ID D9VQ92_9ACTN Unreviewed; 414 AA.
AC D9VQ92;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN ORFNames=SSNG_03800 {ECO:0000313|EMBL:EFL16548.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL16548.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL16548.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL16548.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) 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; GG657750; EFL16548.1; -; Genomic_DNA.
DR RefSeq; WP_007265487.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VQ92; -.
DR STRING; 253839.SSNG_03800; -.
DR eggNOG; COG4552; Bacteria.
DR HOGENOM; CLU_050659_0_0_11; -.
DR Proteomes; UP000005763; 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 3..156
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 414 AA; 44629 MW; A78425CF7A280F4E CRC64;
MSADVRPIAA SELPAWLTTL NSGFLTPGTP TESDVAQRAA HTDLARVQGA FDKETGRCVA
TFRSFAQELT VPGGAAVGSS AISNVAVLPT HRRQGLLTRM MEAELAAAHA RGDVLSTLIA
AEYPIYARYG YGAATVHAEW EVDVARTGLD RSRPAPVDGG RIDLVDAAEV RRVGPALHER
LRAARHGMVD RDARWWSLKT GLEQMSHRPY REKMRAVYRD AAGEVAGLAV YQADDHWTDA
KTPLNTVQVV DFLAATPQAE RALWHFLCSI DWVLKVRSGN RAPDDLLPEL LPDARAARPV
SAADFLWVRV LDVVRALGAR TYEVPGVLVL EVEDATGPAG GRYRLDAGAG TCTRTEEPAG
VRLDVSALGS LYLGDASAVR LAALGRVAEL EPGAVALADA VFRTARRPWC PDVF
//