ID C1AXK2_RHOOB Unreviewed; 401 AA.
AC C1AXK2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN OrderedLocusNames=ROP_14590 {ECO:0000313|EMBL:BAH49706.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH49706.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH49706.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH49706.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01812}.
CC -!- SIMILARITY: Belongs to the acetyltransferase Eis family.
CC {ECO:0000256|ARBA:ARBA00009213, ECO:0000256|HAMAP-Rule:MF_01812}.
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DR EMBL; AP011115; BAH49706.1; -; Genomic_DNA.
DR RefSeq; WP_012688678.1; NC_012522.1.
DR AlphaFoldDB; C1AXK2; -.
DR STRING; 632772.ROP_14590; -.
DR KEGG; rop:ROP_14590; -.
DR PATRIC; fig|632772.20.peg.1538; -.
DR HOGENOM; CLU_050659_0_0_11; -.
DR OrthoDB; 8399956at2; -.
DR Proteomes; UP000002212; Chromosome.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 2.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR HAMAP; MF_01812; Eis; 1.
DR InterPro; IPR041380; Acetyltransf_17.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR025559; Eis_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR022902; NAcTrfase_Eis.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR PANTHER; PTHR37817; N-ACETYLTRANSFERASE EIS; 1.
DR PANTHER; PTHR37817:SF1; N-ACETYLTRANSFERASE EIS; 1.
DR Pfam; PF17668; Acetyltransf_17; 1.
DR Pfam; PF13527; Acetyltransf_9; 1.
DR Pfam; PF13530; SCP2_2; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF55718; SCP-like; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01812}; Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 7..166
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 401 AA; 43692 MW; 028B4F5563500233 CRC64;
MTSTGGITIR TATEQDWPKI VVLNEICFVT PQTEEFTAHW KQLVSGEPPI IALDGDEVVG
ATMDIPMEVT VPGGGSVAAA GVTAVTVAPT HRRRGILRAL YTEHHARIRA SGAPLSILTA
SEGGIYGRFG YGPATVESTV SIDRRFAVPH PKAPDPGGVR MVHPAQARPA FTDVYHRWQQ
VTPGAQVRPE IVWNRIFADR ESERGGGTAL FGLVHDDGYV LYRRASGDNG SFARVEEIRT
VTSDAHAALW RAMLGLDLVR RIEANLTPED PLPYLLTDGR LVRTSSRHDE LWVRIMDVPA
ALEARTFRGD LDVVVQVDDG FLDAGGRFSL SVRDGKAVCT RTDATPHLVL DLDVLGSLYL
GAHRARTFAA ANRLWAADAD VLDRFEHAFG SGRDAQMGWA F
//
