ID   A0A197K6S4_9FUNG        Unreviewed;      1035 AA.
AC   A0A197K6S4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=K457DRAFT_122577 {ECO:0000313|EMBL:OAQ33367.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ33367.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ33367.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ33367.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) 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; KV442021; OAQ33367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A197K6S4; -.
DR   STRING; 1314771.A0A197K6S4; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000078512; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          47..182
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          209..384
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          394..682
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          688..892
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1035 AA;  117818 MW;  763479524F409376 CRC64;
     MTSDKTLPVG FEMSPDGTHA VFTKPIESSP NDERSYRLVR LNNDLEVLLI HDAKADKSAA
     ALDVHVGHLS DPDNLQGLAH YLEHLLFLGT DKYPRENEYK EFLAQHAGKS NASTSLDHTN
     FHFEVGHAHL ERALDRFAQF FISPAFNESC TDREIRAVDS EFKRNLQMDG RRLFQLGKHL
     SGRSHPFWHF GTGNLITLRD LPTQEGINTR DELIKFYHKY YSSSIMKLAI VGREPLDELT
     GWAVEKFSAI RNLGIAPPSY PGPPLTPKEL LTMAYVKPVK DLRTLEIKFP FSDTSRHYTL
     QPARYINHIV GHEGTGSILS LLKRKGWASG ISASNPGGGV GFEFLSFVVS LTKEGLLHCE
     EIIEVVFQFI KLLKQEGVVP HIWDEVTSLA STAFRFKEMM QPADYVVARA GAMQRGYAPE
     WVLSGSELIR SNEPQIIQQF INELQVNTWV GRIVTQDISV VPGGAFTQTE RWYGTQYHVA
     PVSPALLDRL SKGLELHPEL HMPLPNEYLP KDFETHKVDT PEPLTHPTLI KHTPLTRLWH
     KKDDIFWVPK VNIHLRFTAP LATANPSNLV KSMLYVALVK DVLNEETYAA QIAGLDYTLD
     SSIKGIQLSI RGYNDKAHLL LERVIHTMRN LQVEPDRFVR IRDQIERDHR NAYLANPSQH
     ASYHIQVIHQ EKMWTFIERL DALEFVTTPE EIQLFYPEML ARLHVEGLVH GNMDRGQALR
     VSEIVEEGLG AATRPLVPSE LTAMRSLLLP EGCQAVYQRD TPDPSNLNSG IEYFIQMEDV
     PHLPPSSLSP NSKNQDTLAR DHKTTRALTQ ILAQIIQEPC FHQLRTTEQL GYIVQSGIHT
     FGPLTGIKIL VQSERDPVYI ESRIESFLTN RINNLLFNTM TPQDFERQVQ SLVEKKLRKD
     MKLREETGRY WGQILSGYFD FWEIAEEVEV MRRTSLEDAR RFFAEWILPG AVRAKKVSVH
     IRSQMLNKST DTKVKSSKEK ETDESKVEPA VRTLEEVITL KEGTLLIEDV VTFKAGLELS
     RAPVPVIDLL RYSKL
//