ID G5B9G4_HETGA Unreviewed; 938 AA.
AC G5B9G4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
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};
GN ORFNames=GW7_09006 {ECO:0000313|EMBL:EHB05925.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB05925.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB05925.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH169118; EHB05925.1; -; Genomic_DNA.
DR AlphaFoldDB; G5B9G4; -.
DR STRING; 10181.G5B9G4; -.
DR eggNOG; KOG3673; Eukaryota.
DR InParanoid; G5B9G4; -.
DR Proteomes; UP000006813; 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|RuleBase:RU368012};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU368012};
KW Transferase {ECO:0000256|RuleBase:RU368012, ECO:0000313|EMBL:EHB05925.1}.
FT DOMAIN 192..238
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT DOMAIN 336..555
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51613"
FT DOMAIN 855..889
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 154..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 107055 MW; A0BD96EEEA01A8A3 CRC64;
MDSEDLTETH CLRKIRKRRE AEIQEHWFCR WEQQCLAKAE QDQQLLPKLQ EEAAQTQKPP
QQAGPTECVS TQDFLSVPFQ IVVTSVGNLS KEAVDPHQHS FDIGIQISYQ RCGVPSASPL
LFLLLPDILG SEHCTVSAQQ HNCDSVWQTV SVTSLSESDS ENEGKPRSSD SFDDTFKADS
LVEGTSSRYS MYNSVSQKLM AKMGFKEGEG LGKFSQGRKD IVEASNQKGR RGLGLTLQGF
DQELNVDWRD EPEPSACEQV SWFPECTTEI PDTQEMSDWM VVGKRKMTIE DETQFCGAEL
LHSMLQCKSV FDVLDGEEMR RARTRANPYE MIRGVFFLNR AAMKMANMDF VFDRMFTNPR
DSSGLPLVKD RNAELLYFAD VCAGPGGFSE YVLWKKKWHA KGFGMTLRGP NDFKLEDFYS
ASSELFEPYY GEGGVDGDGD ITRPDNIAAF RNFVLDNTDR KGVHFLMADG GFSVEGQENL
QEILSKQLLL CQFLMALSVV RTGGHFICKT FDLFTPFSVG LIYLLYCCFE RVCLFKPVTS
RPANSERYVV CKGLKVGTDD VREYLFSVNM KLNQLRNTDS DVNLVVPLKV IKDDPEFTDY
MVRSNEGHCS LQIKALAKIH AFVQDTTLSE PQVGEIECLR LWEIPDQARV APSSSDPKSK
FFELIQGTEI DIFSYKPTLL TAKTLEKIRP VFDYRCMVSG SQQKFLLGMG KSQIYTWDGR
QSDRWVRLDL KTELPRDTLL SVEIVHELKG EGKAQRKISA IHILDVLVLN GSDVRDQHFN
QRIQLAEKFV KAVSKPSRPD MNPIRVKEVY RLEEVEKIFL RLEMKIIKGS SGTPRLSYTG
RDDRHFVPTG LYIVRTVNEP WTMGFSKSVK RKFFYNKKTR DSTFNIPTDS IAPFHVCYFS
RLFWEWGDGI RVHDSQKLQD VDKLSKEDVL SFIHMHSH
//
