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Database: UniProt
Entry: A0A3B4EAH6_PYGNA
LinkDB: A0A3B4EAH6_PYGNA
Original site: A0A3B4EAH6_PYGNA 
ID   A0A3B4EAH6_PYGNA        Unreviewed;       817 AA.
AC   A0A3B4EAH6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000033547.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000033547.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-
CC         ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end
CC         (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-(ribonucleoside) in
CC         mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67624,
CC         Rhea:RHEA-COMP:17171, Rhea:RHEA-COMP:17315, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623,
CC         ChEBI:CHEBI:172880; Evidence={ECO:0000256|ARBA:ARBA00024488};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67625;
CC         Evidence={ECO:0000256|ARBA:ARBA00024488};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67620, Rhea:RHEA-COMP:17167, Rhea:RHEA-
CC         COMP:17315, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:156461, ChEBI:CHEBI:172880;
CC         Evidence={ECO:0000256|ARBA:ARBA00024618};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67621;
CC         Evidence={ECO:0000256|ARBA:ARBA00024618};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Trimethylguanosine synthase family. {ECO:0000256|ARBA:ARBA00025783}.
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DR   RefSeq; XP_017561479.1; XM_017705990.1.
DR   AlphaFoldDB; A0A3B4EAH6; -.
DR   STRING; 42514.ENSPNAP00000033547; -.
DR   Ensembl; ENSPNAT00000024545.1; ENSPNAP00000033547.1; ENSPNAG00000022249.1.
DR   GeneID; 108432263; -.
DR   CTD; 96764; -.
DR   GeneTree; ENSGT00390000018056; -.
DR   OMA; GWETYWA; -.
DR   OrthoDB; 5473515at2759; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14741; S-ADENOSYLMETHIONINE-DEPENDENT METHYLTRANSFERASE RELATED; 1.
DR   PANTHER; PTHR14741:SF32; TRIMETHYLGUANOSINE SYNTHASE; 1.
DR   Pfam; PF09445; Methyltransf_15; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
FT   REGION          59..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..520
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..585
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   817 AA;  91903 MW;  4211251D4CC953C4 CRC64;
     MVNRGKWQTV PIADIYFHHG VLDEMTIYCL CTRAFVNDRE LYRSDLKSLQ ALTDSVLQDN
     VEDLEDEEPS NSEDEEDVEM DEETILMASM GLPVAFGSSS AQRKAHKWTG YTPHRGSKKA
     NAGHQEAFSE QEDPQQDPEL EPVKNEQQEE KEKVVPVVLE DTPADPESTI SETPWLNYWQ
     LHGETLLWGS WVEKHPEFSS GTPLAPWDCA EWKEAWQEHA SQGYLYYWEQ FDYWAAQGWT
     TDESYSAAAH DDGQCREDEL VEEKNKPSSN WSENMADLNA VDIAERFDSL NLLTDENGSN
     DGQQAFDCNC ADEPCDGGDQ KRPSSSSSVC TKEGNKQASS SSVTNKNGQP VRSGSNKKDE
     SDDDEPPDRK QAKIKRSHEL DVEELAQVPS EEAWETLGLK RSPQLKFTSV LKFREAPGQR
     EGSQSGARWR PTGRKATCKI NKHIFFTEDG QTAVPKISQT LQKVQSFLQR IQTENDSEKE
     AASVLGSTTL QARVSTVDGQ GTLRPQENEE ECREPQPDSG SMESEEPQPL TQPEPEPETL
     AAPDSDPLQD SDSDPRGELQ PLDIPDYLLP DAPKDKQGDT EASTKKKKKK KAKRWRREVD
     VPPEIAAEPE LAKYWAQRYR LFSRFDEGIK LDHEGWFSVT PEKIAEHIAQ RVREVYDTQL
     IVDAFCGVGG NAIQFALTGK RVIAIDIDPV RLELAHHNAE VYGVAQRIDF IQGDFLQLAP
     RLRADVVFLS PPWGGPEYLS AEVFNIKTMM SPDGFEIFRL AKMISENIVY FLPRNADMEQ
     IASLAGPGGK VEVEQNFLNN KLKTITAYFG SLVKADS
//
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