ID G0R826_HYPJQ Unreviewed; 585 AA.
AC G0R826;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR52810.1};
GN ORFNames=TRIREDRAFT_73918 {ECO:0000313|EMBL:EGR52810.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR52810.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR52810.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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; GL985056; EGR52810.1; -; Genomic_DNA.
DR RefSeq; XP_006961662.1; XM_006961600.1.
DR AlphaFoldDB; G0R826; -.
DR STRING; 431241.G0R826; -.
DR EnsemblFungi; EGR52810; EGR52810; TRIREDRAFT_73918.
DR GeneID; 18488268; -.
DR KEGG; tre:TRIREDRAFT_73918; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_73918; -.
DR eggNOG; KOG2360; Eukaryota.
DR HOGENOM; CLU_005316_7_4_1; -.
DR OrthoDB; 102852at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0070475; P:rRNA base methylation; IEA:EnsemblFungi.
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:UP000008984};
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..503
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 327..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..585
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
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 585 AA; 64327 MW; 49731DAA000075AE CRC64;
MSLYHEAAEI LTSSSDTGGS LKSRVFGKKK GKAPPGQLYA LVLETAKWSP VLKEVIEKAD
ILRLERKLTP TLALLLVHDL LLAKGGIALP QSHGLRASVE RHKGRLSSEF TLARLRRKAP
TIEALREQVE RASAGEEANY PRWVRVNALK SSVEEQLETT FAKHTRADSI QDIVTKGGRH
IYIDPHVPNL LAVSPGMDFA KVEAYTSGKI ILQDKASCFP AYLLDPRSED GDVIDACSAP
GNKTTHLAAI LYQHRPEFED APQTIFAFEK DSRRAKTLEK MVNIAGSKPI TRIGFGQDFL
QVDPLSEKYK DVGALLLDPS CSGSGIVGRD SMPELHLPDP PADNRGGKAK PNQANANKKK
RRRDEAEEQA QNVLVDDDGN ETVVKSEKDL EARLEALSAF QLTLLLHAFR FPRAKKITYS
TCSIHSQENE RVVIRALASD IAKAKGWRIL RREDQVSGLR DWPVRGLVEA AEGDETVAEG
CIRSYKGDGR GVMGFFVAGF VRDSVDAGAH DESGPYLRDD DGRIVRDVVG MPVLKSTGKA
VALRDGADEE ENDDDEEEDE DEDDIDDEND GDDGGEDEWE GISDA
//