ID A0A0L0C6T7_LUCCU Unreviewed; 1664 AA.
AC A0A0L0C6T7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Flags: Fragment;
GN ORFNames=FF38_06122 {ECO:0000313|EMBL:KNC27951.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC27951.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC27951.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC27951.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC27951.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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:PRU00076}.
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:KNC27951.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRES01000835; KNC27951.1; -; Genomic_DNA.
DR STRING; 7375.A0A0L0C6T7; -.
DR EnsemblMetazoa; KNC27951; KNC27951; FF38_06122.
DR OMA; NGFTAMH; -.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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 PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF34; CUB AND SUSHI DOMAIN-CONTAINING PROTEIN 3 ISOFORM X1; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF14670; FXa_inhibition; 2.
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; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5.
DR PROSITE; PS51864; ASTACIN; 1.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000037069};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT TRANSMEM 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 731..933
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 935..1051
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1052..1166
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1166..1206
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1209..1326
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1326..1366
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1370..1482
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1483..1600
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 83..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..247
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..625
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 827
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 830
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 836
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 796..818
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 798..799
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KNC27951.1"
SQ SEQUENCE 1664 AA; 189438 MW; 13960AD7E42E2152 CRC64;
VFFSNNIMEK LKFQKYSLRR KQRRRHTNLR NYAAFIITTI FVVVTASCVK SAHLNVNTNT
ASVTAAAATL EPAFVPLTAG TSSLSSSSSS SSSSSLPSDT SLTSVQKLQH LSPDEEEEAE
AAEEAVEIEL QETSLYNLPV VRELKLVTAS SSTTTTMNAL NTAIDTDANN RTNSHNTNAQ
DINSITADSR RNIPTHSENN FSLQENILQQ QKQQVQHTRH PQHQHQHFDH HQHQQQHQHH
HQQHQSHYCN QHQHLSPTSQ HHQHYQHSHN NENNNMQNNY DFIKVNDDAG GDHQQLKQNS
PFPAIISADE YYSQIPWHKH HSKYSIEDLL STKFEKKISN DIDMDPCKAG GFMGDIALPD
VEYDAEGYPV VASTQAWEEL PQGDAPIKEP VLKYNETFQK EMEILKQEVY HEGLQVEEEG
LTDIIRRKTK LPSNKPDLDN DLMQSANELI KPSSNYPSIN LKNEVISSEE QTLSARKYPI
MLETKKHLPI DQNTPDKGAL DKIFNTSGEK FDFNILAKEK SQSEEEKYNK SSIGLGNRNV
DQRKIQSNTK DIELDTGNNF VSERKVVILP TSLPSQRSTL PNVYSNAGGN GMKLDEIQEI
KGSSTIVKRR HRRGRKHRRS YGHHHRAEYN SKLEKLKEEL NRPVGRSRQI KKQQQQNHHH
HIETHAFNNE KFNNISHMEN ETANNEMRYS KVSENFNDED YDKPLDIVPA YEAEQEEDEF
SFVREHRRLP RAVTAKKERV WDFGVIPYEI DGNFSGLHKA LFKQAMRHWE NSTCIKFVER
EPENHPNYIV FTIRGCGCCS FVGKRGNGPQ AISIGRNCDK FGIVVHELGH VVGFWHEHTR
PDRGNHVIIE HNNIMKGQDY NFNKLTPDEV DSLGMAYDYD SIMHYARNTF SKGTYLDTIL
PIEVKGKKRP EIGQRLRLSA GDIAQANLLY RCPKCGRTFQ ENTGIFASPS YYTAGALTNE
TEHCEWRITA THGERVVLKL ENLNIFKSLN CQSDYLEVRD GYWHKSPLIA RFCGKVNSEI
LTTVSSRMLL TYVNTHRTEG HRGFKAEFEV VCGGELSIDD NEGRLESPNY PLDYLPNKEC
VWKITVPKGY QVALKFQSFE VENHDSCVYD FVEVRDGPTQ ESPLIGVFCG YKPPPNMKST
GDTMYVKFVS DTSVQKPGFS ATFMKEVDEC ETQNHGCEHE CINTLGGYEC SCHIGYELHS
DKKHCEDACG GVIEYPNGTI TSPSFPDTYP VLKDCIWEII AQPKHKISLN FTHFDLEGAT
HHQSECGYDK VTIYSKMSEN RLKKIGTYCG SSIPPTATSE GNALRVEFHS DKSIQRSGFA
AVFFTDIDEC SINNGGCQHE CRNTIGSYIC SCHNGYSLHE NGHDCKEGEC KHEISAPFGT
IYSPNYPDLY PPNADCVWHF STTPGHRIKL IFNEFKVEPH QECSYDNVAI YDGDSESSSL
LGRFCGEKIP YPISSSTNQL YMVLKTDKNK QHSGFTAVHS TSCGGYLRAT NQVQQFYSHS
RFGNHNYDTN MDCEWTIQAP PSSNVQLIFL TFDLENSENC TYDYVQVFSG MEDTSGPMYG
QYCGNIIPQD IISLTDSLLV RFKTDSTIDM KGFSASYVAV DPFENSDEDP TSYSSEMVTP
FPGSLKSIYK EEESQETDDY NDFNENQLVI NSPYYTRNRY QNRY
//
