位置:首页 > 蛋白库 > ERMA_AERER
ERMA_AERER
ID   ERMA_AERER              Reviewed;         340 AA.
AC   P09891;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=rRNA adenine N-6-methyltransferase;
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01026};
DE   AltName: Full=Erythromycin resistance protein;
DE   AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein;
GN   Name=ermA;
OS   Aeromicrobium erythreum (strain ATCC 51598 / DSM 8599 / JCM 8359 / NBRC
OS   15406 / NRRL B-3381).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Aeromicrobium.
OX   NCBI_TaxID=31956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=4043733; DOI=10.1016/0378-1119(85)90004-6;
RA   Roberts A.N., Hudson G.S., Brenner S.;
RT   "An erythromycin-resistance gene from an erythromycin-producing strain of
RT   Arthrobacter sp.";
RL   Gene 35:259-270(1985).
CC   -!- FUNCTION: Involved in erythromycin resistance.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M11276; AAA22075.1; -; Genomic_DNA.
DR   AlphaFoldDB; P09891; -.
DR   SMR; P09891; -.
DR   KEGG; ag:AAA22075; -.
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   3: Inferred from homology;
KW   Antibiotic resistance; Methyltransferase; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..340
FT                   /note="rRNA adenine N-6-methyltransferase"
FT                   /id="PRO_0000101666"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   340 AA;  37453 MW;  E99A714C391952B5 CRC64;
     MAGPQDRPRG RGPSSGRPQR PVGGRSQRDR DRRVLGQNFL RDPATIRRIA DAADVDPDGL
     VVEAGPGEGL LTRELARRAG RVRTYELDQR LARRLSTDLA QETSIEVVHA DFLTAPHPEE
     PFQFVGAIPY GITSAIVDWC LTAPTLTSAT LVTQQEFARK RTGDYGRWTA LTVTTWPTFE
     WQYVAKVDRT LFTPVPRVHS AIMRLRRRPQ PLLRDAAARS RFADMVEIGF VGKGGSLYRS
     LTREWPRSKV DSAFARADVH HDEIVAFVHP DQWITLFQLL DGSRGGAARG PGDQRGRRGR
     PGGGPRPDGR AGGGPRRDAG GRRTGDGRGG RPRPPRGGQA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024