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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   24-JAN-2024, entry version 31.
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 of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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:KRY55914.1}.
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DR   EMBL; JYDI01000049; KRY55914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1D2Z2; -.
DR   STRING; 45882.A0A0V1D2Z2; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd19941; TIL; 1.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 4.10.75.10; Elafin-like; 2.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 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; IPR024134; SOD_Cu/Zn_/chaperone.
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   PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
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; Cu,Zn superoxide dismutase-like; 1.
DR   SUPFAM; SSF57256; Elafin-like; 2.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
DR   PROSITE; PS51390; WAP; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00500}; Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT   DOMAIN          72..160
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   DOMAIN          182..233
FT                   /note="WAP"
FT                   /evidence="ECO:0000259|PROSITE:PS51390"
FT   DOMAIN          295..347
FT                   /note="WAP"
FT                   /evidence="ECO:0000259|PROSITE:PS51390"
FT   DISULFID        117..124
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT   NON_TER         1
FT                   /evidence="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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