ID A0A0V0VRI4_9BILA Unreviewed; 1653 AA.
AC A0A0V0VRI4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Insulin-degrading enzyme {ECO:0000313|EMBL:KRX66111.1};
GN ORFNames=T09_11762 {ECO:0000313|EMBL:KRX66111.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX66111.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX66111.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX66111.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX66111.1}.
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DR EMBL; JYDN01000013; KRX66111.1; -; Genomic_DNA.
DR Proteomes; UP000054681; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 2.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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 InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
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 Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS00143; INSULINASE; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 42..286
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 378..621
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 1653 AA; 188507 MW; 1F7EFA498138F94C CRC64;
MQLSFTKATF ATYVENKKIN CGIINFEEAE DSNSKIIKAN RIVGGWVAEE HSFPFMVAVE
RLTSSSKVFA CGATLIQPEP GNGTKIVLTA AHCIFSQIMK GAVHPQNFVV SAGIHNLYKQ
NEEKNRQTVR VRNYLCHDFS FAKQRNDIAL LFLDDWIIYN KHILPICTAK ADQAVPDDSI
CFTAGWGKTE SAHVSDVLRI VDVTFFPEQT CITNPSSPFD KETMICTAGY PRKSGTCMGD
SGGPLVCFVN EKFVQFGIVS WGYKCGDITV FTKLSRFSSW LEESMNDKEN YNPPVPSFPV
FPSRIHAMQQ MKASFPPLWT FRKPAYLIPN SPSISRILYE FISFKNRQIS SAMCVEIDCG
LITVDQSPKN RNENSNRIIG GWTAEPHTFP WIVKLEKVQN FQRKFLCGGT LIQPKKSNGT
NFVLTAAHCT GSLILNQHFH PHELLATVGI HDELKINNPH ERTVRVKSYL HHNYNGKTLK
NDIALLLLDE WITYNEHVLP ICLAKYEEQP LTNSICFSAG WGKTEDNLPS KELRIVDLVF
QSKEVCMPYS HSLFDGKTML CTTGQNNKSG VCMGDSGGPL VCYYKNKFVQ FGVVSWGYQC
GEISVFTKVS HYFHWLKNVM QNPATFPNII HQPMPETNFH SATYPTIFPS FPSLWIPFRP
LFPISNSMLN ESAKFIKHRN DNIIQSPEDK RSYRGLELNN GLKVLLISDP KTDKAAASLD
VSAGHMMDPW NMPGLAHFCE HMLFLGTKKY PKDNEYQSYL VAHGGNSNAY TSTDHTNYHF
DVAPEFLGGA LDRFAQFFIE PLFTVNATER EVNAVDSEMR GNLQSDSWRD YQLERHLSNP
KHDYNKFGTG TRKTLLDDVL ARGDDPREAL LQFYQNHYSA NLMALCIMGK ESLDELQAAY
VPTFASIENK KLEKIVWKEH PYTATELGYR VNVVPVKDLR SINFCFPLPD LQEYYTSNPG
HYIGHLLGHE ASGSLLSELK KHGWVNTLTA GPRTAARGFW FFNIDVEVTE LGLRHVDDIA
QLVFEYISLV RNEGVQEWIH RECENLNKIE FRFKDKEQPM NLTTYLASAL QLYPMEDVMF
GPYRMDHYKP ELVYMVLDQL RPDNMLMTVT SKSFCNAVNS AEPWYGTCYR KKPLGKEFLE
RCQGNGGADG SSKFKLPDPN AFIPTDFTLA DCTQPTKLPR LLTGEPGDED PMARVWYKKD
DEFLTPKTVV RLLLRSPLTN SSPGRMVEAH LYSELVFDAL NEHAYNAMLA GLKYSVVSTL
DGMQINVSGY SEKLPVLLSS IVDKMLSLKV EPTTFDRLKE RFIRRLRNFD MEPPYQQSMY
YSTLLLSDRT WSKKELLREA VGLKIEMIDD FKRILFSEMH IEALVFGNAS EQNARDILNQ
TKSAILEKMH PKPLLASQVT RNREVKLQKG KTFVFEAQNT VHPNSAIEII FQVGLQESRL
NMLLELLVQI LNEPCFHQLR TVEQLGYIVF GGLRRANDTQ GLHIIVQSEE SPAYLDERIE
AFLSQLLEDI KNMPSEEFEE HRAALTSKRL EKPKKLVSAA SKCWSEISSE QYNFERDEKE
VNILQTITKE ELIEFYKQHI AADAPKRRKL STQVYSNNFE INSIRTKRSV VEDQGKLEKI
KNLIDFKKNL PLFPRMKPEM EVPQIGVLST EGI
//
