ID A0A0K0E7A3_STRER Unreviewed; 380 AA.
AC A0A0K0E7A3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000537900.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000537900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A0K0E7A3; -.
DR STRING; 6248.A0A0K0E7A3; -.
DR WBParaSite; SSTP_0000537900.1; SSTP_0000537900.1; SSTP_0000537900.
DR Proteomes; UP000035681; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF877; ZINC METALLOPROTEINASE NAS-34; 1.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Hydrolase {ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 17..380
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5005120614"
FT DOMAIN 12..228
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 223..263
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 227..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 253..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 380 AA; 44382 MW; DEBC88545272C2D3 CRC64;
MLFIVIIISF LNLIQSNDVK NSKLSYTAIT RRKNIASVYD YKQKVMSTSI KYYVQRLSDG
ENIELALARI SSETCFQFQE TNNLTSATLI YKPGYYYSTN RKEENSNLHI IYLSYSRPEV
SKIIRETLYA LGIDYEHDRP DRNRYITVYS QNIYSTYLIL FKRKIQSIFI KYNLGYDYKS
VMHFSCNEFS KNKKKTIEAK NKLIEPFMGK SEYLTFTDAK AVNLKYCINS SLKNAKCINY
GYPNPKTPYT CKCLPFYCGP HCEHKVRNFG YCSPINRFKA KYSTAFRTLH LGGTCYFFIE
TVPGLKIKLL LFFHHNLLTY RKCNNKEYIE VRYSKDISVS GVIYCPRVKP IIIVSEGPLI
VIRSSYSSSK YKVKIAYKLA
//
