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
//