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Database: UniProt
Entry: A0A091LVJ1_CATAU
LinkDB: A0A091LVJ1_CATAU
Original site: A0A091LVJ1_CATAU 
ID   A0A091LVJ1_CATAU        Unreviewed;       221 AA.
AC   A0A091LVJ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
DE   Flags: Fragment;
GN   ORFNames=N323_03490 {ECO:0000313|EMBL:KFP50361.1};
OS   Cathartes aura (Turkey vulture) (Vultur aura).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX   NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP50361.1, ECO:0000313|Proteomes:UP000053745};
RN   [1] {ECO:0000313|EMBL:KFP50361.1, ECO:0000313|Proteomes:UP000053745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP50361.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC       than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
CC       {ECO:0000256|ARBA:ARBA00035020}.
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; KL295549; KFP50361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091LVJ1; -.
DR   Proteomes; UP000053745; 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; 1.10.8.480; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00755; ksgA; 1.
DR   PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 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:UP000053745};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01026};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW   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          1..169
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         13
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP50361.1"
FT   NON_TER         221
FT                   /evidence="ECO:0000313|EMBL:KFP50361.1"
SQ   SEQUENCE   221 AA;  24972 MW;  5EAAC8641C551B9C CRC64;
     AALRRTDVIL EVGPGTGNLT VKMLEKVKKV IACEIDPRLV GELQKRVQGT CLANKLEIKV
     GDILKTDLPF FDACVANLPY NCTNAIKKIS SPFVFKLLLH RPFFRCAILM FQREFALRLV
     AKPGTKLYCR LSINTQLLAR VDHLMKVGKN NFRPPPKVES SVVRIEPKNP PPPINFQEWD
     GLVRIAFVRK NKTLSAAFKS SAVEQLLDHN YRIHCSLHNT V
//
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