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Database: UniProt
Entry: A0A3B4ZMB7_9TELE
LinkDB: A0A3B4ZMB7_9TELE
Original site: A0A3B4ZMB7_9TELE 
ID   A0A3B4ZMB7_9TELE        Unreviewed;       810 AA.
AC   A0A3B4ZMB7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000002817.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000002817.1}
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   AlphaFoldDB; A0A3B4ZMB7; -.
DR   STRING; 144197.ENSSPAP00000002817; -.
DR   Ensembl; ENSSPAT00000002860.1; ENSSPAP00000002817.1; ENSSPAG00000002170.1.
DR   GeneTree; ENSGT00390000018056; -.
DR   Proteomes; UP000261400; Unplaced.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent 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          71..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   810 AA;  89941 MW;  7A35A90502096021 CRC64;
     MCLMSGRPPV SGCEPPEQRS AMMLERSSVT VVADIILGSG RETVLCRCSR AFVQDRELYR
     SDNRELPSDL AETQVRETDD KEEEESESEM LDSEAQLMAS MGLPLAFASS SDKRTAGRRS
     NRKAIMYRDE AAPEEKGQDH LQLDNGADEQ VVCDLQVEET RGIPDAGWEA YWAQQGEALL
     WSTWLEKHPE TQLLCALDPG TATAPWDSPD TKAAWDQHSA ETYCSYWELY TYWAAQGWTT
     DQSAGNGNTG GEEAAVLMDN GVPAQPEGQG KDQTESESHT REDDIEDLND LFEHTCMLKT
     GATCVTDSYH SDRRVDTRQQ AELCGSDDPS DGGNDRRRSD SSSQQNTAEQ TASDPQQAAG
     RPDRQNVTRN KMSDGQGDDD DDEPEGEGGG KLKRSHELDV EESPQVTAEE AWSKVRLKHN
     PQPRFDSVIS FKGRAGPKCK RLRWTKRAAC STNKHTRFSA MGEEGSQPRT STALCKVQHF
     LESVQRATQM TPSDRHQVEG GGTPDIRPPS PVEVTGGGGG ETRRSTELES AEKEEEEGSC
     CVSRLNAERS EGPLPNTSFA SAGGSVEEEE EEEEEVKDQP CRPLTCLQTP DFLLCDAPEE
     SSVKDVKKSK KKNGRRGRNQ EVPAEMAAEP ELAKYWAQRY RLFSHFDEGI KLDREGWFSV
     TPERIAEHIA LRVDHSFSDS HLVIDAFCGV GGNAIQFALT GKRVLAVDID AVRLDMARHN
     AAIYNVADRI DFLQGDFLQL APRLRGDVVF LSPPWGGPDY LTAEVFDIGA MMEPDGFEIF
     RLAKMISDNI VFFLPRNADM DQVCMFIMCK
//
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