ID A0A0V1A3G3_9BILA Unreviewed; 1170 AA.
AC A0A0V1A3G3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=TFE3 {ECO:0000313|EMBL:KRY19366.1};
GN ORFNames=T12_16173 {ECO:0000313|EMBL:KRY19366.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19366.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY19366.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19366.1};
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:KRY19366.1}.
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DR EMBL; JYDQ01000036; KRY19366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A3G3; -.
DR STRING; 990121.A0A0V1A3G3; -.
DR Proteomes; UP000054783; 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 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; SM00209; TSP1; 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:UP000054783};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 215..416
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 457..573
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 760..832
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 1149..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 1170 AA; 134075 MW; 62CFFC06C04A0D51 CRC64;
MEMAFCVLPC FQQFTLSVQA DALVPNHRDV SLRYCTELVH LEKLISSVMV THARVCVCGV
WWKQENPAMP IVANAFLISA IPLMPLQMKR SIWETISFND GIFFSDKLGK TPGRRTTNFP
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 RRICSSADTS TQYCKFVSCC SPYEACIIEQ FLFQQCDESC
IYRHVEKVNC WHCHSLRDCI SDPFFCRTCS FVQPPILCKN YFDFFGLEPS YNLDVSVLTS
RFRSLQSRLH PDRFTQKSEN ERKFSEQQAS LINDAYSTLL KPYPRAVYML ELMGEMISDG
DERSTGVSSQ FLMHIFELNE MLEDCEIESR SSLIALRQKV AADVEQCELS LIDEFDRKNV
TEAKRLTIEM KPFQVRIKVS LITKLRKNSN HTVHVPPLHM SLAVRIGKSG IRFVSQYPPL
NRGRDWVIEG WWIRDHKPDS WPETAEQRKL AAMRYGLREE DYCPYPREMH VGNYPDLGRI
NYALKDPYEN WSYPGMRRNF NEPVDFFYDV IFADRYTVTG VEYKSSWQKL VRLLQYIGGF
GLFLYLTRFM IPTNEVPVRP QKLSARPLHI RTRRLEFNQA KTFRAGLFST CMQATGNAVS
LFKCHKSNRP SPSVHANSAG CMGDHATSNT
//
