ID   A0A420Y8K1_9PEZI        Unreviewed;      1261 AA.
AC   A0A420Y8K1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Insulinase (Peptidase M16) {ECO:0000313|EMBL:RKU44224.1};
GN   Name=IDE1 {ECO:0000313|EMBL:RKU44224.1};
GN   ORFNames=DL546_005132 {ECO:0000313|EMBL:RKU44224.1};
OS   Coniochaeta pulveracea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU44224.1, ECO:0000313|Proteomes:UP000275385};
RN   [1] {ECO:0000313|EMBL:RKU44224.1, ECO:0000313|Proteomes:UP000275385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAB683 {ECO:0000313|EMBL:RKU44224.1,
RC   ECO:0000313|Proteomes:UP000275385};
RA   Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT   "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKU44224.1}.
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DR   EMBL; QVQW01000033; RKU44224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420Y8K1; -.
DR   STRING; 177199.A0A420Y8K1; -.
DR   Proteomes; UP000275385; 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   Reference proteome {ECO:0000313|Proteomes:UP000275385};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          217..367
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          393..572
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          579..869
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          873..1054
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          69..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1261 AA;  143485 MW;  EFA46ACDAC2BED62 CRC64;
     MTSFRLQAPI SKLVISRNSC CGSRCPLNLT IARARQLAQH QSPGHTVQAR LLLYPLRILP
     KPITETFSSQ SSVPVRSSGS QVPSKSVASP HSAQTLVISG PPRPAETSKG ARPPLSTPLG
     QHLAPVSSLR RSIFLGLPLD NSPLLNQLRP YRHIQLPLTY TDNRRFGTAA FMPSLEEPRA
     APVAGAKSVK LVTENLEKPS LDDRSYRVIR LSNELEVLLV HDATTDKASA AMDVNVGAFC
     DEEDMPGMAH AVEHLLFMGT KKYPVENAYA QYLASHSGSS NAYTAATSTN YFFDVSAKPS
     NDQEPSAENP SALYGALDRF AQFFVEPLFL EETLDRELRA VDSENKKNLQ SDQWRLHQLD
     KSLCNPKHPY CHFSTGNLEV LKTEPEARGV NVREKFIEFY EKHYSANRMK LCVFGREPLD
     VLQAWVVELF SDVKNKGLKQ NRWTEETPYT AEQLGTQVFA KPVMDSREIN LTFPFLDEEY
     LYESQPGRYI SHLIGHEGPG SIMAYIKSKG WANGLSAGSY AIAPGSPGCF DCNIRLTEEG
     LKNYKEIVKV FFEYVAMLRE KPPQEWIFEE QKGMSDVDFK FKQKTPASRF TSKIVSTMQK
     PLPREWLLSG NSVFRKFDPK AIQEGLDCLR PDNFRLQIIS RDFPGQWEQK EKWYGTEYTL
     AKMPSEFMEE LKKASALPAK DRNPNLHLPH KNQFIPTKLE VEKKEVKEPA LSPRMVRNDD
     LVRTWFKKDD TFWVPKANLI VSGRTPIIYA SARNAVKARI FTDLVRDALE EYSYDAELAG
     LQYTVSLDGK GLFIEVSGYN DKLPVLLEKV LETMRDVEMR EDRFEILKER LSRGYKNWEL
     QQPFHQIGEY TNWLITPEGD FVVEELLAEL PEITVDDVRS FRRDILSQLH MEVYVHGNFY
     KHDAMKLAKL VESTLKPRVL PRTQWPLQRS LLFPPGSNYV WKKTLKDPKN VNHCMEYWLY
     IGDKADREIR AQTLLLDQVL HEPAFDQLRT KEQLGYVVFS GVRTGATTYG FRFLIQSEKT
     SEYLETRIDS FLTGFRETLE KMEDTAFETH KRSLIAKRLE KPKYLDQETN KHWTQIHSEY
     YDFESAQRDA DYIKPLTKED LINFFNHYIH PESTARAKLA VYLVAQAKSD VSTKQIMELV
     TSLSLSGEAS SQAATDLQAR LSAAGHDEKK EIDGLKDYLI HDLKIGEDKI ETAVEAWKKL
     HAQNTEQKGL VGLDDQTAPT ANGSQPFVIE DVRAFKAGLV ASTGAVPAKD LTEYEESDVK
     L
//