ID A0A183DQ65_9BILA Unreviewed; 627 AA.
AC A0A183DQ65;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 19 {ECO:0000313|WBParaSite:GPUH_0001086901-mRNA-1};
GN ORFNames=GPUH_LOCUS10856 {ECO:0000313|EMBL:VDN18003.1};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001086901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0001086901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN18003.1, ECO:0000313|Proteomes:UP000271098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; UYRT01078195; VDN18003.1; -; Genomic_DNA.
DR WBParaSite; GPUH_0001086901-mRNA-1; GPUH_0001086901-mRNA-1; GPUH_0001086901.
DR Proteomes; UP000050760; Unplaced.
DR Proteomes; UP000271098; 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; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
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:SF159; MIND-MELD, ISOFORM J; 1.
DR Pfam; PF08516; ADAM_CR; 2.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 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.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000271098};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 419..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..89
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 95..171
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 369..402
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 496..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 28
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 44..68
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 46..51
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 143..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 392..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 627 AA; 67709 MW; CD3557155BD72D2B CRC64;
MCSYDFSGGV DMEHSKQAAY VAATVAHEMG HNFGMEHDIS ESECRCPASE CIMSPATGIT
PPTFWSECSM RALQHSLSRG MDYCLRNPPD KAFGGARCGN GISACINKCC NPATCQLAEG
AVCASGECCD LKTCQMLAAT TVCRHATNEC DLPEYCDGQM EHCPADFYVQ DGHSCPDHPD
DYCYNGFCGS RDAQCQYIWG PTGSNAAPAC YDLNLYGSSG GNCGFDYCYN GFCGSRDAQC
QYIWGPTGSN AAPACYDLNL YGSSGGNCGF VHESSRFLPC DRKDVKCGRL HCIHENEKLA
FGDPSTVYTA YTGLQLRSGE EVACRVVWTK YIGRKNERDP GMVPDGAYCG KDEMCVDAKC
QNRTAKVLMA PKCDPPSCNN AGICNNMGNC HCEPGYGGPS CAIPGPGGSV NSGPAVEGGV
IHVGFVVFWL LLVLTIAFIG ASIIVKRKKD FWLHKQIWKK LKKALKIEKL LVPIRKAPPP
PGPPPIRTAE LNAIWGDTPS DASRTTRHQQ SVPPSFSPPV VPCSNFAPFP SKPSIVHSNS
MRPTAPPPQV PQRPRSDVLQ ALYAEKGDEL GINSVKQESP MYCVPPESAA AVKIGRAESF
RPVQAPPPPP HSSEVLLKLP LKFEFLI
//
