ID G4TS38_SERID Unreviewed; 723 AA.
AC G4TS38;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Related to NCL1-tRNA (Cytosine-5-)-methyltransferase / probable Orotate phosphoribosyl transferase {ECO:0000313|EMBL:CCA74131.1};
GN ORFNames=PIIN_08085 {ECO:0000313|EMBL:CCA74131.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA74131.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA74131.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA74131.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:CCA74131.1}.
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DR EMBL; CAFZ01000282; CCA74131.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TS38; -.
DR STRING; 1109443.G4TS38; -.
DR eggNOG; KOG2198; Eukaryota.
DR HOGENOM; CLU_005316_4_2_1; -.
DR InParanoid; G4TS38; -.
DR OMA; QLFTEYV; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000007148; 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:UP000007148};
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 86..429
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..503
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 211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 238
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 723 AA; 81139 MW; D77C4F8A8649888A CRC64;
MEDPKEHPSV SSERNGTQTA TEPTAKTTGE AGGKRTGKDK KEKKKKKAKP QRTGEWATDI
ERKNASFERY YEAQNLFEDR TELDLMLDSL KRDLPTTFRV TGSRITANDV NDIIRKVHVP
NLTGIQHEGV DVDPPRPIPW YLGGLAWQIN VNKSVVRKLV PFQQMQRFLV YETEVGNISR
QEATAQILEA MHTLPSGEPV SSPSGIIIAN DSDYKRAGLL VHQSARLPSP SLVVTNVDAS
YYPNIYIDNQ GMTLEFDRIL CDVPCSGDGT MRKNAVIWRQ WTIQGANGLH CLQLRILQRA
MRMLAPGGRI VYSTCSLNPV ENEAVVAAAI KSSAGEYQLV DVSNRLPELV RRPGITSWQV
CTDKDTMNME SSFTAYWERL NDKQRADSKI VETMFPPQEV HELNLDRCWR IYPHLQNTGG
FFVAVLERSP TYVLPPPKKK HTKRPVDDLA NDSEQDGERT RKRARVDTNV EVTLDTEMAD
PTPVDTEPGP VEKEKKEKGK GTYKEDPYTY VDANSELVTY LLKCLQVQDT ITNARGETEA
FPRHNLFVRN ADATTLRSVY LSNDRVKAVL TSNEPSRLRF ISAGVKLAVR QDAGARKAMA
QGGPDAETAQ KYRVLHDSVS QVLPFMRPED VIHGDTRLLK VFVERMYPLA REFASPYGEV
LGRCELGHHV LQIDPSSADS EVLKGGECAY VIEVWITLTV GQVDAPTDIP HLEVERVAQS
DAR
//
