ID   A0A0U1M9W0_TALIS        Unreviewed;      1160 AA.
AC   A0A0U1M9W0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Insulysin {ECO:0000313|EMBL:CRG92355.1};
GN   ORFNames=PISL3812_09413 {ECO:0000313|EMBL:CRG92355.1};
OS   Talaromyces islandicus (Penicillium islandicum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Islandici.
OX   NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG92355.1, ECO:0000313|Proteomes:UP000054383};
RN   [1] {ECO:0000313|EMBL:CRG92355.1, ECO:0000313|Proteomes:UP000054383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG92355.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; CVMT01000012; CRG92355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1M9W0; -.
DR   STRING; 28573.A0A0U1M9W0; -.
DR   OMA; WIFDEMK; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000054383; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000054383};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          137..217
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          272..325
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          353..531
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          537..825
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          830..1010
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1160 AA;  130766 MW;  7DE65E0C05A630E5 CRC64;
     MSPRSSTTTT TRVSRAIAPW NASLSRPARP GLSLVQRLQE ERNITANFGS TLPRQFASII
     TPPSIRRLVD PRRFSSTLSL SSSSPSPPAS ASSAPPPYCS SPATMSGASH LADRLEKPEL
     DDRSYRVIRL PNRLEALLVH DPDTDKASAS ANVNVGNFSD DDSMPGMAHA VEHLLFMGTE
     KYPKENAYNQ YLAAHSGSSN AYTGAIETNY FFEVAATGES SDGAASNGEA NNGESKQSNG
     VANGTTNGTS NGVTNGVSSS ASSSSSSLVS PLYGALDRFA QFFIAPLFLE STLDRELQAV
     DSENKKNLQS DLWRLMQLNK SLSNPQHPYH HFSTGNLQTL RDDPQARGVE IRSEFINFHK
     KHYSANRMKL VVLGRESLDQ LESWVVELFS GVQNKDLPQN RWDEVQPFSA DQLCTQVFAK
     PVMDSRSLDI YFPFLDEEDL YETHPSRYIS HLIGHEGPGS ILAYIKQKGW ANGLSAGAMP
     VCPGAAFFTI SVRLTEDGLA HHREVVKTIF QYIAMIKEKK PEKWIFDEMK NLAEVDFRFK
     QKSPASRFTS RLSSVMQKPL PREWLLSGNS LFRKFDSDLI TKALSYLRAD NFRLMIVSQE
     LPGEWDSKEK WYGTEYKVEK IPEDFLGEIR GALASGASER IPDLHMPHKN EFIPTRLSVE
     KKDVAHWAKT PKLIRLDDQV RVWFKKDDHF WVPKATVYVT LRNSLVWATP ANSVKAKIYC
     ELVRDALVEY SYDAELAGLD YNLSASVFGL DVCVSGYNDK MSVLLEKVVS TMRELEVKPE
     RFRIIKERLT RAYKNAEYQA PYSQVGEMTR YLTSERTWVN EQYAAELEHI EADDISIFYP
     QLLRQNHIEV LVHGNLYKED ALKMTNIIEQ TVRSRPLPQS QWHVRRNIVF PPGSNYIYER
     QLKDPQNVNN CIEYYLFVGS VIDDTLRAKL LLFAQMTEEP AFDQLRSKEQ LGYVVWSGAR
     YSPTTIGYRV IIQSERTAQY LEGRIDAFLG EFGQTLQEMS EEEFEGHKRS IINKRLEKLK
     NLGSETGRFW THIGSEYFNF VQHEIDAASV RGLSKADLTA FYSQYIDPKS ETRAKVSIHL
     NSPAAEVDKK LPVDKSETAE GADALHGQKT NGVNGLKPKQ TAREPIYVTN VPQFKASLPV
     SAGPSPVVDL CEFEDFDYKL
//