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CARB_STRTH
ID   CARB_STRTH              Reviewed;         299 AA.
AC   P13079;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=rRNA methyltransferase;
DE            EC=2.1.1.-;
DE   AltName: Full=Carbomycin-resistance protein;
GN   Name=carB;
OS   Streptomyces thermotolerans.
OG   Plasmid pOJ159.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=80858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11416 / CBS 960.69 / DSM 40277 / JCM 4519 / NBRC 13088 / NRRL
RC   B-2345 / VKM Ac-1821;
RX   PubMed=3036668; DOI=10.1016/0378-1119(87)90094-1;
RA   Epp J.K., Burgett S.G., Schoner B.E.;
RT   "Cloning and nucleotide sequence of a carbomycin-resistance gene from
RT   Streptomyces thermotolerans.";
RL   Gene 53:73-83(1987).
CC   -!- FUNCTION: Probable RNA methylase. Confers resistance to carbomycin and
CC       several other macrolides, lincomycin and vernamycin B, but not to all
CC       macrolide-lincosamide-streptogramin B antibiotics.
CC   -!- INDUCTION: By certain macrolide antibiotics.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR   EMBL; M16503; AAC32026.1; -; Genomic_DNA.
DR   RefSeq; WP_063844794.1; NG_047830.1.
DR   AlphaFoldDB; P13079; -.
DR   SMR; P13079; -.
DR   PRIDE; P13079; -.
DR   KEGG; ag:AAC32026; -.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.100; -; 1.
DR   Gene3D; 3.40.50.150; -; 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; PTHR11727; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; Methyltransferase; Plasmid; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..299
FT                   /note="rRNA methyltransferase"
FT                   /id="PRO_0000101692"
FT   REGION          14..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         57
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         82
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         144
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   299 AA;  34138 MW;  63990AA894C044C6 CRC64;
     MAALLKRILR RRMAEKRSGR GRMAAARTTG AQSRKTAQRS GRSEADRRRR VHGQNFLVDR
     ETVQRFVRFA DPDPGEVVLE VGAGNGAITR ELARLCRRVV AYEIDRHFAD RLREATAEDP
     RIEVVAGDFL KTSQPKVPFS VVGNIPFGNT ADIVDWCLNA RRLRTTTLVT QLEYARKRTG
     GYRRWSRLTV ATWPEVEWRM GERISRRWFR PVPAVDSAVL RLERRPVPLI PPGLMHDFRD
     LVETGFTGKG GSLDASLRRR FPARRVAAGF RRARLEQGVV VAYVTPGQWI TLFEELHGR
 
 
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