ID A0A066XLL4_COLSU Unreviewed; 385 AA.
AC A0A066XLL4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=mRNA-capping enzyme subunit alpha {ECO:0000256|ARBA:ARBA00019171};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
DE AltName: Full=GTP--RNA guanylyltransferase {ECO:0000256|ARBA:ARBA00029909};
DE AltName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00030702};
GN ORFNames=CSUB01_05227 {ECO:0000313|EMBL:KDN66915.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66915.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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 -!- SIMILARITY: Belongs to the eukaryotic GTase family.
CC {ECO:0000256|ARBA:ARBA00010237}.
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:KDN66915.1}.
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DR EMBL; JMSE01000878; KDN66915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XLL4; -.
DR STRING; 1173701.A0A066XLL4; -.
DR eggNOG; KOG2386; Eukaryota.
DR HOGENOM; CLU_021710_0_2_1; -.
DR OMA; KDYYVCE; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000027238; 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: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};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 50..244
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT DOMAIN 248..367
FT /note="mRNA capping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03919"
FT ACT_SITE 72
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036959-1"
SQ SEQUENCE 385 AA; 44877 MW; C6A00D5615C48147 CRC64;
MEGVQGPPPE GPIASIAEPG IKADGQLLFD LRREVASLLH RNQTSFPGAQ PVSFARKHLE
ELRNKDYYVC EKSDGIRYLL YLTEDDGREI HYLIDRKNDY WFIKNNSFHF PRKEDLTKFH
TRTLIDGELV MDDTGKGQKE PRFLVFDCLV LDGQDLMSRT LDKRLAYFNE NIYKPYRDLF
KQYPEERDFQ PFLVEMKAMQ LSYGIEMMFR EILPKLRHGN DGLIFTCVSS DYKHGTDPHI
LKWKPPEENT VDCRLRLSFP TVQPGEGDDG VDGPFIDYEA VPQAQLWSFL GDGRYQYFAD
VHISEDEWEI LKGLGDPLND RIVECHKDDL GRWRIIRFRD DKSEANHIST IKSVMESIED
RVTEKDLAEA AKGIKDNWKT RNAKR
//
