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Database: UniProt
Entry: A0A0D8X8E7_DICVI
LinkDB: A0A0D8X8E7_DICVI
Original site: A0A0D8X8E7_DICVI 
ID   A0A0D8X8E7_DICVI        Unreviewed;       650 AA.
AC   A0A0D8X8E7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Methyltransferase domain protein {ECO:0000313|EMBL:KJH40840.1};
GN   ORFNames=DICVIV_13197 {ECO:0000313|EMBL:KJH40840.1};
OS   Dictyocaulus viviparus (Bovine lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX   NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH40840.1, ECO:0000313|Proteomes:UP000053766};
RN   [1] {ECO:0000313|EMBL:KJH40840.1, ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH40840.1,
RC   ECO:0000313|Proteomes:UP000053766};
RA   Mitreva M.;
RT   "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX   PubMed=26856411; DOI=10.1038/srep20316;
RA   McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA   Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA   Sternberg P.W., Gasser R.B., Mitreva M.;
RT   "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT   lungworm biology and support future intervention.";
RL   Sci. Rep. 6:20316-20316(2016).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; KN716997; KJH40840.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D8X8E7; -.
DR   STRING; 29172.A0A0D8X8E7; -.
DR   Proteomes; UP000053766; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR026113; METTL2/6/8-like.
DR   InterPro; IPR049561; NSUN5_7_fdxn-like.
DR   InterPro; IPR048889; NSUN5_RCM1_N.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22809:SF11; METHYLTRANSFERASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR22809; METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF13489; Methyltransf_23; 1.
DR   Pfam; PF21148; NSUN5_fdxn-like; 1.
DR   Pfam; PF21153; NSUN5_N; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000053766};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          399..650
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        634
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         534
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         561
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         581
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   650 AA;  75466 MW;  29749CDE383505A4 CRC64;
     MSDSTVRFPT TDTWVNDRPE CKPFGTRYLV DETRVWDYNA WDNVDWSDEM ERRALQAVDA
     QKAHAVDNLR AKKLIEEPSK QWDAFYSKHT NNFFKDRKWL LKEFPELDMA NYPEDSTIRI
     LEVGCGVGNT SYPLLMWDKH HRLFIYSCDY SYVAVQALKR DVKYDQSRIY GFVWDITEDA
     PRDAPDENSL DYVVCIYVIS AIHPSKVRKA IDNLIRLLKP GGMLLFKDYG KFDLTQLRFK
     KERYIEENLY CRGDGTLVYF FNKDELDALL QSSGLIKKTS ILDKRLIVNR AKRVKMYRQW
     LQNKKSLLRL SSETLRFRSV FDDLLKAPEI RKLLAHSELK GDIYLTYVLF YEFLVGAGLE
     KASARVKAVI NKYSKAIHDR EKSLAVIGRG IAAVKENEKP RQFARFIPRY ARVNTLRWTM
     REAVERLIYE GWKVVFLTAA DDFAHEVKNM SGYQVFVDPH IENLLVFPQS ADFYSYWLVE
     QGYLILQDKA SCLPAYLLSP SLDSHVFDAC AAPGMKTSHV AAILRGGGRV WAMDRSENRV
     KIMTKLLKQC GAENISILHG DFLKIDINDK RFSKVNYAIV DPPCSGSGMV KRMDELTGQN
     FTPERLKKLK NLQAMILKHA LKFPYLKRLV YSTCSVHEEE NEQVVDEVLY
//
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