ID   G7XDD8_ASPKW            Unreviewed;      1103 AA.
AC   G7XDD8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=A-pheromone processing metallopeptidase Ste23 {ECO:0000313|EMBL:GAA84809.1};
GN   ORFNames=AKAW_02923 {ECO:0000313|EMBL:GAA84809.1};
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:GAA84809.1};
RN   [1] {ECO:0000313|EMBL:GAA84809.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA84809.1};
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   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; DF126452; GAA84809.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XDD8; -.
DR   STRING; 1033177.G7XDD8; -.
DR   VEuPathDB; FungiDB:AKAW_02923; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   InParanoid; G7XDD8; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          33..197
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          224..403
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          409..696
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          701..881
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          113..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1103 AA;  125482 MW;  20756BC5C319F5DB CRC64;
     MGSIERLAEQ LEKPELDDRS YRVIRLPNKL EALLVHDPDT DKASAAVNVN VGNFSDADDM
     PGMAHAVEHL LFMGTMKYPK ENAYNQYLAS NSGSSNAYTA ATETNYFFEV GATTASTDDT
     PNGANGTSNG TDTPAKPNHP TSPLYGALDR FAQFFVEPLF LESTLDRELQ AVDSENKKNL
     QSDLWRLMQL NKSLSNPAHP YHHFSTGNLQ TLKEEPQKRG LEVRQEFIKF YQAHYSSNIM
     KLVVLGRDSL DEMEQWVGDL FKHVKNQDLP QNRWDHVQPC LPEHLGKQIF AKPVMDMRSL
     DLYFPFMDEE SLFESQPSRY LSHLIGHEGP GSILAYIKAK GWANGLSAGV MPVCPGSAFF
     TISVRLTPEG LKQYREVTKV VFEYIAMIKE REPQQWIFDE MKNLAEVEFR FKQKSPASRF
     TSRLSSVMQK PYPREWLLSG NLLRKFEPEL VKKALSYLRP DNFRMVIVAQ DYPGDWNCRE
     KWYGTEYKVE DIPEDFMDSI RKAAETSPES RLSELHIPHK NEFVPTRLTV EKKEVSEPAK
     TPKLIRHDDH VRLWYKKDDR FWVPKATVHV TLRNPLAYAT PANLVKTKFY CELVRDALNE
     YSYDAELAGL DYSLSASLFG LDISVGGYND KMSVLLEKVL TSMRDLVIKP DRFNIIKERM
     TRNYKNAEYQ QPFYQVGDYT RYLTAERTWL NEQYAAELVH IEAEDVSCFF PQLLRQNHIE
     VLAHGNLYKE DALRMTDLVE STLQSRALPE SQWHVRRNMI LPPGANYVYE RALKDPANVN
     HCIEYYLFVG KLDDDALRAK LLLFAQMTDE PAFDQLRSKE QLGYVVWSGA RYSATTMGYR
     VIIQSERNAA YLESRIDAFL TGFGKSLANM SEQEFESHKR SVINKRLEKL KNLSSETNRF
     WSHIGSEYFD FVQNESDAAN VRSLTKADLI QFYQQFVYPK SATRAKLAIH LKAQAGAHAH
     ATKPEEQKAQ VVSFLGKQLE AAGFAVDTER LSTAFATVDV SSGDEAQILA TLKAFLESGM
     SLSEQQTKPV IAQLESSLGL QLKQAGIEPK SDGTAVQPNG TNGDLQQSTY INNVPEFKAR
     LAVSAGPSPV TDLSEFEDFD AKL
//