ID   CMTR1_DANRE             Reviewed;         829 AA.
AC   Q803R5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE            EC=2.1.1.57 {ECO:0000250|UniProtKB:Q8N1G2};
DE   AltName: Full=Cap methyltransferase 1;
DE   AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE            Short=MTr1;
DE   AltName: Full=FtsJ methyltransferase domain-containing protein 2;
GN   Name=cmtr1; Synonyms=ftsjd2; ORFNames=zgc:55336;
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 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:0000250|UniProtKB:Q8N1G2}.
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:0000250|UniProtKB:Q8N1G2};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N1G2}.
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DR   EMBL; BC044371; AAH44371.1; -; mRNA.
DR   RefSeq; NP_956427.1; NM_200133.1.
DR   AlphaFoldDB; Q803R5; -.
DR   SMR; Q803R5; -.
DR   STRING; 7955.ENSDARP00000049372; -.
DR   PaxDb; Q803R5; -.
DR   GeneID; 393102; -.
DR   KEGG; dre:393102; -.
DR   CTD; 23070; -.
DR   ZFIN; ZDB-GENE-040426-696; cmtr1.
DR   eggNOG; KOG3673; Eukaryota.
DR   InParanoid; Q803R5; -.
DR   OrthoDB; 1336442at2759; -.
DR   PhylomeDB; Q803R5; -.
DR   PRO; PR:Q803R5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR   GO; GO:0097309; P:cap1 mRNA methylation; ISS:UniProtKB.
DR   GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR   CDD; cd00201; WW; 1.
DR   InterPro; IPR030376; Cap_mRNA_MeTrfase_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; PTHR16121:SF0; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF53335; SSF53335; 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   2: Evidence at transcript level;
KW   Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..829
FT                   /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT                   methyltransferase 1"
FT                   /id="PRO_0000251243"
FT   DOMAIN          79..125
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   DOMAIN          223..442
FT                   /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT   DOMAIN          745..779
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2..16
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   ACT_SITE        396
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT   BINDING         195..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         269..275
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         327..328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         366..368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         431
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
SQ   SEQUENCE   829 AA;  94900 MW;  7F52A825F7F735C7 CRC64;
     MKRAAQASDE PLKKRKTARE ESSDEDEESS QRTTSQDSSQ SESLSDVEDH KPSFSRPSDS
     QNSQGSMAHN EASNKFAMYN NVSQKLMAKM GFREGEGLGK YGQGRKEIVE ASTQRGRRGL
     GLMLKGFQGD LNVDWEDEPE PSAIEQVSWF PESSPEIPDS DELRDWMTIG EKKLKIDDEI
     EFCSENLLHL LLRCKTVFDD LEGEEMRRAR TRSNPYETIR GAFFLNRAAM KMANMDHVFD
     YMFTNPKDSQ GKVLTRDKEG ELLYFGDVCA GPGGFSEYVL WRRRWHAKGF GMTLKGANDF
     KLEDFYAAPS ELFEAYYGEG GIDGDGDITR PENISAFRNF VLDSTEGRGL HFLMADGGFS
     VEGQENLQEI LSKQLLLCQF LTALSVVRPG GHFLCKTFDL FTPFSVGLIY LLYLCFERVS
     LFKPVTSRPA NSERYVVCKG LKPGTDAVRE YMFTINLKLN QFRHSDRDVI EVVPLDIIKG
     DTDFFQYMIG SNESYCAVQI KALAKIHAYV RDTTLFEARQ ADIRKECLKL WGIPDKARVT
     PSTSDPKNKF YELVKGSEMD SFNSRPTALN SVNLEKLQHV LDYRCIVGGG EQLFLLALGR
     SQIYTWDGKA PSRWKKLENF KMELPRDTLL SVEIVQELKG EGKAQRRINA VHVLDALVLN
     GTDVRDQHFN QRIQMVEKFV KAVSKPSRPD MNPIRVKEVY RLEEMEKIFV RLEMKITKSS
     GGMPRLSYTG RDDRHFLPTG LYIIKTVNDP WTMAFSKSSK RKFFYNKQTK ESTYDLPATS
     VAPFYVCHQD RLFWAWEEGV RVHDSQTRIN PDKLSKDDVV SFIHKHYQQ