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