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Database: UniProt
Entry: A0A2K1K4G2_PHYPA
LinkDB: A0A2K1K4G2_PHYPA
Original site: A0A2K1K4G2_PHYPA 
ID   A0A2K1K4G2_PHYPA        Unreviewed;       204 AA.
AC   A0A2K1K4G2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   10-APR-2019, entry version 8.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=PHYPA_013148 {ECO:0000313|EMBL:PNR48671.1};
OS   Physcomitrella patens subsp. patens (Moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR48671.1, ECO:0000313|Proteomes:UP000006727};
RN   [1] {ECO:0000313|EMBL:PNR48671.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B.,
RA   Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K.,
RA   Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A.,
RA   Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R.,
RA   Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J.,
RA   Sanderfoot A., Schween G., Shiu S.H., Stueber K., Theodoulou F.L.,
RA   Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L.,
RA   Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R.,
RA   Grigoriev I.V., Quatrano R.S., Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the
RT   conquest of land by plants.";
RL   Science 319:64-69(2008).
RN   [2] {ECO:0000313|EMBL:PNR48671.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D.,
RA   Casacuberta J.M., Vandepoele K., Reski R., Cuming A.C., Tuskan G.A.,
RA   Maumus F., Salse J., Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss
RT   genome structure and evolution.";
RL   Plant J. 93:515-533(2018).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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:PNR48671.1}.
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DR   EMBL; ABEU02000009; PNR48671.1; -; Genomic_DNA.
DR   EnsemblPlants; Pp3c9_24840V3.1; Pp3c9_24840V3.1; Pp3c9_24840.
DR   EnsemblPlants; Pp3c9_24840V3.2; Pp3c9_24840V3.2; Pp3c9_24840.
DR   EnsemblPlants; Pp3c9_24840V3.3; Pp3c9_24840V3.3; Pp3c9_24840.
DR   EnsemblPlants; Pp3c9_24840V3.4; Pp3c9_24840V3.4; Pp3c9_24840.
DR   EnsemblPlants; Pp3c9_24840V3.5; Pp3c9_24840V3.5; Pp3c9_24840.
DR   EnsemblPlants; Pp3c9_24840V3.6; Pp3c9_24840V3.6; Pp3c9_24840.
DR   Gramene; Pp3c9_24840V3.1; Pp3c9_24840V3.1; Pp3c9_24840.
DR   Gramene; Pp3c9_24840V3.2; Pp3c9_24840V3.2; Pp3c9_24840.
DR   Gramene; Pp3c9_24840V3.3; Pp3c9_24840V3.3; Pp3c9_24840.
DR   Gramene; Pp3c9_24840V3.4; Pp3c9_24840V3.4; Pp3c9_24840.
DR   Gramene; Pp3c9_24840V3.5; Pp3c9_24840V3.5; Pp3c9_24840.
DR   Gramene; Pp3c9_24840V3.6; Pp3c9_24840V3.6; Pp3c9_24840.
DR   OMA; MAKAVCT; -.
DR   Proteomes; UP000006727; Chromosome 9.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; -; 1.
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; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006727};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       61    199       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   204 AA;  20662 MW;  5F214BADD92521CA CRC64;
     MAATTMSTLS TSLVAPTVAA SQSAFQGASV RVNLMPAVGV VKSRPLTIVA ATKKAVAVLK
     GNANVEGVVT LLQEDDGPTK VNVKITGLAP GKHGFHLHEF GDTTNGCMST GPHFNPEGKT
     HGAPEDQNRH AGDLGNVIAG DDGVVEVTLE DSQIPLSGPN SVVGRAFVIH EAEDDLGKGG
     HELSSTTGNA GGRLACGVVG LTPL
//
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