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Database: UniProt
Entry: W5NIV4_LEPOC
LinkDB: W5NIV4_LEPOC
Original site: W5NIV4_LEPOC 
ID   W5NIV4_LEPOC            Unreviewed;       416 AA.
AC   W5NIV4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020563.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000020563.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; AHAT01027741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006626127.1; XM_006626064.2.
DR   AlphaFoldDB; W5NIV4; -.
DR   STRING; 7918.ENSLOCP00000020563; -.
DR   Ensembl; ENSLOCT00000020598.1; ENSLOCP00000020563.1; ENSLOCG00000016646.1.
DR   GeneID; 102692181; -.
DR   KEGG; loc:102692181; -.
DR   CTD; 64216; -.
DR   eggNOG; KOG0820; Eukaryota.
DR   GeneTree; ENSGT00950000183142; -.
DR   HOGENOM; CLU_051778_0_0_1; -.
DR   InParanoid; W5NIV4; -.
DR   OMA; GRCEMIL; -.
DR   OrthoDB; 5320952at2759; -.
DR   Proteomes; UP000018468; Linkage group LG1.
DR   Bgee; ENSLOCG00000016646; Expressed in pharyngeal gill and 13 other cell types or tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0034246; F:mitochondrial transcription factor activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR   GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR   GO; GO:0006391; P:transcription initiation at mitochondrial promoter; IBA:GO_Central.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF13; DIMETHYLADENOSINE TRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000018468};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01026};
KW   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          97..296
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   416 AA;  46787 MW;  24C0F42D59D3A37A CRC64;
     MRRGQLWGPS PVVRAYSIDA APFAGGTLKP QAQPQPEKPS HCHSLTQRNL SAVALSSKGQ
     CRPLSRYDFL DVGEVEEHTK KALACRTLRR FIVDPALAQL VADKLEGDLA DSRAVLFECN
     PGPGVLTRTL LNSGAQRVIA LESDKQFLPD LQALENSLDG QLEVVHCDFF KLDPIGQGSM
     KPPAMYSEKL FNDLGISQVP WTADVPVKVV GIFAQKNERS MLWKLIYALY ERLSVFRFGR
     VELIMFISEK EYTKMVASPG EMKNYLALGC LWQMACDIQL LHKEPWSSFV TTSKHGGLAI
     PKSSLTNDHL CLVRMTPRRD LFTDTLTTST GATLVMMIKQ CLAKRKAKLV DRLNSWSPGT
     GQKLLLQMEL PEDIFTGHLY PEEYKKLFEA MEHSEEFAQS WLYEEILENT QNTGFQ
//
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