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Database: UniProt
Entry: A0A1A9WC30_9MUSC
LinkDB: A0A1A9WC30_9MUSC
Original site: A0A1A9WC30_9MUSC 
ID   A0A1A9WC30_9MUSC        Unreviewed;      1527 AA.
AC   A0A1A9WC30;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   05-JUN-2019, entry version 23.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS   Glossina brevipalpis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Hippoboscoidea; Glossinidae; Glossina.
OX   NCBI_TaxID=37001 {ECO:0000313|Proteomes:UP000091820, ECO:0000313|VectorBase:GBRI014021-PA};
RN   [1] {ECO:0000313|Proteomes:UP000091820, ECO:0000313|VectorBase:GBRI014021-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820,
RC   ECO:0000313|VectorBase:GBRI014021-PA};
RA   Saikia M., Chaudhari Y., Khan M., Devi D.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|VectorBase:GBRI014021-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|VectorBase:GBRI014021-PA};
RG   VectorBase;
RL   Submitted (JUL-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   VectorBase; GBRI014021-RA; GBRI014021-PA; GBRI014021.
DR   Proteomes; UP000091820; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UP000091820};
KW   Disulfide bond {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}; Membrane {ECO:0000256|SAM:Phobius};
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973802}.
FT   TRANSMEM     12     33       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      800    916       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      917   1031       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN     1031   1071       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN     1074   1191       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN     1191   1231       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN     1235   1347       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN     1348   1465       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   REGION      125    156       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1A9WC30}.
FT   REGION      379    400       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1A9WC30}.
FT   REGION      513    536       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1A9WC30}.
FT   ACT_SITE    692    692       {ECO:0000256|PIRSR:PIRSR001199-1}.
FT   METAL       691    691       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       695    695       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
FT   METAL       701    701       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001199-2}.
SQ   SEQUENCE   1527 AA;  174609 MW;  93B8730A73EBD314 CRC64;
     MAQTHIRGRN RRYVAIANYA TFTLTAIFVL ISACARSAQV NFNTFSSLPS PYESSLNIKV
     QSTRPQASPD ETFASSLDVP ENALSIHADD KNVSPSKEHI ALESSRTQIV QEPEQFRPDI
     KSYHHSHHSY HSHHQNEPYH GHGVNRTGQQ RRQHRRKNLG SDLWLHHRYY QPQHQHQHHH
     RNHYRDHNMI PQSQHIIRID PVQQLIVPAQ VPKHKYRSKY TIEELLNTKF ERKISDDIDM
     DPCKAGGFMG DIALPETTYD DYPIVAHTTI GKVLETSPSR EAIIKFNDTF QKEMEILKQE
     VYHEGLQVEE EGLTDIIRRK TKLPSIKPEL NTDFLSNANE LVKPFHYHQS RESYNYMDKN
     HKNDVISSEG FLNQIKRNPS AGREEHTTVN AKEDDEETDK EDFKKIYHHT PGKKFSFPTE
     KTYIYSPPEK VNKPPVGLSN RNVDQRKIQS NTKDIELDAN NNFVSERKFV ILPTASPTQR
     TTLPNVYSNA GGNGMKMDDI QEFKGSSTIV RRKHRRRRKN ELNPPVQKHP TIDHHHHHQQ
     LMAKENNHQI VDIQSNEVFV KHLLHVDNHS EPLAVFPSRD NDDEFSLISE RRRSIRAVTA
     KKERIWDYGV IPYEIDGNFS GLHKALFKQA MRHWENFTCI KFVERDTELH PNYIVFTIRG
     CGCCSFVGKR GNGPQAISIG RNCDKFGIVV HELGHVVGFW HEHTRPDREK HVIIDHINIM
     KGQDYNFNKL TPDEVDSLGM AYDYDSIMHY ARNTFSKGTY LDTILPIEIK GKKRPEIGQR
     LRLSSGDIAQ ANLLYKCPKC GRTFQENTGL FASPSYYTGG ALTNETEHCE WRITATHGER
     VILRIENLNI FKSEHCQSDY LEIRDGYYHK SPLIARFCGK VSNEALKTET SRMLLTYVNA
     HRTNGFRGFK AEFEVICGGE ITIDENEGRL ESPNYPLDYL PNKECVWKIT APKGYQVALK
     FQSFEVENHD SCVYDFVEVR DGPTQDSPLI GVFCGYKPPP NMKSSGDVMY MKFVSDTSVQ
     KPGFSATFMK EVDECETKNH GCEHECINTL GGYECNCRIG YELHSDKKHC EDACGGVIEY
     PNGTITSPSF PDNYPILKDC IWEIIAPPKH KISLNFTHFD LEGAAHHQSE CGYDKVTIYS
     KLSENRLKRI GTFCGSSMPP AATSEGNALR IEFHSDKSIQ STGFAAVFFT DVDECSVNNG
     GCQHECRNTI GSYICSCHNG YSLHENGHDC KEGECKHEIS APFGTIYSPN YPDSYPPNAD
     CVWHFLTTPG HRIKLIFNEF KLESHQECAY DNVAIYDGDS ESSSILGRFC GDKIPYPISS
     STNQLYMVLK TDKNKQHNGF TAVHSTSCGG YLRATNQIQQ FYSHARYGNQ PYDANMDCEW
     LIQAPPSSNV QLIFLTFDLE TSENCTYDYV QVFSGMEDTS GPMYGQYCTN TLPQDIISIT
     DSLLVRFKTD GSITMKGFSA SYVAVDPFEN SEEDPTSYSS EMVTPFPGSL KSIYKEDGSH
     ETDDYNDFNE NQLIVNNPYL KRYRREN
//
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