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Database: UniProt
Entry: E2B578_HARSA
LinkDB: E2B578_HARSA
Original site: E2B578_HARSA 
ID   E2B578_HARSA            Unreviewed;       294 AA.
AC   E2B578;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN   ORFNames=EAI_16111 {ECO:0000313|EMBL:EFN89152.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN89152.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN89152.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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; GL445729; EFN89152.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2B578; -.
DR   STRING; 610380.E2B578; -.
DR   EnsemblMetazoa; XM_011147125.3; XP_011145427.1; LOC105186726.
DR   InParanoid; E2B578; -.
DR   OMA; LWLTCRQ; -.
DR   Proteomes; UP000008237; 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   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; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF17; DIMETHYLADENOSINE TRANSFERASE 1, 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:UP000008237};
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          4..164
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         1
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         12
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         41
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   294 AA;  34395 MW;  2ACB39B9A30A5D9B CRC64;
     MKRLPERIVL VEKDKRFEPT LDILADSFAM INRKVDIIFD DIMRAHIESL FPKEKKMNWN
     DKPPDLFLIG NLPFNVSTPL IIQWLHSIAE RRGAWAFGRT KMTLTFQKEV AERLVAPESS
     EQRCRLSVMA QAWTFPVLRF VIPGHVFVPQ PDVDVGVVSF TPLTKPCTQH DFKFFEKIVR
     HVFSFRQKYS IRCVETLFPL HCRKELAMMM YKLSDLDPTI RPTQLTVNDI DRLATAYKYL
     LEKHPELEMY NYRASRHLLP QFNTQNVVVE DKVSGDIEER NESSRSTVVV DSHI
//
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