ID A0A4Y9YJQ3_9AGAM Unreviewed; 740 AA.
AC A0A4Y9YJQ3;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=EVG20_g6571 {ECO:0000313|EMBL:TFY62786.1};
OS Dentipellis fragilis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Dentipellis.
OX NCBI_TaxID=205917 {ECO:0000313|EMBL:TFY62786.1, ECO:0000313|Proteomes:UP000298327};
RN [1] {ECO:0000313|EMBL:TFY62786.1, ECO:0000313|Proteomes:UP000298327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105465 {ECO:0000313|EMBL:TFY62786.1,
RC ECO:0000313|Proteomes:UP000298327};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Dentipellis fragilis.";
RL Submitted (FEB-2019) 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:TFY62786.1}.
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DR EMBL; SEOQ01000446; TFY62786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9YJQ3; -.
DR STRING; 205917.A0A4Y9YJQ3; -.
DR Proteomes; UP000298327; 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:UP000298327};
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 24..377
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 121..127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 740 AA; 79443 MW; CEA4C4E8A402EB6C CRC64;
MHPPPAPLSP TPSTSPSDND DDNDVTLCTD CSPASTSTAA ARTSPSSLDT LAQNENRYPE
GLAWQFNVPK KVLRKSPEFK KFHSFLVFET EVGNVSRQEA VSMLPPLFLD VLPHHKVLDM
CAAPGSKTAQ LLEALHLADE PTTSSIPPGL LIANDSDYKR THLLIHQSAR LPSPALMVTN
VDASIFPVLR LPAGQGSKME PLLFDRILCD VPCSGDGTIR KNVGIWKYWN PMDGNGLHGL
QLRILQRAMR MLHSDGRLVY STCSLNPVEN EAVIAEALRT IPGFELVDVS TSLPTLQRCP
GMTAWVPTTD RNLMFHDTYE AYIASIPEAK RKEAKMGKSH WPPPAEEVKG LHLDRCMRIY
PHLQDTGGFF VAVLQRKSAG KAASASPSSA VKRTADELPD VEESEAKKAK LEADVVASKD
EPMDQDTPAE TPTEATPAPE AAPKGDGNVK GKGKERQDGD SRFKENPYTY IPSDDVIVQS
CVRQLSLKPT FPAANVLVRN PSGEPSRSLY LTNDLVHAVL DANDFKKMRL MTAGTKIFTK
QDSGFGRANK NAAAAKEGEE KVEKEAVESQ WRLLSEGLPV VLPYVEPASI IEAELASGAL
RTLVEGYYPL TSTFAEVFRV LVEVKSLGSH VVRFKTGTGD GASLTHDLVL PIWKSQHSVS
LMIDKKAKSA MSLRVFGEDL TVAGREAAAK QKKPTASGVS AANTPAVASG ASGAAIPAAA
SGASAVSTPA PVAVAGEAGA
//
