ID   A0A0L6WSC9_9AGAR        Unreviewed;      1066 AA.
AC   A0A0L6WSC9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Putative zinc protease {ECO:0000313|EMBL:KNZ78447.1};
GN   ORFNames=J132_00810 {ECO:0000313|EMBL:KNZ78447.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ78447.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; KQ412478; KNZ78447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WSC9; -.
DR   STRING; 1306850.A0A0L6WSC9; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000053712; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
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.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KNZ78447.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          51..185
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          208..380
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          394..688
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          691..871
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1066 AA;  120839 MW;  FD53C486076CB8D9 CRC64;
     MTTVATNDVD WSLASSGLAP PYSIYNKPIQ KSEQDDRDYR IIRLENGLHA TLIHDANADK
     AAASLDVAVG HLYDPADMPG LAHFCEHLLF MGTEQFPKEN EYSEYLAKNN GSANAYTSTS
     NTNYYFNVAT PALAGALERF AGFFHSPLFA PSCTTRELNA VDSEHKKNHQ ADIWRIFQLN
     KHLSKEGHPW SKFDNDTEAD GGAIGRETRR RLLEWWSHEY CASRMRLCVI GKESVDELSE
     LTSILFSPIP NRGCDALPMI SDHPFGPNEK GTLVSVQTVM SFHALEISFP LAWQPPSWRH
     KPANFLSFLL GHEGAGSLHS YLKKKGWITS LNSQPQNLAR GFAMFKVTVH LTEDGFQHHR
     DVIHAAFQYI SLLRASKFDA FHQHEIAKVS DIKFRFKEKR RPDEYATSIT EYMSWPVPKD
     LILKAPAVTW DWDSATGENE VRKCLETFRI TEGRVVLMAT AAEHAKITST DVIWEKEPWY
     GTSYRVERFD EQFINKAEAP NAISELFLPG PNEFIPTDLQ VDRRIVTEPL KRPHLIRETP
     LSTLWHKKDD HFFVPKAHVV IDIRSPVVNE TARAAVMTKL YADVVNDSLT EYSYAADLAG
     LSYNFMSHTN GLYISIHGYN DKLSMLVRKI LETMKGLSVD PQRFDIIKEQ NQREWRNFFL
     GQSYTLSDYF GRYLLTADQW LLEEKLKELS SITPNEIQIH IKQLLSQVNL RMLVAGNIYR
     DEALKIADIA EDGMGISSLS AMELNDRALL LPQGSNHTWT CPIPNPNQAN SSLTYYVHFG
     PIADQKLRVV SSLLTQILSE PAFNVLRTQE QLGYVVQCGP WMLAGSSEKG MRIVVQSEKT
     PGYLEERVES FLDGMKSTIE NLSEVEVAEQ KGGLERKWLE KDKNLADETS YFVNQITTGH
     LDFLRRENDA RLLRSVTKND VLDLFLSCVH PSSATRSKLS VHMISQKTRP KKVSVAASQA
     FDVLLREAGV KFDAETWKKS LGDEKPLATD FINYWKQVLE IEPNAARLLS AIPEFVERYP
     VPGESKDVPR SNVTYINDIK AFKTSLAESV DPGPMVQWGD LPMSRC
//