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Database: UniProt
Entry: A0A061HBJ5_9BASI
LinkDB: A0A061HBJ5_9BASI
Original site: A0A061HBJ5_9BASI 
ID   A0A061HBJ5_9BASI        Unreviewed;       496 AA.
AC   A0A061HBJ5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE            EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN   ORFNames=PFL1_04278 {ECO:0000313|EMBL:EPQ27951.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27951.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ27951.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27951.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KE361636; EPQ27951.1; -; Genomic_DNA.
DR   RefSeq; XP_007879996.1; XM_007881805.1.
DR   AlphaFoldDB; A0A061HBJ5; -.
DR   GeneID; 19318384; -.
DR   KEGG; pfp:PFL1_04278; -.
DR   eggNOG; KOG2386; Eukaryota.
DR   HOGENOM; CLU_021710_0_2_1; -.
DR   OrthoDB; 49440at2759; -.
DR   Proteomes; UP000053664; Unassembled WGS sequence.
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; 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   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE   4: Predicted;
KW   mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          46..247
FT                   /note="mRNA capping enzyme adenylation"
FT                   /evidence="ECO:0000259|Pfam:PF01331"
FT   DOMAIN          251..390
FT                   /note="mRNA capping enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03919"
FT   REGION          409..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  55374 MW;  2F56EB9FF4FAAD91 CRC64;
     MAPPGHTATV PEIPGRKVDN PLQLDFLRDH VRNLCRLSHS RFPGAQPVSF DKDSIDLLTK
     EDYWVCEKSD GVRVLILIVI PSGTNVQEVF LIDRKNDYYQ VEGLVFPHHM PNLPEVAKAR
     GMRNHTLMDG ELVIDTYPDG RRKLVLLLFD LIVIDRELLA ERPLSKRYGR LNTFIHPPYA
     KFLQKNPHLA ARQPFEVQVK KMDLSYGIQT VWYDVVPNLK HGNDGLIFTC LNSGYVMGTD
     PKILKWKPPS ENSIDFKLVL RFPPDLARDP RGNLPDLTSL PFFELHQYLG SDGRGGPGGD
     YDFFDELWVE PAEWEAMVES GEQFDDRIVE CVWETDPTPA TDMYRERGLQ LPPRWRMMRI
     RDDKHHGNHH SIVHKILKSI RDGVDADELV ASAAKIRAAW KSSEREMLRQ KLNQAPSSSS
     SSSLPSAAGA VTAVPLHDGP GPHGNAVGAT TTTTTTTATT YDPTIPFGGL AYLGVRGKAP
     PVSSAGAAAS LGLVRR
//
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