ID A0A090LLC4_STRRB Unreviewed; 484 AA.
AC A0A090LLC4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Zinc metalloproteinase {ECO:0000256|PIRNR:PIRNR036365};
GN ORFNames=SRAE_2000523900 {ECO:0000313|EMBL:CEF70614.1,
GN ECO:0000313|WBParaSite:SRAE_2000523900.1,
GN ECO:0000313|WormBase:SRAE_2000523900};
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:CEF70614.1};
RN [1] {ECO:0000313|EMBL:CEF70614.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000523900.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF70614.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000523900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR036365}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; LN609529; CEF70614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LLC4; -.
DR EnsemblMetazoa; SRAE_2000523900.1; SRAE_2000523900.1; WBGene00265499.
DR WBParaSite; SRAE_2000523900.1; SRAE_2000523900.1; WBGene00265499.
DR WormBase; SRAE_2000523900; SRP09241; WBGene00265499; -.
DR OMA; SAICRNG; -.
DR OrthoDB; 359054at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR017050; Metallopeptidase_nem.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF888; ZINC METALLOPROTEINASE NAS-38; 1.
DR Pfam; PF01400; Astacin; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000035682};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036365};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 134..329
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 373..484
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 173..328
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 484 AA; 55812 MW; F565F976701DD099 CRC64;
MIEKFILFNA FFTVFKILYL INGNTLDYFT NAEHTARAMR VMADMHRRLR RQSAIRMPNA
VNQKKPFDPK LMWKKAVMKV RIINVMKNPS LYQGDVMLTK QQALHLVEKT RQHLAKKGIR
YPIFSFANST RIKRKVAGGN FHKWSMPIHY FIEQGVNVNN VEMGLRDLQM RTCLRFKRVG
HPIPGSPGLH YFFGQGCVSY IGKIDNTKFQ QISLGSDCNS VSIAQHETLH AMGLFHEQSR
IDRDKYIYIV TQNIIPKHLH NFDIVDKDDS NSYGLPYDYT SIMHYPINLF GINDQQTTSP
KDKTYTFSIG TQEQPTFIDT QTVNIHYCSN ICRQKIFCDN WGYQDPNDCS KCICPPGFSG
RDCGWIGVSP PECGQTIFEA TNKVQGINVN GRKKCYFMIT SPEGTKIAYK ITEHIISPFY
LDSCTYQNSV EIKFWEDKSV SGARYCKTAM NLPLISHYHQ LIVIYRSNET TNYAVIAFKA
VTKF
//
