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Database: UniProt
Entry: T5AK35_OPHSC
LinkDB: T5AK35_OPHSC
Original site: T5AK35_OPHSC 
ID   T5AK35_OPHSC            Unreviewed;       750 AA.
AC   T5AK35;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=NOL1/NOP2/sun domain protein {ECO:0000313|EMBL:EQL02771.1};
GN   ORFNames=OCS_01509 {ECO:0000313|EMBL:EQL02771.1};
OS   Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS   caterpillar fungus) (Hirsutella sinensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL02771.1, ECO:0000313|Proteomes:UP000019374};
RN   [1] {ECO:0000313|EMBL:EQL02771.1, ECO:0000313|Proteomes:UP000019374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC   TISSUE=Fruit-body {ECO:0000313|EMBL:EQL02771.1};
RX   DOI=10.1007/s11434-013-5929-5;
RA   Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA   Liu X., Wang C.;
RT   "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT   fungus.";
RL   Chin. Sci. Bull. 58:2846-2854(2013).
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; KE652267; EQL02771.1; -; Genomic_DNA.
DR   AlphaFoldDB; T5AK35; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   HOGENOM; CLU_005316_7_4_1; -.
DR   Proteomes; UP000019374; 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   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; IPR049561; NSUN5_7_fdxn-like.
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:UP000019374};
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          343..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..741
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        419
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         237..243
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         269
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         298
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   750 AA;  80843 MW;  262F412D5E1B4BE4 CRC64;
     MSLYHEAAQV LSAPWSEGGS LKSRIFGRRD IKSQPNQLYA LVLETSKWSA VVKEVIEATE
     LLKHERKLSP VLSLLLVHDL LLTKGGIALP QSHGLRASVE RHRGRLKSEL TRARLRRKEV
     SLEALREQIE RDAAGEEAGY PRWVRINSLH SSIEEQLEST FSAYARAESI ADVVSKPGKH
     LYIDPHVPNL VAVTPSLDMS KTDAYSSGKI ILQDKASCFP AYLLDPRSED GDVVDACAAP
     GNKTTHLASI LHQHSPEFAS KPQMIFAFEK DTRRAQTLEK MVRIAGSKSM TRIGFGQDFL
     QVDPQDAKFK DVGALLLDPS CSGSGIIGRD SMPELHLPGA PCEHAARGAA GPSKTRKRKL
     SQVRDESDKV MRDDDGNETV INSETDLAAR LEALSSFQLM LLLHAFQFPA AKKVTYSTCS
     IYSEENEAVV MAALQSDVAR RRGWRILLRD KQVGGMKEWP VRGLVGACGG DAAVADGCIR
     SQKDDGRGVM GFFVAGFIRD GARDGARDGS RDGARDGSRD GARDGSRDGA RDGSRDGARD
     GSRDGARDGS RDGARDGSRD GARDGSRDGA RDGSRDGARD GSRDGARDGS RDGARDGSRD
     GARDGSRDGA RDGSRDGARD GSRDGARDGS RDGARDGSRD GARDGSRDGA RDGSRDGARD
     GSRDGARDGS RDGARDGSRD EDSSPKTVAA EEEGPYLRDE DGRIVRDVMG MPALKSNGEP
     VRLDPREDAD RGGRSSGDGD ESDEWNGFGD
//
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