ID A0A0V1A4G3_9BILA Unreviewed; 1089 AA.
AC A0A0V1A4G3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Flags: Fragment;
GN Name=TFE3 {ECO:0000313|EMBL:KRY19372.1};
GN ORFNames=T12_16173 {ECO:0000313|EMBL:KRY19372.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19372.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY19372.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19372.1};
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:KRY19372.1}.
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DR EMBL; JYDQ01000036; KRY19372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A4G3; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd11397; bHLHzip_MITF_like; 1.
DR CDD; cd00041; CUB; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
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 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 PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS01180; CUB; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000054783};
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 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 369..422
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 740..931
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 972..1088
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 132..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..456
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 824
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 827
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 833
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:KRY19372.1"
SQ SEQUENCE 1089 AA; 122462 MW; 962021A237F7712D CRC64;
LLTKLLYLVM TCEISPNTHD RLVAAIWKYC CVQTRPQKQL HCVILFCLPK KYRLQQIFHN
FPMLFKTFTD FARLLLVLLI ILSAIIPLFI DEYDDIVVND EERDEEEQGE LFITVMQSRI
VPKLQVVRER AISERQTSQT NSSSKPSTTA ANGGKAKTSR AFSAASASSP AFASLPVRFS
STRVVHLQPQ VFHVNSNKES IAEWRSALLS SSLPTSLNHS RCLKNVPYSN NISKSSRDGG
VGRVNTAKSA FTFAQSSLIG DGGGNNSPVT PHSPPQYTDS PRSASFTSAQ SELDDIIIDE
ILSMEDDIQQ NTRGSHPCSG NLEALLSEGR VQYSTRKVSS SAPSTSSLDA DLFGHDDMIR
EQESMRDRRK KDIHNMIERR RRYNINDRIK ELSTLLPKSC TEEMKLNKGS ILKASVDYIR
QLRKDQERLY QLLQKQMALE AENKRLSNRN QDLEEQMRLH GLLPDHTVGM DTVGLGSRST
YGGKQMKVES SLEGDYPFNV SPTSQFTCAD YSSSSVLAGR GAGGQHNFLD RSSPCFRTTT
PLSPDSAGSS DCAYTGLPLL HEQALFSAGV GGHGSVQADA LVPNHRDVSL RYCTELVHLE
KLISSVMVTH ARVCVSIWET ISFNDGIFFS DKLGKTPGRR TTNFPYDLFN SDHLNHVKLA
LNKLMLLADQ NFYPDKYTEN EIISATENLD KTFLSNDAEK LQVNSEADLL FEGDILLTPV
QANQILDDHM PFVKRKLLKR SLEKNLQKRW QGGVIKYRFH NSIAEENHAL IRQALQFWQS
HTCMRFVFDE NANSEDHLLF FRGGGCYSMV GRYGGVQLGI ISHEVGHAMG LWHQQSRPDA
DSYIRIRPEN VMKGALYNFL KRNTNQVTTM DVPYDLGSVM HYGPTAFTRD YTQRTIVTLK
PGYQRTIGQR EHPSFLDVEI INRAYCEQSC PRKLPCQNGG YTHPRSCAEC ICPDGLGGIY
CDRNERSQGA QCGGIISAPK FPEWFEITSP NYPNTYKDGQ FCSWLIKADP GARITAEFVG
PMEFFCSETC KDYVEVKNSS DLRPTGMRFC CTEKPVAPIW SDGNQMVIIF KTTSGYPHIG
FKAKFFLIK
//
