ID A0A0V0WCH9_9BILA Unreviewed; 971 AA.
AC A0A0V0WCH9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Flags: Fragment;
GN Name=nas-36 {ECO:0000313|EMBL:KRX73303.1};
GN ORFNames=T06_5999 {ECO:0000313|EMBL:KRX73303.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX73303.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX73303.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX73303.1};
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 -!- SIMILARITY: Belongs to the HscB family.
CC {ECO:0000256|ARBA:ARBA00010476}.
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:KRX73303.1}.
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DR EMBL; JYDK01000180; KRX73303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WCH9; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:InterPro.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal 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 HAMAP; MF_00682; HscB; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR008699; NDUFB8.
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 NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF849; ZINC METALLOPROTEINASE NAS-36; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR Pfam; PF05821; NDUF_B8; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 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; PS50076; DNAJ_2; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000054673};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 87..278
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 319..435
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 589..661
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT ACT_SITE 171
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"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX73303.1"
SQ SEQUENCE 971 AA; 112588 MW; 747692600A16CC72 CRC64;
LNHVKLALNK LMLLADQNFY PDKYTENEII SATENLDKTF LSNDAEKLQV NSEADLLFEG
DILLTPVQAN QILDDHMPFV KRKLLKRSLE KNLQKRWQGG VIKYRFHNSI AEENHALIRQ
ALQFWQSHTC MRFVFDENAN SEDHLLFFRG GGCYSMVGRY GGVQLGIISH EVGHAMGLWH
QQSRPDADSY IRIRPENVMK GALYNFLKRN TNQVTTMDVP YDLGSVMHYG PTAFTRDYTQ
RTIVTLKPGY QRTIGQREHP SFLDVEIINR AYCEQSCPRK LPCQNGGYTH PRSCAECICP
DGLGGIYCDR NERSQGAQCG GIISAPKFPE WFEITSPNYP NTYKDGQFCS WLIKADPGAR
ITAEFVGPME FFCSETCKDY VEVKNSSDLR PTGMRFCCTE KPVAPIWSDG NQMVIIFKTT
SGYPHIGFKA KVQQFFSHKI TIFNIDDFKM KPTTSSSTTQ SVETTTEATI LTTSTRVTVA
PTVESWTPWS SWTHCSRTCG ACGLQSRFRS CQTSTRICSA QWKTAKWTLL NMRRCIIEHF
LFQQCDESCI YRHVEKVNCW HCHSLRDCIS DPFFCRTCSF VQPPILCKNY FDFFGLETSY
NLDVSVLTSR FRSLQSRLHP DRFTQKSENE RKFSEQQASL INDAYSTLLK PYPRAVYMLE
LMGEKISDGD ERSTGVSSQF LMHIFELNEM LEDCEIESRS SLIALRQKVA ADVEQCELSL
IDEFDRKNVT EAKRLTIEMK YNLNLLENID KKLINVRIKV SLITKLRKNS NHTVHVPSLH
MSLAVRIGKS GIRFVSQYPP LNRGRDWVIE GWWIRDHKPD SWPETAEQRK LAAMRYGLRE
EDYCPYPREM HVGNYPDLGR INYALKDPYE NWSYPGMRRN FNEPVDFFHD VIFADRYTVT
GVEYKSSWQK LVRLLQYIGG FVLFLYLTRF MIPTNEVPVK PKQYAYDYEW AFPYRDPKNF
PLVHYTFEPE D
//
