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Database: UniProt
Entry: A0A1C5CQP3_9ACTN
LinkDB: A0A1C5CQP3_9ACTN
Original site: A0A1C5CQP3_9ACTN 
ID   A0A1C5CQP3_9ACTN        Unreviewed;       440 AA.
AC   A0A1C5CQP3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Predicted acetyltransferase {ECO:0000313|EMBL:SCF73024.1};
GN   ORFNames=GA0115259_101697 {ECO:0000313|EMBL:SCF73024.1};
OS   Streptomyces sp. MnatMP-M17.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839780 {ECO:0000313|EMBL:SCF73024.1, ECO:0000313|Proteomes:UP000198886};
RN   [1] {ECO:0000313|EMBL:SCF73024.1, ECO:0000313|Proteomes:UP000198886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MnatMP-M17 {ECO:0000313|EMBL:SCF73024.1,
RC   ECO:0000313|Proteomes:UP000198886};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; FMDK01000165; SCF73024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5CQP3; -.
DR   OrthoDB; 8399956at2; -.
DR   Proteomes; UP000198886; 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:UP000198886};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01812}.
FT   DOMAIN          25..174
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  48289 MW;  56B703228F3C7047 CRC64;
     MFALPTDQPV LSRPGRPSAP SVSTVEVRNV TDAEIPQWTR TWASAYLQPL VEGTADFMRE
     TIAHDRVIGA FDLGQCVGTY RSSAQELTVP GGGFLPASAV SKVSVAGTHR RRGLLSRMLG
     MDLRGALERG EPVAVLDAAE YPIYGRFGFG PATSMAWFEI DVHRAGLDPR RTTDTGGVET
     VSADEYRKLA PEAYERFRLD QAGALRRDAM WWREATGQRV RPGTTWTEPF YAVRRTPDTG
     EVDGLLCFTA EETWASMVPR SPLYIRDLIA LSPAAERALL RYAVTVDWVD TVHLPYRAPD
     TLAPLWLDDP RAARLTTLSD YMWLRILDVP RTLAARTYGV EGTLVLEVRD ADGYAAGTWL
     LHGGPEGASC VRTTQPSDLR LDVGDLARLY LGDEAATRLA AVGCVEEVHG GALRRADLMF
     RTGRRSWSPR AAVRSAAGPA
//
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