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Database: UniProt
Entry: D6ZEF9_SEGRD
LinkDB: D6ZEF9_SEGRD
Original site: D6ZEF9_SEGRD 
ID   D6ZEF9_SEGRD            Unreviewed;       593 AA.
AC   D6ZEF9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:ADG99435.1};
GN   OrderedLocusNames=Srot_3008 {ECO:0000313|EMBL:ADG99435.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS   44985 / JCM 13578).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG99435.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG99435.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA   Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA   Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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DR   EMBL; CP001958; ADG99435.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6ZEF9; -.
DR   STRING; 640132.Srot_3008; -.
DR   KEGG; srt:Srot_3008; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   CDD; cd05931; FAAL; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   PANTHER; PTHR22754:SF32; DISCO-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:ADG99435.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN          33..430
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   593 AA;  63635 MW;  5DF5F47934CF8647 CRC64;
     MGPPPEKQAM TTTRRGTALK NATGFTDYLT TVRAWADTRP EHVAVGFLTE KSGRLEAQEW
     SYRELLSRGD AVAAQLREEH QPGETALLLY PPGLSFVAAF FGCLASGVIA VPAPIPDGRD
     KAKERLAGIV ADSGARTILT DTTTAALLAG WAATLPGKVR VRPTDSIPAD RGGSFEPLAA
     KPSDIAFLQY TSGSTSDPKG VMVTRGNLAH NVREIQRSVH SSEDTSMVSW LPQFHDMGLI
     GMILHPLFIG GSSRFLSPVT FIKRPIQWIR AMSDHAATFA MVPNFAFDLV ARRYNADDFD
     GVDLSSVRYI FNGSEPVQLE SMRRFTELLS PKGLAPNAVL PVYGLAEATL FVTATSPGTA
     AVRASVDRDA LADNRLVLVP ADEPNARVLV ASGHPQSLEV IVVDADGWRL GDGRVGEIWI
     RGESVAAGYW NRPELSAHTF GASPVGETGG WLRTGDLGAL LGGELFITGR VKDVIIVNGR
     NLHAHDIEAA ARSAAPELAR GVGAAFAVGS PERLVLVHEI RPEDIESRSP DDVAASVRTA
     IFADFATPLS DCLLVPKGSV SRTTSGKIRR SHMRELYENG QLQPFAEAAN EHV
//
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