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A8IGH1 (A8IGH1_CHLRE) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase RuleBase RU000414
EC=1.15.1.1 RuleBase RU000414
Gene names
Name:FSD1 EMBL EDP05850.1
ORF Names:CHLREDRAFT_182933 EMBL EDP05850.1
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. RuleBase RU000414

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2. RuleBase RU000414

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family. RuleBase RU004477

Sequences

Sequence LengthMass (Da)Tools
A8IGH1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: FB176831824065F2

FASTA23425,915
        10         20         30         40         50         60 
MALAMKAQAS SLVAGQRRAV RPASGRRAVI TRAALELKSP PYALDALEPH MSKQTLEFHW 

        70         80         90        100        110        120 
GKHHRAYVDN MNKQVAGTPL DGKSLEEIVL ASWNNGQPTP VFNNAAQVWN HTFFWESMKP 

       130        140        150        160        170        180 
NGGGAPTGAL AEAITRDFGS LDKFKEEFKQ AGMTQFGSGW AWLNADKTGK LSISKSPNAV 

       190        200        210        220        230 
NPVVEGKTPI LTVDVWEHAY YIDVQNRRPD YITTFMEKLI NWDAVAQRYA AATK

« Hide

References

« Hide 'large scale' references
[1]"The Chlamydomonas genome reveals the evolution of key animal and plant functions."
Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P. expand/collapse author list , Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.
Science 318:245-250(2007) [PubMed: 17932292] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC-503 and CC-503 cw92 mt+ EMBL EDP05850.1.
[2]"Two mechanisms for maintenance of superoxide dismutase capacity in iron deficient Chlamydomonas."
Page D., Allen M., Urzica E., Merchant S.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Dangeard C-9 EMBL ACV41089.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		GQ413964 mRNA. Translation: ACV41089.1.
DS496117 Genomic DNA. Translation: EDP05850.1.
RefSeqXP_001690591.1. XM_001690539.1.
UniGeneCre.8669.

3D structure databases

ProteinModelPortalA8IGH1.
SMRA8IGH1. Positions 33-232.
ModBaseSearch...

Proteomic databases

PRIDEA8IGH1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5716112.
KEGGcre:CHLREDRAFT_182933.

Phylogenomic databases

PhylomeDBA8IGH1.
ProtClustDBCLSN2920939.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. SODismutase. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SODismutase. 1 hit.
SSF54719. SODismutase. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA8IGH1_CHLRE
AccessionPrimary (citable) accession number: A8IGH1
Entry history
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: December 14, 2011
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info