ID A0A0V0WBP8_9BILA Unreviewed; 1648 AA.
AC A0A0V0WBP8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=nas-36 {ECO:0000313|EMBL:KRX73302.1};
GN ORFNames=T06_5999 {ECO:0000313|EMBL:KRX73302.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX73302.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX73302.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX73302.1};
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:KRX73302.1}.
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; JYDK01000180; KRX73302.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0046983; F:protein dimerization activity; IEA:InterPro.
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; cd11397; bHLHzip_MITF_like; 1.
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; 4.10.280.10; Helix-loop-helix DNA-binding 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; IPR011598; bHLH_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
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; PF00010; HLH; 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; SM00353; HLH; 1.
DR SMART; SM00209; TSP1; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding 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; PS50888; BHLH; 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 Coiled coil {ECO:0000256|SAM:Coils};
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}; 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:UP000054673};
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 74..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 377..430
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 725..926
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 967..1083
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1266..1338
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 135..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..464
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 819
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 818
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 828
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 1648 AA; 187525 MW; 5E81320C0F35926E CRC64;
MLNGFQITCE ISPNTRSTCG SHLEILLCSN AYISSLQGPQ KQLHCVILFC LPKKYRLQQI
FHNFPMLFKT FTDFARLLLV LLIILSAIIP LFIDEYDDIV VNDEERDEEE QGELFITVMQ
SRIVPKLQVV RERAISERQT SQTNSSSKPS TTAANGGKAK TSRAFSVASA SSSAFASLPV
RFSSTRVVHL QPQVFHVNSN KESIAEWRSA LLSSSLPTSL NHSRCLKNVP YSNNISKSSR
DGGVGRVNTA KSAFTFAQSS LIVDVGGNNS PVTPHSPPQY TDSPRSASFT SAQSELDDII
IDEILSMEDD IQQNTRSHQA CGSHPCSGNL EALLSEGRVQ YSTRKVSSSA PSTSSLDADL
FGHDDMIREQ ESMRDRRKKD IHNMIERRRR YNINDRIKEL STLLPKSCTE EMKLNKGSIL
KASVDYIRQL RKDQERLYQL LQKQMALEAE NKRLSNRNQD LEEQMRLHGL LPDHTVGMDT
IGLGSRSTYG GKQMKVESSL EGDYPFNVSP TSQFTCADYS SSSVLAGRGA GGQHSFLDRS
SPCFRTTTPL SPDSAGSSDC AYTGLPLLHE QALFSAGVGG HGSVQADALV ANHRDVSLRY
LTELVHLEKL ISSVMVTHAC VCVTYGFTFP YDLFNSDHLN HVKLALNKLM LLADQNFYPD
KYTENEIISA TENLDKTFLS NDAEKLQVNS EADLLFEGDI LLTPVQANQI LDDHMPFVKR
KLLKRSLEKN LQKRWQGGVI KYRFHNSIAE ENHALIRQAL QFWQSHTCMR FVFDENANSE
DHLLFFRGGG CYSMVGRYGG VQVVSIGSGC EYLGIISHEV GHAMGLWHQQ SRPDADSYIR
IRPENVMKGA LYNFLKRNTN QVTTMDVPYD LGSVMHYGPT AFTRDYTQRT IVTLKPGYQR
TIGQREHPSF LDVEIINRAY CEQSCPRKLP CQNGGYTHPR SCAECICPDG LGGIYCDRNE
RSQGAQCGGI ISAPKFPEWF EITSPNYPNT YKDGQFCSWL IKADPGARIT AEFVGPMEFF
CSETCKDYVE VKNSSDLRPT GMRFCCTEKP VAPIWSDGNQ MVIIFKTTSG YPHIGFKAKV
QQYDFKMKPT TSSSTTQSVE TTTEATILTT STRVTVAPTV ESWTPWSSWT HCSRTCGACG
LQSRFRSCQT STRICSGESY EHRRCETTPC TGYTECTKLL YLDMPCQTNG RRICSSAQWK
TAKWTLLNMR RCIIEHFLFQ QCDESCIYRH VEKVNCWHCH SLRDCISDPF FCRTCSFVQP
PILCKNYFDF FGLETSYNLD VSVLTSRFRS LQSRLHPDRF TQKSENERKF SEQQASLIND
AYSTLLKPYP RAVYMLELMG EKISDGDERS TGVSSQFLMH IFELNEMLED CEIESRSSLI
ALRQKVAADV EQCELSLIDE FDRKNVTEAK RLTIEMKYNL NLLENIDKKL INVRIKVSLI
TKLRKNSNHT VHVPSLHMSL AVRIGKSGIR FVSQYPPLNR GRDWVIEGWW IRDHKPDSWP
ETAEQRKLAA MRYGLREEDY CPYPREMHVG NYPDLGRINY ALKDPYENWS YPGMRRNFNE
PVDFFHDVIF ADRYTVTGVE YKSSWQKLVR LLQYIGGFVL FLYLTRFMIP TNEVPVKPKQ
YAYDYEWAFP YRDPKNFPLV HYTFEPED
//
