ID G1X5K0_ARTOA Unreviewed; 654 AA.
AC G1X5K0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=AOL_s00054g144 {ECO:0000313|EMBL:EGX51445.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX51445.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX51445.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX51445.1}.
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DR EMBL; ADOT01000084; EGX51445.1; -; Genomic_DNA.
DR RefSeq; XP_011119762.1; XM_011121460.1.
DR AlphaFoldDB; G1X5K0; -.
DR STRING; 756982.G1X5K0; -.
DR GeneID; 22890654; -.
DR eggNOG; ENOG502QSHE; Eukaryota.
DR HOGENOM; CLU_009942_2_0_1; -.
DR InParanoid; G1X5K0; -.
DR OMA; MEGAMWD; -.
DR OrthoDB; 147994at2759; -.
DR Proteomes; UP000008784; 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:SF24; AMIDOHYDROLASE FAMILY 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:UP000008784};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..654
FT /note="Amidohydrolase 3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003425762"
FT DOMAIN 137..646
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 654 AA; 72340 MW; D9908573992CC414 CRC64;
MRFFHGLPAG PLVLASFIFS LFSPSIAHPD HEEETGSCLT GHIKLAEIIF GKITPSDFDT
SAVSRRFSRP EKRTSDQNVP IIFYSSSQQN RRPIITMAND RLSPVEALAI HEGKVIAVGS
LASVRKKAGD RRIFRNLHKQ VILPGFVEPH LHIMLSALLK GYFLDISPLR APSFESAMQQ
LRDELKTLKQ GEWLIAYGYD PSRLNWHDLS KEDLDKEVSL TTPIVVINAS GHLAYANSLA
FQEVGITKNT PNPEGGEYAK DPKTGELTGV LVESGAILQF SAKATLANLG RTGRVKEGLA
KILGQWLAKG LTTVFDGGLG AVTPQDLETV ANLTEVSPIR IRAAVADFKP GDAEKMLGTG
NMPAGGFKRK GLIVKTVKLW SDGSTQGFTA AVKQNYLSEH FPTYFVGKEK GVLVWPDSAN
VGESAFNTTM YDEMLKWLNR GYQLMIHANG DRASDIVLGN FEKIFKKYPK HNPKRSGIIH
RIEHFTVTET SQVRKAKDLG IAVSHTMGHV HYWGDTFRFG VLGKERAERI DPVKDDVNSG
VIYSFNSDSP VTDADPLLWV GTAISRRVYK SNNILGKAQR VGLEDALKGV TSYPAKQILW
EKEVGSLEAG KFADFVIVSR DLWCFDWERK NTNEIKVLET WIGGVRRYSA LGSV
//
