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Database: UniProt
Entry: A0A1Y1ZDP0_9FUNG
LinkDB: A0A1Y1ZDP0_9FUNG
Original site: A0A1Y1ZDP0_9FUNG 
ID   A0A1Y1ZDP0_9FUNG        Unreviewed;       371 AA.
AC   A0A1Y1ZDP0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000313|EMBL:ORY08294.1};
GN   ORFNames=K493DRAFT_201235 {ECO:0000313|EMBL:ORY08294.1};
OS   Basidiobolus meristosporus CBS 931.73.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC   Basidiobolus.
OX   NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORY08294.1, ECO:0000313|Proteomes:UP000193498};
RN   [1] {ECO:0000313|EMBL:ORY08294.1, ECO:0000313|Proteomes:UP000193498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORY08294.1,
RC   ECO:0000313|Proteomes:UP000193498};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:ORY08294.1}.
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DR   EMBL; MCFE01000002; ORY08294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1ZDP0; -.
DR   STRING; 1314790.A0A1Y1ZDP0; -.
DR   InParanoid; A0A1Y1ZDP0; -.
DR   OrthoDB; 317522at2759; -.
DR   Proteomes; UP000193498; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 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:SF3; SAM_MT_RSMB_NOP DOMAIN-CONTAINING PROTEIN; 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}; Reference proteome {ECO:0000313|Proteomes:UP000193498};
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          86..371
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          42..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        311
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         258
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   371 AA;  42019 MW;  E051ED1BED96135F CRC64;
     MYQSLISRRY TLGIGRVYNA LTCRAQTERS FSQNAWLSKQ KAKQAEEPVA TERHRKSKAQ
     KTLDEVEKEY SEFYESIYGT ARWTQLHPSL KSPQRYSCLL NKYSSPEENP SIPDSMQELK
     LEKLPFKSLE CFQVSEDIGG YSFPRPEKNE TTGLLTHYLL DAGSVLATEA LDIQPGEHVL
     DMCASPGGKS LCILQRMSGV IGGHLTSNEP SPTRRKTLSR VMAEYIPKEF NVDLRITGEE
     GWKFLFFGLD RYDKVLVDAP CSSDRHILHD SSEFKLWTPS RSKNLAKRQF ALLQSALKVV
     RPGGTIVYST CALSELENDG VIERALNKSK VPFEIVQENW PLGEKTKHGW ICLPDAAHGY
     GPLYFAKLKK L
//
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