ID A0A1W7CXC1_9ACTN Unreviewed; 418 AA.
AC A0A1W7CXC1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=GNAT family N-acetyltransferase {ECO:0000313|EMBL:ARQ69319.1};
GN ORFNames=CAG99_10955 {ECO:0000313|EMBL:ARQ69319.1};
OS Streptomyces marincola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2878388 {ECO:0000313|EMBL:ARQ69319.1, ECO:0000313|Proteomes:UP000194218};
RN [1] {ECO:0000313|EMBL:ARQ69319.1, ECO:0000313|Proteomes:UP000194218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ69319.1,
RC ECO:0000313|Proteomes:UP000194218};
RA Ma L., Zhu Y., Zhang W., Zhang G., Tian X., Zhang S., Zhang C.;
RT "Complete genome sequence of Streptomyces sp. SCSIO 03032 revealed the
RT diverse biosynthetic pathways for its bioactive secondary metabolites.";
RL Submitted (MAY-2017) 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; CP021121; ARQ69319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7CXC1; -.
DR KEGG; smao:CAG99_10955; -.
DR OrthoDB; 8399956at2; -.
DR Proteomes; UP000194218; Chromosome.
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:UP000194218};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 3..159
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 45523 MW; 0D8DF73FE88AA2AE CRC64;
MSPHFRTVTD DNPADGDAWV RAVSAGFLSP PESNPRGLAQ RRERLDVPGS RPRGAFEGDR
CVATLRSFDQ RLTVVGGREV AANAISAVTV LATHRRRGLL RRMMTDDLAE ARERGDVAAT
LVATEYPIYG RFGFGAASTF TAWRVDASRS GLDPKWSLPA NEGSLTFVDG AEVRKVGPEL
HERFRRGQPG AVDRSEQVWQ LRTGALWFGP DPWVEPFHVL YRDPAGVPQG LATFATDNAW
REGLPEGTAS VRSLLATSPA VEALLWRFLL SIDWVVTVDS GRTPPDSVLP LILPNPRAAR
IREQADHLWL RPLDLPALLG ARSYATEGEL VLDVRDPLGL AEGRYLLTAS PEGGLAVPTT
REPDLTLPTN ALAGLYLGDE SAARLVAAGL ADEGTTRAAS RADLLFRTGR RPWCPDIF
//