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Database: UniProt
Entry: A0A2A4EAX5_9MICO
LinkDB: A0A2A4EAX5_9MICO
Original site: A0A2A4EAX5_9MICO 
ID   A0A2A4EAX5_9MICO        Unreviewed;       435 AA.
AC   A0A2A4EAX5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN   ORFNames=AUC47_01800 {ECO:0000313|EMBL:PCE14904.1};
OS   Microbacterium sp. SZ1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1849736 {ECO:0000313|EMBL:PCE14904.1, ECO:0000313|Proteomes:UP000217958};
RN   [1] {ECO:0000313|EMBL:PCE14904.1, ECO:0000313|Proteomes:UP000217958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZ1 {ECO:0000313|EMBL:PCE14904.1,
RC   ECO:0000313|Proteomes:UP000217958};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCE14904.1}.
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DR   EMBL; LPVV01000012; PCE14904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4EAX5; -.
DR   OrthoDB; 8399956at2; -.
DR   Proteomes; UP000217958; Unassembled WGS sequence.
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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01812}.
FT   DOMAIN          24..177
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   435 AA;  46198 MW;  29D9F9D61C3258DB CRC64;
     MTIIDARDIP ADSASAGRLS ARGLDYRVID VSDAAAAEAF QRAVSRGFLG PESTAEALAF
     GRPTFESRRN TGVYDSAVPD GRPVATIDSW VTPMTLPGGG ELPMWAISGV TVSATHRRRG
     IARALLEGEL RAAAAAGVPL AGLTVSEATI YGRYGFGSAV PVMRYRVDAR RAGWAAPAAP
     GRLEYIDRDA LADELGAVHE RARTGRPGQI PGWSARWGGM AGLSPSDSDR DRVRGVRYRD
     GSGEVRGAMA YTLAEEGSGT AWRHTLSVRL LVAETAEATA ELWRFALEHD LVDGVEAELR
     PVDDPLPWLV HDQRGVTQTL HDHGWLRILD VAACLTARRY AAPLDLVLGV RDVLGFADGE
     WRLRIGADGA AQVEPASTGA PDVELDVSAL SSLYAGGVRA SALHGAGRIE ADADAVAAID
     RSFMSTPAPG LDIWY
//
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