ID A0A2M9IKP8_9ACTN Unreviewed; 419 AA.
AC A0A2M9IKP8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=GNAT family N-acetyltransferase {ECO:0000313|EMBL:PJM95159.1};
GN ORFNames=CG719_14760 {ECO:0000313|EMBL:PJM95159.1};
OS Streptomyces sp. CB01373.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020325 {ECO:0000313|EMBL:PJM95159.1, ECO:0000313|Proteomes:UP000232070};
RN [1] {ECO:0000313|Proteomes:UP000232070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01373 {ECO:0000313|Proteomes:UP000232070};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJM95159.1}.
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DR EMBL; NNBK01000008; PJM95159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9IKP8; -.
DR OrthoDB; 8399956at2; -.
DR Proteomes; UP000232070; 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}; Reference proteome {ECO:0000313|Proteomes:UP000232070};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 8..159
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 419 AA; 45830 MW; 104E84C67B5CBE6F CRC64;
MTAASPDIDV RTITEAEIPD WGRALKTGFL RPPGVSEAEI ADLRTYVEPS RTLGAFDAGR
CVATFRSFPQ EITAVGGATV PADAITNVSV TATHRRRGLL TRMMAQDLAA AKERGDVVAT
LIAAEYPIYG RYGFGPAAWM TEWAIDVPRA GLDPRRSGPE DGGRVDLVDA EDVRKLGPEL
HERLRRAQPG AVDRSDRWWQ VSTGVVRPDP SRWTERFHAV YRAADGTVEG LAVYQCDETW
SDAKQPLNTA TVKDLVAVTP AAERSLWLHL CSIDWIMKVK SGWRASDDLL PHFLPDPRAA
TVTTHADWLW VRILDVRRAL EARTYEGTGT LILDVLDPAG MAGGRWRLEA SPAGVSCTPT
TGSADLTLDV AQLATLWLGD ESAVRLAALG RVREERAGAA RGADALLRTS RRPWCPDMF
//