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Database: UniProt
Entry: A0A383ZI89_BALAS
LinkDB: A0A383ZI89_BALAS
Original site: A0A383ZI89_BALAS 
ID   A0A383ZI89_BALAS        Unreviewed;       394 AA.
AC   A0A383ZI89;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   Name=ACY1 {ECO:0000313|RefSeq:XP_007174860.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007174860.1};
RN   [1] {ECO:0000313|RefSeq:XP_007174860.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007174860.1};
RG   RefSeq;
RL   Submitted (JAN-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_007174860.1; XM_007174798.1.
DR   AlphaFoldDB; A0A383ZI89; -.
DR   STRING; 310752.A0A383ZI89; -.
DR   GeneID; 103005903; -.
DR   KEGG; bacu:103005903; -.
DR   InParanoid; A0A383ZI89; -.
DR   OrthoDB; 158507at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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   CDD; cd05646; M20_AcylaseI_like; 1.
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.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 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:UP000261681};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR036696-2}.
FT   DOMAIN          175..284
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|RefSeq:XP_007174860.1"
SQ   SEQUENCE   394 AA;  43910 MW;  A54C8EF10BCED4C6 CRC64;
     LFRQYLRIRT VQPEPDYGAA VAFLEERACQ LGLGCQKVEV AAGRVVTVLT WPGTNPRLSS
     LLLNSHTDVV PVFKEHWSHD PFEAFKDADG YIYGRGAQDM KCVSIQYLEA VRRLKAEGHH
     FPRTIHLTFV PDEEIGGHQG MELFVKQPEF QALRAGFALD EGLANPTDAF TVFYSERSPW
     WVQVTSTGKP GHGSRFIEDT AAEKLHKVVS SILAFREKER QRLQSDPQLK QGAVTSVNLT
     KLEGGVAYNV VPATMSASFD FRVAPDVDLK AFEEQLQGWC QAAGEGVTFE FAQKWTEPRV
     TSTDDSDPWW AAFSGVCKDM NLTLEPEIFP AATDSRYLRA VGVPALGFSP MNHTPVLLHD
     HDERLHEAVF LHGIDIYTRL LPALASVPTL PSES
//
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