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Database: UniProt
Entry: A0A2H0ZGV2_CANAR
LinkDB: A0A2H0ZGV2_CANAR
Original site: A0A2H0ZGV2_CANAR 
ID   A0A2H0ZGV2_CANAR        Unreviewed;       479 AA.
AC   A0A2H0ZGV2; A0A5Q7YL75;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=B9J08_004874 {ECO:0000313|EMBL:PIS49847.1};
OS   Candida auris (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS49847.1, ECO:0000313|Proteomes:UP000230249};
RN   [1] {ECO:0000313|EMBL:PIS49847.1, ECO:0000313|Proteomes:UP000230249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B8441 {ECO:0000313|EMBL:PIS49847.1,
RC   ECO:0000313|Proteomes:UP000230249};
RX   PubMed=27988485; DOI=.1093/cid/ciw691;
RA   Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA   Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA   Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA   Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT   "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT   continents confirmed by whole-genome sequencing and epidemiological
RT   analyses.";
RL   Clin. Infect. Dis. 64:134-140(2017).
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:PIS49847.1}.
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DR   EMBL; PEKT02000009; PIS49847.1; -; Genomic_DNA.
DR   STRING; 498019.A0A2H0ZGV2; -.
DR   EnsemblFungi; B9J08_004874-t37_1; B9J08_004874-t37_1-p1; B9J08_004874.
DR   VEuPathDB; FungiDB:B9J08_004874; -.
DR   VEuPathDB; FungiDB:CJI96_0004279; -.
DR   VEuPathDB; FungiDB:CJI97_004578; -.
DR   VEuPathDB; FungiDB:CJJ07_000746; -.
DR   VEuPathDB; FungiDB:CJJ09_004895; -.
DR   VEuPathDB; FungiDB:QG37_06650; -.
DR   OMA; KDYYVCE; -.
DR   OrthoDB; 49440at2759; -.
DR   Proteomes; UP000230249; 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; 3.30.1490.430; -; 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:UP000230249};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   479 AA;  55586 MW;  ED41477687A221B8 CRC64;
     MIQLGDRDMP EIPGTKLAGE ELHELRLMLA DLLKRRNTSF PGSQPVSFER HHLEVLKNRD
     YFVCEKSDGL RCLLFLVHDP ARGEGVFLVT RENEFYHIPG IHFPSQVNEE NGETFHHGTL
     LDGELVLETK NVSEPFLRYC IFDALVVNEK DVTNRPLPKR LGYITEHVMK PFDSFKARHP
     EIVNSADFPF KVSFKMMKSS YRANVVLAMQ DQLFHESDGL IFTCAETPYI FGTDATLLKW
     KPAHENTIDF KMSMVFKSFQ DPDMDPRDPD STYTDYDSKP EQFKLSVWKG GKEYEEFAEL
     DMPEEDWEQL KELNEPLQGR IIECRKNIDN PPYWEMLRFR NDKSNGNHYT IVEKILHSIA
     DGVTEQELKA ACPSIEKAWK QREFERAQKA KQGQHHPPAP TSQHHQHHSS VHHQHQTGPQ
     PNLKSISPRT SPQQQKRRPS ETENSVPRKV QKNNNVTNSD EAKMLQDMMP DYEEESDSE
//
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