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Database: UniProt
Entry: G3PBT8_GASAC
LinkDB: G3PBT8_GASAC
Original site: G3PBT8_GASAC 
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
//
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