ID   A0A383VZV5_TETOB        Unreviewed;       698 AA.
AC   A0A383VZV5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=BQ4739_LOCUS10188 {ECO:0000313|EMBL:SZX69926.1};
OS   Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX   NCBI_TaxID=3088 {ECO:0000313|EMBL:SZX69926.1, ECO:0000313|Proteomes:UP000256970};
RN   [1] {ECO:0000313|EMBL:SZX69926.1, ECO:0000313|Proteomes:UP000256970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Cai Z.;
RL   Submitted (OCT-2016) 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; FNXT01000963; SZX69926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A383VZV5; -.
DR   Proteomes; UP000256970; Unassembled WGS sequence.
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   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; IPR002478; PUA.
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   Pfam; PF01472; PUA; 1.
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:UP000256970};
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          208..694
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          364..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        555
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         304..310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         356
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         505
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   698 AA;  71985 MW;  3B97CBD3436CD432 CRC64;
     MTQTTSSNPN EHAFTEVSWD PQVSGFLAAA LGAEQFRRIQ AAIAVPPLST CVRVNTLRTS
     TQGVMQQLQG LLPQQHSAVH FAPHPQLPMA ILLQGSGPHS ISPAAAGAAK QVVISRKAGE
     AVLRGAQLFV PGVLAVTSGL QAGDLVAVMV ALDKPGSPHS GITRGTVLPA AAAAAAANGS
     NFSHPSAAAG IVAAAAPLAE AQHATAAAAA GTDDPADSTA AASVPVAAAG SLICIGLGRA
     KMGRVEMFRV QHGVAVEMEQ RVYEVPSPTL DGPLKGLVML QNLPSILAAQ VLNPQPGSRV
     LDMCAAPGGK TTMLAQLMQG KGQVIALDRS HAKVDDIRAL AEELGCSHCV TALKMDATKA
     VAKQRSSSTG SAQQEEVQEK GQQQQEGQQC AEQQQQQPER QQSCQAHEQL PLPEQQHCEA
     ADSKSQQQQQ QQQQQQQQPQ QQPQQQQSPS TAGLSAKAQA RLQRRIAAMA ARGQAPPVAE
     YRLYGLGPAK CPGFAPETFD AVLLDAPCTA LGLRPRLLQQ QQLSLLLETA AYQRALLAAA
     VQLVKPGGVL VYSTCTISPA ENEVNVRHAL DSYPCLQLVP AEPQLGGTGL TGPADAQAMA
     AAMLPFVGPA AGGAAETAAA APSNGSAASG EAAACKEPAA AEAADAGSWS SSSVAQGCSQ
     QQWLSPAEAA MVQRFDPAGQ ADTIGFFVAK FVKTCSCL
//