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Database: UniProt
Entry: W7AKW6_9APIC
LinkDB: W7AKW6_9APIC
Original site: W7AKW6_9APIC 
ID   W7AKW6_9APIC            Unreviewed;       517 AA.
AC   W7AKW6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE            EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN   ORFNames=C922_03708 {ECO:0000313|EMBL:EUD65981.1};
OS   Plasmodium inui San Antonio 1.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD65981.1, ECO:0000313|Proteomes:UP000030640};
RN   [1] {ECO:0000313|EMBL:EUD65981.1, ECO:0000313|Proteomes:UP000030640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD65981.1,
RC   ECO:0000313|Proteomes:UP000030640};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; KI965475; EUD65981.1; -; Genomic_DNA.
DR   RefSeq; XP_008817519.1; XM_008819297.1.
DR   AlphaFoldDB; W7AKW6; -.
DR   EnsemblProtists; EUD65981; EUD65981; C922_03708.
DR   GeneID; 20038982; -.
DR   VEuPathDB; PlasmoDB:C922_03708; -.
DR   OrthoDB; 49440at2759; -.
DR   Proteomes; UP000030640; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 2.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
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; 2.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 2.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE   4: Predicted;
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   ECO:0000313|EMBL:EUD65981.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EUD65981.1}.
FT   DOMAIN          40..170
FT                   /note="mRNA capping enzyme adenylation"
FT                   /evidence="ECO:0000259|Pfam:PF01331"
FT   DOMAIN          322..379
FT                   /note="mRNA capping enzyme adenylation"
FT                   /evidence="ECO:0000259|Pfam:PF01331"
FT   DOMAIN          383..506
FT                   /note="mRNA capping enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03919"
FT   REGION          171..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  59634 MW;  9576E67714A9E6C4 CRC64;
     MITDIYHPGE KIENEFVKEK IRSKINDMLK WKRKGFPGSN PVSLTKNNIR NLFSKDYLIC
     EKTDGVRYFL FIASNTTFLI DRNYDIFKND IHIPTHDDLH AKQQLTLLDG ELVQDTIFNK
     KKGVEENKIV YLIYDGLFIH RKDVTSLNYL ERLTNVYNFV IVPLKKYRRW TKQRKRSSGP
     TPPSRSAFES DDGNVNHWRS INGSRDDSKN VSANGSKNGS TNEGKNVSAD GSRNVSANIS
     DTGSLRGRVN QMGDKDNSTD QWSDHNDTHP VARSATPSGF EEHSMDRKEA HINSQHDGTP
     IDGQLCDESD ETIPSDEGSL PEEENLPFEI YLKDFYSISQ IKELIQTIKK LPHPSDGIIF
     TPLNYPYRTG NFFELLKWKP LNLNTVDFGI ETIYDQQNFP EKFELFISIR GVRTSYRTYL
     AEYGDVYKEL LTLALNNKIS HYIIECYYVA KHIFSIFKNE NGMEEKIEGG WIAQKIRFDK
     NIPNDISTLN KVIQSILDNI TIDSLIKEIS RNRRGKR
//
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