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
//