MTR1_CAEEL
ID MTR1_CAEEL Reviewed; 918 AA.
AC Q9NAA5; H8ESH8; H8ESH9; H8ESI0; H8ESI1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE EC=2.1.1.57;
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE Short=MTr1;
GN ORFNames=Y53F4B.13;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 to produce m(7)GpppNmp (cap1). Cap1 modification is linked
CC to higher levels of translation. {ECO:0000250}.
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;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a;
CC IsoId=Q9NAA5-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9NAA5-2; Sequence=VSP_044213;
CC Name=c;
CC IsoId=Q9NAA5-3; Sequence=VSP_044215, VSP_044217, VSP_044218;
CC Name=d;
CC IsoId=Q9NAA5-4; Sequence=VSP_044214, VSP_044216;
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DR EMBL; AL132949; CCG28112.1; -; Genomic_DNA.
DR EMBL; AL132949; CCG28113.1; -; Genomic_DNA.
DR EMBL; AL132949; CCG28114.1; -; Genomic_DNA.
DR EMBL; AL132949; CCG28115.1; -; Genomic_DNA.
DR RefSeq; NP_001254457.1; NM_001267528.1. [Q9NAA5-1]
DR RefSeq; NP_001254458.1; NM_001267529.1. [Q9NAA5-2]
DR RefSeq; NP_001254459.1; NM_001267530.1. [Q9NAA5-3]
DR RefSeq; NP_001254460.1; NM_001267531.1. [Q9NAA5-4]
DR AlphaFoldDB; Q9NAA5; -.
DR SMR; Q9NAA5; -.
DR BioGRID; 40433; 1.
DR STRING; 6239.Y53F4B.13a; -.
DR EPD; Q9NAA5; -.
DR PaxDb; Q9NAA5; -.
DR PeptideAtlas; Q9NAA5; -.
DR EnsemblMetazoa; Y53F4B.13a.1; Y53F4B.13a.1; WBGene00013160. [Q9NAA5-1]
DR EnsemblMetazoa; Y53F4B.13b.1; Y53F4B.13b.1; WBGene00013160. [Q9NAA5-2]
DR EnsemblMetazoa; Y53F4B.13c.1; Y53F4B.13c.1; WBGene00013160. [Q9NAA5-3]
DR EnsemblMetazoa; Y53F4B.13d.1; Y53F4B.13d.1; WBGene00013160. [Q9NAA5-4]
DR GeneID; 175156; -.
DR KEGG; cel:CELE_Y53F4B.13; -.
DR UCSC; Y53F4B.13; c. elegans. [Q9NAA5-1]
DR CTD; 175156; -.
DR WormBase; Y53F4B.13a; CE47372; WBGene00013160; -. [Q9NAA5-1]
DR WormBase; Y53F4B.13b; CE47245; WBGene00013160; -. [Q9NAA5-2]
DR WormBase; Y53F4B.13c; CE47183; WBGene00013160; -. [Q9NAA5-3]
DR WormBase; Y53F4B.13d; CE47272; WBGene00013160; -. [Q9NAA5-4]
DR eggNOG; KOG3673; Eukaryota.
DR GeneTree; ENSGT00940000157172; -.
DR HOGENOM; CLU_011097_1_0_1; -.
DR InParanoid; Q9NAA5; -.
DR OMA; GGILMFC; -.
DR OrthoDB; 1336442at2759; -.
DR PhylomeDB; Q9NAA5; -.
DR PRO; PR:Q9NAA5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00013160; Expressed in embryo and 3 other tissues.
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 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 PANTHER; PTHR16121:SF0; PTHR16121:SF0; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Methyltransferase; mRNA capping; mRNA processing;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..918
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000399800"
FT DOMAIN 86..132
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 236..465
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 298
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 379
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT VAR_SEQ 457..477
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_044213"
FT VAR_SEQ 589..594
FT /note="YCKKVC -> FWKKSF (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_044214"
FT VAR_SEQ 593
FT /note="V -> M (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044215"
FT VAR_SEQ 595..918
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_044216"
FT VAR_SEQ 615
FT /note="L -> F (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044217"
FT VAR_SEQ 616..918
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044218"
SQ SEQUENCE 918 AA; 105265 MW; F23EC7238FA6966D CRC64;
MADRKSDEGE DEYQHKEQMV TNRTSSFQPK STEDSISKLA KMRAADRREE FMEERASFSA
VKRGYQAGDD EEDDFTAEEE PPAKKPLTVA ERLMAAMGHK AGEGLGKHGQ GISEPIASST
QRGRTGLGHN AGKATARDFN EVWDETTEEK TVVERVEWMT DIEEEKRAEI CEQLKDDKWM
VIGKEKRTID DETKFCSQQS ITEMIEAKNV FDLMSDKDLR EARTRANPYE TIGSAFFQNR
AAMKTANMDK IYDWILSREN TENDRFLLKN PLQESQTAEN VDRSEDLFYF ADVCAGPGGF
SEYMLWRKGF YNAKGFGFTL AGKDDFKLFK FTASSQYFFE TFYGTKDNGD VMDPVNIDSL
EAHISRGTSG LGVHLMMADG GFSVEGQENI QEILSKRLYL CQLLVSLCIV REGGNFFCKL
FDIFTPFSVG LIYLMRVCYQ SVSLHKPHTS RPANSERYIT CKGLRKEFAN VVKEYLKRVN
RKLDELKNKK SHDDVTDLMP LDVIEADQIF MDEIIRHNEF LANRQTLYLR KYQSFAKNQG
QFDKDQGNLR DECLKYWQVP NKQRPRGGDR GNRHDNMQRL NPLQVYGKYC KKVCGESEIG
NTFPDFSLNC LDAPLPNIPY EEYRFVPLAS SGSPNLLIAA GDSAFIFRSG RFESISADHI
RIPENTILLV DWAEEVVRGD GNRIKISSEP QVVRIIDAAV LFGDDVSNLP YEERMKAAEK
FVAALKQTNR KVKKGWGHRA EMIKPHLKIC AKTYSLAELD EFRSNLEKLE HNRELAVLFT
EGEFTFRCQA LRFTRIIKQE WRMGWSKSQQ KPYAHSQEHQ NAGSIPVELW AEKSIYSSFW
DSVICLNKDK KKLMEAMEHT KGKCPIPSSI WSWKACIRTP YGPEKILNYP EPFEGKPTIA
ALKAQIENTD LIVKRVRN
