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Database: UniProt
Entry: A0A1S9DL55_ASPOZ
LinkDB: A0A1S9DL55_ASPOZ
Original site: A0A1S9DL55_ASPOZ 
ID   A0A1S9DL55_ASPOZ        Unreviewed;       853 AA.
AC   A0A1S9DL55;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Amidase {ECO:0000313|EMBL:OOO09676.1};
GN   ORFNames=OAory_01054840 {ECO:0000313|EMBL:OOO09676.1};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO09676.1, ECO:0000313|Proteomes:UP000190312};
RN   [1] {ECO:0000313|EMBL:OOO09676.1, ECO:0000313|Proteomes:UP000190312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC7051 {ECO:0000313|EMBL:OOO09676.1,
RC   ECO:0000313|Proteomes:UP000190312};
RA   Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA   Jeennor S., Laoteng K.;
RT   "Genome sequencing of Aspergillus oryzae BCC7051.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the amidase family.
CC       {ECO:0000256|ARBA:ARBA00009199}.
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:OOO09676.1}.
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DR   EMBL; MKZY01000004; OOO09676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9DL55; -.
DR   VEuPathDB; FungiDB:AO090003001399; -.
DR   VEuPathDB; FungiDB:AO090003001400; -.
DR   eggNOG; KOG1211; Eukaryota.
DR   Proteomes; UP000190312; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR11895:SF67; AMIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190312};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        45..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          400..813
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  93312 MW;  59A2B94EAE26499E CRC64;
     MDGTKDSGTD HVEQYVENPK DQDLRSVPTA LLDWSPEERR QREKVLVCVN ILFVGYLLMQ
     VPSNMILNRL GKPSIYLPGC MIVWGIISCL TAVTKDFGGL LAVRFSLGFV EAAYFPGCLY
     LLSAWYTRKE LVERTALLYV GSLISGTFSG LISAGITSGL NGARGIAAWR WLFIIEGSLT
     IFVALLAWFI VPDLPRTTSW LSNDEKVLAA WRLEEDIGED DWVDSEHQSM FHGAKLAILD
     PKAWLLLGVI YGCTSSGAVT TFFPRPDLPP TYDRKPNPAL RGIILSVGAW LLDWLWFLPQ
     IIWSNAGFGS LRTIRSHLDY IEPRYDPTVV PLKGNSDENP DGSVADTVSA PPVKYSTKYY
     SVADYHELYK SGELTPIAVV KGLLPLIRRD LSTPGKHSIA FVDSRVDLVL TAAEESTRRY
     KEGRPLGLFD GVPAAVKDEF DLDGYRTNMG SLNDYTLEPK SDDPSITNWC IRQLEKAGAI
     VVGKVSMHEF GLDTTGNNIH YGTPPNPYHP DYYTGGSSSG CAYAVSTGLV PIALGTDGGG
     SVRIPSSFCS VVGLKPTHNR LSHYPSVNYA STTSVIGPLA ADIRSLAEAY RVFATPGPDT
     PFPAPGPLSL TPSTRGKKIL GIPEVWFSRS TPDVQRLCRS LLDKLVTEKD YTIVPIDIPF
     LVEGQTAHAM TILADGAALL PDTTNITAPN RILLTLGRTT PATDYLLAQK LRRLLMQHLA
     ALWQEFPGMI IVTPTTACAG WPVVSKSELK WGLSDGDRTL KAMEYVWLAN FTGIPAISVP
     AGYADPEGKH STEGTVPVGL MGNGEWGSEE QLLQWGLEAE ELGADLRERP PIWEDVIQRA
     KWVGSSSGSQ ETA
//
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