ID   A0A183BTB8_GLOPA        Unreviewed;       944 AA.
AC   A0A183BTB8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Superoxide dismutase {ECO:0000313|WBParaSite:GPLIN_000385400};
OS   Globodera pallida (Potato cyst nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Globodera.
OX   NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000385400};
RN   [1] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Aslett M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA   Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA   Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA   Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT   "The genome and life-stage specific transcriptomes of Globodera pallida
RT   elucidate key aspects of plant parasitism by a cyst nematode.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:GPLIN_000385400}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457}.
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DR   WBParaSite; GPLIN_000385400; GPLIN_000385400; GPLIN_000385400.
DR   Proteomes; UP000050741; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 2.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 2.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 2.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 2.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..944
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008146596"
FT   DOMAIN          73..117
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   DOMAIN          223..346
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          394..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..423
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   944 AA;  107605 MW;  3F1E1601E6700D4A CRC64;
     MLFLLFLLLQ LAPSVENDGR GYGPIGYGYG QIGHGHGRPP PHSGNCVTRV VQARVLMFKA
     TNNTDSTPSQ PIGVVDIFES AYGTTSLNGS INGLTPGDHG FHFHQFGDLS QAKKTKGSGN
     GDKFKQLLHS KEELMTVIME YVQRKLDDMR VQYQAYAAQV AKWPENIQNV SEAFGPDKEA
     YKAYMEVAAT WTESKPAKDS LKNIHTKXLT EHAAKFDEFR AYGTTSLNGS INGLTPGDHG
     FHFHQFGDLS QACAGAGAHF NPHNKKHGAP DATERHVGDL GNLVANAHGV AVVNIHDHMV
     TLNNNGVNSV VGRALVLHEK KDDLGLAANE ESLKTGNSGK RVACGLVFLF DHALTLKVDD
     LKQELDTDIH THAAFNKMNP ADFFNNPKWS VKLKEDEKKK QDDDDDDDGD EDDDDDDDDG
     EDDVPMAVSA LLEAILKGRD GFMPNAKLDL RNLPKWDGKP NKKISIMAIV KKCMRFVGKM
     MVWPLRVIRK QSKKLIHKAM YALKSKKEKA DLQKQLDDVM KDDLLNIYRS LDGSKLNKQK
     IAEHIKKSME KQGMNPDEEV VDHYAHEQLT KASRQQHPFT YLQTVRYDLH IKPADKLFDQ
     LYPDQYDQLM RFYADPFAFY EHQRLDSDTI YVARKFVETN KHLLKLYKKP YYLIHEFFAD
     PVQFYRRGNK LDKTMKKALT ETLKSFKKSG QKLNNKGQAE KLENLLNDPN KYLGSIEQLD
     DAVLGALTKA LHDNKVTVTN ALMNNKNLMK SKRNDNQTGE KKAQQFYKEL ETFFENPIEF
     YNKKMNNKLN MDAFQAFRDA LEVVNDKDSN QELDELNTEQ YKQLMLFLED PDEFLESTNL
     DEEVVVVLRN VFEEKIAMFN HLSNKQLSQL KKFLDNPEQF YAKNGTLDKS IFKQYRDTLP
     AHAKEGKIQR IKDFFKVWVG HAHHTNFQME FNHFSNDGTP KKKN
//