ID CMTR2_PONAB Reviewed; 769 AA.
AC Q5RAY7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2;
DE EC=2.1.1.296 {ECO:0000250|UniProtKB:Q8IYT2};
DE AltName: Full=Cap methyltransferase 2;
DE AltName: Full=Cap2 2'O-ribose methyltransferase 2;
DE Short=MTr2;
DE AltName: Full=FtsJ methyltransferase domain-containing protein 1;
GN Name=CMTR2; Synonyms=FTSJD1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of
CC mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-
CC capped mRNA and small nuclear RNA (snRNA) (cap0) to produce
CC m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently
CC of its N(7) methylation status. Display cap2 methylation on both cap0
CC and cap1. Displays a preference for cap1 RNAs.
CC {ECO:0000250|UniProtKB:Q8IYT2}.
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:0000250|UniProtKB:Q8IYT2};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYT2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8IYT2}.
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DR EMBL; CR858874; CAH91073.1; -; mRNA.
DR RefSeq; NP_001125622.1; NM_001132150.1.
DR AlphaFoldDB; Q5RAY7; -.
DR SMR; Q5RAY7; -.
DR STRING; 9601.ENSPPYP00000008505; -.
DR GeneID; 100172540; -.
DR KEGG; pon:100172540; -.
DR eggNOG; KOG3674; Eukaryota.
DR InParanoid; Q5RAY7; -.
DR OrthoDB; 5488054at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR GO; GO:0097310; P:cap2 mRNA methylation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..769
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 2"
FT /id="PRO_0000326182"
FT DOMAIN 109..322
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT ACT_SITE 117
FT /evidence="ECO:0000250|UniProtKB:Q8IYT2"
FT ACT_SITE 235
FT /evidence="ECO:0000250|UniProtKB:Q8IYT2"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
SQ SEQUENCE 769 AA; 88166 MW; ED69511D9E5BFBF6 CRC64;
MSKCRKTPVQ QLASPTSFSP DILADIFELF AKNFSYSKPL NNEWQLPDPS EIFTCDHTEF
NAFLDLKNSL NEVKNLLSDK KLDEWHEHTA FTNKAGKIIS HVRKSVNAEL CTQAWCKFHE
ILCSFPLIPQ EAFQNGKLNS LHLCEAPGAF IASLNHYLKS HRFPCHWSWV ANTLNPYHEA
NDDLMMIMDD RLIANTLHWW YFGPDNTGDI MTLKFLTGLQ NFISSMATVH LVTADGSFDC
QGNPGEQEAL VSSLHYCEVV TALTTLGNGG SFVLKMFTMF EHCSINLMYL LNCCLDQVHV
FKPATSKAGN SEVYVVCLYY KGREAIHPLL SKMTLNFGTE MKRKALFPHH VIPDSFLKRH
EECCVFFHKY QLETISENIR LFECMGKAEQ EKLNNLRDCA VQYFMQKFQL KHLSRNNWLV
KKSSIGCSTN TKWFGQRNKY FRTYNERKML EALSWKDKVA KGYFNSWAEE HGVYHPGQSS
ILEGTASNLE CHLWHILEGK KLPKVKCSPF CNGEILKTLN EAIEKSLGGA FNLDSKFRPK
QQYSCSCHVF SEELIFSELC SLTECLQDEQ VVEPSNRIKC LLVGFSTLHN IKMHIPLEVR
LLESAELTTF SCSLLHDGDP TYQRLFLDCL LHSLRELHTG DVMILPVLSC FTRFMAGLIF
VLHSCFRFIT FFCPTSSDPL RTCAVLLCVG YQDLPNPVFQ YLQSVNELLS TLLNSDSPQQ
VLQFVPMEVL LKGALLDFLW DLNAAIAKRH LHFIIQRERE EINSLQLQN
//
