ID A0A3Q3B9Y7_KRYMA Unreviewed; 601 AA.
AC A0A3Q3B9Y7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000026593.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000026593.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|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 RefSeq; XP_017267219.1; XM_017411730.1.
DR RefSeq; XP_017267220.1; XM_017411731.1.
DR AlphaFoldDB; A0A3Q3B9Y7; -.
DR STRING; 37003.ENSKMAP00000026593; -.
DR Ensembl; ENSKMAT00000026932.1; ENSKMAP00000026593.1; ENSKMAG00000019710.1.
DR GeneID; 108233334; -.
DR KEGG; kmr:108233334; -.
DR CTD; 8732; -.
DR GeneTree; ENSGT00940000156953; -.
DR OrthoDB; 49440at2759; -.
DR Proteomes; UP000264800; Unplaced.
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 InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_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.
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|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036958};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR036958}; Nucleus {ECO:0000256|PIRNR:PIRNR036958};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, 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="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 188..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..601
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 297
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT BINDING 302
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 318
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 346..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 461..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 531..536
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ SEQUENCE 601 AA; 68109 MW; DCCEA7325D1AF14A CRC64;
MSQTGPPPRW RNCPRRGQPV AGKFLPMKTM LGPRYDDQVA EENRFHPSML SNYLKSLKVK
MGLLVDLTNT TRFYDRNDIE KEGIKYVKLQ CKGHGECPSK ETTAMFIRLC EHFIDKNPTE
LIGVHCTHGF NRTGFLICAY LVEKMDWSIE AAVAAFSQAR APGIYKGDYL KELFCRYGDG
DDTPSAPALP EWCFDDDDGE ADDDGNAVGQ ESGPSSSGSA PGKRKKEKLK LGAVFLEGIS
VKGVTQVTNQ PKLGEIQRMC QEMAEWDKSG FPGAQPVSMD RQNLRFLEQN PYKVSWKADG
TRYMTLINGK NEVFMIDRDN TVFHIENLEF PFRKDPRVHL SNTLLDGEMI IDKVNGQPVP
RYLIYDIIKF NGQPVGQCDF NIRLVCIEKE IISPRMEKMK LGQIDKTKEP FSVRNKPFFD
IHASRKLLEG SFTSQVSHEV DGLIFQPCGK YKAGRCDDIL KWKPPNLNSV DFRLKITKVG
GEGLIPQIVG LLYVGNYDRP FATMRATKEL KQYDNKIIEC TFANNSWVFM RQRVDKSFPN
SYTTAMAVCK SIQEPVTKEI LLEFLDRCAQ GVNVPNRKRP SDPDSQLMPP PPPKRPNLAT
P
//
