ID   A0A5D2SST1_GOSMU        Unreviewed;       618 AA.
AC   A0A5D2SST1;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=E1A91_D11G175900v1 {ECO:0000313|EMBL:TYI55951.1};
OS   Gossypium mustelinum (Cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=34275 {ECO:0000313|EMBL:TYI55951.1, ECO:0000313|Proteomes:UP000323597};
RN   [1] {ECO:0000313|EMBL:TYI55951.1, ECO:0000313|Proteomes:UP000323597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1408120.09 {ECO:0000313|EMBL:TYI55951.1};
RA   Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA   Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA   Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA   Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA   Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT   "WGS assembly of Gossypium mustelinum.";
RL   Submitted (JUL-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}.
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DR   EMBL; CM017659; TYI55951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5D2SST1; -.
DR   Proteomes; UP000323597; Chromosome d11.
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; cd21150; PUA_NSun6-like; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
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; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF34; TRNA (CYTOSINE(72)-C(5))-METHYLTRANSFERASE NSUN6; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 2.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS50890; PUA; 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:UP000323597};
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          226..613
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        533
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         319..325
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         343
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         370
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         482
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   618 AA;  67989 MW;  098F60EADDECA83A CRC64;
     MKKKGRNLLA AFRQTFLTLQ NMTPQAEAEA EIQLNAASAR YSYNPILRWN PQVEDYFIKA
     YGSLHFAQIS KALTRPSCYS CIRVNTLKST SDAVIEKLQE IMRKSGSQND VVGINLKENK
     ASNDIDLDMV EKQSSLQNES ITKCQIPGLE YVVFVKGSGP HEIDYGYLPD KPPKEVLVSR
     KCAEAVLRGA QVYVPGIMAC SSHVEEGDLV AVSVAVEQPF PDGGWGLGIT RGTVLQGLPT
     DPYHFERHGL YIGQGTTMLS RAGIFRASQG IAVDMNNRVF KLPSFYDVLE GEIFLQNLPS
     IIAAHALDPQ KGERILDMCA APGGKTTAIA ILMKDEGEVI AADRSHNKVI DIQKLAAELG
     LTCITTYKLD ALKAVRKRNG SSDMTTLCCN KDNNDVVNQR SDSGPLGNGV SSTTFVGSNA
     DTTFKENVSN EKANERTYTS KADIRKNTRR MRNGPGRNQS LGGRVENSKG FLPNSFDRVL
     LDAPCSALGL RPRLFAGEET IESLRNHGKY QRRMFDQAVQ LVRPGGVLVY STCTINPGEN
     EALVRYALDT YKFLSLAPQH PRIGGAGLVG RCEFPDGYVE EWLRPGEEEL VQRFDPSSQL
     DTIGFFIAKF AVGPKDDI
//