ID A0A091W2Q2_NIPNI Unreviewed; 579 AA.
AC A0A091W2Q2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00012475};
DE EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
DE Flags: Fragment;
GN ORFNames=Y956_07845 {ECO:0000313|EMBL:KFR09330.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR09330.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFR09330.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR09330.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KL411541; KFR09330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091W2Q2; -.
DR STRING; 128390.A0A091W2Q2; -.
DR eggNOG; KOG2386; Eukaryota.
DR Proteomes; UP000053283; 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-KW.
DR GO; GO:0140818; F:mRNA 5'-phosphatase activity; 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; 3.30.1490.430; -; 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 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR036958-
KW 3}; 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 ECO:0000256|PIRSR:PIRSR036958-3};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000053283};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..162
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 83..150
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 159..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-1"
FT ACT_SITE 276
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-2"
FT BINDING 281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 325..327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 440..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT BINDING 510..515
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR036958-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR09330.1"
FT NON_TER 579
FT /evidence="ECO:0000313|EMBL:KFR09330.1"
SQ SEQUENCE 579 AA; 66307 MW; B58EA5DDC5A33ABB CRC64;
GKFLPLKTML GPRYDEQVAE ENRFHPSMLS NYLKSLKVKM GLLVDLTNTT RFYDRNDIEK
EGIKYIKLQC KGHGECPTPE NTETFIRVCE HFSDKNPSEL IGVHCTHGFN RTGFLICAFL
VEKLDWSIEA AVATFAQARP PGIYKGDYLK ELFRRYGDED DAPSPPELPE WCFEEDEEED
DDNGKTGGQE SEPGSSSSSF GKRRKERLKL GAIFLEGITV KCVTQVTTQP KLGGIQQKCQ
QFCGWEGSGF PGAQPVSMDK QNIKFLEQKP YKVSWKADGT RYMMLIDGKN EVYMIDRDNS
IFHVSNLEFP FRKDLRTHLT NTLLDGEMII DKVNGQVVPR YLIYDIIKFN GQPVGDCDFN
VRLACIEKEI IFPRHEKMKN GLIDKAQEPF SVRNKPFFDI YTSRKLLEGS FAREVSHEVD
GLIFQPTGKY KPGRCDDILK WKPPSLNSVD FRLKITRIGG EGLLTQNVGL LYVGNFDRPF
AQIKVTKELK QYDNKIIECK FENNSWVFMR QRIDKSFPNA YSTAMAVCNS IQNPVTKEML
FEFIDRCTAA SQGQTRKHHL DPDTELMPPP PPKRPRTIT
//
