ID A0A0K0EJH1_STRER Unreviewed; 396 AA.
AC A0A0K0EJH1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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_0000961700.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000961700.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|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:PRU01211}.
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DR AlphaFoldDB; A0A0K0EJH1; -.
DR WBParaSite; SSTP_0000961700.1; SSTP_0000961700.1; SSTP_0000961700.
DR Proteomes; UP000035681; Unassembled WGS sequence.
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 Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 21..396
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5005120712"
FT DOMAIN 31..238
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="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|PROSITE-ProRule:PRU01211"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 396 AA; 46507 MW; 419BC9C49FD34FEE CRC64;
MKYLVTYFII FNVILNYVES VKLNSKFFEK NSILLRKRRA TYLEGRGKFN EFPIKYKIDK
NVRRKLVKDA IALVEKETCV KFKEDKRLNG SGLIFILSHD HYYAEYVGKV SSIRPLKIGI
AKKPVRVGFA VHEILHALGL FHEHERLDRE KYIEIKFDNI QEKYHDQFKL ANPITKETFG
IKYDYGSMLH YEREAGHKED TDSNITITTH NKHYFYSIGQ RTDISFLDGK LLNKRYCNDK
CKDKPKLHCY YGGYPNPKKC DECKCPTFYE PPFCKFVKKS HEKCGKKIRM ATEKEQVLKM
KGKYDCYYII RAKKNQIVEM KIKKLRSFLK PICQPGSGLN IKFLKNKAIS PACFCGKVTN
YKIESEGREV VLRFAGKSKC NYFVLTYKSV EKFVSV
//