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Database: UniProt
Entry: M0M1C9_9EURY
LinkDB: M0M1C9_9EURY
Original site: M0M1C9_9EURY 
ID   M0M1C9_9EURY            Unreviewed;       558 AA.
AC   M0M1C9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:EMA39228.1};
GN   ORFNames=C447_06918 {ECO:0000313|EMBL:EMA39228.1};
OS   Halococcus hamelinensis 100A6.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1132509 {ECO:0000313|EMBL:EMA39228.1, ECO:0000313|Proteomes:UP000011566};
RN   [1] {ECO:0000313|EMBL:EMA39228.1, ECO:0000313|Proteomes:UP000011566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=100A6 {ECO:0000313|EMBL:EMA39228.1,
RC   ECO:0000313|Proteomes:UP000011566};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMA39228.1}.
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DR   EMBL; AOMB01000020; EMA39228.1; -; Genomic_DNA.
DR   RefSeq; WP_007692222.1; NZ_AOMB01000020.1.
DR   AlphaFoldDB; M0M1C9; -.
DR   PATRIC; fig|1132509.6.peg.1568; -.
DR   eggNOG; arCOG04201; Archaea.
DR   OrthoDB; 193284at2157; -.
DR   Proteomes; UP000011566; Unassembled WGS sequence.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
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   PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011566}.
FT   DOMAIN          48..408
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          462..540
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   558 AA;  61547 MW;  FFF1B6F5FFB99992 CRC64;
     MATHNLPDYE AARESFSWTD IYDEADWDAP DELNIAHEVC DRHADGSGRV ALEYAGVEGE
     RETLTFDDLA ERSNRFANLL ENQDVERGDR VFTYLPRIPA HYVALVGTLK RGAVFGGVNE
     RFGPEGIAYR LVDCDATAVV TTSANRETVE RALADVPTVE TVVTIDRGDG IEEGDVDYER
     AMADAGTDYD LVRTGSEDDA LLYYTSGTTG LAKGVLHRHR WVAGVAATQR YAVDLRDDDL
     YWSTADLGWL TGPINTLGAW FWGTSQFAYE GEFSPQEWAS LLSEYPITVL FSVPTAYRML
     RANEDVLDAD LDLRHALSIG EPLSAGVVEW AEDALGVTVL DTYGQTETGN MVINNYPTME
     LRPGSMGKPL PGIESAIVDP ETGEVLPPGE TGEIAHRGDF PCFFAEYWNN PGKTAACFVE
     GSDGRWYRSG DLAHRDEDGY FWFEGRADDV ILSSGYRIGP FEVESSLGEH PAVAEAAVVP
     KPHPERGNIV KAYVVLAGGY DPSDDLAEGI RTHVREELSA HEYPREVEFV DDLPKTVTGK
     IRRTELRDRT AETDSTAD
//
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