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Database: UniProt/TrEMBL
Entry: A0A0E3SHQ5_9EURY
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Original site: A0A0E3SHQ5_9EURY 
ID   A0A0E3SHQ5_9EURY        Unreviewed;       203 AA.
AC   A0A0E3SHQ5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=MSHOH_2875 {ECO:0000313|EMBL:AKB79358.1};
OS   Methanosarcina horonobensis HB-1 = JCM 15518.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434110 {ECO:0000313|EMBL:AKB79358.1, ECO:0000313|Proteomes:UP000033101};
RN   [1] {ECO:0000313|EMBL:AKB79358.1, ECO:0000313|Proteomes:UP000033101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB-1 {ECO:0000313|EMBL:AKB79358.1,
RC   ECO:0000313|Proteomes:UP000033101};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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; CP009516; AKB79358.1; -; Genomic_DNA.
DR   RefSeq; WP_048140959.1; NZ_CP009516.1.
DR   EnsemblBacteria; AKB79358; AKB79358; MSHOH_2875.
DR   GeneID; 24832196; -.
DR   KEGG; mhor:MSHOH_2875; -.
DR   PATRIC; fig|1434110.4.peg.3709; -.
DR   KO; K04564; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   Proteomes; UP000033101; Chromosome.
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; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000033101};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AKB79358.1}.
FT   DOMAIN        6     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        30     30       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        78     78       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   203 AA;  23938 MW;  1729D2A094764C23 CRC64;
     MAKELYKLPP LKYGYADLEP YISEEQLRIH HDKHHQAYVN NANSLIEMMD KARKEGTDFD
     YKATAKALTF NMGGHVLHDY FWWEMTPESN ASKEPVGELA DVIKEDFGGF DRFKKEFSQV
     ASSVEGSGWA ALTYCKDTQR LMIMQIEKHN VNLVPDYPII MDLDVWEHAY YIDYKNDRGK
     FIEGFWNIVN WEEIDKYFKE IQK
//
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