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Database: UniProt
Entry: A0A383WGH3_TETOB
LinkDB: A0A383WGH3_TETOB
Original site: A0A383WGH3_TETOB 
ID   A0A383WGH3_TETOB        Unreviewed;       391 AA.
AC   A0A383WGH3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN   ORFNames=BQ4739_LOCUS16903 {ECO:0000313|EMBL:SZX76520.1};
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:SZX76520.1, ECO:0000313|Proteomes:UP000256970};
RN   [1] {ECO:0000313|EMBL:SZX76520.1, 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. rRNA adenine N(6)-methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|RuleBase:RU362106}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01026}.
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DR   EMBL; FNXT01001260; SZX76520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A383WGH3; -.
DR   STRING; 3088.A0A383WGH3; -.
DR   Proteomes; UP000256970; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF27; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000256970};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}; rRNA processing {ECO:0000256|RuleBase:RU362106};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01026};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}.
FT   DOMAIN          68..307
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         221
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   391 AA;  43377 MW;  F0D02AA9F0F4FDD1 CRC64;
     MEEQPRRRTD EQPRRRSEEP LLKEDFEVPA VGWMWEPNTA AATKSSLKSA NIKAKKSLGQ
     NFCTDDQILA DIVTAARVAP SDVVIEVGPG TGNLTRHLLA TRARVLAVEK DDTLIERLRE
     EFKQVPNLQL VHGDVMRLDL KALVAQMAAA AAAAAQLDSQ ASSNEPQQEQ QQQQQQLQQP
     PPPEQQQQPA DESSSSISSS RSSSSAAPAK QRRRGVKVVA NLPYNITKEF LQAMLPQGGV
     VSELSIMIQE EVAHRLVDPT PGRPDYRAMS LITHYYSKPV YRFLIPKEKY FPVPGVDGAL
     VTFKLLPPSK RVQVSGERGF ISLINKAFSE RRKMMRNTLQ PLYTPQQVEA ALQKAGVRPD
     ARAQDLDVEQ FAAVYNNLQA EQIAAVSAVQ Q
//
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