ID A0A1I8C0L7_MELHA Unreviewed; 618 AA.
AC A0A1I8C0L7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 Meloidogyne hapla (Root-knot nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne.
OX NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig819.frz3.gene15};
RN [1] {ECO:0000313|WBParaSite:MhA1_Contig819.frz3.gene15}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 AlphaFoldDB; A0A1I8C0L7; -.
DR WBParaSite; MhA1_Contig819.frz3.gene15; MhA1_Contig819.frz3.gene15; MhA1_Contig819.frz3.gene15.
DR OMA; FWDIWMS; -.
DR Proteomes; UP000095281; 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 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|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR036958};
KW 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|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR036958}; Nucleus {ECO:0000256|PIRNR:PIRNR036958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036958}.
FT DOMAIN 133..193
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT BINDING 339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 378..380
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 496..498
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 569..574
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
SQ SEQUENCE 618 AA; 71995 MW; 7E70D53E12CFF1C4 CRC64;
MSKRIRQENS VNGNNGNVQS PNKQWLKPKT RLPARWLYCP PMGKVVARKF LPMKTPLDTS
YDHLIESPKY YFHPEMVFRT PLRDVNSGAQ ILLWIDLTNS NSFYQPCEIP SPCKYEKIKM
VGHGEAPSVE QTDKFIEIVD KFFEEHPNDI VVVHCTHGFN RTGFLISSYL FKHDGLSIEM
AIQEFASARP MGIYKQLYLD ELHQRYGDED DEKIESHGRP LWENGPLSNE EFTMDGIFTI
GEEKNLNDDF IPSTSNLNID NSNSPGKKAK KTPLFMDGRV PNVYFVEDPE LRKSVQSQPV
SLEGPYGDGT SNNIQFLEME PYIYLVLIDG YNRVFAFDRD NNPFQINNVT FLNKKAKCLS
PLKSLISEED YLKGTLVDAE MVIDNVEGKE IPRLLIYDLI YFNNINLKKE KFSIRFKAID
DELIKPRIEA LKLGIINRDC QSMGVRRKDF WPIKETYKIF QPGFLENVTS CHEIDGLVFQ
PVNRPYVAGR YDYLLKWKPP ELATIDFRLE IKKIQRPGEL TEWIGELHVL HLDTPFARLL
KVTNQMRQYD RKIIECKYVR EKGGWEFMRE RTDKSHPNAY LTAKSVLNTI KYPINRNDIL
NFIHSFVTRK EQLKNENN
//
