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Database: UniProt
Entry: A0A0N0SHP5_9ACTN
LinkDB: A0A0N0SHP5_9ACTN
Original site: A0A0N0SHP5_9ACTN 
ID   A0A0N0SHP5_9ACTN        Unreviewed;       417 AA.
AC   A0A0N0SHP5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN   ORFNames=ADK56_12115 {ECO:0000313|EMBL:KOU50918.1};
OS   Streptomyces sp. MMG1522.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU50918.1};
RN   [1] {ECO:0000313|EMBL:KOU50918.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1522 {ECO:0000313|EMBL:KOU50918.1};
RA   Noorani M.;
RL   Submitted (JUL-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:KOU50918.1}.
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DR   EMBL; LGDF01000108; KOU50918.1; -; Genomic_DNA.
DR   RefSeq; WP_053606870.1; NZ_LGDF01000108.1.
DR   AlphaFoldDB; A0A0N0SHP5; -.
DR   PATRIC; fig|1415545.3.peg.2608; -.
DR   Proteomes; UP000037713; Unassembled WGS sequence.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
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          3..155
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   417 AA;  45103 MW;  2C2C2B0DF2D263AF CRC64;
     MSLEVRTVAP SEFPGWMRAV RAGFLTAGGL PSDEVVEDRR ADVDLSRVQG VFDGGRCVAT
     FRSFEQRLTV VGGATVASDA ITGVTVAPTH RRRGLLSRMM AADLAAAKER GEPVASLIAA
     EYPIYGRYGF GPAAWTAEWE VSVPRAGLDP RRSGQPADGG RIEMVDGEDV RKAGPEVHAA
     LAARRPGVVS RGERWWRQAT GVAPRTPQET WTEPFYVMHR AADGEIDGLM IYGTDDKWGD
     GNQPQNTASV RDMIALNPAA ERALWHYLCS VDWVTAVRSG DRAPDDLLPL LLPDPRAARL
     VGGSDFLWLR LLDVPRALEA RTYAVGASLV LDVRDGAGLA GGRFLLEVAE DGARCVPTTR
     SADLALGVEE LATLYLGDES VRRLADLGRA EELRAGAVTM ADAVFRTGRR PWCPDVF
//
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