ID A0A090LNY9_STRRB Unreviewed; 378 AA.
AC A0A090LNY9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=SRAE_2000455000 {ECO:0000313|EMBL:CEF69904.1,
GN ECO:0000313|WBParaSite:SRAE_2000455000.1,
GN ECO:0000313|WormBase:SRAE_2000455000};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF69904.1};
RN [1] {ECO:0000313|EMBL:CEF69904.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000455000.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF69904.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000455000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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:PRU01211}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN609529; CEF69904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LNY9; -.
DR STRING; 34506.A0A090LNY9; -.
DR EnsemblMetazoa; SRAE_2000455000.1; SRAE_2000455000.1; WBGene00264782.
DR WBParaSite; SRAE_2000455000.1; SRAE_2000455000.1; WBGene00264782.
DR WormBase; SRAE_2000455000; SRP09483; WBGene00264782; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:SF887; ASTACIN-LIKE METALLOENDOPEPTIDASE; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 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|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:UP000035682};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 22..378
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5015017728"
FT DOMAIN 28..227
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
SQ SEQUENCE 378 AA; 43935 MW; 721B4BE0BBE0CD92 CRC64;
MLNNILILST ILIHYLSLSN AIFTNDDNII RSRRTSNKTN ILYPKVIPYR INVGFESKTI
RNVFSYLQKQ TCLKFVEKNA DSLSLIFKLG QEDRVSNIGA NPNAPTTIQM KYNCTQNEGC
VKHLLGLALG LYLEITRHDR DNYIEVFWGN ITESEKHWIK KVEWKDSWVR NTGFDYGSIM
ASPIKWKSKN GKAIFKSKLS KYYDFMVGQR YEYAFNDIKH INDLYCGNTC KRKVKGCTNG
GYPDPKKCKH CRCPEGFAGK QCTTIRRNKP ICGKRMLRAT REMRELIIEG IKDCFFYIKS
DRHKKIRIIV AEINTPVQRP CFKNMGLEIK YRHNKGATGL CLCGHYRKYS LNPFNSRVLV
HYTGQTENDK LHLKYIVS
//
