ID A0A1R0GL90_9FUNG Unreviewed; 404 AA.
AC A0A1R0GL90;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=N-acyl-aliphatic-L-amino acid amidohydrolase {ECO:0000256|ARBA:ARBA00011913};
DE EC=3.5.1.14 {ECO:0000256|ARBA:ARBA00011913};
DE AltName: Full=N-acyl-L-amino-acid amidohydrolase {ECO:0000256|ARBA:ARBA00029656};
GN ORFNames=AYI68_g8309 {ECO:0000313|EMBL:OLY77657.1}, AYI68_g8385
GN {ECO:0000313|EMBL:OLY77581.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY77657.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY77657.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY77657.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(2016).
RN [2] {ECO:0000313|EMBL:OLY77657.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY77657.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:OLY77657.1}.
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DR EMBL; LSSL01007788; OLY77581.1; -; Genomic_DNA.
DR EMBL; LSSL01007752; OLY77657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R0GL90; -.
DR STRING; 133383.A0A1R0GL90; -.
DR Proteomes; UP000187455; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
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; IPR001261; ArgE/DapE_CS.
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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036696-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000187455};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR036696-2}.
FT DOMAIN 194..299
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
SQ SEQUENCE 404 AA; 45428 MW; 10716A3B54101272 CRC64;
MTISEPASVT RFRDYVKIET VHPTPDYAKC TEFLIAQAEE IGLGHQVVEL VKGKPVVILK
LEGSDPSLPA ILLNSHTDVV PVYREKWDYD PFAATRVEVE NGDHRIYGRG TQDMKVTGSL
YLEAFRQIKA SGKKFLRNVY STFVPDEEIY SIEGMMPFSK SQEFKDLNIG FGIDEGGPSI
NENTYYFTSE RTTCPVTFTA HGNTGHGSQF IEGTAIEKLL PIINELMLLR ETQLSKLKKI
GGIMLFNQGQ VTSVNLTMLE GGKQPNVVPA TFSATFDIRI TPLLDLAEFY KYLEDLAEKN
ECDIEFHYRD EPNKSLKITE TNPFMVEIKS ACSKHGLNPV EMVMPAATDA RFVRQAGIQA
VGINPMINHK LLAHDHNEYI IESEYIKSIP FYTDLIERLA SVPN
//
