ID A0A0V0U3S9_9BILA Unreviewed; 1068 AA.
AC A0A0V0U3S9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 30.
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:KRX45912.1};
GN ORFNames=T05_421 {ECO:0000313|EMBL:KRX45912.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX45912.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX45912.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX45912.1};
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:KRX45912.1}.
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DR EMBL; JYDJ01000067; KRX45912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0U3S9; -.
DR Proteomes; UP000055048; 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: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 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..403
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 719..910
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 951..1067
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 113..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 410..437
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 803
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 802
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 806
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 812
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:KRX45912.1"
SQ SEQUENCE 1068 AA; 120006 MW; 55CD97B3607FB399 CRC64;
LEILLCSNAY ISSLQGPQKQ LHCVILFCLP KKYRLQQIFH NFPMLFKTFT DFARLLLVLL
IILSAIIPLF IDEYDDIVVN DEERDEEEQG ELFITVMQSR IVPKLQVVRE RAISERQTSQ
TNSSSKPSTT TANGGKAKTS RAFSVASASS PAFASLPVRF SSTRVVHLQP QVFHVNSNKE
SIAEWRSALL SSSLPTSLNH SRCLKNVPYS NNISKSSRDG GVGRVNTAKS AFTFAQSSLI
VDEGGNNSPV TPHSPPQYTD SPRSASFTSA QSELDDIIID EILSMEDDIQ QNTRGSHPCS
GNLEALLSEG RVQYSTRKVS SSAPSTSSLD ADLFGHDDMI REQESMRDRR KKDIHNMIER
RRRYNINDRI KELSTLLPKS CTEEMKLNKG SILKASVDYI RQLRKDQERL YQLLQKQMAL
EAENKRLSNR NQDLEEQMRL HGLLPDHTVG MDTVGLGSRS TYGGKQMKVE SSLEGDYPFN
VSPTSQFTCA DYSSSSVLAG RGAGGQHSFL DRSSPCFRTT TPLSPDSAGS SDCAYTGLPL
LHEQALFSAG VGGHGSVQAD ALVANHRDVS LRYCTELVHL EKLISSVMVT HARVSIWETI
SFNDGIFFSD KLGKTPGRRT TNFPYDLFNS DHLNHVKLAL NKLMLLADQN FYPDKYTENE
IISATENLDK TFLSNDAEKL QVNSEADLLF EGDILLTPVQ ANQILDDHMP FVKRKLLKRS
LEKNLQKRWQ GGVIKYRFHN SIAEENHALI RQALQFWQSH TCMRFVFDEN ANSEDHLLFF
RGGGCYSMVG RYGGVQLGII SHEVGHAMGL WHQQSRPDAD SYIRIRPENV MKGALYNFLK
RNTNQVTTMD VPYDLGSVMH YGPTAFTRDY TQRTIVTLKP GYQRTIGQRE HPSFLDVEII
NRAYCEQSCP RKLPCQNGGY THPRSCAECI CPDGLGGIYC DRNERSQGAQ CGGIISAPKF
PEWFEITSPN YPNTYKDGQF CSWLIKADPG ARITAEFVGP MEFFCSETCK DYVEVKNSSD
LRPTGMRFCC TEKPVAPIWS DGNQMVIIFK TTSGYPHIGF KAKFFLIK
//
