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   03-AUG-2022, entry version 68.
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}.
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; 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   CTD; 55783; -.
DR   eggNOG; KOG3674; Eukaryota.
DR   InParanoid; Q5RAY7; -.
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   InterPro; IPR025807; Adrift-typ_MeTrfase.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01728; FtsJ; 1.
DR   SUPFAM; SSF53335; SSF53335; 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