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Database: UniProt
Entry: G0WDI1_NAUDC
LinkDB: G0WDI1_NAUDC
Original site: G0WDI1_NAUDC 
ID   G0WDI1_NAUDC            Unreviewed;       496 AA.
AC   G0WDI1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   Name=NDAI0G00660 {ECO:0000313|EMBL:CCD25842.2};
GN   OrderedLocusNames=NDAI_0G00660 {ECO:0000313|EMBL:CCD25842.2};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD25842.2, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD25842.2, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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   EMBL; HE580273; CCD25842.2; -; Genomic_DNA.
DR   RefSeq; XP_003671085.2; XM_003671037.2.
DR   AlphaFoldDB; G0WDI1; -.
DR   STRING; 1071378.G0WDI1; -.
DR   GeneID; 11497238; -.
DR   KEGG; ndi:NDAI_0G00660; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   HOGENOM; CLU_005316_7_4_1; -.
DR   OMA; SFKSRIY; -.
DR   OrthoDB; 102852at2759; -.
DR   Proteomes; UP000000689; Chromosome 7.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
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; IPR048889; NSUN5_RCM1_N.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF21153; NSUN5_N; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000689};
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          144..496
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          348..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         250..256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         281
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         309
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   496 AA;  56952 MW;  46F715F8D5DD0478 CRC64;
     MNFYRDATWV LEYVEQQEAK GRISGSLQTL VLQSCTKYKL KCNPKHVYAV IDSCWKYKPY
     LEKVMKKSGI LDDIPKKKGK PMYSRLTLML LCHDLLFSKS KRIQMGKHPI KEYVLKHKSR
     LHSELVRLKL KLKVKNLSEI VDNNDSTEDV TPVRWIRINP LRCYQGRDVN AVLEELGKKF
     PKRVENWNDI VPGSIYYDEY IPHLYGIHPQ DKITSHELYK QGKIIIQDRA SCFPAHILNP
     SKDDIIIDAC AAPGNKTTHV ASYMFGDAKQ EDPHVQIYAF EKDPERAKIL EKMIKVAGCS
     KNIQVTVGDF TKAATPDKFK DVTGFIVDPS CSGSGIFGRK YVDSLNRQRN NDTTDKDKKS
     TEEDDEVPDE QEDYNKKEDL KTRLAKLSSF QFQVIKHAMS FPTAKKIVYS TCSIHAEENE
     RVVLDLLLDS KVKQWGWKVA AKESVIPTWP RRGKIEEFEE VFRDDPAKCQ ALADGCIRAL
     PRDDGGIGFF AVCFER
//
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