ID F0W435_9STRA Unreviewed; 345 AA.
AC F0W435;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Aminoacylase1 putative {ECO:0000313|EMBL:CCA15832.1};
GN Name=AlNc14C15G1720 {ECO:0000313|EMBL:CCA15832.1};
GN ORFNames=ALNC14_019750 {ECO:0000313|EMBL:CCA15832.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA15832.1};
RN [1] {ECO:0000313|EMBL:CCA15832.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA15832.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR036696-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR036696-
CC 2};
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DR EMBL; FR824060; CCA15832.1; -; Genomic_DNA.
DR AlphaFoldDB; F0W435; -.
DR EnsemblProtists; CCA15832; CCA15832; ALNC14_019750.
DR HOGENOM; CLU_021802_5_0_1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004046; F:aminoacylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010159; N-acyl_aa_amidohydrolase.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01880; Ac-peptdase-euk; 1.
DR PANTHER; PTHR45892; AMINOACYLASE-1; 1.
DR PANTHER; PTHR45892:SF1; AMINOACYLASE-1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF036696; ACY-1; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036696-2};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR036696-2}.
FT DOMAIN 147..275
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
SQ SEQUENCE 345 AA; 38887 MW; B0EC95F847182895 CRC64;
MLDVKVIELV DKKPIVLATW KGSNSSLPCI ILNSHYDVVP AVREKWDLDP FQPKVLGDGH
IYGRGTQDMK SVCIQYVEAI RRLKTQDESF TPERDIHLLF VPDEEIGGAD GMNVFLQSED
FKRLQPIACV FDEGLANPEK AYTVFYGERV PWWLYVKAEG PTGHGSRFIA NTATSKIIDI
CNKALAFRKT QEAMLHVDDG CKHGDMKKKT LGDVTTINLT HLKSGVSVDG GKTYALNVIP
TEAIAGFDVR ISPKMDILSL HAMLDEWCAD EGLSWEFAQK NSLYEHYTTK LDDNNHWWQL
FQSVSKEFGV RLETEVFPAA TDSRFIRKLG IPAFESVSSY DRFGS
//
