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Database: UniProt
Entry: A0A1R2AXC2_9CILI
LinkDB: A0A1R2AXC2_9CILI
Original site: A0A1R2AXC2_9CILI 
ID   A0A1R2AXC2_9CILI        Unreviewed;       240 AA.
AC   A0A1R2AXC2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SteCoe_33150 {ECO:0000313|EMBL:OMJ69193.1};
OS   Stentor coeruleus.
OC   Eukaryota; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ69193.1};
RN   [1] {ECO:0000313|EMBL:OMJ69193.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ69193.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S.,
RA   Prabakaran S., Witkowska E., Larue G.E., Fisher S., Freeman R.M.,
RA   Gunawardena J., Chu W., Stover N.A., Gregory B.D., Nowacki M.,
RA   Derisi J., Roy S.W., Marshall W.F., Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OMJ69193.1}.
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DR   EMBL; MPUH01001229; OMJ69193.1; -; Genomic_DNA.
DR   EnsemblProtists; OMJ69193; OMJ69193; SteCoe_33150.
DR   OrthoDB; 1353361at2759; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    240       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5013249517.
FT   DOMAIN       33    115       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      125    225       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        57     57       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       108    108       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       194    194       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       198    198       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   240 AA;  28377 MW;  1BF5B5526BF39D0F CRC64;
     MICLGKRIIF LLSLVYAFCP KDEYKPRNEK NVFSLPTLPY NYKELEPVLW SQIVYFHHKK
     EHAKFIEPLN SLIAEDSTYE SLTVTDLILQ FGLENNDIAL NAGGYYNHAL LWWSLLPSSC
     NKYQPEGQLL EDIELYFGDF ETFKDEFSRR AISLFGSGWI WLCRNPDGHL TINGKNKEYS
     PLAGNECLPL LGIDMWEHAY YLFYMDDIED YVYRWWGIVD WELVEYWYQE YISKGLPIPV
//
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