ID   A0A2I2Z5Q8_GORGO        Unreviewed;       597 AA.
AC   A0A2I2Z5Q8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   29-SEP-2021, entry version 23.
DE   RecName: Full=mRNA-capping enzyme {ECO:0000256|PIRNR:PIRNR036958};
DE   Includes:
DE     RecName: Full=Polynucleotide 5'-triphosphatase {ECO:0000256|PIRNR:PIRNR036958};
DE              EC=3.1.3.33 {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   Name=RNGTT {ECO:0000313|Ensembl:ENSGGOP00000042416};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000042416, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000042416, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000042416, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000042416}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2018) to UniProtKB.
CC   -!- FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-
CC       triphosphatase 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.
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:ARBA00024268,
CC         ECO:0000256|PIRNR:PIRNR036958};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a
CC         5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate;
CC         Xref=Rhea:RHEA:11008, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13942,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:138276, ChEBI:CHEBI:138288; EC=3.1.3.33;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036958};
CC   -!- SUBCELLULAR LOCATION: Nucleus {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}.
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DR   EMBL; CABD030046545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030046546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030046547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030046548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030046549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030046550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030046551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018885636.1; XM_019030091.1.
DR   SMR; A0A2I2Z5Q8; -.
DR   Ensembl; ENSGGOT00000056332; ENSGGOP00000042416; ENSGGOG00000007863.
DR   GeneID; 101136858; -.
DR   KEGG; ggo:101136858; -.
DR   CTD; 8732; -.
DR   GeneTree; ENSGT00940000156953; -.
DR   OrthoDB; 1544021at2759; -.
DR   Proteomes; UP000001519; Chromosome 6.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule.
DR   CDD; cd07895; Adenylation_mRNA_capping; 1.
DR   Gene3D; 3.90.190.10; -; 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_PHOSPHATASE_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
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; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR036958};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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|PIRNR:PIRNR036958,
KW   ECO:0000256|PIRSR:PIRSR036958-3};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR036958};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR036958};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Transferase {ECO:0000256|PIRNR:PIRNR036958}.
FT   DOMAIN          25..183
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          104..171
FT                   /note="TYR_PHOSPHATASE_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   NP_BIND         343..345
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   NP_BIND         458..460
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   NP_BIND         528..533
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   REGION          181..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..207
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..597
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        126
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT   ACT_SITE        294
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT   BINDING         299
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT   BINDING         315
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ   SEQUENCE   597 AA;  68557 MW;  51CEEC1B190603DE CRC64;
     MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK
     MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE
     LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI
     EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG
     VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY
     MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL
     IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT
     SRKLLEGNFA KEVSHEMDGL IFQPTGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG
     LLPQNVGLLY VGGYERPFAQ IKVTKELKQY DNKIIECKFE NNSWVFMRQR TDKSFPNAYN
     TAMAVCNSIS NPVTKEMLFE FIDRCTAASQ GQKRKHHLDP DTELMPPPPP KRPRPLT
//