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Database: UniProt
Entry: A0A182QG59_9DIPT
LinkDB: A0A182QG59_9DIPT
Original site: A0A182QG59_9DIPT 
ID   A0A182QG59_9DIPT        Unreviewed;      1572 AA.
AC   A0A182QG59;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   05-JUN-2019, entry version 25.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|Proteomes:UP000075886, ECO:0000313|VectorBase:AFAF009500-PA};
RN   [1] {ECO:0000313|Proteomes:UP000075886, ECO:0000313|VectorBase:AFAF009500-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886,
RC   ECO:0000313|VectorBase:AFAF009500-PA};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|VectorBase:AFAF009500-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|VectorBase:AFAF009500-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001199-2,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001199-
CC       2, ECO:0000256|RuleBase:RU361183};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   EMBL; AXCN02001184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   VectorBase; AFAF009500-RA; AFAF009500-PA; AFAF009500.
DR   Proteomes; UP000075886; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00041; CUB; 5.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 5.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR015446; BMP_1/tolloid-like.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR034036; ZnMP_TLD/BMP1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 5.
DR   PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 5.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 5.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01180; CUB; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000075886};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00059,
KW   ECO:0000256|SAAS:SAAS00601599};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00438935};
KW   Hydrolase {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973787};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001199-2,
KW   ECO:0000256|RuleBase:RU361183, ECO:0000256|SAAS:SAAS00973795};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS01068076};
KW   Protease {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973825};
KW   Repeat {ECO:0000256|SAAS:SAAS00792548};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973802}.
FT   DOMAIN      832    948       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      949   1062       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN     1062   1102       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN     1105   1223       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN     1223   1263       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN     1267   1379       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN     1380   1497       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   REGION      167    248       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   REGION      285    414       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   REGION      432    599       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    168    208       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    285    330       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    361    376       Basic. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    377    413       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    435    459       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    460    476       Basic. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    477    495       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    531    547       Basic. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   COMPBIAS    548    574       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A182QG59}.
FT   ACT_SITE    724    724       {ECO:0000256|PIRSR:PIRSR001199-1}.
FT   METAL       723    723       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       727    727       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       733    733       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   DISULFID    949    976       {ECO:0000256|PROSITE-ProRule:PRU00059}.
SQ   SEQUENCE   1572 AA;  177917 MW;  502BD8CAFADAF73F CRC64;
     MEPAEQMMIR PTVCCRNLRR ASHRQQPVSD LVRHHKPYRP AARTVAWRWM PIVMVIAVFI
     NQLTEGLELN ETLITLKHRH HGFTIDELLD ARFPKSISGD IDMDPCKSSG FMGDIAMPNV
     NYETEWQRQR MNKSLEQDIV KLKQEVYLEG LQVEEEGMTD MIRKKTKQRA STPLSGMTPG
     GQYARTPSGT SYESENSITD SSGEPTVRAT IIDNRDNIIA PREAIGDSLS DRKAATPNKK
     NATGPVRNID HNRIQSDTKD IVIDSVSDNI ISSNHASRKV VSFTLPTKPP STLRTTLTAS
     STTRASAAVR RNDGDSLETA SSNENVVTST SKPKVRERQD QANEQDIQPV TNGNREQVVE
     KARRRHHRRR RQQHHSSLQH PQPLEGITTN GDSTAKTASG KPLPNGTVNK NSYHSRLERL
     RVELGTVTYS VRDRNLRSSH QHQHQDRGED DPVERRSQNR TPKKKQRRRT AGGDSKRKHH
     QHVITNDHGN NNEQRAKDTG VDMGSFGLNK ASGERMWEAS GADRQSYHPR AQHQPQHHHH
     HPDHHRHHPE QPPRTRSTRI EQNDENDDAM NLHFRPDLKI PTPVSRDPPL PRLPVEDADN
     VDDDAESHIH YASDHQHHDE HDHHRSARAA TAKKERIWDF GVIPYEIDGN FSGIHKALFR
     QAMRHWENYT CIKFVERNPI DHPNYIVFTE RACGCCSFVG KRGNGPQAIS IGKNCDKFGI
     VVHELGHVVG FWHEHTRPDR ENHVVIEKNN IVVGQEYNFN KLTEDEVNSL GLPYDYDSIM
     HYARNTFSKG TYLDTIFPIE VPGRKRPEIG QRLRLSEGDI AQANLLYKCA KCGRTFQENS
     ASFTSPTYYS TTPPSEPERC EWRITATHGE RIVLNITDLD IYKSNSCRSD YLEIRDGYWH
     KSPILGKFCG SGKVNELIRS TGSRMLLTYT TTFRQASMRG FAANYEAICG GDMNLESGGR
     LESPNYPVDY LPNKECIWRI TVPKDYQVAL KFQSFEVENH DNCIYDYVEV RDGGAADSRL
     IGVFCGYKIP PDMKSTSNKL FVKFVSDGSV QKAGFSATFM KEVDECEHMD HGCEHECINT
     LGGYECACYI GYELHSDKKS CENACGGQLD TPNGTILSPS FPKEYPIMKE CVWEIVALPQ
     HKITLNFTHF DLEGNTFYQA SECEYDFVAV LSKSPDGTLH KHGSFCGYNI PAPITSEWNI
     LRVIFKSDKT IQKTGFAAVY FTDIDECAVN NGGCQQECKN TVGSYVCSCR NGYTLHDNGH
     DCKESGCKHE IFTPNGQILS PNYPDYYPPK KDCIWHFTTT PGHRIRLVFN VFDIEPHQEC
     AYDHIVIYDG NSPDSHTLGR FCGAKLPHPI SSSSNQMYMV FNTDTSVQRK GFFASHSTAC
     GGRLKATEVK NHFYSHIKFG SGMYDNGADC EWTIVADSGQ NVQLKFLSFE LEEEKMCSYD
     YVEVYGGLDD ESGPLHGKYC GNANPPEIIS MHEALMVRFR SDDTVGFKGF SAAYVAFKSN
     LDVLTTDEEG SDSSDIIPFP GSLKTVFIKQ GEDMDEEEED DDIDYEIYPN RPTNSKVHIA
     VHNEIRSSQA ID
//
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