ID S4PC13_9NEOP Unreviewed; 358 AA.
AC S4PC13;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
OS Pararge aegeria (speckled wood butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Satyrini; Parargina; Pararge.
OX NCBI_TaxID=116150 {ECO:0000313|EMBL:JAA86863.1};
RN [1] {ECO:0000313|EMBL:JAA86863.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:JAA86863.1};
RX PubMed=23622113; DOI=10.1186/1471-2164-14-283;
RA Carter J.M., Baker S.C., Pink R., Carter D.R., Collins A., Tomlin J.,
RA Gibbs M., Breuker C.J.;
RT "Unscrambling butterfly oogenesis.";
RL BMC Genomics 14:283-283(2013).
RN [2] {ECO:0000313|EMBL:JAA86863.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:JAA86863.1};
RA Carter J.-M., Baker S.C., Pink R., Carter D.R.F., Collins A., Tomlin J.,
RA Gibbs M., Breuker C.J.;
RL Submitted (MAY-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; GAIX01005697; JAA86863.1; -; Transcribed_RNA.
DR AlphaFoldDB; S4PC13; -.
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; 3.30.1490.430; -; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 38..227
FT /note="mRNA capping enzyme adenylation"
FT /evidence="ECO:0000259|Pfam:PF01331"
FT DOMAIN 232..325
FT /note="mRNA capping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03919"
FT REGION 336..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 41544 MW; 97775A5C92A1BBD4 CRC64;
MPGVRGVQLF EIEPRASEVQ KKAREFCKWS GKNFPGSQPV SMDLQNISYL NVKPYRVSWK
ADGVRYMMLI DGKDEVYMID RDNCVFKVPN LRFLHNKEGR HLTDTLLDGE LVIDKVDGVE
KPRYLCYDII RFDNINVGKE PFHPVRLGCI DREIIQPRNR AITDGRISKE KEPFGVILKG
FWDVTMAGPL LEEKFARTLH HDPDGLIFQP SKEPYIPGPN PDVLKWKPSH MNSVDFKLVI
TVDNRKGMVK KKIGQLYVGG NTLFDTMRIT RAVKDLHNKI VECKFENNEW VFMRERTDKS
FPNSFETAIA VVESIKNPVK TEYLLDYINN KRYIDDSDRM PPPSKRARRE DGSQIAWH
//