ID A0A2Z6SJ63_9GLOM Unreviewed; 404 AA.
AC A0A2Z6SJ63;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=RclHR1_09780004 {ECO:0000313|EMBL:GBC10612.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBC10612.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBC10612.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBC10612.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-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:GBC10612.1}.
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DR EMBL; BEXD01004401; GBC10612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6SJ63; -.
DR STRING; 94130.A0A2Z6SJ63; -.
DR Proteomes; UP000247702; 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:UP000247702};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR036696-2}.
FT DOMAIN 184..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 143
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 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT BINDING 373
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; 46137 MW; 1BCAB4411B7A36D2 CRC64;
MADGENPSVT RFREYLRIKT VQPNPDYESC KNWLLNQAKE IGLSSQVFEY VKGKPIILLT
WTGRDPELPA ILLNSHTDVV PVFEDKWSCD PFEAIKHENG DILARGAQDM KCVGASYLEA
IRCLKDQDKQ PCRTIHLSYV PDEEIGGYDG MKLFVKSEDF KKLNIGFALD EGIACPHNAL
KVFYGERTAW WVNVVTRGST GHGSQFINDT AVSKLRRIIN RLLDFREFQE KQLEIGRDRN
GRKYTLGDVT SINLTLLEAG VQHNVIPQEA KAGFDIRISP DVDLKDFEQL LEKFIKSESD
TTLEYVQYHG DNSCTPLDDS NVWWVTFRDF CDVRNISIEP EIFPAATDSR YLREIGIPAL
GVSYIKNTPV LLHDHDERIN ENLFLEGIEF YTDLITHLAN IQTI
//
