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
//