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Database: UniProt
Entry: G7XT02_ASPKW
LinkDB: G7XT02_ASPKW
Original site: G7XT02_ASPKW 
ID   G7XT02_ASPKW            Unreviewed;       416 AA.
AC   G7XT02;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:GAA90072.1};
GN   ORFNames=AKAW_08186 {ECO:0000313|EMBL:GAA90072.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA90072.1};
RN   [1] {ECO:0000313|EMBL:GAA90072.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA90072.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; DF126471; GAA90072.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XT02; -.
DR   STRING; 1033177.G7XT02; -.
DR   VEuPathDB; FungiDB:AKAW_08186; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   InParanoid; G7XT02; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05652; M20_ArgE_DapE-like_fungal; 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; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..416
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003505825"
FT   DOMAIN          213..320
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   416 AA;  43630 MW;  FDDADB4AEA98D1B4 CRC64;
     MKSPISLLAA VGVASAASPQ TLLSLASTAS DIIDASPFLS FHRDIVQIPS VSGNETAVGT
     FVAEFLESHN FTVIKQPVPS SSKGDPDRFN IFAYPSTSPS QDRPEILLTS HIDTVPPFIP
     YGLHDDANNN SNILISGRGT VDAKASVAAQ IFAVLDTLES NPSASLGLLF VVDEEVGGLG
     MRTFSDNSTL NPSPSPYHTV IFGEPTEQAL VAGHKGMLEF PIIATGQAAH SGYPWLGSSA
     ISALLPALSR VDHLGKIPEA EGGLPASDKY GETTVNIGRV DAGVAANVVP SSAIAEVAIR
     LAAGTPDEAR DIVARAVRNA TGGDEHVYCD FAAYAGGYAP QDLDTDVPGF EITTVNYGTD
     VPNLKVSEGV KRYLYGPGSI HVAHGDNEAI TVGQLEEAVR GYKRLIEAAV QRARRN
//
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