ID A0A803KW44_CHEQI Unreviewed; 831 AA.
AC A0A803KW44;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
OS Chenopodium quinoa (Quinoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Atripliceae; Chenopodium.
OX NCBI_TaxID=63459 {ECO:0000313|EnsemblPlants:AUR62003252-RA:cds, ECO:0000313|Proteomes:UP000596660};
RN [1] {ECO:0000313|EnsemblPlants:AUR62003252-RA:cds}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PI 614886 {ECO:0000313|EnsemblPlants:AUR62003252-RA:cds};
RX PubMed=28178233; DOI=10.1038/nature21370;
RA Jarvis D.E., Ho Y.S., Lightfoot D.J., Schmoeckel S.M., Li B., Borm T.J.A.,
RA Ohyanagi H., Mineta K., Michell C.T., Saber N., Kharbatia N.M.,
RA Rupper R.R., Sharp A.R., Dally N., Boughton B.A., Woo Y.H., Gao G.,
RA Schijlen E.G.W.M., Guo X., Momin A.A., Negrao S., Al-Babili S., Gehring C.,
RA Roessner U., Jung C., Murphy K., Arold S.T., Gojobori T.,
RA van der Linden C.G., van Loo E.N., Jellen E.N., Maughan P.J., Tester M.;
RT "The genome of Chenopodium quinoa.";
RL Nature 542:307-312(2017).
RN [2] {ECO:0000313|EnsemblPlants:AUR62003252-RA:cds}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2021) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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}.
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DR AlphaFoldDB; A0A803KW44; -.
DR EnsemblPlants; AUR62003252-RA; AUR62003252-RA:cds; AUR62003252.
DR Gramene; AUR62003252-RA; AUR62003252-RA:cds; AUR62003252.
DR OMA; KSLWPQG; -.
DR Proteomes; UP000596660; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:UniProtKB-ARBA.
DR FunFam; 3.40.50.150:FF:000153; S-adenosyl-L-methionine-dependent methyltransferase superfamily protein; 1.
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; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR018314; RsmB/NOL1/NOP2-like_CS.
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-RELATED; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF25376; Pre-PUA_NSUN2; 1.
DR Pfam; PF25378; PUA_NSUN2; 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 Reference proteome {ECO:0000313|Proteomes:UP000596660};
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 73..482
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 831 AA; 92864 MW; 6285994B886F8413 CRC64;
MGGRGRSRTQ RKHFKQSRDN VWKNGSKSDA SSAAADGENN SGDAERKTRE NWEPLKTQNA
EQGIVAPEEW DDFMECLRKP LPAAFRINSS SQFCLDIRSQ LEDDFVKSLQ SEFTGDEAEA
LRPLPWYPET LAWHSEFSRK QLRKTQTLER FHEFLKLAHE IGNITRQEAV SMVPPLFLDV
HPNHFVLDTP GSKTFQLLEI IHRANEPGSL PTGMVVANDV DIQRSNLLIH QTKRMCTANL
IVTNHEAQDF PGCRLSKFHH NSSDIQSEKG LSINQLDFDR VLCDVPCSGD GTLRKAPDIW
RKWNVGMGNG LHCLQLKIAM RGISLLKVGG RMVYSTCSMN PVENEAVVAE ILRRCGDSLE
LLDVSNELPL LVRRPGLKKW KVRDKGLWLS SYKDVPKYRR PSVLSSMFPS GRNIVDSSED
SGDHVVAEAK EDDKNEIVQP NTAPLSEVND DEISSLPLER CMRIVPHDQN CGAFFIAVFH
KHSPFPVVQE KNGENVQLLH KSEESAEGAG EIASNLNDVS EAKLCEATSV GNAETDAGSL
ADVPSPKLEE EVAEDQQDLD KEETSPKNVG KKRKLQTQGK WKGVDPVILF KDETVINSIK
AFYGIDDSFP LNGHVVTRNN DTDSVKRIYY ISKSVKEVLE LNLLVGQQLK IASVGLKMFE
RQTSKDGNAT ECRYRISSEG LPVLLPYITK QILLAPIVDF KHLLQYKSIK FDALVDAELV
EAASKLELGC CVVVLKEADQ VSSFPIQVKS STIAIGCWRG RSNLNVMVTG LDCKDLLERL
EKRMETGNAE IAEPQNGGVN GDSNPNDTDM KEESKNDVDM KDEETVNMVE L
//
