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Database: UniProt
Entry: A0A0A2W0Y2_BEABA
LinkDB: A0A0A2W0Y2_BEABA
Original site: A0A0A2W0Y2_BEABA 
ID   A0A0A2W0Y2_BEABA        Unreviewed;       634 AA.
AC   A0A0A2W0Y2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Putative methyltransferase C2C4.06c {ECO:0000313|EMBL:KGQ12272.1};
GN   ORFNames=BBAD15_g1985 {ECO:0000313|EMBL:KGQ12272.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ12272.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ12272.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ12272.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ12272.1}.
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DR   EMBL; ANFO01000130; KGQ12272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2W0Y2; -.
DR   STRING; 1245745.A0A0A2W0Y2; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   HOGENOM; CLU_005316_7_4_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProt.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent 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; IPR001678; MeTrfase_RsmB/NOP2.
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; PF21148; NSUN5_fdxn-like; 1.
DR   Pfam; PF21153; NSUN5_N; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030106};
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          132..500
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          341..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..563
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..596
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..634
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        437
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         244..250
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         277
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         306
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         326
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   634 AA;  69580 MW;  B11A87C16157439A CRC64;
     MSLYHEGADV LVASSTEGGS LKSRIFGRRN IKSSPGQLYA LVFETCKWSL VLKEVIDAAA
     ILSIEKKLTP ILALLLAHDL LLAKGGVALP KTHGLRVTIE KHKARLTSEL TRARLRRKAP
     TMEALKQQID RAAAGEEALI PRWVRINTIK TTVEEQLSTT FKGFQQVTTI DEVLASATTS
     TGAKQRRILI DHHIPNLVAV TQGIDLSKTE AYKSGKIIFQ DKASCFPAYL LDPLPEDGDV
     VDGCAAPGNK TTHLAAICYA RRPDFVTPDP QKIFAFEKDK RRSQTLTKMV KIAGSQGWTR
     VGFGQDFCQV DPTGQQFSKV GALLLDPSCS GSGIVGRDTM PELHIPGASP AAAAGKKMDK
     GKGKANDERG GENKKRKLDD KDAAQSSIMI DDEGNETVID SEKDLEARLQ ALAGFQLKIL
     LHALTFPTAK KVTYSTCSIH SQENEHVVMK VLESEVAQRR VRGLKESCGG DAEVADACIR
     SYKGDGHGVM GFFVAGFVRD GSKDEAMDPD GPYMRDERGM IVRDGMGMPY LKKTGKPVEL
     LPRDESEDGD EDEDEDEEEM DPDGPYVRDG AGLIIRDDDG MPFLKRKSKP GELVKIEESE
     DDDEEEDEDE DSESDDDDDE DDDDDEEGWE GFDE
//
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