ID E7A1Q3_SPORE Unreviewed; 593 AA.
AC E7A1Q3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=sr14069 {ECO:0000313|EMBL:CBQ73410.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ73410.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ73410.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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DR EMBL; FQ311472; CBQ73410.1; -; Genomic_DNA.
DR AlphaFoldDB; E7A1Q3; -.
DR EnsemblFungi; CBQ73410; CBQ73410; sr14069.
DR VEuPathDB; FungiDB:sr14069; -.
DR eggNOG; ENOG502QWA6; Eukaryota.
DR HOGENOM; CLU_009942_5_0_1; -.
DR OrthoDB; 147994at2759; -.
DR Proteomes; UP000008867; Chromosome 7.
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;
FT DOMAIN 74..571
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 573..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 64971 MW; 3FFC77625E52847D CRC64;
MTTKLFKNAL FFTAQAQELE PASLLKQNYI DADAIANRFA ECIVVQHGKL AYVGNLANTP
PELKHKAEQV DLCGDKLVVP GFIDGHTHLL NFGQSLDKVD VGKCKNLEQI QQKIKEAAEA
KPDAPRILAS VWMQNSTDGK ALASWIDEVV PDRPVYIESF DLHSHWCNTA ALNELGITDD
TPDPEGGEIV RDSATGKASG LLLEMANILF VWPKLANLAT KEEQEANFMR ACDSYHQSGF
TGGIDMAMDP LSLDCILRVK AKMKGKLPIR VAAHWLVRPD PDVDACIAQV KHAHELSQKH
NDEWFRIVGI KLVCDGVIDS CTAALKEPYY NKTNAELMWP LPLLSAVVQC ADSLDLQVAI
HAIGDLAVHT AVEAIATLGE KLAGQGRSIR DRRHRIEHLE LTDPKDVEKL GRLGITASIQ
GVHCDPSIMD NWCRMLGDKP NEGRCARAFA FREFFEAGAP IALGSDAPTA HHWILPNLYT
AVTRHSGREP ELTSRTTPQF ALPLATAMAA ATYGAAHSCK AESWSGTLEE GKSADFVVLD
TDLFKEHGTG DKEQTILKTK ILQTWLTGEK VFDSSSGKDG ISESRNRSGC TVL
//
