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Database: UniProt
Entry: A0A453RZY4_AEGTS
LinkDB: A0A453RZY4_AEGTS
Original site: A0A453RZY4_AEGTS 
ID   A0A453RZY4_AEGTS        Unreviewed;       444 AA.
AC   A0A453RZY4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET7Gv20770800.7, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET7Gv20770800.7}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {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; A0A453RZY4; -.
DR   EnsemblPlants; AET7Gv20770800.7; AET7Gv20770800.7; AET7Gv20770800.
DR   Gramene; AET7Gv20770800.7; AET7Gv20770800.7; AET7Gv20770800.
DR   Proteomes; UP000015105; Chromosome 7D.
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; IPR023267; RCMT.
DR   InterPro; IPR023269; RCMT_subfamily_9.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF16; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 2.
DR   PRINTS; PR02010; RCMT9.
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:UP000015105};
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          69..438
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         185
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         213
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   444 AA;  48537 MW;  194030F675C7D0AD CRC64;
     RLCALWAGGR RHHCRRPRTP SDPSRSPVSL LWRAMDSPEI PPSDRREERP PASLPLPAAF
     LEFLGENGLD PALYSKADTI PRYIRLKPGM ESSVVTEIES ELKCDLMRVS WLPDFYAIPP
     EIQIAGSKAY QQGKIYGIDA ASGAAILALD VQSGDHVLDL CAAPGAKLCM LADMLGSSGS
     LTGVDVAKHR LAACRTMLQK YSLGDRSRLF VADGTSFSIL PVNSNLGSME AFVGIEDNGS
     IFSEWTSKRS WKDRQKSKKA KAAGSPHLPS TSEPELIYYG KDSGLVGLQK RYVLHPSTDA
     AACTSGYDKV LVDAECTHDG SIKHIQKFEF WGWKTLDRRV LNVERTGNLL HLQLGLLTNG
     FKLLKTGGSL VYSTCSLTVA QNENVVQQFL SKHPSAELLK INPADSWPCR SGGIQKTLRF
     DPATSQTSGL FVAKTGAVHL RRQA
//
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