ID A0A081CJE5_PSEA2 Unreviewed; 455 AA.
AC A0A081CJE5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN ORFNames=PAN0_014d5015 {ECO:0000313|EMBL:GAK66791.1}, PSANT_05528
GN {ECO:0000313|EMBL:SPO47840.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK66791.1, ECO:0000313|Proteomes:UP000053758};
RN [1] {ECO:0000313|Proteomes:UP000053758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA Morita T.;
RT "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT Lipids.";
RL Genome Announc. 2:e00878-e00814(2014).
RN [2] {ECO:0000313|EMBL:GAK66791.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK66791.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPO47840.1, ECO:0000313|Proteomes:UP000325008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC {ECO:0000313|EMBL:SPO47840.1};
RA Guldener U.;
RL Submitted (MAR-2018) 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; DF830081; GAK66791.1; -; Genomic_DNA.
DR EMBL; OOIQ01000015; SPO47840.1; -; Genomic_DNA.
DR RefSeq; XP_014655206.1; XM_014799720.1.
DR AlphaFoldDB; A0A081CJE5; -.
DR GeneID; 26305841; -.
DR HOGENOM; CLU_021710_0_2_1; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; 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; 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 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:SPO47840.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053758};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SPO47840.1}.
FT DOMAIN 46..247
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT DOMAIN 251..386
FT /note="mRNA capping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03919"
FT REGION 397..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 51547 MW; EC674F7B874561E7 CRC64;
MAPLGHTASV PKVPGRKVED PQQLAFLRQH VRDLCEVPHM RFPGAQPVSF EKASIDLLQS
EDYWVCEKSD GQRVLILIVT PASTGRQEVF LIDRKNDYYK VEGIVFPHHM PHDPEAARLG
GMRNHTLMDG ELVIDCDDRG NQKLVLLLFD LIVLDRELLA NRPLSKRYGR LKSYIYPPYV
DYLKRNPAMV ARRPFDVQVK KMDLAYGIQK VLFETVPNLL HGNDGLIFTC LNSGYVMGTD
PKILKWKPPY ENTIDFKLVL RFPPDLERDP RGNLPNLSTM PFFELHQYLG DSASDDYEFF
DELWVEPEEW RQMAASGEQF DDRVVECVWS VDPQPATEPY VSQGVSLPPR WRMMRIRDDK
HHGNHRSIVE KILKSIRDGV DADELVSAAP AIRAAWKSPE REKLRQGAGQ APAPPALPPA
GKFNPNIPFG GMAYQGVKGK APPFPSGGPP GLVRR
//
