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Database: UniProt/TrEMBL
Entry: A0A1R4A4P4_9EURY
LinkDB: A0A1R4A4P4_9EURY
Original site: A0A1R4A4P4_9EURY 
ID   A0A1R4A4P4_9EURY        Unreviewed;       205 AA.
AC   A0A1R4A4P4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=CPM_0030 {ECO:0000313|EMBL:SJK83934.1};
OS   Cuniculiplasma divulgatum.
OC   Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
OC   Cuniculiplasmataceae; Cuniculiplasma.
OX   NCBI_TaxID=1673428 {ECO:0000313|EMBL:SJK83934.1, ECO:0000313|Proteomes:UP000187822};
RN   [1] {ECO:0000313|EMBL:SJK83934.1, ECO:0000313|Proteomes:UP000187822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM4 (JCM 30641 \VKM B-2940)
RC   {ECO:0000313|Proteomes:UP000187822};
RA   Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; LT719092; SJK83934.1; -; Genomic_DNA.
DR   RefSeq; WP_077075763.1; NZ_LT719092.1.
DR   GeneID; 30926683; -.
DR   KEGG; cdiv:CPM_0030; -.
DR   KO; K04564; -.
DR   Proteomes; UP000187822; Chromosome i.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000187822};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN       19     86       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        78     78       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   205 AA;  24079 MW;  92A1768BE8281470 CRC64;
     MVEKWEKKNQ FKPKGLDGIS DQQIEYHFET HYNGYVTKLN EIWEKLPNAD RSKANQNYSE
     FRELKLEETF NYDGSLLHEI YFESLKKDGL KNLSEELKKK ISEDFGSYEK WVEDFKATGT
     AFRGWALLVY DLNTGKLRNI GADVHNTNGI WNAIVVMALD VYEHAYYVDY GAKRAPYLDA
     FMKNVDWASV NKRFEKAHKA YLAFK
//
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