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Database: UniProt
Entry: A0A0V1D2Z2_TRIBR
LinkDB: A0A0V1D2Z2_TRIBR
Original site: A0A0V1D2Z2_TRIBR 
ID   A0A0V1D2Z2_TRIBR        Unreviewed;       664 AA.
AC   A0A0V1D2Z2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   18-JUL-2018, entry version 15.
DE   SubName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000313|EMBL:KRY55914.1};
DE   Flags: Fragment;
GN   Name=SOD1 {ECO:0000313|EMBL:KRY55914.1};
GN   ORFNames=T03_4255 {ECO:0000313|EMBL:KRY55914.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY55914.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY55914.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY55914.1};
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRY55914.1}.
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DR   EMBL; JYDI01000049; KRY55914.1; -; Genomic_DNA.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   Gene3D; 4.10.75.10; -; 2.
DR   Gene3D; 4.10.800.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR008197; WAP_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   Pfam; PF01826; TIL; 1.
DR   Pfam; PF00095; WAP; 2.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SMART; SM00211; TY; 1.
DR   SMART; SM00217; WAP; 2.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   SUPFAM; SSF57256; SSF57256; 2.
DR   SUPFAM; SSF57567; SSF57567; 1.
DR   SUPFAM; SSF57610; SSF57610; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
DR   PROSITE; PS51390; WAP; 3.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054653};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00500,
KW   ECO:0000256|SAAS:SAAS00485231};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT   DOMAIN       72    160       Thyroglobulin type-1.
FT                                {ECO:0000259|PROSITE:PS51162}.
FT   DOMAIN      182    233       WAP. {ECO:0000259|PROSITE:PS51390}.
FT   DOMAIN      295    347       WAP. {ECO:0000259|PROSITE:PS51390}.
FT   DOMAIN      366    417       WAP. {ECO:0000259|PROSITE:PS51390}.
FT   DISULFID    117    124       {ECO:0000256|PROSITE-ProRule:PRU00500}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KRY55914.1}.
SQ   SEQUENCE   664 AA;  71357 MW;  8640775FA53F7617 CRC64;
     LSNLLHCLPK EVGAACPVPW KISTSTYSIP QLKQMVIHKI PLAFLLTTLW FTLGKGAICP
     GKRMSVGRCT LTRACPKNFN CIHGYCCPKC AQVALRPGPD GFRPSCTPDG NYEPVQCDAR
     SGECWCVTEK GQEIEGSRKT APSTKMTQMM NPSRAGLLPC DMLREQHRQV KPPMLGGAEM
     YNSAKVGRIR PAKVCRPQPA MNMCSDRCQA DTDCAQLEQC CYNGCGRQCQ IPPSEEFKLQ
     PNLQVQVQPQ PYTISGEFPS QSLMKGGEPS SPMTFGQPYP DTSAMQRPAQ IVPVVTEKPG
     YCPAQRAGPP PLRVMALGSP HCQMDVHCPD TKKCCETPVG RRCLAVQESV TSIDPYNIKP
     GFATETISQS GPCPPSGGAG FQLQPSGQAT PFRQLDKCQG DFECPAGMRC CRISAMCVPE
     TALDVMSASG TSFEKHPSKG QQFITCDRQD EEYSNCVPTC QVGCDNLHTA AYCTQTECKP
     GCVCRIGYVR LHSKDPTSAC VPKAQCQESH EPQAPPTTQV GVASDKAVIS LTSKNGQVSG
     VLSMEEFQGR TEVTGTVNGL PEGRYELHVH ENGDISEPCT SAGPFFGQQA SGSFNSFQQV
     SLIGMTEADS AGHANVSIET KQFTLSGPTS VVGRTLVFHR KGAPGFGTPV LESNGIACGV
     IGLA
//
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