ID A0A165CU20_9BASI Unreviewed; 624 AA.
AC A0A165CU20;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=CALCODRAFT_460505 {ECO:0000313|EMBL:KZT51398.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT51398.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT51398.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT51398.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV424109; KZT51398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165CU20; -.
DR STRING; 1353952.A0A165CU20; -.
DR InParanoid; A0A165CU20; -.
DR OrthoDB; 5475921at2759; -.
DR Proteomes; UP000076842; 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:UP000076842}.
FT DOMAIN 140..619
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 624 AA; 68619 MW; 25620F8C78E53F1F CRC64;
MAADRATERL MMQDALRKNA TVGATPPRPP RRGTDFLTIR ARVQALVSAV VIAAVFILWK
SPKSSLPTTY ALCSKSRQIY TVEPDLPTVE CVVVDGAYIA DLGSREDITQ RWGDKYKTGP
IPGSPQSVAK SGLVFKTLPK GHAVVPGLSD SHAHVLDYGK TMQLPLAGSR SVEEIVKRTR
EYIERHPDVL NDTSIWIQGG GWDQTLWEGG EFPTWRDLDA DPVLKGRPIV LDRIDVHASW
VSSRVLEILS PLPDGVEGGH IIRDGDGAPT GVFVDNARQL IAARKPPDTE AQLFAYYKTA
MRDALEHGLT HIQDAATYPN YVDFFVNMAD KNMLPIRLTL MAHIDGDDYW GGNFTKLFGY
ADNRLTMRSV KLFMDGALGS WGAAMIEPYS DKPTEHGLLL SQPQAMLKLI DQFIADDWQV
NVHCIGDRAN NIVLDALETA LAKHTHGDRR PRIEHAQILT PGDLRRFGKL GVIASVQPTH
ATSDMGYAEQ RLGPERIKGA YAWRSLVENG ARLALGSDFP VEGINPLLGF YAAVTRLRPD
GTSPHGPGGW YPAQALSRQE ALHGLTLGAA YAAFQETQLG SLRVGKRADL VVLDQDIMTV
PLERILRTRV RATIVDGRVG WGKV
//
