ID S8ABI7_DACHA Unreviewed; 844 AA.
AC S8ABI7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=H072_7778 {ECO:0000313|EMBL:EPS38481.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS38481.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS38481.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS38481.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC 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:EPS38481.1}.
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DR EMBL; AQGS01000546; EPS38481.1; -; Genomic_DNA.
DR RefSeq; XP_011113520.1; XM_011115218.1.
DR AlphaFoldDB; S8ABI7; -.
DR STRING; 1284197.S8ABI7; -.
DR eggNOG; KOG2198; Eukaryota.
DR HOGENOM; CLU_005316_4_2_1; -.
DR OMA; QLFTEYV; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 58..464
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..844
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 176..182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 264
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 844 AA; 94396 MW; D5754B0C961AE77A CRC64;
MSRKNRNKRG ADKKGRGGRS NGNQERTDYT QLPKDNAKFE NYYVAQGIVP DEEEFKKFWQ
SLKDTLPTTW RFTGSKGHAI SVRNTLLTKH IPQLTNTTFE GTTIPAPTPL SWYPDQLAWQ
LTVGKQVIRR SPPFKQLQAF LVSETSSGNI SRQEAVSMIP PLLMDVEPHH TVLDMCAAPG
SKTAQLIEAI HAGEEERVLE ASAQLKDTDP TSHPLEANVE VPEKLLGRAT GLVIANDADY
KRSHLLIHQT KRLNTPNFIV TNYDATLYPS LRLPAEQSED GKRAKQQYLK FDRVLCDVPC
SGDGTVRKNP LIWRDWSPAN GNGLWSTQAR ILVRGLQLLK VGGRLVYSTC SLNPIENEAV
VHAAIERCGG AGVVEIVDVS DRLPGLIRRE GMKKWKVMDR DGTWFESWEE VRGKGEPYTD
RLTRGMFPPE DAEGQLAGML NRAVRVYPHL QDTGGFFITV LHKKGAIKAA PEGETVRTGG
QRMKGVAVEG GNSGNGVAAT ADIDVPMVEE VGISSASTAN GVKRALFVEE EEVADPGSPT
KRQKLDSTVD TPVTEKDDDN DAPAPLDIPS ANQNTKVEKE AEEEQEVKVS TKKPRGNFNE
EPFKFLPASH QVLDIIKKFY VLSPYFPLDN FLVRNAEGIP VRTIYFTSTL ARQILTENEG
RGVRFVHCGV KMFNRQEVQD PEACQWRIQN EGLGLVESWV GEKRVVHLKQ KETLRWLMKE
LFPRVEDCGE IRERVESVGA GCCVLRVDLA EDEAGKEVGR LVLPLWKSRF TLNLMLPKEE
RKAMLLRLFD DTEGPRDSTK EQREADAKAR REAKAKEEGE DVEEAVEEED EDDILGDVEG
DEEN
//
