ID   CMTR2_DANRE             Reviewed;         743 AA.
AC   Q7ZVS8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
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; ORFNames=zgc:55686;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) 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). {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; BC045425; AAH45425.1; -; mRNA.
DR   RefSeq; NP_998598.1; NM_213433.1.
DR   AlphaFoldDB; Q7ZVS8; -.
DR   SMR; Q7ZVS8; -.
DR   STRING; 7955.ENSDARP00000052804; -.
DR   PaxDb; Q7ZVS8; -.
DR   PRIDE; Q7ZVS8; -.
DR   GeneID; 406742; -.
DR   KEGG; dre:406742; -.
DR   CTD; 55783; -.
DR   ZFIN; ZDB-GENE-040426-2775; cmtr2.
DR   eggNOG; KOG3674; Eukaryota.
DR   InParanoid; Q7ZVS8; -.
DR   OrthoDB; 1327262at2759; -.
DR   PhylomeDB; Q7ZVS8; -.
DR   PRO; PR:Q7ZVS8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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:0097309; P:cap1 mRNA methylation; IBA:GO_Central.
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..743
FT                   /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT                   methyltransferase 2"
FT                   /id="PRO_0000326183"
FT   DOMAIN          113..326
FT                   /note="Adrift-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYT2"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYT2"
FT   ACT_SITE        279
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT   BINDING         152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
SQ   SEQUENCE   743 AA;  83655 MW;  FF1299B2079A73B1 CRC64;
     MNRGRGVRKR NAPEKASILE TCDEEIRAEV AQLFNKVRSY VPPAGEKWTL PDPNVVLCDP
     HVSHPRLQAL KHSLNEVKNQ LSDKDLSVWH QHTCFTNRAG TVTSHLRSTT NAELCTQAWA
     KFYEILGTFQ LLPDSALKTG ELNSIHLCEA PGAFISALNH FLKTSSLHCD WNWIANTLNP
     YYEANGRGCT ITDDRLIVHT LPWWFFGSDN TGDIMLQKHL LELPRFVSNM RSVDLVTADG
     SFDCQGDPGE QERLVAPLQH CEAICALLLL GTGGSFVLKM FTLFEHSSVC LLYLLACCFR
     SVNIFKPGTS KSGNSELYIV CLDYQAKEQI RPLLSKLIRN YGPDLASTAS LFPRRCIPDS
     FLSQHEEICT FFQALQVNTI QENLRLFVCM STEQRRRLEQ LREYAAEFYT KRFSVQYLPR
     KSWVCRGGVV RWVKVCERKQ MGSLNQRKEM ELQGWKQRLA QGNYGPFIEK HLVAAEGCEV
     VLNGPLDECD LGAWFALEGA ALPKVCSSIF CDQEMLDFLN EALEGNLRVK TVNWSLKALP
     TCSSCSSDSP VSILSEICSH PDVTSCLVLG SQSWCDDKLT GVRIQPEFLQ GPSYCGVQNV
     TMHDGQPDYQ LELLNAVLFA LQKQDQGSTL VIPLSSALTR FTSGLVFTLH LCFRYITFRC
     LSGWPPAALV CMGFSPPSAL PSLLDFLQNV MEKMKKVELG RQVLQFVPLE ELLRGELPHF
     LSSFNTAVIR QQLHMLIQLD QST