ID M3XA37_FELCA Unreviewed; 766 AA.
AC M3XA37;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 {ECO:0000256|ARBA:ARBA00021134};
DE EC=2.1.1.296 {ECO:0000256|ARBA:ARBA00012770};
GN Name=CMTR2 {ECO:0000313|Ensembl:ENSFCAP00000023490.2,
GN ECO:0000313|VGNC:VGNC:61005};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000023490.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000023490.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000023490.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000023490.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000023490.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000023490.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000023490.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(ribonucleotide) in mRNA + S-adenosyl-L-methionine =
CC a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(2'-O-methyl-ribonucleotide) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67024, Rhea:RHEA-COMP:17169,
CC Rhea:RHEA-COMP:17170, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:167612, ChEBI:CHEBI:167614;
CC EC=2.1.1.296; Evidence={ECO:0000256|ARBA:ARBA00024560};
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DR EMBL; AANG04002512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003998268.1; XM_003998219.4.
DR RefSeq; XP_019675583.1; XM_019820024.1.
DR RefSeq; XP_019675584.1; XM_019820025.1.
DR RefSeq; XP_019675585.1; XM_019820026.1.
DR RefSeq; XP_019675586.1; XM_019820027.1.
DR AlphaFoldDB; M3XA37; -.
DR STRING; 9685.ENSFCAP00000023490; -.
DR PaxDb; 9685-ENSFCAP00000023490; -.
DR Ensembl; ENSFCAT00000028223.3; ENSFCAP00000023490.2; ENSFCAG00000030250.3.
DR GeneID; 101081592; -.
DR KEGG; fca:101081592; -.
DR CTD; 55783; -.
DR VGNC; VGNC:61005; CMTR2.
DR eggNOG; KOG3674; Eukaryota.
DR GeneTree; ENSGT00940000161773; -.
DR HOGENOM; CLU_019427_0_0_1; -.
DR InParanoid; M3XA37; -.
DR OMA; LHYCEAT; -.
DR Proteomes; UP000011712; Chromosome E2.
DR Bgee; ENSFCAG00000030250; Expressed in liver and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0097309; P:cap1 mRNA methylation; IBA:GO_Central.
DR GO; GO:0097310; P:cap2 mRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.12760; -; 2.
DR InterPro; IPR025807; Adrift-typ_MeTrfase.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16121:SF2; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 2; 1.
DR PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51614; SAM_MT_ADRIFT; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00946};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00946};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00946}.
FT DOMAIN 107..320
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51614"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
SQ SEQUENCE 766 AA; 87268 MW; D5219CFE5699512A CRC64;
MSKCRKPPLG SSPETFSPDV VADIFELFAK NFSYGKPLNN EWQLPDPGEI FTCDHTEFNA
LLDLKNSLNE VKNLLSDKKL DEWHEHTAFT NKAGKIISHV KKSVNAELCT QAWCKFHEIL
CSFPLIPQEA FQNGKLNSLH LCEAPGAFIA SLNHYLKSHR FPCDWSWVAN TLNPYHEAND
NLMMIMDDRL IANTLHWWYF GPDNTGDIMN LKYLTGLQNF ISNMATVHLI TADGSFDCQG
NPGEQEALVS SLHYCEVVTA LTTLGNGGSF VLKMFTLFEH CSINLMYLLN CSFDQVHVFK
PATSKAGNSE VYVVCLRYKG REAIHPLLSK MVLNFGTEMT QKALFPHHVI PESFLKRHEE
CCMFFHKYQL ETISENIRLF QCMGKGEQTK LNTLRDCAVQ YFMEKFQLKP LSRSNWLVKK
SSIGCSTNTK RFGQRNRYFK TYNERKMLET LSWKDKVAKG YFNSWAEEHA VYHSGQSSLL
EGTASSLECH LWDILEGKKL PKVKCSPFCD GEILKALNEA IEKSLGGALN LDSKFWPKQQ
DYCSCHIFTE ELIFTELFSL TKCLQDEQVV EPSNRIKCLL VGFPTLSDIK THIPLEVQFL
EPAELMTCSC SLLHDGDPFY QQLFLDCFLR ALQQLQTGDA MILPVLSCFT RFMAGLIFVL
HNCFRFITFS CPTSSEPLKT CAVLLCVGYQ DLPNPVFQYL QNVNDLLSSL LNSDAPQQVL
QFVPMEVLLK GALLDFLWDL NAAIAKRHLH VIIQGEREEI ISSLQL
//
