ID   A0A0D0CL05_9AGAR        Unreviewed;      1070 AA.
AC   A0A0D0CL05;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Acetyl-CoA synthetase-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GYMLUDRAFT_44941 {ECO:0000313|EMBL:KIK59187.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK59187.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK59187.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK59187.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN834781; KIK59187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0CL05; -.
DR   HOGENOM; CLU_002220_1_0_1; -.
DR   OrthoDB; 2230730at2759; -.
DR   Proteomes; UP000053593; Unassembled WGS sequence.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR   PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593}.
FT   DOMAIN          31..359
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          698..935
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
SQ   SEQUENCE   1070 AA;  117579 MW;  3B1C987FCFE97345 CRC64;
     MSSNIVWPDL KSPLDLPKIL EFSLEHNANF PAFVFPEQGT GNPVTISTLE YVRGIYRVGN
     SVLGDSKPGD VVAIIANLDN VVYMAVMNGL MNIGLVPFPI SPRNSAPAIV DLLRKSSAHR
     ILTTYTTLKA VIDGVRSELK SGEPFELSVE EAPGLYEVYP YLGKETANDP SDPPPVPYLP
     KDTDTAIYLH SSGSTGFPKA IRLSHTNFKS YISLLCMQDM RDLGFGPYGA AGLPPFHVMA
     VFNQAYVPLY GRVTVSMFTP TVTKPDALPV ILSPETVIET VRLTKAKSML TVPTFLHLWS
     HSEDAIKVLA QCILVFYGGG PLPQSTGDYL VSRGVKVVTA FGGTEFGLIV KAAVTPEDWS
     YMQFVDAVKV RWAPQGDGTY EAQFLTHDKY QPAVENLPDT RGYATSDLFV PHPTDPKKWK
     IIGRIDDVII HSSGEKTVPA PMEAVITATS LIRGAVMFGR ERDQPGILVE PSPSHKVDVN
     DPNEVAAFRN LLWPLVDEAN RIAPAFSRIF KEMILISSAD KPLPRVGKGT VARKAAISLY
     EPEINELYAL IESNSGGDSV EPPKAWNTEE VQSWLTQQVM EILSNGINVH TTKDLFEQGF
     DSIMATILRL HIVSVLRKSN RLAGAREVPQ NLVYTYPSIE HLTNAILEIT NSPTTSSATT
     KSHPELIEEM IEKYSQGLDV PPPISKIDFT GQSHHVLLTG STGNIGAELL AGLVLADSVQ
     RVYALNRPSS SGVSIVDRHR TRFEDKGLDV SILSSPKIVF LESEISDDHL GLPQDVLREL
     RSNLTVVIHN AWKLDFNLSL SSFESHIRGA RSLINLARTS RQSSNIRFLF TSSIASTQSW
     DTSKGLYPEE VVMDAKYAVG SGYGESKYVT ERILARSGLQ ATSFRIGQVA GGEPNGAWAT
     TDWLPILVKS SLTLNKLPDA HGFVSWVPMD AVTQALLDTV FLANAAPIAV NIVHPNPTSW
     STVMQHIRQA LIREKGLSPN AIPLIPIQQW ISDIEQHSNN PSDDLPALKL LEFFKNVAKA
     DDPSNRGESM RTTPLKLENV KAVSPRMRKL EPLAETTADQ WVKYWIRSGM
//