ID A0A1Q4CMN0_9GAMM Unreviewed; 659 AA. AC A0A1Q4CMN0; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-JUN-2017, entry version 3. DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:OJY24626.1}; GN ORFNames=BGO90_03825 {ECO:0000313|EMBL:OJY24626.1}; OS Legionella sp. 40-6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=1895903 {ECO:0000313|EMBL:OJY24626.1, ECO:0000313|Proteomes:UP000186293}; RN [1] {ECO:0000313|EMBL:OJY24626.1, ECO:0000313|Proteomes:UP000186293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=40-6 {ECO:0000313|EMBL:OJY24626.1}; RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., RA Anantharaman K., Tringe S., Hettich R.L., Harrison S.T., RA Banfield J.F.; RT "Genome-resolved meta-omics ties microbial dynamics to process RT performance in biotechnology for thiocyanate degradation."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OJY24626.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MKVI01000355; OJY24626.1; -; Genomic_DNA. DR Proteomes; UP000186293; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. DR InterPro; IPR002656; Acyl_transf_3. DR Pfam; PF01757; Acyl_transf_3; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:OJY24626.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000186293}; KW Membrane {ECO:0000256|SAAS:SAAS00103232, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000186293}; KW Transferase {ECO:0000313|EMBL:OJY24626.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 92 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 163 179 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 191 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 265 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 277 300 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 312 333 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 345 368 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 5 330 Acyl_transf_3. {ECO:0000259|Pfam: FT PF01757}. SQ SEQUENCE 659 AA; 75876 MW; 3B16C20E8ABFE480 CRC64; MNYRPDIDGL RALAIIFILL YHGGMSLIPS GFIGVDIFFV ISGFLITSII HQALLDDTFS FSQFYNRRIW RLQPAFLLVI LVATILAFLF FLPPDLIIYA KSASKSTFFN ANNYFNKITS SYFAPISQQL PLLHFWSLAL EWQIYLILPL IIFALYRTLK HHLIWGLMGL LFLSFYFSWQ SALAHPEHTY YLLISRFYEF LMGACIAVLL PKLPRLTRFP AELLSISALT ALVWIAGQSN ILQGYPNHYA LLVCCLTVCL IWLGACGSKQ TLTGRVLSSK SVVFIGLLSY SLYLWHWVIF AVVRYQNIPE TIMVKTLMFT FTFVFAYCSW RYVEKPLRRG SSRNVYQTLA FVVCVPIIFT FALSHWVVIH HGLPQRFNQE LVDVEQKLET YAYKIRPTCI SDKAVDIAPQ CRLGAPNSNK TALMIGDSFA NHYWGFMDVL GKRAKVSILA HSTSSCLTLP GIYLYDWWHF KDKVYAACHQ QTKRYYNLIR KNHFNYVILG QIWPNYYSAK VIHRMGDERS LTPGKKRIAA ALDRALNIIV QAGSRPIILD TTAIMEKNFH ECFYRHIKQR QPYDSRQCQF NLRLGEGDIW MIRLFQKMQA KYPQLVIIDP KQVQCELGIC KADLDGVPVY RDVGHITDYA SYHLGTSYAL QHANPLTSG //