ID A0A2Y9NX62_DELLE Unreviewed; 835 AA.
AC A0A2Y9NX62;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 {ECO:0000256|ARBA:ARBA00021136, ECO:0000256|RuleBase:RU368012};
DE EC=2.1.1.57 {ECO:0000256|ARBA:ARBA00011923, ECO:0000256|RuleBase:RU368012};
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
GN Name=CMTR1 {ECO:0000313|RefSeq:XP_022437506.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022437506.1};
RN [1] {ECO:0000313|RefSeq:XP_022437506.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022437506.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA to produce m(7)GpppNmp (cap1).
CC {ECO:0000256|RuleBase:RU368012}.
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:0000256|ARBA:ARBA00002664}.
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:0000256|ARBA:ARBA00024256,
CC ECO:0000256|RuleBase:RU368012};
CC -!- SUBUNIT: Interacts with POLR2A (via C-terminus).
CC {ECO:0000256|ARBA:ARBA00011551}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}.
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DR RefSeq; XP_022437506.1; XM_022581798.2.
DR AlphaFoldDB; A0A2Y9NX62; -.
DR Ensembl; ENSDLET00000031357; ENSDLEP00000028550; ENSDLEG00000020459.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule.
DR GO; GO:0097309; P:cap1 mRNA methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.12760; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 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; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 1; 1.
DR PANTHER; PTHR16121; UNCHARACTERIZED; 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; S-adenosyl-L-methionine-dependent methyltransferases; 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU368012};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042,
KW ECO:0000256|RuleBase:RU368012};
KW mRNA processing {ECO:0000256|RuleBase:RU368012};
KW Nucleus {ECO:0000256|RuleBase:RU368012};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU368012};
KW Transferase {ECO:0000256|RuleBase:RU368012}.
FT DOMAIN 87..133
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT DOMAIN 231..450
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51613"
FT DOMAIN 752..786
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 835 AA; 95179 MW; 0748F3AB2E2818FE CRC64;
MRRRNDSECT APLKKQKKRV AELALNLSST SDDEPPSSVN HAAKASATSL SGSDSETEGK
QRSSDSFDDA FKADSLVEGT SSRYSMYNSV SQKLMAKMGF KEGEGLGKYS QGRKDIVEAS
NQKGRRGLGL TLQGFDQELN VDWRAEPEPS ACEQVSWFPE CTTEIPDTQE MSDWMVVGKR
KMIIEDETEF CGEELLHSVL QCKNVFDVLD GEEMRRARTR ANPYEMIRGV FFLNRAAMKM
ANMDFVFDRM FTNPRDSYGK PLVKDREAEL LYFADVCAGP GGFSEYVLWR KKWHAKGFGM
TLKGPNDFKL EDFYSASSEL FEPYYGEGGI DGDGDITRPE NITAFRNFVL DNTDRKGVHF
LMADGGFSVE GQENLQEILS KQLLLCQFLM ALSVVRTGGH FICKTFDLFT PFSVGLIYLL
YCCFERVCLF KPITSRPANS ERYVVCKGLK VGIDDVRDYL FSVNIKLNQL RNTDSDVNLV
VPLEVIKGDH EFTDYVIRSN ESHCSLQIKA LAKIHAFVQD TTLSEPRQAE IRKECLRLWG
IPDQARVAPS STDPKSKFFE LIQGTEIDIF SYKPTLLTSK TLEKIRPVLD YRCMVSGSEQ
KFLIGLGKSQ IYTWDGRQSD RWVKLDLKTE LPRDTLLSVE IVHELKGEGK AQRKISAIHI
LDVLVLNGSD VREQHFNQRI QLAEKFVKAV SKPSRPDMNP IRVKEVYRLE EMEKIFVRLE
MKIIKGSSGT PKLSYTGRDD RHFVPTGLYI VRTVNEPWTM GFSKSFKRKF FYNKKTKNST
FDLPSDAIAP FHICYYGRLF WEWGDGIRVH DSQKPQDPDK LSKEDVLSFI QTHSA
//
