ID A0A074ZQH8_9TREM Unreviewed; 1066 AA.
AC A0A074ZQH8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Disintegrin {ECO:0008006|Google:ProtNLM};
GN ORFNames=T265_06992 {ECO:0000313|EMBL:KER25590.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER25590.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER25590.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) 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; KL596772; KER25590.1; -; Genomic_DNA.
DR RefSeq; XP_009170673.1; XM_009172409.1.
DR AlphaFoldDB; A0A074ZQH8; -.
DR STRING; 6198.A0A074ZQH8; -.
DR GeneID; 20321171; -.
DR KEGG; ovi:T265_06992; -.
DR CTD; 20321171; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000054324; 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 CDD; cd04269; ZnMc_adamalysin_II_like; 1.
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 InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR Pfam; PF08516; ADAM_CR; 1.
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; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; 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:UP000054324};
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 691..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..289
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 344..447
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 638..668
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 924..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 204..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 419..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 658..667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1066 AA; 118741 MW; C23D2B1FFFC561CE CRC64;
MQTNLSRSSS SVWSVQDAAD THGLREKPAI TTSKRRIPRH VPQQAEALLA DTESTTGESC
EDLQAKNLFT IILLDFSQKV EPMPILHRPD QPPPRILELY MVVDEALVNL FNRDYDMLIF
RVNSLISHVN ALYAPFNIAI VVVRLELWMQ DRDRLNIEEH HILPTLAQFK RMHTTVRHDC
LHALLGERKE GSPNKGKANS HTMCVFSRCV GYTRDSPSSD ILETARTMAH ELGHNFGLRH
DTEECKCQSC IMATGVEFGT NLMAWSPCSV RDLSVLLDYG MGVCLHDTPV HTVVAISAYN
QPRNLTVSSA VRVYDWTTQS SSEVRPPALS PRYRHSSRRS TATDRLCGNG VLDPGEECDC
GTRESCPIQL QDCCDAQRCR LKPGSECAGG PCCKIQRVPA TRSTLERFQC RLAPAGTVCR
NESGNCDLPE YCDGLSGWCP LDVFKADGIP CWTEEGTESY CARGGCREAD SWCRVLWGKR
GRRAHPYCFD ENHGIPKGVP VDPVANCGKR KPLSEERWED PKSWPGIRCP SVQDAECGRL
WCHHQNEKAM ILGWIESQTR YLSSVEQSCS ALVYDPVWPA SDPSTWDASK KRQMNLNVAG
VGLLSAVTQD AGMVPDGTPC SRGMCYNGSC VPHSEIRARF QCDCRGHGIC NNLGHCHCDP
GFHPPVCEFG GDGGSVDSGP PPSDLIPKPS LVIGISLLVF FGLPLVVFTV YCAIYHRCRW
IPIGADPMIP TKSGLRTPFD RGLLPCIRQC CRRAGNKPRG VSYIAGDASY PAIHRNAHQP
SSLHVRSNRR SNGDKLIRVV VNPVQNGTIT SVSNNDLKSN GLKVTKMQNR RYQPPPMAPK
PLGLITVNGY KSNCNAFTAP ERPMNWTDHN EQNPMFSSRA NHELDNCNGY VKKSDCARTN
LHCSGNAQKP ITGLLQQRSI QIIEGKPKSR NNDAVPSPIS HDSESKDRQT IDISEPHLKD
MTYRGPICSL SEALNTLRRG DQVSSIEPSQ VAKKQRRVVR RPSRLKTLDY GSLLKKPSFR
RTQSQHREPS MSQVQPRWDI SAPRLESTTY TESLNDLDTA RMLISR
//
