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Database: UniProt
Entry: A0A0V0UCB9_9BILA
LinkDB: A0A0V0UCB9_9BILA
Original site: A0A0V0UCB9_9BILA 
ID   A0A0V0UCB9_9BILA        Unreviewed;       825 AA.
AC   A0A0V0UCB9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE   Flags: Fragment;
GN   Name=dpy-31 {ECO:0000313|EMBL:KRX48911.1};
GN   ORFNames=T05_310 {ECO:0000313|EMBL:KRX48911.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX48911.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX48911.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX48911.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
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:PRU00059}.
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:KRX48911.1}.
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DR   EMBL; JYDJ01000022; KRX48911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0UCB9; -.
DR   STRING; 144512.A0A0V0UCB9; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR000859; CUB_dom.
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; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF813; ZINC METALLOPROTEINASE DPY-31; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00209; TSP1; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS50092; TSP1; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01211}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW   ProRule:PRU01211};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
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        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          351..550
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          594..710
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   REGION          276..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        447
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         446
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         450
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         456
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        394..549
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX48911.1"
SQ   SEQUENCE   825 AA;  94600 MW;  AFAEFFAEE2E5729A CRC64;
     YAGWIANACN SFNGSQRRRT PSCHCDRVGF WYLSVRKYYR GSVIFSPYYF FKYLFHFHHF
     VLSVVLLFAL FGLLCSTSFR LTACRTKTKK RIRERSSAFG LYPFAHLLTT SPPFLPLSLS
     LHHSVFVQDL PKIIFSHLLL PNKTVMQISS LLLSLICLID IHCHAENADE HHRQQRSAEV
     VKQKPGRDLL TADVDNPTSD LIDSNIRKKA FTFGQTKQQR DRINFILKQM QQLMLSNVKM
     ERLAVADTKS MVPSLEKRIS NQIEANLYQS EDSFHRRLQD QRKNASNSSI DYLKHKPHKE
     QPGRFMDSDP HGKSPEESGS HYEGDIVLTP EQAEELYSSL VHKNDRRQKR KFIALNARHW
     DSSVPIDYSF DGSHTSKQER LIELALKHWE NVTCLRFRRR FDTPKGNRII FTDVDGCASN
     VGRNPMKEPQ YVSLSLDCMK LGVIAHEVAH ALGFWHEQSR PDRDRFVNVV WRNIDEGSLA
     QFLKEQTREV DSKGIPYDYG SIMHYRSKAF AKNGDLYTLL TNVQNYQRTI GQRDHLSFND
     IRLMNQIYCS HVCTPLNCQR GGYTDPKKCS RCRCPDGFTG KLCEIVMPGF DANCGGLVAV
     KSRWHYFSSP NYPKAFKAGQ ECSWLFRASD GLRVELEFIE RFDIYCKAEH SLCMDYIEIR
     NSSDFANTGM RLCCHNIPKQ RIYSSTTDML VLFRSFYRSG LGFRARVRAV VKGERLRSIR
     SVPPSGEWEK WGEWSPCSVS CGGCGVQTRQ RKCPKDSLCA GESTSVQSCG NVPCEKCKEE
     KLVSVSCGLW GLFRCEAMQS VEVPCKEKCC TGYTVVNGVC EPVTL
//
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