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Database: UniProt
Entry: E9DD44_COCPS
LinkDB: E9DD44_COCPS
Original site: E9DD44_COCPS 
ID   E9DD44_COCPS            Unreviewed;       409 AA.
AC   E9DD44;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=CPSG_08006 {ECO:0000313|EMBL:EFW15569.1};
OS   Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN   [1] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
RN   [2] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA   Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA   Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Coccidioides posadasii strain Silveira.";
RL   Submitted (MAR-2010) 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; GL636500; EFW15569.1; -; Genomic_DNA.
DR   STRING; 443226.E9DD44; -.
DR   VEuPathDB; FungiDB:CPSG_08006; -.
DR   VEuPathDB; FungiDB:D8B26_002329; -.
DR   eggNOG; KOG2386; Eukaryota.
DR   HOGENOM; CLU_021710_0_2_1; -.
DR   OMA; KDYYVCE; -.
DR   Proteomes; UP000002497; 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:UP000002497};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036959}.
SQ   SEQUENCE   409 AA;  47866 MW;  D982B1C1CBE212A1 CRC64;
     MANTVPDLDS VGIKAEPELA DQFRREVAHL LGRSSLNFPG AQPVSFSSRH LLELQKQDYY
     VCEKTDGIRC LMYFARGDPD SDTPEIHYLI DRKNDYRYVP GLHFPMPDDE SFQSFHVDTI
     VDGELVNDIY EDGTEQLKFY VFDCLVLDGT SLMHRTLDKR LAYFKEKVLK PYNAMYKKFP
     EERQHRAFAV EDKSTQFSYG IEMMFRDIIP KVKKIHGNDG LIFTCRGTPY KIGTDEHILK
     WKPPEENSID FRMRLEFPMV EPDSEDESAG VTEAYPDYDA IPICHLFVFY RQNDYRHFGL
     MHLEESEWDE LKALQKPLDD TIVECYRDEH GRWRFLRFRE DKADANHIST VEKVLESIED
     RVTEEDLIRA APAIKTAWKK RQADEEAARR KPNGVPHPSV NGVKRKYEE
//
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