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Database: UniProt
Entry: A8XLQ0_CAEBR
LinkDB: A8XLQ0_CAEBR
Original site: A8XLQ0_CAEBR 
ID   A8XLQ0_CAEBR            Unreviewed;       555 AA.
AC   A8XLQ0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 {ECO:0000256|ARBA:ARBA00021134};
DE            EC=2.1.1.296 {ECO:0000256|ARBA:ARBA00012770};
GN   ORFNames=CBG15196 {ECO:0000313|EMBL:CAP33554.2,
GN   ECO:0000313|WormBase:CBG15196}, CBG_15196
GN   {ECO:0000313|EMBL:CAP33554.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP33554.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP33554.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP33554.2,
RC   ECO:0000313|Proteomes:UP000008549};
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., 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., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC         ribonucleoside)-(ribonucleotide) in mRNA + S-adenosyl-L-methionine =
CC         a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC         ribonucleoside)-(2'-O-methyl-ribonucleotide) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:67024, Rhea:RHEA-COMP:17169,
CC         Rhea:RHEA-COMP:17170, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:167612, ChEBI:CHEBI:167614;
CC         EC=2.1.1.296; Evidence={ECO:0000256|ARBA:ARBA00024560};
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DR   EMBL; HE601055; CAP33554.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XLQ0; -.
DR   STRING; 6238.A8XLQ0; -.
DR   WormBase; CBG15196; CBP38227; WBGene00035518; -.
DR   eggNOG; KOG3674; Eukaryota.
DR   eggNOG; KOG3935; Eukaryota.
DR   HOGENOM; CLU_432275_0_0_1; -.
DR   InParanoid; A8XLQ0; -.
DR   OMA; PYFENRS; -.
DR   OrthoDB; 5488054at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR   GO; GO:0097309; P:cap1 mRNA methylation; IBA:GO_Central.
DR   GO; GO:0097310; P:cap2 mRNA methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.12760; -; 1.
DR   InterPro; IPR025807; Adrift-typ_MeTrfase.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR16121:SF2; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51614; SAM_MT_ADRIFT; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00946};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00946};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00946}.
FT   DOMAIN          91..300
FT                   /note="Adrift-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000259|PROSITE:PS51614"
FT   ACT_SITE        253
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT   BINDING         213
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
SQ   SEQUENCE   555 AA;  64595 MW;  66CB73DE0B58B790 CRC64;
     MSENTKLDAN PIEFMSNQEM DNYYNNHVFT FLDHQKMDSK LDTFEFQNHS KRLEEVALKI
     RSINNSKSYD EHTDLMHDYW RCPNILRNHF ICKNKAFLKM LEILESGFLN HLPWDNLNSF
     HLCEGPGYFL DAIYVHRLRT TSQHSEWHWG ANTLNPYFEN RSCFEKLIDD SHIRGHERNW
     YFGPSDDGDV AKLTEDYLIE KGLKGTFDLV TADGSTNTQG KEGQIEEIVG PLIRAEVNAA
     LLLLKPGGSL ILKTYRFCEK QIQDVMFLLA DNFSEIRVVK PMASRPGSSE RYLICNGFGG
     HLPLPMDLLV LCDEFFIIRQ VSRMDLHVKT FENEHGNQKL SWKNRKRFME QMKSYVFEEK
     IPKNLKKMFP SGTSPWLSLY GHDLIRRNTL ENQTFAIQNY INSANLFPKD NFDPEWIMDQ
     ILGQSKMLVT SDIKLESKDS LFIEPIALQA LLSNQNLELT NLPTNGFWLS RISASMFVLL
     KLVFQNMESG EGWLKWQGRI SNNRIHDLLS RLLLELSLLP DGTSIRCFVP IDVLDLFHQH
     ICFQNVMILH SMKCL
//
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