ID A0A0N5AFD3_9BILA Unreviewed; 1047 AA.
AC A0A0N5AFD3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Insulin-degrading enzyme {ECO:0000313|WBParaSite:SMUV_0000298101-mRNA-1};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000298101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000298101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR AlphaFoldDB; A0A0N5AFD3; -.
DR STRING; 451379.A0A0N5AFD3; -.
DR WBParaSite; SMUV_0000298101-mRNA-1; SMUV_0000298101-mRNA-1; SMUV_0000298101.
DR Proteomes; UP000046393; Unplaced.
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; 5.
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 35..171
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 198..363
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 409..704
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 710..890
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 1047 AA; 120034 MW; 818FEE764B4D6DDE CRC64;
MSKEEVIAQR FNNIVKSAED KRLYRGLELR NGLRLLLVSD PKADKSAASM DVCVGHLMDP
WELPGLAHFC EHMLFLGTDK FPSENEYGKY ISSHGGMTNA FTASDHTNYH FDIAPEFLKG
ALDRFVQFFL CPQFTESATE REVCAVDSEN SNNLKNDSWR LLQLERSLSK PGHDYGKFGT
GSKKTLLEDA RSNNIEPREA LLNFHKRNYS SDLMCCCIVG NETLEELEDM VVSLGFGNIE
KKNLKRKTWE NPYGSEQLGV KVELVPIKDL RQMSLNFPIP DYTDYYKTGP AHYVAHLIGH
EGPGSLLSEL KRRGWVSTLS AGSRKMARGF SSFNISVNLS EDGLENTENI IKIMFEEIAL
LEKVGPLNWV QDELKKLHDI KFRFKVCFLA VEVIVDNFSY YVLIRCHLFF FKDVETPINL
VTHMSSNLQS FPMEDVVYCD YRLDEFDKGE CIFLGPKVNK KVIVDLLRRL NPHNMWYSVV
SKKFANRADN QREKWYGTEY KKTKFEQSTY EHWALAKHTI SDTLKLPLAN QYIATKFDQK
KLDDAPTNAP RIISDDEWAR VWFVQDDEYK LPKCFTKVAV HSPLISSSPM NTFLSTMYIS
TLQDALAEFT YSPELAGLSS SFIETSSSLT LKITGYDEKQ KLLTKNLLEK LVNFVPDEKR
YEILKEDICR YLRCFKQTQP YTQCNYYTCL LLNTSEWTKE QILACAESCD VTRLKNFIKS
VYEAIYLEIF VCGNMQEKEV LELKEDVVGI FKAVPGIRPL FASEISRCRA HIIPNGSGFI
LKRVQNTHKN SAVGFVMQTG EQSTRENALL ELVVQLISEP AFNQLRTNEQ LGYIVHTGTF
RNFGAQGLQI IVQGEHDPEF VAQRIEGFLD EFRQKLSSMS EEEFKENVES LAMKMLEKPK
TLNSKACRYW TEISSGFYHF NRGHACSALG FFEKHTLANT WSCFISLHSF LEQDEVPLLR
TLTKDDVISY FDKHFAHDSP ERRKLCTIVY ADNEKAADNN NEKDLSNSKA ESLITNIDSF
KSSMGLYPLP QPVINIPPLA FKNNSDQ
//
