ID A0A158Q3X9_DRAME Unreviewed; 874 AA.
AC A0A158Q3X9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
GN ORFNames=DME_LOCUS290 {ECO:0000313|EMBL:VDN50317.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000342401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000342401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN50317.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81;
CC Evidence={ECO:0000256|ARBA:ARBA00001809};
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; UYYG01000002; VDN50317.1; -; Genomic_DNA.
DR STRING; 318479.A0A158Q3X9; -.
DR WBParaSite; DME_0000342401-mRNA-1; DME_0000342401-mRNA-1; DME_0000342401.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; 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 Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR049038; ADAM10_Cys-rich.
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:SF2; KUZBANIAN, ISOFORM A; 1.
DR Pfam; PF21299; ADAM10_Cys-rich; 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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756};
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 724..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..474
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 498..597
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 773..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 874 AA; 97700 MW; 0619D83F0FE727CA CRC64;
MNKFLNSYET LNYEPIKHRL KRSADGSIVA TNIRFNTHNR SFDLILYSIN NDPSPVFDSQ
IMFDVDGIPV DFRPDEYLLH GIDKNNRGSA VYGSIQDGIL DGLIYHNDGH VFTIVRANQF
FPVNERPLHF HSIVYSDDSI NFWKSRKKRS AKDKHGCGLH GRVRKDMEAF QKSVILDNDP
VVSSSFKVHH PIQDSFPYRY FMDSQRTKRD VPETKIINGK QIYTVRACYV YLQADHKLYQ
HIFEKEGNFD EVRTREEIAS LFYNHIKAVN QIYEDTDFNG INGVTFVIQR ISLYTPQTCS
GKTDGISENP FCEDNVDVSN FLNLNSRKNH SDFCLAYAFT FRDFVGGTLG LAWVASQNHN
TAGGICQQYT KYSEGTNFVY RSLNTGIITL VNYGNRVPNR VSQLTLAHEI GHNFGSPHDY
PLECQPGLPD GNYIMFASAT SGDKKNNAQF SKCSIANISI VLSEVLQQRP IDTENSYLRL
GGFGIGAGKR NCFRETKSAF CGNQVKEPGE ECDCGYTAAD CETMNDKCCH SRDTGSGCKR
RSKATCSPSE GPCCNAQECA FHPSSAKKIC RAVSECLEEQ RCDGRTAECP PSKAKKNGLP
CQDSTKVCNA GSCNGSVCAE IGLKDCFLTK GTPEILCHLA CEEKGVCKSS FELPHFANGR
FNQISRENKQ GLILLPGSPC NNYKGYCDIF RKCRSVDADG PLARLKNVIF NPKTLSEVRY
WIQINWWIVL LCGIGILIFM AAFIKCCAVH TPSTNPNKAP ALNIYDTLRR PKTFIQGQRR
TRSQTRVNGG PMHASRGRHG THTDRTSSQA FHNVPSAPPP PSAPPPSSII VVEPPPPYTA
STDPASALGG PKRGRRKQKA LNNNEIRGRK NRRK
//
