFIPQGG LHFPIPRDVA GFHINTLIDG
ELVLDKLADG TTQPKYLVFD CMVLDGNSLM NRTLDKRLAY FKERIFDPYK QLLNAYPEEK
QYMHFIVELK SMQFSYAIEM MFRQILPSLP HGNDGLIFTC RMTDYKAGTD PNILKWKPES
ENSVDFRLCL DFPQIQPDEQ DRAEGITEPY YDYDALPICN LHVNVGKGEE DSWYSTMFLE
PSEWESLKSL NQPLNDRIVE CYMDSRKRWR YMRFRDDKTV ANHSSTVESV IESIMDRVTE
KDLIAAAKGI RDEWKRRAAE DVAREKKEAE RKRVATGGNG TIQGAKRKAD EQGGGRPSPG
PPGKP
//
