ID A0A0B7N8X3_9FUNG Unreviewed; 393 AA.
AC A0A0B7N8X3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN Name=PARPA_08025.1 scaffold 31147 {ECO:0000313|EMBL:CEP13889.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP13889.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP13889.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP13889.1};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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}.
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DR EMBL; LN730585; CEP13889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N8X3; -.
DR STRING; 35722.A0A0B7N8X3; -.
DR OrthoDB; 8499at2759; -.
DR Proteomes; UP000054107; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
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; IPR023269; RCMT_subfamily_9.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22807:SF16; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 2.
DR PRINTS; PR02010; RCMT9.
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:UP000054107};
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 41..389
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 199..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 393 AA; 44380 MW; 779AA67A97A65564 CRC64;
MSYNDNNGQV DSMKRDHATS FDIKRLPDSF KKFLLDNSID PQIYTVANLP RYIRINTHLP
DDKRPTLEDL KSQFETDKVY AVDGIDNFFM VQLEGTTQRI SDITAYKNQA VFGIDLSSAI
AVKALEIQKD DQVLDLCCAP GAKLCMIANI LGKDGLGTAT GVDLAGHRLA TCRSMLKKYK
VGEKVRLFEA DGTTFQVPAP SRLGNKMIDP EESEQDGARK RQKTSLVEPF WSARLLRHDK
QTSNTLYDKV LVDAECTHDG SIAHILKYEK WGWDAFETNF MDPRRIDNIA ELQCNLMKQG
WNMLKSGGTM VYSTCSLSIR QNEDNVAWFL NEYQDAALEK IPSFNLKPAK IKQQQGFPAL
QDKIEANCLR FDPISSSTSG FFVARFVKKP LFA
//