CMTR1_XENLA
ID CMTR1_XENLA Reviewed; 846 AA.
AC Q6GQ76;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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; BC072871; AAH72871.1; -; mRNA.
DR RefSeq; NP_001085512.1; NM_001092043.1.
DR AlphaFoldDB; Q6GQ76; -.
DR SMR; Q6GQ76; -.
DR BioGRID; 102101; 1.
DR IntAct; Q6GQ76; 1.
DR MaxQB; Q6GQ76; -.
DR DNASU; 443938; -.
DR GeneID; 443938; -.
DR KEGG; xla:443938; -.
DR CTD; 443938; -.
DR Xenbase; XB-GENE-970210; cmtr1.S.
DR OrthoDB; 1336442at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 443938; Expressed in spleen and 20 other tissues.
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 InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR16121:SF0; PTHR16121:SF0; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 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..846
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000251244"
FT DOMAIN 87..133
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 231..450
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT DOMAIN 752..786
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2..20
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT ACT_SITE 364
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT ACT_SITE 404
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 203..207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 277..283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 335..336
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 374..376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
SQ SEQUENCE 846 AA; 97259 MW; CE7FD1AA36D3DC48 CRC64;
MKRKSDSEQQ PSVQCRKKKR IEELGLNLSS TSDDDTQYSN HGTQESSTSS TSSDSDNEEK
RPVFGSGRNE TLPDTLAEGS SSHYSMYNSV SQKLMAKMGF REGEGLGKFG QGRKEIVETS
KQKGRRGLGM VLKGFEKELN INWRSEPEAT AYEEVDWFPE CTTDIPDSDE LSDWMIVGKR
KLIIDDETEF CRDNLLTSLL QCKSAFDELE GEEMRRARTR SNPYEMIRGV FFLNRAAMKM
ANIDHVFDYM FTNPKDSQGK PKLKDKESEL LYFADVCAGP GGFSEYVLWR KKWHAKGFGM
TLKGPNDFKL EDFYAAPSEL FEPYYGEGGV DGDGDVTRPE NITAFRNFIL DNTDHKGVHF
MMADGGFSVE GQENIQEILS KQLLLCQFLV GLHVIRTGGH FICKTFDLFT PFSVGLIYLL
YCCFERVCLF KPLTSRPANS ERYVVCRGLK EGIDDVRNYL FNVNRRLNHL RNSDQDVTLV
VPLEVLRGDK QFNEYMVRSN ESCCEVQIKA LAKIHAFVQD STLSESRQAD IRRECLKLWG
VPDQARVAPT NTDARTKFFQ LIQSQNIEVF GYKPTPLTAK TLEKLIHVFD YRCMVCGSEP
KFLLGLGRSQ IYTWGGRSNE RWTRLDLKTE LPRDTLLSVE IVHELKGEGK AQRKISAIHV
LDVLFLNGTD VRTQHFTQRI QLAEKFVRAV AKPSRPDMNP IRVKEVYRLE DIEKIFLRLD
MKHIKSSGGY LRLSYTGRDD RHFVPCGLYI VKTINEPWSM AYSKSQKRKY FYNSKTKNSQ
FELPVESIAP FHTCYYERLF WEWGEGVQIH DSQRRDPDSD KLSKDAVLQF IQAHHPCMPS
SLTEDR
