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Database: UniProt
Entry: A0A5E4E7J0_PRUDU
LinkDB: A0A5E4E7J0_PRUDU
Original site: A0A5E4E7J0_PRUDU 
ID   A0A5E4E7J0_PRUDU        Unreviewed;       500 AA.
AC   A0A5E4E7J0;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=PREDICTED: probable 28S rRNA {ECO:0000313|EMBL:VVA11754.1};
GN   ORFNames=ALMOND_2B011368 {ECO:0000313|EMBL:VVA11754.1};
OS   Prunus dulcis (Almond) (Amygdalus dulcis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3755 {ECO:0000313|EMBL:VVA11754.1, ECO:0000313|Proteomes:UP000327085};
RN   [1] {ECO:0000313|Proteomes:UP000327085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Texas {ECO:0000313|Proteomes:UP000327085};
RX   PubMed=31529539; DOI=10.1111/tpj.14538;
RA   Alioto T., Alexiou K.G., Bardil A., Barteri F., Castanera R., Cruz F.,
RA   Dhingra A., Duval H., Fernandez I Marti A., Frias L., Galan B.,
RA   Garcia J.L., Howad W., Gomez-Garrido J., Gut M., Julca I., Morata J.,
RA   Puigdomenech P., Ribeca P., Rubio Cabetas M.J., Vlasova A., Wirthensohn M.,
RA   Garcia-Mas J., Gabaldon T., Casacuberta J.M., Arus P.;
RT   "Transposons played a major role in the diversification between the closely
RT   related almond and peach genomes: results from the almond genome
RT   sequence.";
RL   Plant J. 101:455-472(2020).
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; CABIKO010000004; VVA11754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5E4E7J0; -.
DR   SMR; A0A5E4E7J0; -.
DR   EnsemblPlants; VVA11754; VVA11754; Prudul26B011368.
DR   Gramene; VVA11754; VVA11754; Prudul26B011368.
DR   InParanoid; A0A5E4E7J0; -.
DR   OMA; SFKSRIY; -.
DR   OrthoDB; 102852at2759; -.
DR   Proteomes; UP000327085; Chromosome 1.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 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; 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:UP000327085};
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          160..448
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        382
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         249..255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         320
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   500 AA;  55488 MW;  DD450E0D7C06972D CRC64;
     MARRKHRATP PSAAAEKSDN RRHLSMERSA YFARREAAKV LKLVLQGDAK RQSVGSIKTL
     VYGPSVRNKR GTFALICQTL KYLLIIQDLL KTADVLNSKW KKQDELVYIV TYDILFGQVS
     SSAVGDAEKF LMRRKEALQA ALARLLVKKK VKSVEELIAL YDIPDISNPR YVRVNTLKMD
     VETAVLELQK QFKVQKDDLV PDLLVLPPGS DLHDHHLIKN GNVFMQGKAS SMVAAALAPK
     PEWEVLDACS APGNKTVHLA ALMREKGKVI ACELNEERVK RLKETIRLSG ASNIKVVHGD
     FLDLNPEDPP YSKVRAILLD PSCSGSGTAS ARLDHLLPSS APGQAADFTS TERLNKLAAF
     QRKALAHALS FPDVERVVYS TCSVNQVENE DVVKSVLPLA ASNGFQLETP FPEWHRRGLP
     VVEGAECLLR TDPKEDKEGF FIALFVRRSS GNQSEKPNAD GHTHSASTAK RSYVGAHLNL
     FKMFAHAHLR RRNCSHCDCC
//
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