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Database: UniProt
Entry: A0A195F2Z7_9HYME
LinkDB: A0A195F2Z7_9HYME
Original site: A0A195F2Z7_9HYME 
ID   A0A195F2Z7_9HYME        Unreviewed;      1911 AA.
AC   A0A195F2Z7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Insulin-degrading enzyme {ECO:0000313|EMBL:KYN34459.1};
GN   ORFNames=ALC56_10946 {ECO:0000313|EMBL:KYN34459.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN34459.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN34459.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN34459.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN34459.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) 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; KQ981856; KYN34459.1; -; Genomic_DNA.
DR   STRING; 34720.A0A195F2Z7; -.
DR   Proteomes; UP000078541; 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; 9.
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; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 4.
DR   Pfam; PF16187; Peptidase_M16_M; 3.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 9.
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:UP000078541};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          2..136
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          166..344
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          350..552
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          594..711
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          736..912
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          920..1195
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          1201..1384
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          1437..1595
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          1600..1783
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1911 AA;  223573 MW;  BC5D59B39E25F53A CRC64;
     MKVLLISDPT TDKSAAAMDI NAGSMCDPDD LPGLAHFCEH MMFLGTKKYP QQNDFKKFLS
     RNGGEYNAST GLDHTVYYFD VATEKLEGAL DRFAQFFLAP LFTENLTELE LNAINSEYEK
     NVTSYGARFN QLERSSASSD HPFSKFNIGN RETLDTIPKQ KGINVRNKLL EFHENYYSAN
     IMSLSVLGKE SLDELENIVV DLFCEVRNNE IEVPIWPEHP FKDEHFRTIW YIVPIRDIRY
     LDISFPSPDM RQHYGFSPEY YVYYLLEHKG KGSLLSALKA KGWCNLIGSR IHPSTRGFRI
     FNINVDLTEE GIKHIEDIVL MVFQYINMLK SKGPIKWIYD EYKNIANTYF RFKEKSSPLI
     SVKCTVRELQ EITMNEFGCA VSAWRPDLIE EIMEYLIPQN VRIHVTAKAC ENIADEIESW
     YGTKYKKVKI SKEIINTWNS PGFNDDLKLP VKNEFIATTF DIKLQTNVEK FPIILENTSF
     VRLWYKKDDE FLVPKAKMIF AFFSPFASMD PLSCNYTYMF IQLFRDSLNE YTYAADLAGL
     RWELNNFKYG ITYIRILQNF DAEQPYEHAV NYLITLLTKQ TWLNKEYLEA TICSMCDPDD
     LPGLAHLCEH MLFLGTKKYP QQNDFKKFLS QNGGVCNAIT GLDHTMYYFD VATEKLEGGL
     DRFAQFFLAP LFTKNLIELA LNTINSEYEN NLASDSERFN QLVMSTASSD HPFSKFRAGN
     RETLDTIPKQ KGINVRNKLL EFHEKYYSAN IMSLSVLGKE SLDELENMVV NLFCEVRNKE
     IEVPTWPEHP FKDEHFGTIW YIVPKTNIGN LVIDFPLPDM RQHYRSSPDR YVSHLLEHQG
     EGSLLSALKT KKLGHYIKST KRTTARGFSI FSILIHFTKR GFRHIKDIIL LVFQYINMLK
     LKGPVKWIYD EYTDIENINF RFRGKSSPLT CVKFNSRLLQ EIPMNEIYCA NSEWRPDLIE
     EIMEYLIPQN VRIHITAKAY ENIANEIESW YGTKYKKVKV TKKLMDMWNS PGFNDDLKLP
     PKNKFIATKL DIKPQTNIEK FPIILENTSY VRLWYKKDDE FFTPTASMNF NFWCPFAHMD
     TLSSNYTYIF IKLFRDSLNE YTYAAHLAGL RWELFNSRCG ITLSINGYDD KQRGLLEKII
     DRMINFKVDP KRFEILKENY ISNLKELRFT RLYKHAIYYL DMLLTKKPFL QEDFLRTTSY
     LNVDGLQQFI PQLFSKVHVE CLIHGNVTVT EATDILKLIE SKLTAAVPNI MPLLEQQLVL
     DRKIKLENGC HFLFQTENNL HKSSCTLVYY QIGLQSTESN VLLELLKQII KEPCFNTLRT
     NEQLGYIVFT NIHILDGVQG LQIVVQSDKH PQYVEKRINL FLDSMLNHIS TMTEEQFEEN
     KKALAVLRLE KPKSSTVRCA LYWKEIKFQQ YNFDRVNVEM AYLKTISRQQ LLNFFKIEKF
     PIILEDTSFV RLWYKKDDEF LVPKAKMIFD FFSPFASMDP LSYNYIRMFT YLFRDSLDEY
     TYAADLAGLQ WKLGNSKYGI RLSIDGYDDK QRGLLEKLMD QMINFEVDPR RFKILKENYI
     RNLKNCVAEQ PHKHAVNYLL ILLTKQTWLN EELLETTIYL NVDGLRQFIP QLLSKVHVEC
     LIHGNVTVTE ATDILKLIES KLTTGVPNII PLLEQQLILP REIKIENGCH FLFEAENNFH
     KSSCTLVYYP TGLQSTESNM LLKLLAQIIK EPCYDTLRTK EQLGYTVFSD AREWCVAQGL
     QIVVQSNKHP QYVEKRINLF LNSMLNHIST MTEEQFEENK KALATLLSVK PGNLTARCDL
     YWNEIETQRY NFDRVNIEVA YLKTISRQQL LNFFKENVHS KDRCKFSIHV ISTSSEKSSI
     EEIADLSVYE EVKKIYDILS FRNSQYHYPL IKPFKKFFLR KGVRPSKLSK R
//
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