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Database: UniProt
Entry: Q9CD64_MYCLE
LinkDB: Q9CD64_MYCLE
Original site: Q9CD64_MYCLE 
ID   Q9CD64_MYCLE            Unreviewed;       353 AA.
AC   Q9CD64;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Acetyltransferase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=ML0187 {ECO:0000313|EMBL:CAC29695.1};
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC29695.1, ECO:0000313|Proteomes:UP000000806};
RN   [1] {ECO:0000313|EMBL:CAC29695.1, ECO:0000313|Proteomes:UP000000806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN {ECO:0000313|EMBL:CAC29695.1,
RC   ECO:0000313|Proteomes:UP000000806};
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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DR   EMBL; AL583917; CAC29695.1; -; Genomic_DNA.
DR   PIR; C86932; C86932.
DR   RefSeq; NP_301261.1; NC_002677.1.
DR   AlphaFoldDB; Q9CD64; -.
DR   STRING; 272631.gene:17574003; -.
DR   KEGG; mle:ML0187; -.
DR   PATRIC; fig|272631.5.peg.293; -.
DR   Leproma; ML0187; -.
DR   eggNOG; COG0664; Bacteria.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_836314_0_0_11; -.
DR   OrthoDB; 190266at2; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR24567:SF80; CRP-LIKE CAMP-ACTIVATED GLOBAL TRANSCRIPTIONAL REGULATOR; 1.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000806}.
FT   DOMAIN          40..142
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          176..338
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   353 AA;  38407 MW;  966BE33620D0A18D CRC64;
     MAGSWQCGHC ESCASPLGPR DIAVVELIAD RAEEFAAMDI FRGLPAEDLM SVAVSVEPVL
     AAAGEVLMQQ GEQAVSFLLI SSGNVEVRRV DDDGAVIVGQ ASHGMIIGEI ALLRDGRRTA
     TVITTEPLTG WVGDIDAFAQ MVQIPSITRR LLLTVRQRLA AFITPIPVQL RDGTHLMLRP
     VLPGDTERSL RGHVRFSRET LYLRFMSARA PSDELMHYLS EVDYVDHFVW VVTDGGDPVA
     DARFVRDESD PTLAEIAFTV ADAYQGRGVG NFLISALSIA AHVNGVNRFS ARMLTDNGPM
     RAIMDHHGAV WRRYDVGVIT TVIDVPRQRD LIIGRAMADQ IAGVVRQVIG AVG
//
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