ID A0A4D9EVY9_9SAUR Unreviewed; 893 AA.
AC A0A4D9EVY9;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
GN ORFNames=DR999_PMT05396 {ECO:0000313|EMBL:TFK11342.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK11342.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK11342.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK11342.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK11342.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK11342.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK11342.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK11342.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TFK11342.1}.
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DR EMBL; QXTE01000033; TFK11342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4D9EVY9; -.
DR STRING; 55544.A0A4D9EVY9; -.
DR Proteomes; UP000297703; Unassembled WGS sequence.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000297703}.
FT REGION 52..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..588
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 REGION 645..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 100982 MW; F66A6C6046773C9B CRC64;
MPYEPRSRLV AELLLQADEG AGSILCLCSR AFVEDRKLYK LGLKGFYGKE DYDSTGKEQT
EEEKEGNHHP NVAKNSNNNH SLGLEEDELD SEAELMRSMG LPLQFGGLSA HKEFVASENS
RKRNKIVKKK KLQQKPLNEI MWETWEEDCE DHNQSFSDDP ALHTEQTEEK KTCQLLNEDN
CENRDCSIND ALPSELKEKW EKYWSEYGEG LLWQSWLEKH MEVELSENAP TSEPWNSPDT
KDKWKQHYSE LYWYYWEQFQ YWASQGWTVD SPHNDGTEIN VFKLETGPTG EVDCVSTDAV
SRQVLDSQLS SYPPSNISCK ENPSSRDEHH NEILSGISNI NLDLEEVEES KLALTISDGH
QNLSSTSSTR QCPCVSSQKE SCNGGTRKSA SSDNKSANQS DSQESSRSNS NDKRGSHNND
KKEDEEEEEP PEYKHAKLKR RQVINHHELD ADENPVADPE ETCSLLGFKH GTGQKYGGIS
NFSCRKVQYL EKNAKLKSQF LDMRKPVKRK NKHIFFTEES EMLSCQKSKT LSKVEKFLKQ
VSEPVEETMS QESFAQEKVQ GSSTSSDSEE QESSQSNNLS AKKHDPLSSS IVSYELGTNN
LEEKEKEDAA ASGSISQSSG RQDCHSGRQL VALDIPDYLQ VETESVSQVV AEPTERRNTQ
KKKNKKKKKN RTTPPSLPAE IAADPELAKY WAQRYRLFSR FDEGIKLDRE GWFSVTPEKI
AKHIASRVRQ SFNCDIVVDA FCGVGGNAIQ FALASKRVIA IDIDPVKISL ARNNAEVYGV
ANQIDFICGD FMFLASHIKA DVVFLSPPWG GPDYATAEIF DVRTMISPDG YPFKLSQKIT
NNIVYFLPRN ADIDQVASLA GPGGQVEIEQ NFLNNKLKTI TVYFGDLIRR DVS
//
