ID A0A2X4X136_9NOCA Unreviewed; 410 AA.
AC A0A2X4X136;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:SQI30144.1};
GN Name=eis {ECO:0000313|EMBL:SQI30144.1};
GN ORFNames=NCTC10994_01436 {ECO:0000313|EMBL:SQI30144.1};
OS Rhodococcus coprophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI30144.1, ECO:0000313|Proteomes:UP000249091};
RN [1] {ECO:0000313|EMBL:SQI30144.1, ECO:0000313|Proteomes:UP000249091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI30144.1,
RC ECO:0000313|Proteomes:UP000249091};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; LS483468; SQI30144.1; -; Genomic_DNA.
DR RefSeq; WP_072699915.1; NZ_LS483468.1.
DR AlphaFoldDB; A0A2X4X136; -.
DR STRING; 1219011.GCA_001895045_01960; -.
DR KEGG; rcr:NCTC10994_01436; -.
DR Proteomes; UP000249091; Chromosome 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000249091};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 9..153
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 410 AA; 44439 MW; B18C279FA83E1B59 CRC64;
MSRNVEPEVR VLESETERLQ AMALFRTAMV GLPSVNYPAG RIDDYLEPGR TYGAFVDGVL
AGTVDAFSGE IALPGGARVG HAAVTHIGVL PTHTRRGVLT ALVHRQLRDA RAGGEVIATL
RASEATIYGR FGFGIASWSA ETEIDVRRAS LRPGAPEGGA VRLVSAPGHW SVLRDTYARN
LPTRPGTLDR WSRWWASQEL RAESNPGPQY VAVHGEAGHE NGFVRYRPVP ADPHQWFSSD
SPAVLVDDFF APSPEAHAGL LRFLLRLDLV DRIRFAELPT DDPMPWLLRD HRAVRVRSVS
DETWLRILDV ERALACRTYE GTGTVTIGVV DPLFPENEGT YAISSGGVAR SGDPADLRAG
VAEVGSVLLG GVTWRELAAA GRVEVRHADA VPTADGLFDW PTAPFAGTSF
//
