ID   A0A0N8H828_9HYPO        Unreviewed;       537 AA.
AC   A0A0N8H828;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=AK830_g3111 {ECO:0000313|EMBL:KPM43412.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM43412.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM43412.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM43412.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPM43412.1}.
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DR   EMBL; LKCW01000033; KPM43412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8H828; -.
DR   STRING; 78410.A0A0N8H828; -.
DR   OrthoDB; 147994at2759; -.
DR   Proteomes; UP000050424; 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:SF20; AMIDOHYDROLASE 3 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 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:UP000050424}.
FT   DOMAIN          55..534
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   537 AA;  57946 MW;  EE106590B6A13858 CRC64;
     MASLFINGRI LSKAGAGVEG TPTFAESMFV KDGVITAIGS QDDIAAKYQG EGVVTQDLKG
     RTVLPGFVDG HMHLLLLGQA LRKVGVEHCK SLEDILATLR TYAKANPDVP RILAKGWMHS
     MTPDGVNASM LDDIDPRPIF VDTKDLHSTW CNSAGLAEMG IADMADPAGG TIQRDEQGKP
     SGVLSEGAVL AIAWPHLAEV ASEQERIDCM LAAFDSYHAN GYTGLVEMAM DELSWNALIA
     LREQRPDFCM RIAAYWLIRP SNSKEERSRQ VARAVELSKV YNKETSPDLR IVGIKIICDG
     IIDACTAYLS EPYAVAPSPP PVWTREDLDP IVKQAADAGV QIALHAIGDA AIGMAVDMLE
     KHASAGGRHR IEHLELASPE DAKRLGALGL TASIQPVHAD PAILRAWPRL LGEHRCGRAF
     AYREFADAGA LMALGSDSPT APWNPLHNIY VAATRRSARE PGSDEVVNEH FRLGLCEAVV
     AGTAGAARSV FADDRVGSLE VGKQADMVVV DMEWEARSLL KSEIKETWFG GKKVWSG
//