ID A0A0R3RHE9_9BILA Unreviewed; 662 AA.
AC A0A0R3RHE9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000086901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000086901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0R3RHE9; -.
DR STRING; 1147741.A0A0R3RHE9; -.
DR WBParaSite; EEL_0000086901-mRNA-1; EEL_0000086901-mRNA-1; EEL_0000086901.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProt.
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 S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00946};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00946}.
FT DOMAIN 93..303
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51614"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
SQ SEQUENCE 662 AA; 76197 MW; 6A8F8160B8C8B6AA CRC64;
MAEVEQLKSN YGQVVDSLFS KHVKLKPLPI DALSKIVTDE ELASQSRNLS ICLNELREMI
PSDHLDDWRR HTSFTHPLRS FIRERARSAY SAEYSTQAFF KFYEILIRFS HLCLPCSDTV
RSFHLCESPG AFISALNVYL TLQKDKPSWQ WYANSLNPHY EWNSPFDMFL DDELITSTYP
NWLFGPDNSG DILKWTDEYI DSIAEKVGKF SLITADGSVY CQDNPAEQER IIFPLLQKEI
EISLSLLGTN GTFIVKMYTS FLNDTITLLS RLIMCFEEIH VIKPSCSKPG NSEVYLLCAS
YAPNEQCEEE AAELSTFYRK VLLECSKFFV EHQMQMIWFN IATFGKVKGD LKDFIEQKKI
QAAGIYEQIM NTSKFEKFAA ELFSASFTLF KRPNPWKFSK LGGFIEELRN ITTEEMQILI
ENMIIYDFMK GDNVEAQQKF DISLCRICDC CRWVDNFCIS NSSASAEIIS LEEILEMGNV
PSEASIKHTL FLEPKTLALF KCTSLEVLDI CCVVSSYTIN VSLEKPETTL HHKSTAEISS
SVLRSQFDWI LVLEEIFLHA SNHQARYLLQ IHFAFRNTKT KKKLVSKLCI RIPSSLMLTR
FTISFMAFCS LCYKNVVLLC PEENSRTTSN QLICCNSRKN VHSCAEFLHY LSIIKEKLLG
RL
//
