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Database: UniProt
Entry: A7RV47_NEMVE
LinkDB: A7RV47_NEMVE
Original site: A7RV47_NEMVE 
ID   A7RV47_NEMVE            Unreviewed;       422 AA.
AC   A7RV47;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 64.
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};
DE   Flags: Fragment;
GN   ORFNames=NEMVEDRAFT_v1g163068 {ECO:0000313|EMBL:EDO44686.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO44686.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO44686.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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; DS469542; EDO44686.1; -; Genomic_DNA.
DR   RefSeq; XP_001636749.1; XM_001636699.1.
DR   AlphaFoldDB; A7RV47; -.
DR   STRING; 45351.A7RV47; -.
DR   EnsemblMetazoa; EDO44686; EDO44686; NEMVEDRAFT_v1g163068.
DR   GeneID; 5516727; -.
DR   KEGG; nve:5516727; -.
DR   eggNOG; KOG3674; Eukaryota.
DR   HOGENOM; CLU_019427_1_1_1; -.
DR   InParanoid; A7RV47; -.
DR   OMA; MFEERTI; -.
DR   OrthoDB; 5488054at2759; -.
DR   PhylomeDB; A7RV47; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00946};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00946}.
FT   DOMAIN          114..325
FT                   /note="Adrift-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000259|PROSITE:PS51614"
FT   ACT_SITE        278
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         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT   BINDING         238
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT   NON_TER         422
FT                   /evidence="ECO:0000313|EMBL:EDO44686.1"
SQ   SEQUENCE   422 AA;  48525 MW;  B5852C92AB98DBFC CRC64;
     MAPKRRNKQR YHPYGESALL SAETLQFIEE ETTRLYNKRF TLKAKDKQCE LPSSELLFTT
     TPETINVLQE MKRNLNESKS MLNDIDIVEW HQHTRRTHKA GLVVKTLRET MRAEMCTQAF
     AKLYEVLASY NVVPTEAVSS KKLYGVHLCE APGAFVAATN HYLRNHHPDL EWVWLGATLN
     PYYEGHSPKA LLDDDRFIVE TLQNWDFGAD GTGDLMQLEN LNHLAEACQG KVHLVTADGS
     IDCSDEPEEQ ENAVSQLIFC EAVTALTVLA TGGCYVFKMF TTLEHHMVCL MYLMCCLFEE
     VHVIKPGTSK GGNSEVYITC CGYTGNLSPQ YHEILYTAYQ QDTAEKVLFP LNSIPREFLY
     LIKECQEYFI NLQNQEISMN IQYFHHMNRL EKKQLFHLRK QAAGYYMEKF GVQPIAEEER
     VV
//
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