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Database: UniProt
Entry: A0A0N5D9G9_THECL
LinkDB: A0A0N5D9G9_THECL
Original site: A0A0N5D9G9_THECL 
ID   A0A0N5D9G9_THECL        Unreviewed;       707 AA.
AC   A0A0N5D9G9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=ADAM 17-like protease {ECO:0000313|WBParaSite:TCLT_0000977801-mRNA-1};
GN   ORFNames=TCLT_LOCUS9767 {ECO:0000313|EMBL:VDN07423.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000977801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000977801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN07423.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   EMBL; UYYF01004875; VDN07423.1; -; Genomic_DNA.
DR   STRING; 103827.A0A0N5D9G9; -.
DR   WBParaSite; TCLT_0000977801-mRNA-1; TCLT_0000977801-mRNA-1; TCLT_0000977801.
DR   OMA; NTTWNSE; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd14246; ADAM17_MPD; 1.
DR   Gene3D; 4.10.70.30; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR032029; ADAM17_MPD.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR45702:SF6; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 17; 1.
DR   Pfam; PF16698; ADAM17_MPD; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF13574; Reprolysin_2; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   TRANSMEM        654..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..451
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          452..547
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         387
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   707 AA;  79012 MW;  72D4577638192098 CRC64;
     MEVALKTSLS RDDTDLSNRL KYYEIIKINR RLEKRGIVDI NVPYNKQERL IFRAFNRLFD
     IYLTPKKGLL HRNFKCREVD GYGFEKLCTV NPDDHFGGHI HGATDSIVSL TYDDEGSLLG
     IIWVAGDLYI FEPARIHFVI FFQYVMLNKN AQPWEVLAYR NSDLKMKYIT SSNGSFCSAI
     SLGNQNNVSN LKSTRSKRQI LLPPVLKNRC ALRVVADYQF FKTIGNGSQA FSARYLINVI
     DRVNALYTTT DWGIDEDGRR LINMGFMIKE MIIHTSPTVD QPNHYNSVSN VKRSVKAVLD
     NFSRIQGSDK YCLVHLFTAQ SFENGVLGLA YISSPELNAA GGICSVQNRD RLGVVYYNTA
     LSSTKATHGG TVVSREADIV TAHELGHNWG ATHDDMSLEC SPPYGSGGSY IMNTFSVSGY
     DENNNHFSPC SRRLIGKVLS RKADICFEPE MSAFCGNGRV EVSTDGFAEE CDVGGLISET
     VDKCCTSDCR LKPNAICSPK NSPCCSSDCQ FLPSTHLCLH ENRFQCKLSS YCTGNSGECP
     EPGFVEDGTS CIEDGECLNG QCLTFCERPS VNKKPCMCSR EAVACLRCCR SENGTCEPYS
     RDPKYVLKDG TRCIHGTCSR AVCIKEVADV VSHFWNIIEN LDETNFWKFV SDNLVGIIVA
     VVLIVWVPAS VLIHKMDKVY EAAAKEESDN RIEVVGEKSI YKYILNS
//
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