ID A0A1V9WYU3_9ACAR Unreviewed; 499 AA.
AC A0A1V9WYU3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 18-like {ECO:0000313|EMBL:OQR66332.1};
DE Flags: Fragment;
GN ORFNames=BIW11_14233 {ECO:0000313|EMBL:OQR66332.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR66332.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR66332.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR66332.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR66332.1}.
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DR EMBL; MNPL01032908; OQR66332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9WYU3; -.
DR STRING; 418985.A0A1V9WYU3; -.
DR InParanoid; A0A1V9WYU3; -.
DR OrthoDB; 3042901at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF275; STALL, ISOFORM C; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:OQR66332.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 182..397
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT NON_TER 499
FT /evidence="ECO:0000313|EMBL:OQR66332.1"
SQ SEQUENCE 499 AA; 55878 MW; 1FE3807E6FF56906 CRC64;
MVVRVSANLS FYIELEPQID TTLHSRLERV HVLYDNYSEH HQLHDVQRCQ FIGRVISPVN
GIASVNTCPN STEAYAIMIT ERGVFYLKPQ MIEWRGDKDR PHVFTRLGSE RDNQFCGIHT
FKEEVALDDV SHVAPNTTIS SERTAGSDET DIDGSAIHWK TTDENIVMIH SRRKRAAEGG
IKYIETGIFV DRHMFDAVEK TKPPDTVRAI VNIVMAILHQ VQLIYEYQSM KAYDFKLIIV
KFEILRNTRT SPNTAGGNID RYLDSFCAWQ CKKLHSLGSR DRWDHAIMLT GLDMFKMSGN
VKNDKVLGLA WVNGMCRCEY SCTINEGNSA EAAFVIAHEM GHSLGMQHDG SGNSCDSNKY
IMSDRTGAGK VNWSKCSNDY VKQADRKGQY KCLANEAKPA SSAVDIARQA QLPGEEYSAS
QQCQMALSPK HKPYTTASAP FNDVCRELWC LEGQWATPAH PALDGTKCGS GKWCRQGACV
AKNSDSKFEP TTDGPADRP
//
