ID A0A3B4V7Q9_SERDU Unreviewed; 765 AA.
AC A0A3B4V7Q9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000026622.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000026622.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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; A0A3B4V7Q9; -.
DR STRING; 41447.ENSSDUP00000026622; -.
DR Ensembl; ENSSDUT00000027098.1; ENSSDUP00000026622.1; ENSSDUG00000019312.1.
DR GeneTree; ENSGT00940000161773; -.
DR OMA; LHYCEAT; -.
DR Proteomes; UP000261420; 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; -; 2.
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 114..329
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51614"
FT ACT_SITE 282
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
SQ SEQUENCE 765 AA; 85076 MW; 3280D11B4467D5B1 CRC64;
MSSGNGTRRK VGKLQHFNNM VAPDPETLTE VQGLFSKVRI YVKPSNGEWC IPDPNIALKH
QSEEHCRLQA LKVSLNAVKN QLSDKNVQVW HQHTNSTNRA GKVIAAVRSA ANPEICTQAW
CKFYEILGTF DLLPDEALQS GELNTVHLCE APGAFITALN HYIKTSDCTR YCDWSWAANT
LNPYHEANGG STTIADDRLI ANTLPWWFFG SDNTGNIMIQ KHLLELQVFV SNMRRVDMVT
ADGSFDCQEN PDEQEALVAS LHYCEVTAAL LLLSPGGSFV LKMFTLYEHS SVCLLFLLNC
CFHSVNVFKP ATSKAGNSEV YVVCLNYDGK EAVRPLLSKL IRNYGPHLAD REALFPNALI
PESFLKQHEE VCSYFHTQQV ETITENLRLF EGMSTEQRQR LDHVRDCMAH EYLQRFQVSF
LPRSRWISRN TVSPACCSVS AGRPLGQKKQ TGSFNERREL QTLTWRERIE RGYHANWIQR
HCTEAEGTGC VLEGPLSECR VDSWYVIVGA ALPALRNSPF CEGGLLNHLN EALMETVVDW
SCVTPCDSCH LVCTASILSS IAGICVDGDS DGNKKKSQCL VFGSRSVWGA CGSQIGDLVL
TFSVEPSFPQ RGCIALHDGE PLYQQQLLGC VVFSLQTLNS GDALLLPVFS ALTRVTAAVV
LCLHVCFRSV TFRCPPPSGV VGTVLVCVGF CPEAAARILP VLTEVHNCMS QLLRGEEGKS
QSPGWDRQVL QFIPMEELLS GGLTEFLWTM NSEIIQQKLH LLMQS
//