ID   A0A1I8D032_9BILA        Unreviewed;       632 AA.
AC   A0A1I8D032;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Disintegrin domain-containing protein {ECO:0000313|WBParaSite:RSKR_0000999000.1};
OS   Rhabditophanes sp. KR3021.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC   Rhabditophanes.
OX   NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000999000.1};
RN   [1] {ECO:0000313|WBParaSite:RSKR_0000999000.1}
RP   IDENTIFICATION.
RC   STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000999000.1};
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   AlphaFoldDB; A0A1I8D032; -.
DR   WBParaSite; RSKR_0000999000.1; RSKR_0000999000.1; RSKR_0000999000.
DR   Proteomes; UP000095286; Unplaced.
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; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF248; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN UNC-71; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01421; Reprolysin; 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   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00068}.
FT   DOMAIN          1..186
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          192..281
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   REGION          562..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        253..273
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   632 AA;  70466 MW;  A54F6E42DEF5A280 CRC64;
     MLNLSMTESI RYALDVINTA DLILARNLNV RLSIVYGEWW TDVERIDVNE DIEKTLSGVL
     DYTTGHIYNV KKDNTVFLTG SAFSHKEQAS STFASICTAR ALSLVKAIDR RQVFETSQLL
     AQSIGHNFGI DHDSLDCTCD NSNKCVMSKE AGSNGTPFIY GFSKCSQGRM HSALRSGELQ
     CLLNKPFHTS ELHHCGNGIV EGNEECDCGS KSREECTDPC CDPITCTLRA HAQCASHQSC
     CHRCELRKTG HICRTSRSPC DVIEICDGIS ADCPADGYLI DGTNCDIDGK CWKGDRCIKK
     DEYFSKKVCI DGSCLPLTKA SPPVYCPSNN LALQCSGNKK VYDALNRISE VIDERDTNSM
     KSRESEHISV HNESSSIYGV GHNRQLPSRG NYVMCDDGTR IRHELSGSQR SLLRMNEPTL
     ALHPNNIFDD TAERFYSQYD RGIRNSPCKS DYGGYTSKMK REPRSDLGYS TRNYEQPYEG
     IGNLYNDNDL ACYSSRYSIQ QPPYLPQSYK NISTMSPSSS SYTGSISKLK HTPLKLNNIQ
     TLLKQLDDND SACLDIRNMD TEESELSNGE HHQDRNSHPD SIPSADLGYS SNATYPCRET
     FSIAGNSDDG DTFPGRPSFL SERLKVDIPD QF
//