ID G3PBT8_GASAC Unreviewed; 826 AA.
AC G3PBT8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 {ECO:0000256|ARBA:ARBA00021136, ECO:0000256|RuleBase:RU368012};
DE EC=2.1.1.57 {ECO:0000256|ARBA:ARBA00011923, ECO:0000256|RuleBase:RU368012};
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000015062.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000015062.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000015062.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA to produce m(7)GpppNmp (cap1).
CC {ECO:0000256|RuleBase:RU368012}.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1).
CC Displays a preference for cap0 transcripts. Cap1 modification is linked
CC to higher levels of translation. May be involved in the interferon
CC response pathway. {ECO:0000256|ARBA:ARBA00002664}.
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(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000256|ARBA:ARBA00024256,
CC ECO:0000256|RuleBase:RU368012};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}.
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DR AlphaFoldDB; G3PBT8; -.
DR STRING; 69293.ENSGACP00000015062; -.
DR Ensembl; ENSGACT00000015090.1; ENSGACP00000015062.1; ENSGACG00000011365.1.
DR eggNOG; KOG3673; Eukaryota.
DR GeneTree; ENSGT00940000157172; -.
DR InParanoid; G3PBT8; -.
DR OMA; TNINACT; -.
DR TreeFam; TF314897; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000011365; Expressed in spleen and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule.
DR GO; GO:0097309; P:cap1 mRNA methylation; IEA:UniProtKB-UniRule.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.40.50.12760; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR025816; RrmJ-type_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001202; WW_dom.
DR PANTHER; PTHR16121:SF0; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 1; 1.
DR PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU368012};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042,
KW ECO:0000256|RuleBase:RU368012};
KW mRNA processing {ECO:0000256|RuleBase:RU368012};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368012};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU368012};
KW Transferase {ECO:0000256|RuleBase:RU368012}.
FT DOMAIN 76..122
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT DOMAIN 220..439
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51613"
FT DOMAIN 742..776
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 94313 MW; 82415E86930C9920 CRC64;
MKRRAEAPLT VVQGTKRVCE DSSSDEESQL SRQDSSQNDS LSDQDDQRPG FSMPSISSCD
DQDNDPTQAS SNFSMYNSVS QKLMAKMGFR EGEGLGKFGQ GRKEIVEASN QRGRRGLGLT
LQGFQGELNV DWRDEPEPTA AQKVDWFPEC TTETPDSDEL RDWMKVGARK LKIEDETEFC
TEDLLHTLLR CKTVFDNLEG EEMRRARTRS NPYETIRGGI FLNRAAMKMS NIDHCFDQMF
TNPKDSQGKP LTKDREGELL YFGDVCAGPG GFSEYILWRR RWHAKGFGMT LKGPCDFKLE
DFFAAPSELF EPYYGEGGVD GDGDITRPEN ITAFRNFVQE STERRGLHIL MADGGFSVEG
QENIQEILSK QLLLCQFLTA LSSLRTGGHF VCKTFDLFTP FSVGCVYLLY LCFERISLFK
PVTSRPANSE RYVVCRGLKP GSEAVREYMF RVNLKLNQLR DTDRDVTDVV PLSIIKEDLD
FYQFMVNSNE SLCVVQIKAL AKIHAFVVDP TLMEAKQADI RKECLKLWGV PDMARVTPAS
SDPKSKFHKL IKNSEVESFQ SKLTPLNSTT LEKLRHILDH RCIVGGGEQI FLLSLGKSQI
YTWDGKMPPR WKKLESFKLE LPRDTLLSVE IVQELKGEGK AQRRINAVHV MDALVLNGTD
VRDQHFNQRI QMAEKFVKAV AKPSRPDMNP IRVKEVYRLE EMEKIFVRLE MKVTKSSGGV
PRLSYTGRDD RHFLPTGLYV IKTVNEPWTM AYSKNSKMKF FYNKTTKTST YEMPPNSAAP
FNVCHSERLF WAWVDGVIVH DSQTRMDHEK LSKDDVLSFV HQNYQQ
//