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Database: UniProt
Entry: G1QEB3_MYOLU
LinkDB: G1QEB3_MYOLU
Original site: G1QEB3_MYOLU 
ID   G1QEB3_MYOLU            Unreviewed;       826 AA.
AC   G1QEB3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-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   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000022046.1, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000022046.1, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000022046.1}
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   -!- SUBUNIT: Interacts with POLR2A (via C-terminus).
CC       {ECO:0000256|ARBA:ARBA00011551}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}.
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DR   EMBL; AAPE02041123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02041124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02041125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02041126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1QEB3; -.
DR   STRING; 59463.ENSMLUP00000022046; -.
DR   Ensembl; ENSMLUT00000029093.1; ENSMLUP00000022046.1; ENSMLUG00000024254.1.
DR   eggNOG; KOG3673; Eukaryota.
DR   GeneTree; ENSGT00940000157172; -.
DR   HOGENOM; CLU_011097_0_0_1; -.
DR   InParanoid; G1QEB3; -.
DR   OMA; DQFNLGA; -.
DR   TreeFam; TF314897; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
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   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:UP000001074};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU368012};
KW   Transferase {ECO:0000256|RuleBase:RU368012}.
FT   DOMAIN          84..130
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   DOMAIN          228..447
FT                   /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000259|PROSITE:PS51613"
FT   DOMAIN          743..777
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   826 AA;  94544 MW;  3EACF5CE54A3059E CRC64;
     MKRRNDPKCT APIKKQEKRV AEFSMSLNST SDDEPPSSIN HAAKVSTTSF SGSDSETEGK
     QRSSDEAFKA DSLVEGTSSR YSMYSSVSQK LMAKMGFREG EGLGKYSQGR KDIVEASNQK
     GRRGLGLTLQ GFEQELNVDW RDEPEPSACE QVSWFPECTT EIPDTEEMSD WMVVGKRKMI
     IEDKTEFCGE DLLHSVLQCK SMFNVLDGEE MWRALTRANP YEMIQGVFFL NRAAMKMANM
     DFVFDRIFTN PRDSYGKPLV KDREAELLYF ADICAGPGGF SEYVLWRKKW HAKGFGMTLK
     GPNDFKLEDF YSASSELFES YYGEGGIDGD GDVTRPENIT AFRNFVLDNT DGKGVHFLMA
     DGSFSIEGQE NLGEILSKQL LLCQFLMALS VVRTGGHFIC KTFDLFTPFS VGLIYLLYCC
     FERVCLFKPI TSHPANSERY VVCKGLKVGI DDVRKYLFSV NIKLNQLRNT DSNVNLVVPL
     EVIKADHEFT DYMIRSNESH CSLQIKALAK IYAFVQDTTL SEPRQAEIRK QCLRLWGIPD
     QTRVAPSSSD PKSKFFELIR GTEVDIFSYK PTLLTSKTLE KIRPVIDYCC MVSGFLLSLG
     KSQIYTWDGR QSFRWVKLDL KTLPRDTLLF VEIVHELKGE GKAQRKMSAI HILDVLVLNG
     SDVREQHFNQ RIQLAEKFVK AVSKPSRPDM NPIRVKEVYR LEEMEKIFVR LEMIIKGSSG
     IPKLSYTGRD NQHFVPTGLY IVRTVNEPWT MGFNRSFKRK FFYNRKTRSS TFELPADAIA
     PFHICYYGRL FWEWGDGIRV HYSRKPQDPD RLSKEDVLSF IQTHRA
//
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