ID A0A0C9Y3C0_9AGAR Unreviewed; 610 AA.
AC A0A0C9Y3C0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=K443DRAFT_677460 {ECO:0000313|EMBL:KIK02613.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK02613.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK02613.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK02613.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler 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., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
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 (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN838590; KIK02613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9Y3C0; -.
DR STRING; 1095629.A0A0C9Y3C0; -.
DR HOGENOM; CLU_009942_1_1_1; -.
DR OrthoDB; 5475921at2759; -.
DR Proteomes; UP000054477; 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 Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT DOMAIN 128..607
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 67226 MW; 5B6A771C801959E5 CRC64;
MSKLHHRPIT PPEAAKEKES PSAPLHKRPA PAAPSKPLSW GFKLLYVAVA LSTLAYLSPR
DDSNISGTYA VCAGKRKGIF TVDEQNIQVD CMLVEGPYIR DSGSLHDIRE RWKLAGGKSF
TVRHLAPGTI VVPGLSDSHC HILEYGASRQ IPLSLGKNAK ETASFVSDYI KAHPDLESDP
THIIEGWGWD HASWDVEKMP TWRDLDAYPL IKGRPIILQS RDGHAIWVSR ATLDANAPFP
DSVEGGVIMR DESGEPTGVF MDNAQELIKH PTLTDDDLYR RFKTTVDHSL QHGLTSLHDA
GFKPDSLAFF RRQTALGPLP IRIYGMTYFD ENGPYWGNQI TPLVGTPDDR LTARSIKIFA
DGALRTGGAA LYEPYADNPS TSGQMRLPDH VFHEVIPRFL KDGWQVNVHA IGDRANGIVL
DAFEEALKGA NISALRPRLE HAQIMTKEDM ARLGRLGVIA SIQPTHAISD MWFAEPRLGP
ERVKGLYAFR SLLNNSARIT LGSDFPVEGV NPLAGFYAAI TRVSFDGKSP HGKGGWFPEQ
RLTRLEALRG MTIDPAYASF TEDILGSLEV GKRADFVVLD RDIMEVSAEE IMETRVLATL
LDGAAVFGSL
//
