ID A0A0N5C4E9_STREA Unreviewed; 914 AA.
AC A0A0N5C4E9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001283000.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001283000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR AlphaFoldDB; A0A0N5C4E9; -.
DR STRING; 174720.A0A0N5C4E9; -.
DR WBParaSite; SPAL_0001283000.1; SPAL_0001283000.1; SPAL_0001283000.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 4.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF31; CUB DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 4.
DR Pfam; PF14670; FXa_inhibition; 2.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 4.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 4.
DR PROSITE; PS01186; EGF_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 40..243
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 355..467
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 510..627
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 671..786
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 787..910
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 137
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 106..128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 108..109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 914 AA; 105061 MW; A70E292B2A7A86BB CRC64;
MLLIYKWNFI VIIFLCNNIY SKIINDIFKN NNFLNRQKRG ATADRSRLWP NGLIPYEIDE
TFSGQHYRLF KMAMRLWMNL TCLTFIPKAD GSLITKDYIY FTADECGCCS YVGKHMDGKQ
IISIGRKCDK FGIVLHEIGH TIGFWHEHTR EDRDKYVDIF YSSIKDDQEY NFDKSKPGEV
DSLGETYDYE SIMHYSRNTF SRSIYLDTIL PKHNINGKKP EIGQRTHLSV GDIRQTNKLY
QCETCFKTFY ERKGVISIKN EKKCIFRILG AQGEKIKLKV FGRNITKMGG DRRKSEKLLI
IRDGFHDRSK ILTIIKTDNF NDVEFVSKSN FMYIQFKNTL QIEDELTIGE YKFLCGGKLK
EKKGFIESPN FPEVYPYNIT CQWEIEVSKG MLVAVKILYI EIEKSGDCMY DNIEFYEEPG
NELLSKTCGS HNEITSVVTK ESNKMKIIFK SDSSNNKNGF LLQYLTEENE CKKRNDLCEH
ICINEIGSYS CQCHPGFSLG KDKHSCYNKC GGHLKNLTGA ILSPNYPNQY PPNTECTWDI
VLKDDFQIFL NFSFVSLEGV ITDCSYDSIL VYELDNNMSV NYSSTLQICG YHTEPILMKS
TGNKIRIKFQ SDSSVEKFGF IASYIGFHDE CLSSNGGCEQ ICESNINSYK CKCLDGFTLS
DDGYSCLEDV CSFQLFDSKG SLASPNYPEG YPDDKVCKWH FITTPGHTIE LTFHEFDLEE
SPNCSYDNVS VYNSYESSND ELLGLFCYKN RSSEFSISSN GNQMFLIMKT DSSIMHSGFK
ASYHSNCGGT LFVDNEIGYV YSHDKYGEGN YYSNSHCEWR LTMKDDSLIK DNIIKIKFVK
FNLESSDNCS CDSVQILEHN NIDEDGKVID KFCGNKLPPI ILSRRQIVTV IFTSDESMEG
KGFVFEYELS KVVA
//
