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Database: UniProt
Entry: A0A183CD42_GLOPA
LinkDB: A0A183CD42_GLOPA
Original site: A0A183CD42_GLOPA 
ID   A0A183CD42_GLOPA        Unreviewed;       328 AA.
AC   A0A183CD42;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=SAM_MT_RSMB_NOP domain-containing protein {ECO:0000313|WBParaSite:GPLIN_001079400};
OS   Globodera pallida (Potato cyst nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Globodera.
OX   NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001079400};
RN   [1] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Aslett M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA   Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA   Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA   Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT   "The genome and life-stage specific transcriptomes of Globodera pallida
RT   elucidate key aspects of plant parasitism by a cyst nematode.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:GPLIN_001079400}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   AlphaFoldDB; A0A183CD42; -.
DR   WBParaSite; GPLIN_001079400; GPLIN_001079400; GPLIN_001079400.
DR   Proteomes; UP000050741; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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          64..328
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        321
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         188..194
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         245
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         268
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   328 AA;  37524 MW;  5F74E29B0FC153EC CRC64;
     MGDSFPLKIE SEHRQKAIAS LKQRPPAKGI RQNYELNRFE RRNDALFEFF KQQGIVPDSE
     WDQFRESVVS ELPSSFRIQR SLPERDCLAD YLERHFFKQI ASIKENEAVP TESDSNGIHP
     PKPIPFVRYA YQTKMARATI RRHPILKEFH QFLVNETELG NISRQEACSM VPPLLLDVQP
     HHRVLDACAA PGSKTMQIIE LMHENCSNPE GLVVANDSDY KRCYLLVRQT LKRMPTANVV
     VVSHDASQLP TVLDANKRPV LFDRILCDLI CSGDGTLRKN PELWKSWDPL KGVNLHKLQL
     QIALRCLELL AEGGLMIYST CSLNPVEI
//
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