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Database: UniProt
Entry: A0A2A4JQW3_HELVI
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ID   A0A2A4JQW3_HELVI        Unreviewed;       588 AA.
AC   A0A2A4JQW3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=mRNA-capping enzyme {ECO:0000256|PIRNR:PIRNR036958};
DE   Includes:
DE     RecName: Full=mRNA 5'-triphosphate monophosphatase {ECO:0000256|PIRNR:PIRNR036958};
DE              EC=3.6.1.74 {ECO:0000256|PIRNR:PIRNR036958};
DE     AltName: Full=mRNA 5'-phosphatase {ECO:0000256|PIRNR:PIRNR036958};
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase {ECO:0000256|PIRNR:PIRNR036958};
DE              EC=2.7.7.50 {ECO:0000256|PIRNR:PIRNR036958};
DE     AltName: Full=GTP--RNA guanylyltransferase {ECO:0000256|PIRNR:PIRNR036958};
DE              Short=GTase {ECO:0000256|PIRNR:PIRNR036958};
GN   ORFNames=B5V51_14386 {ECO:0000313|EMBL:PCG73800.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG73800.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG73800.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG73800.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG73800.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-
CC       triphosphate monophosphatase activity in the N-terminal part and mRNA
CC       guanylyltransferase activity in the C-terminal part. Catalyzes the
CC       first two steps of cap formation: by removing the gamma-phosphate from
CC       the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and
CC       by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of
CC       RNA via a covalent enzyme-GMP reaction intermediate.
CC       {ECO:0000256|PIRNR:PIRNR036958}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end
CC         diphospho-ribonucleoside in mRNA + H(+) + phosphate;
CC         Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036958};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR036958}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase
CC       family. {ECO:0000256|PIRNR:PIRNR036958}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the non-receptor
CC       class of the protein-tyrosine phosphatase family.
CC       {ECO:0000256|PIRNR:PIRNR036958}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG73800.1}.
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DR   EMBL; NWSH01000867; PCG73800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4JQW3; -.
DR   STRING; 7102.A0A2A4JQW3; -.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140818; F:mRNA 5'-phosphatase activity; IEA:InterPro.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd07895; Adenylation_mRNA_capping; 1.
DR   CDD; cd17664; Mce1_N; 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   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR017074; mRNA_cap_enz_bifunc.
DR   InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR   InterPro; IPR013846; mRNA_cap_enzyme_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR   PANTHER; PTHR10367:SF17; MRNA-CAPPING ENZYME; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF03919; mRNA_cap_C; 1.
DR   Pfam; PF01331; mRNA_cap_enzyme; 1.
DR   PIRSF; PIRSF036958; mRNA_capping_HCE; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|PIRNR:PIRNR036958, ECO:0000256|PIRSR:PIRSR036958-
KW   3}; Hydrolase {ECO:0000256|PIRNR:PIRNR036958};
KW   mRNA capping {ECO:0000256|ARBA:ARBA00023042,
KW   ECO:0000256|PIRNR:PIRNR036958};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|PIRNR:PIRNR036958};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR036958};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR036958};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR036958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036958}.
FT   DOMAIN          108..175
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          201..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT   ACT_SITE        298
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT   BINDING         303
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         319
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         347..349
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         464..466
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         534..539
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ   SEQUENCE   588 AA;  68434 MW;  5FD1843656E57791 CRC64;
     MSQRDPGPIP NRWLRCPRKA TGLVADKFMA FKTPLGSQFN DKVPEENRFT PSMLFVYMKS
     MKIQLGLWID LTNTSRFYNK AEVEEAGCKY VKMQCRGHGE TPSPEQTREF INLVARFISQ
     KPLEYIGVHC THGFNRTGFL LVSYMVEHLD CSVQAAINEF ARMRPPGIYK QDYLQELFRR
     YDEVELTPAA PALPDWCHEE EEDFDDDVPS NSTNTSSSNQ RKHKGKGRRE TTHKKATFMP
     GVRGVEPFDT QPRLSEVQKK AQQFCKWNTT GFPGSQPVSM DMVNLRKLHE KPYRVSWKAD
     GVRYMMLIDG EGEVYMLDRD NCVFKVFGLR FPHRKDLRRH LKNTLLDGEM VIDKVDNKDI
     PRYLCYDVIS FEGTDTGRME FYPTRLSYIE NEIVNPRHQA MKEGKIKKEQ EPFSIRLKQF
     WELPMARQLL GEKFAKTLSH EPDGLIFQPS KERYIAGPCE DVLKWKPSHM NSVDFKLKIV
     TQGGQGILPT KVGYLYVGKM DQPFASMKVT KDIKHLDNKI IECTFENGRW VFMRERTDKS
     FPNSFNTASS VCESIKDPVT KEILLDYIDN HRFHDDSDMM PPPKRMRR
//
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