ID A0A232ETW5_9HYME Unreviewed; 1113 AA.
AC A0A232ETW5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
GN ORFNames=TSAR_010186 {ECO:0000313|EMBL:OXU21792.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU21792.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU21792.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU21792.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU21792.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
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 -!- 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:OXU21792.1}.
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DR EMBL; NNAY01002212; OXU21792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232ETW5; -.
DR STRING; 543379.A0A232ETW5; -.
DR Proteomes; UP000215335; 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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd07895; Adenylation_mRNA_capping; 1.
DR CDD; cd17664; Mce1_N; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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 InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
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; 2.
DR Pfam; PF01331; mRNA_cap_enzyme; 2.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR SUPFAM; SSF101908; Putative isomerase YbhE; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT DOMAIN 22..194
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 112..179
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REPEAT 745..777
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 210..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 127566 MW; 1310E9C63925E3DD CRC64;
MSNWNREDGK GPIPPRWLHC PRKSTKLIHN KFLAFKTPLS SDFDSQVPEE CRFSVEMLVA
SLRSMKLKMG LWIDLTNTNR FYDKNEIERN GMRYLKLPCR GHGETPSIDQ TKSFVHVCKN
FIAQHPLEII GVHCTHGFNR TGFLIVSFLV ETDEYSLDAS LARFTDARPP GIYKGDYIEE
LYKRYDDPED TPEPPPRPAW CLEYDDSNVE DQDEGTSVES DVQEPPHKKR KREQFKKNPV
FMAGVPGVKA ITDIQIASGI QRRIQDICHW NNSGFPGAQP VSMDVENVRL LHEKPYRVSW
KADGTRYMMM IQGDGQVYFA DRDNSIFQVE RLTFPHLKDS NRRLRDTLLD GEMVIDKVNG
KEMPRYLAYD VIMFDGKDVS KLSFYPDRYT IIDREIIAAR RHAMQQGKIL RDKEPFSVRL
KEFWDITQTS SLLSEKFAKQ LSHEPDGLIF QPSKEPYKGG QCPDILKWKP ASLNSVDFRL
KIVVESGEGI VRKTIGELYV GGLEVPFQKI KMTKTLRELN NKIIECKFEN NQWVFMRERT
DKSFPNSFNT AKAVCQSISN PVTKEKLLDY IRKHRFSLDE ELMPPPRMRS NRPDLERKSL
RVNIEYDHAS LVRWSPDGKA FIIHKALANV VEVYKIAKKP DGTPSSATKV LEFPKQHHED
AIDLDIACNG RFIITCSKVN DLVVWDLKGQ ILSTVDTVLG STHRARISPC GRFVAASGFT
PDVKVWEVTF TKSGEFKQVA KGFDLAGHSS GVYDFAFNSD TSRMATVSKD GTYRFYDTKV
EFEKGEDPRL ISSGQWEGTT PANIALSPNA EIIVISHGSS ISFYSTVNGK LDTTIDDIFN
GPIKCLKFDS LGEYVIVAGD RHIKIFRNIP GYRASIETSR KKLAQRQTSA TKERLEKTIV
DCENKLSFYP DRYTIIDREI IAARRHAMQQ GKILRDKEPF SVRLKEFWDI TQTSSLLSEK
FAKQLSHEPD GLIFQPSKEP YKGGPCPDIL KWKPASLNSV DFRLKIVVES GEGIVRKSIG
ELYVGTLDRP MATIKMTKAL RELHNKIIEC KFENNQWVFM RERTDKSIPN SYNTAMAVCQ
SISNPVTKEK LLDFIHKHRF SLDEELMPPP RMR
//
