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Database: UniProt
Entry: K3VSE1_FUSPC
LinkDB: K3VSE1_FUSPC
Original site: K3VSE1_FUSPC 
ID   K3VSE1_FUSPC            Unreviewed;       514 AA.
AC   K3VSE1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Peroxisomal-coenzyme A synthetase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FPSE_01206 {ECO:0000313|EMBL:EKJ78612.1};
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ78612.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ78612.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ78612.1,
RC   ECO:0000313|Proteomes:UP000007978};
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
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:EKJ78612.1}.
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DR   EMBL; AFNW01000026; EKJ78612.1; -; Genomic_DNA.
DR   RefSeq; XP_009252601.1; XM_009254326.1.
DR   AlphaFoldDB; K3VSE1; -.
DR   EnsemblFungi; EKJ78612; EKJ78612; FPSE_01206.
DR   GeneID; 20359826; -.
DR   KEGG; fpu:FPSE_01206; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_0_1; -.
DR   OrthoDB; 3109088at2759; -.
DR   Proteomes; UP000007978; Chromosome 1.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   CDD; cd05926; FACL_fum10p_like; 1.
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   InterPro; IPR045310; Pcs60-like.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000007978}.
FT   DOMAIN          25..370
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          421..496
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   514 AA;  56257 MW;  A37CD85179092E0C CRC64;
     MSTLQSAINK SNPLAEAIII PSKPKALTVS YANLESDVSA FQRKLADLGI TKAAPVSIAL
     INSYEFIVSF LAASWQRGIA APLNPAYKQD EFEFYIDDVK SAIVLVPRGA YAAGAPSVKA
     AKKFNAAVAE CYWDEAKGEV ALDVKDYGLL KGKKEKVLTA EPDDVALILH TSGTTSRPKV
     VPLTHRNLTR TMNNIKNTYE LTPKDRTMLV MPLFHVHGLL CGLLAPLFTG GSMVVPTKFS
     ASEFWTDFNT HKANWYTAVP TIHQILLKNP PPSPKPNIRF IRSCSSPLSP TVFQQLEETY
     NAPVLEAYAM TEAAHQMTSN PLPPAKRKAG TVGIGQGVEV KILTDQGEEV PQGAEGEICI
     IGENVTKGYL NNDKANAESY HKNGFFRTGD QGKKDEDGYI IITGRIKELI NKGGEKISPI
     ELDNVLTRHP QISEAVSFAI PDEVYGQDIG VAVVLKNGEK LTAQELKAWV EERSAKFKVP
     KKVYFTEVMP KTATGKIQRR IVAETMMTAP KAKL
//
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