ID   A0A3Q0KGP4_SCHMA        Unreviewed;      1120 AA.
AC   A0A3Q0KGP4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Nardilysin (M16 family) {ECO:0000313|WBParaSite:Smp_061510.1};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_061510.1};
RN   [1] {ECO:0000313|Proteomes:UP000008854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [2] {ECO:0000313|WBParaSite:Smp_061510.1}
RP   IDENTIFICATION.
RC   STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_061510.1};
RG   WormBaseParasite;
RL   Submitted (DEC-2018) 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; A0A3Q0KGP4; -.
DR   STRING; 6183.A0A3Q0KGP4; -.
DR   EnsemblMetazoa; Smp_061510.1; Smp_061510.1; Smp_061510.
DR   WBParaSite; Smp_061510.1; Smp_061510.1; Smp_061510.
DR   InParanoid; A0A3Q0KGP4; -.
DR   Proteomes; UP000008854; 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:UP000008854};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          75..189
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          234..380
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          453..747
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          751..876
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          39..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1120 AA;  128375 MW;  9EA7ADC5778F64EF CRC64;
     MNCDGFAELE KSRIDYRSYR YIELDNGLRA ILVSNLKPGE EAPDDSLPDS DLESNSSESL
     EDEDVDIEEN AIGDQEAKSA AALCIKVGSF SDPIEAQGLS HFLEHMVFMG SLKYPTENDF
     DAYLSQRGGT NNAWTGNEYT LFHFDVKRKH FASCLDKFAN FFISPLLSKD STDREINAVN
     NEFELAYTKD SSRLHYLIGH LSRKDSPYKL FGYGNCKSLR EIPEQNGTDI YSLLNKHRKN
     FYSSERMTLA VQSKHHLDDL EVLVRKIFSD IPKIGLPVTN LQCVEPFDVN SFAKLYKVYP
     LSVKEKLRIV WILPPLINHY ESSPMEVLSS LIGHEGRGSV LALLKKENLA VSLSAGVTCT
     SDFDNSSLCT IFTVNIQLTD YGRDHIFQVC GILFDYIKIL LHSALTSTSI CLMNGGLEGN
     NNDNGERVHT NHCHKHTFAT YLPEYQMVKT ANFLYTEPEE AEDTVVNLAN MLHLVKCEHV
     YSGYRLLKKP NIELYIELLR LMTPNRAAIF FLSSTFASSV KDDESRLEHE PWFNVAYQKE
     DIPEDIMNGW IHSKPDDEQL HLPYENKFLT TDFSLLDSKT DMKQPVDLNL EPGAESRLKY
     GHLWFQQSTR FKCPKASVMI HLWSDIVSKT KENMALHTLM VYGLNQSLST ITYEAGEADL
     VQDVAFRDNG LRICISGFSE KLFYFYSTIL DHILDQTQDL SKEYFESYRD AVLQIYYNEA
     LKPNVLNTHL QFYLLRKEAY LITDILSALK NLSVADLAAY KQKFLSTLHI TIYAYGNITR
     QDAISFFDYT VEKIQPIPRS TRKLIDTSIL DPGTYYLRVM NCNPNDVNMC LARIHLLGES
     DIKQQCYNKL LAFILSEPAF DYLRTKETLG YTVYLRYWRS SPGGTLHSGI SLVAYSPANK
     YSIDYVAGRL TAFWRRIAPR IIAAMPSETF KTSVESLISV HQLEDPNMMT EFERNWDEIM
     ESTANFNYRE ECVKILSTIT QESLLNFFLT EYLDVKKQRS LFVQVDVIAN PELTTTTVSN
     SYCLDFNTIN TNLETLKNEY ISINSIDIGN ALMTCGYDEK EAMKFMMKSY SNTNNNSNTI
     DDNLLLEHEE NESDEQKTMI FINNLFKFRS TIQYQTGRNV
//