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Database: UniProt
Entry: A0A314KTU3_NICAT
LinkDB: A0A314KTU3_NICAT
Original site: A0A314KTU3_NICAT 
ID   A0A314KTU3_NICAT        Unreviewed;       447 AA.
AC   A0A314KTU3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Aminoacylase-1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A4A49_34740 {ECO:0000313|EMBL:OIT32134.1};
OS   Nicotiana attenuata (Coyote tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=49451 {ECO:0000313|EMBL:OIT32134.1, ECO:0000313|Proteomes:UP000187609};
RN   [1] {ECO:0000313|EMBL:OIT32134.1, ECO:0000313|Proteomes:UP000187609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC   TISSUE=Leaves {ECO:0000313|EMBL:OIT32134.1};
RA   Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA   Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA   Timmermann B., Baldwin I.T.;
RT   "The genome of Nicotiana attenuata.";
RL   Submitted (NOV-2016) 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   -!- 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:OIT32134.1}.
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DR   EMBL; MJEQ01001119; OIT32134.1; -; Genomic_DNA.
DR   RefSeq; XP_019226277.1; XM_019370732.1.
DR   RefSeq; XP_019226278.1; XM_019370733.1.
DR   AlphaFoldDB; A0A314KTU3; -.
DR   STRING; 49451.A0A314KTU3; -.
DR   EnsemblPlants; OIT32134; OIT32134; A4A49_34740.
DR   GeneID; 109207749; -.
DR   Gramene; OIT32134; OIT32134; A4A49_34740.
DR   KEGG; nau:109207749; -.
DR   OrthoDB; 158507at2759; -.
DR   Proteomes; UP000187609; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IPR010159; N-acyl_aa_amidohydrolase.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR01880; Ac-peptdase-euk; 1.
DR   PANTHER; PTHR45892; AMINOACYLASE-1; 1.
DR   PANTHER; PTHR45892:SF3; PUTATIVE-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF036696; ACY-1; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036696-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187609};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR036696-2}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..447
FT                   /note="Aminoacylase-1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016326387"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-1"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
FT   BINDING         405
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036696-2"
SQ   SEQUENCE   447 AA;  50242 MW;  957B2DA34B774029 CRC64;
     MFNPLQRVPL LLFFLALSTI SAAESDTPIS RFQNYLRINT AHPNPNYTSP ITYLINFANS
     IPNLHSKVLH LTPTIPLLLL TWPGTSTPSL PSILFNSHLD SVPAEPEKWT HPPFSAHKTS
     DGRIFARGAQ DDKCIGMQYL EAIKTIQSKD PDFKPLRNVH ILYVPEEEVG GFDGMGKFVE
     TKEFKELNVG FVMDEGQAST NDEFRVFYAD RTPWHMVIKA VGTPGHGSRL YDNTAMENLM
     KSIEVITKFR ESKFDIVKAG LAANSEVISV NPVFLKAGIP SPTGFVMNMQ PSEAEAGFDI
     RMPPTADPQL MRKIIEEQWA PAWRNMTYEI TEKGFLRDNM GCPLMTLTSD SNPWWSVFNE
     AVTRAGGKLS KPEILASTTD ARFMRRLGIP TFGFSPMKNT PILLHDHNEF LKDTVYLEGI
     KVYESIIKSL SSFEGSYEHR CNAVSQQ
//
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