MTR1A_CAEBR
ID MTR1A_CAEBR Reviewed; 874 AA.
AC A8XYX2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1A;
DE EC=2.1.1.57;
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1A;
DE Short=MTr1A;
GN ORFNames=CBG20906;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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;
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DR EMBL; HE600928; CAP37839.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XYX2; -.
DR SMR; A8XYX2; -.
DR STRING; 6238.CBG20906; -.
DR PRIDE; A8XYX2; -.
DR WormBase; CBG20906; CBP45920; WBGene00039810; -.
DR eggNOG; KOG3673; Eukaryota.
DR HOGENOM; CLU_011097_1_0_1; -.
DR InParanoid; A8XYX2; -.
DR OMA; GGILMFC; -.
DR OrthoDB; 1336442at2759; -.
DR Proteomes; UP000008549; Chromosome II.
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 Methyltransferase; mRNA capping; mRNA processing; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..874
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1A"
FT /id="PRO_0000399807"
FT DOMAIN 60..106
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 211..440
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 354
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
SQ SEQUENCE 874 AA; 100139 MW; 68DA894FA70B2BCE CRC64;
MSERGDDDRT TSTINSLAKR RYQDNLDTFQ EERAGFQQKR PHAVDDEDED FETAAPPTKQ
KTKAEEMMER MGYKAGEGLG KNKQGIQEPV ALSTQRGKTG LGHEGAKAVA RDMNEQWDDS
TENKTVEETV IWMTDIDEGI RREICDKLIK DDQWMVVRKE KKVIDDETEF CSEKELKDMI
EAKNVFDSMS DKDLREARTR ANPYETIGSA FFQNRAAMKT ANMDKIYDWI LSRENTGNNS
FLLKNPLQEG TTAENVDRHE DLFYFADVCA GPGGFSEYML WRKAFYNAKG FGFTLAGKDD
FKLQKFTASS AYFFETFYGT KKNGDVMDPE NIDSLEKFIS EGTDGQGVHL MMADGGFSVE
GQENIQEILS KRLYLCQLLV SLCIVREGGN FFCKLFDIFT PFSVGLIYLM RVCYDSISLH
KPHTSRPANS ERYITCKGLR KEFAGVVKDY LKRVNRKLDE LKNKNSKDDV MELMPLDVIK
SDEQFMKEII EHNEVLAHRQ TVYLQKYKSF AKNQGQFDKD QGNLRDECLK YWQVPNKQRP
RGGDRGSRNG NQERLNPNVV LGKYTSKICG EAELGISFRG LGAASDPQLL IGTGDAVFIY
RHGHFEQIDR DYARIPENTI LLVDCAEEVK TDGSKIRISS DPHMIRIADA AVLYGDNVSQ
LPYEARMKAA QKFALALKLT KKTIQIGWGF RAKDITPHQV CCAQTYSLKE LDEFQSNLIE
LKQRGEVIVL FKEGDRQFKT QSLRLTRIIK QDWQMGWSKS QQVPYVHSPL HQKEGSILED
QWKKREIHSS FWDSVILTNK DKQKMTEMMQ HGHNAVPSTI WSWKPCMRTE YGPYKIMNHP
EAFDGKPTIS AIKSQIAETD LSTLRSKYTP LTAL
