ID A0A162KM19_CORDF Unreviewed; 614 AA.
AC A0A162KM19;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:OAA76938.1};
GN ORFNames=LEL_06622 {ECO:0000313|EMBL:OAA76938.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76938.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76938.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76938.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA76938.1}.
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DR EMBL; AZHF01000004; OAA76938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162KM19; -.
DR STRING; 1081108.A0A162KM19; -.
DR OrthoDB; 5475921at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
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 Hydrolase {ECO:0000313|EMBL:OAA76938.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT DOMAIN 121..610
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 66233 MW; BE102B96EF37526E CRC64;
MDAPGDKVGK GLATDTPPSD GRPSSPVKPP KGRYGMGTIP SLLVAVSLVA LGLRAKYHHA
GAGDDHDSQT YCYTGVQTLH SDQPVAQCFT VANGLFTAVT SGSEPELKRR SSEDTTTAAV
DGFVIPGLWD GHGHLVDYGE MLVNVDLFGV ATLDDMRARL RDHIAQHPGS GTKERWLRGI
GWDQTDFGRM PTAADIEEDP ALRGIYLFID RIDGHCALVS QAVLDLLPDP IPDVPGGEVV
RDPPGLGVFC DNALGMILAH YPKPDDATKT RYVKAAMRAL NAVGLVGMHN AGTDPATVDL
LQSLAGGDDW TVRVYAMREC AARNTFCAAD ATRVERDDGL LNVRSVKLFA DGALGSWGAA
MLEPYADDPS TTGSLLIDET ALAAVTKQWT AAGFQVNIHA IGDRANRAAI DAFEAALRQE
CGPSANLATC EHNRRFRIEH AQIITPEDQQ RLHSLRVIPS IQPTHATSDM RYAAARLGAE
RTSRAAYRMR SFLDLQPVLG SDFPVEPPNP FHGMYAAVAR KSPATGLGRD EDGGKGWHRE
EALTLEQALW GFTGAPAYGG FLEGKAGQIR EGAYADWVVL DEPFGGQGFD VESLRTLKVR
ETWVAGKRVY KRDD
//
