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
//