GenomeNet

Database: UniProt
Entry: A0A182GAD1_AEDAL
LinkDB: A0A182GAD1_AEDAL
Original site: A0A182GAD1_AEDAL 
ID   A0A182GAD1_AEDAL        Unreviewed;       264 AA.
AC   A0A182GAD1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   ORFNames=RP20_CCG006292 {ECO:0000313|EMBL:KXJ83417.1};
OS   Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7160 {ECO:0000313|EMBL:KXJ83417.1};
RN   [1] {ECO:0000313|EMBL:KXJ83417.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ83417.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ83417.1};
RX   PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA   Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA   Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA   Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA   Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA   Yan G., Tu Z.J., Fang X., James A.A.;
RT   "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT   insights into its biology, genetics, and evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN   [2] {ECO:0000313|EMBL:KXJ83417.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ83417.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ83417.1};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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DR   EMBL; KQ560270; KXJ83417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A182GAD1; -.
DR   VEuPathDB; VectorBase:AALC636_009568; -.
DR   VEuPathDB; VectorBase:AALF006292; -.
DR   VEuPathDB; VectorBase:AALFPA_073962; -.
DR   Proteomes; UP000249989; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF879; METALLOENDOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249989};
KW   Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           28..264
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5039777183"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   264 AA;  29202 MW;  8D04CBC2D421B3CB CRC64;
     MRNRTQGKKL AFLLWFVPLL LAGVTDGAPL DVEVQPADVA AEEAGGHFQG DIILDSNQEE
     ILSTGRSALI GASYRWPSQI VYYYITPGHF TTSQQNSIIA ALDELMANSC VKFVARTTQT
     DYVRVTGEYS GCWSYLGHVG GAQQLNLQPN GCMSKGTIMH EFLHALGFVH MQSSSDRDFY
     VKINWGAIQG GKESNFYRYD STVINDLGVP YDYNSVMHYR ADAFTSNGDA TIIPIESGVT
     IGQRVGLSYK DIKRLNLLYP TCNN
//
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