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Database: UniProt
Entry: K3VUS8_FUSPC
LinkDB: K3VUS8_FUSPC
Original site: K3VUS8_FUSPC 
ID   K3VUS8_FUSPC            Unreviewed;       595 AA.
AC   K3VUS8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=FPSE_00474 {ECO:0000313|EMBL:EKJ79334.1};
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:EKJ79334.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ79334.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ79334.1,
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   -!- 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:EKJ79334.1}.
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DR   EMBL; AFNW01000010; EKJ79334.1; -; Genomic_DNA.
DR   RefSeq; XP_009251869.1; XM_009253594.1.
DR   AlphaFoldDB; K3VUS8; -.
DR   EnsemblFungi; EKJ79334; EKJ79334; FPSE_00474.
DR   GeneID; 20359094; -.
DR   KEGG; fpu:FPSE_00474; -.
DR   eggNOG; ENOG502QSHE; Eukaryota.
DR   HOGENOM; CLU_009942_1_1_1; -.
DR   OrthoDB; 5475921at2759; -.
DR   Proteomes; UP000007978; Chromosome 1.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007978};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..595
FT                   /note="Amidohydrolase 3 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003867091"
FT   DOMAIN          82..589
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          387..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  65430 MW;  44F6E816D24833E3 CRC64;
     MTAAGSFIRW GLILPLIVVA FAVAYRLQQP LTASENENPV TYCYKSIRTH DTEQVEAQCF
     TVTDGVFTAV GSSDADQTTM DGHVIPGLWD GHGHLLQYGE FLHSVDLFGA QSLDEARTRI
     KSYISENPGA GSKDNWVRGV GWDQTFFGRM PTAADITQDP ELSNVYLMLD RIDVHCTWVS
     QPVLDLLPAD LPEVIPGGEI IRDPGLGVFC DNAMDLVISI WPQPGQDFKA RTIKTAMKKL
     NEVGLVGMHD AGSTPETLTM YNELSSSDDW TLRVYAMLEC PQRNSYCPDE AVKFARDDDR
     FAVQSVKLFA DGALGSWGSA LLDPYSDHPW TSGSLLINAS ALTDVTKRWA ADGYQVNIHA
     IGDLANRNAV DALEAALVQQ CLNEATAQGA SPSTPGQSSH NSQGQIEARA ACQSRHRFRI
     EHAQIIHPDD QKRILSLGII PSIQPTHATS DMKYAQSRLG KDRVSSSAYR MRSLLPARPV
     LGSDFPVEPP NPFQGIYAAV ARRSPHTGRG TDESPDGWHT DEALSLYEAM WGFTEAPAYG
     AFLDGRAGVI REGALADWVV LDKPIESYEI EELRSLRVKE TWVAGKRVYT RSDDD
//
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