CMTR1_BOVIN
ID CMTR1_BOVIN Reviewed; 835 AA.
AC A2VE39;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) 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 -!- SUBUNIT: Interacts with POLR2A (via C-terminus).
CC {ECO:0000250|UniProtKB:Q8N1G2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N1G2}.
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DR EMBL; BC133559; AAI33560.1; -; mRNA.
DR RefSeq; NP_001075899.1; NM_001082430.2.
DR AlphaFoldDB; A2VE39; -.
DR SMR; A2VE39; -.
DR STRING; 9913.ENSBTAP00000022726; -.
DR PaxDb; A2VE39; -.
DR PRIDE; A2VE39; -.
DR Ensembl; ENSBTAT00000022726; ENSBTAP00000022726; ENSBTAG00000017091.
DR GeneID; 509620; -.
DR KEGG; bta:509620; -.
DR CTD; 23070; -.
DR VEuPathDB; HostDB:ENSBTAG00000017091; -.
DR VGNC; VGNC:27489; CMTR1.
DR eggNOG; KOG3673; Eukaryota.
DR GeneTree; ENSGT00940000157172; -.
DR HOGENOM; CLU_011097_0_0_1; -.
DR InParanoid; A2VE39; -.
DR OMA; GGILMFC; -.
DR OrthoDB; 1336442at2759; -.
DR TreeFam; TF314897; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000017091; Expressed in diaphragm and 106 other tissues.
DR ExpressionAtlas; A2VE39; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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 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 Acetylation; Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..835
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000399798"
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..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..835
FT /note="Interaction with POLR2A"
FT /evidence="ECO:0000250"
FT MOTIF 2..19
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..57
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"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC3"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC3"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
SQ SEQUENCE 835 AA; 95142 MW; 05530E236806A230 CRC64;
MKRRNDSECT APLKKQKKRV AELALSLSST SDDEPPSSVN HAAKASATSL SGSDSETEGK
QRSSDSFDDA FKADSLVEGT SSRYSMYNSV SQKLMAKMGF KEGEGLGKYS QGRKDIVEAS
NQKGRRGLGL TLQGFDQELN VNWRDEPEPS ACEQVSWFPE CTTEIPDTQE MSDWMVVGKR
KMIIEDETEF CGEGLLRSVL KCKSVFDVLD GEEMRRARTR ANPYEMIRGV FFLNRAAMKM
ANMDFVFDRM FTNPRDSYGK PLVKDREAEL LYFADVCAGP GGFSEYVLWR KRWHAKGFGL
TLKGPHDFKL EDFYSASSEL FEPYYGEGGI DGDGDITRPE NINAFRNFVL DNTDHKGVHF
LMADGGFSVE GQENLQEILS KQLLLCQFLM ALSVVRTGGH FICKTFDLFT PFSVGLIYLL
YCCFERVCLF KPITSRPANS ERYVVCKGLK VGIDEVRDYL FSVNIKLNQL RNTDSDVNLV
VPLEVIKGDH EFTDYMIRSN EGHCSLQIKA LAKIRAFVQD TTLIEPRQAE IRKECLRLWG
IPDQARVAPS STDPKSKFFE LIQGTEIDIF SYKPTPLTAK TLEKIRPVLD YRCMVSGSEQ
KFLIGLGKSQ IYTWDGRQSD RWVKLDLKTE LPRDTLLSVE IVHELKGEGK AQRKISAIHI
LDVLVLNGSD VREQHFNQRI QLAEKFVKAV SKPSRPDMNP IRVKEVYRLE EMEKIFVRLE
MKIIKGSSGT PKLSYTGRDD RHFVPTGLYI VRTVNEPWTM GFSKSFKRKF FYNKKTKNST
FDLPADAIAP FHICYYGRLF WEWGDGIRVH ESQKPQDPDK LSKEDVLSFI QTHSA
