CMTR1_PONAB
ID CMTR1_PONAB Reviewed; 835 AA.
AC Q5R981;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 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=Brain cortex;
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 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; CR859510; CAH91679.1; -; mRNA.
DR RefSeq; NP_001125983.1; NM_001132511.1.
DR AlphaFoldDB; Q5R981; -.
DR SMR; Q5R981; -.
DR STRING; 9601.ENSPPYP00000018525; -.
DR Ensembl; ENSPPYT00000019263; ENSPPYP00000018525; ENSPPYG00000016562.
DR GeneID; 100172922; -.
DR KEGG; pon:100172922; -.
DR CTD; 23070; -.
DR eggNOG; KOG3673; Eukaryota.
DR GeneTree; ENSGT00940000157172; -.
DR HOGENOM; CLU_011097_0_0_1; -.
DR InParanoid; Q5R981; -.
DR OMA; GGILMFC; -.
DR OrthoDB; 1336442at2759; -.
DR TreeFam; TF314897; -.
DR Proteomes; UP000001595; Chromosome 6.
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 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.
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_0000251241"
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..67
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; 95321 MW; 03919512A73C30FB CRC64;
MKRRTDPECT APIKKQKKRV AELALSLSST SDDEPPSSVS HGAKASTTSL SGSDSETEGK
QHSSDSFDDA FKADSLVEGT SSRYSMYNSV SQKLMAKMGF REGEGLGKYS QGRKDIVEAS
SQKGRRGLGL TLRGFDQELN VDWRDEPEPS ACEQVSWFPE CTTEIPDTQE MSDWMVVGKR
KMIIEDETEF CGEELLHSVL QCKSVFDVLD GEEMRRARTR ANPYEMIRGV FFLNRAAMKM
ANMDFVFDRM FTNPRDSYGK PLVKDREAEL LYFADVCAGP GGFSEYVLWR KKWHAKGFGM
TLKGPNDFKL EDFYSASSEL FEPYYGEGGI DGDGDITRPE NISAFRNFVL DNTDRKGVHF
LMADGGFSVE GQENLQEILS KQLLLCQFLM ALSIVRTGGH FICKTFDLFT PFSVGLVYLL
YCCFERVCLF KPITSRPANS ERYVVCKGLK VGIDDVRDYL FAVNIKLNQL RNTDSDVNLV
VPLEVIKGDH EFTDYMIRSN ESHCSLQIKA LAKIHAFVQD TTLSEPRQAE IRKECLRLWG
IPDQARVAPS SSDPKSKFFE LIQGTEIDIF SYKPTLLTSK TLEKIRPVFD YRCMVSGSEQ
KFLIGLGKSQ IYTWDGRQSD RWIKLDLKTE LPRDTLLSVE IVHELKGEGK AQRKISAIHI
LDVLVLNGTD VREQHFNQRI QLAEKFVKAV SKPSRPDMNP IRVKEVYRLE EMEKIFVRLE
MKIIKGSSGT PKLSYTGRDD RHFVPMGLYI VRTVNEPWTM GFSKSFKKKF FYNKKTKDST
FDLPADSIAP FHICYYGRLF WEWGDGIRVH DSQKPQDQDK LSKEDVLSFI QMHRA
