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Database: UniProt/TrEMBL
Entry: A9RN26_PHYPA
LinkDB: A9RN26_PHYPA
Original site: A9RN26_PHYPA 
ID   A9RN26_PHYPA            Unreviewed;       157 AA.
AC   A9RN26;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   28-MAR-2018, entry version 71.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=PHYPA_028596 {ECO:0000313|EMBL:PNR28004.1}, PHYPADRAFT_176592
GN   {ECO:0000313|EMBL:EDQ79642.1};
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|Proteomes:UP000006727};
RN   [1] {ECO:0000313|EMBL:EDQ79642.1, 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:PNR28004.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29237241; DOI=.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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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}.
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DR   EMBL; DS544907; EDQ79642.1; -; Genomic_DNA.
DR   EMBL; ABEU02000024; PNR28004.1; -; Genomic_DNA.
DR   RefSeq; XP_001755582.1; XM_001755530.1.
DR   UniGene; Ppa.3388; -.
DR   ProteinModelPortal; A9RN26; -.
DR   STRING; 3218.PP1S18_84V6.1; -.
DR   PRIDE; A9RN26; -.
DR   EnsemblPlants; PP1S18_84V6.1; PP1S18_84V6.1; PP1S18_84V6.
DR   GeneID; 5918827; -.
DR   Gramene; PP1S18_84V6.1; PP1S18_84V6.1; PP1S18_84V6.
DR   KEGG; ppp:PHYPADRAFT_176592; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; A9RN26; -.
DR   KO; K04565; -.
DR   OMA; HIHEATE; -.
DR   Proteomes; UP000006727; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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       14    151       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   157 AA;  15650 MW;  9E34EA8944CF8951 CRC64;
     MAPLKAICVL AGPSDSVTGV ISFVQDGAGP TIVEGTVKGL NPGKHGFHVH ALGDTTNGCM
     STGPHFNPKG LEHGAPEDEV RHAGDLGNVI AGEDGIAKVS LKDAHIPLGG PNSIIGRAVV
     VHADPDDLGK GGHELSKSTG NAGARIACGI IGFQASA
//
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