A8JAX1 (A8JAX1_CHLRE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Superoxide dismutase RuleBase RU000414
EC=1.15.1.1 RuleBase RU000414

Gene names

Name:	MSD2 EMBL EDO98932.1
ORF Names:	CHLREDRAFT_193511 EMBL EDO98932.1

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii) [Reference proteome]

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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

Ontologies

Keywords
Molecular function	Oxidoreductase RuleBase RU000414
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	metal ion binding Inferred from electronic annotation. Source: InterPro superoxide dismutase activity Inferred from electronic annotation. Source: UniProtKB-EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A8JAX1 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 1E0F0A1A29E7F1B1	FASTA	223	24,852
	10 20 30 40 50 60 MLARVALGLA RDGQSAVPTM TRAMSSVKLP DLPYSYGALE PYISGQIMEL HHSKHHATYV 70 80 90 100 110 120 ANLNKALEQQ AEAEHKGDVA KLISLQSAIK FNGGGHVNHD IFWTNLCPHK EWQPPSGDLK 130 140 150 160 170 180 ALIEAQWKTL DNFTTTFSAQ TAAVQGSGWG WLGYNKATHK LEVVTLPNQD PLSVTGLVPL 190 200 210 220 LGIDVWEHAY YLQYKNVRPD YLKAIWNIVN WQNVEQRLAA AKK

References

	« Hide 'large scale' referencesShow '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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CC-503 and CC-503 cw92 mt+ EMBL EDO98932.1.
[2]	Page D. Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: CC-1690 wild type mt+ 21gr EMBL ACV41091.1.
[3]	"Fe Sparing and Fe Recycling Contribute to Increased Superoxide Dismutase Capacity in Iron-Starved Chlamydomonas reinhardtii." Page M.D., Allen M.D., Kropat J., Urzica E.I., Karpowicz S.J., Hsieh S.I., Loo J.A., Merchant S.S. Plant Cell 24:2649-2665(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: CC-1690 wild type mt+ 21gr EMBL ACV41091.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GQ413966 mRNA. Translation: ACV41091.1. DS496151 Genomic DNA. Translation: EDO98932.1.
RefSeq	XP_001699077.1. XM_001699025.1.
UniGene	Cre.2383.
3D structure databases
ProteinModelPortal	A8JAX1.
SMR	A8JAX1. Positions 29-223.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	3055.JGI193511.
Proteomic databases
PRIDE	A8JAX1.
ProMEX	A8JAX1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	EDO98932; EDO98932; CHLREDRAFT_193511.
GeneID	5724629.
KEGG	cre:CHLREDRAFT_193511.
Phylogenomic databases
eggNOG	COG0605.
KO	K04564.
OMA	IDSHFGS.
ProtClustDB	CLSN2699936.
Family and domain databases
InterPro	IPR001189. Mn/Fe_SOD. IPR019833. Mn/Fe_SOD_BS. IPR019832. Mn/Fe_SOD_C. IPR019831. Mn/Fe_SOD_N. [Graphical view]
PANTHER	PTHR11404. PTHR11404. 1 hit.
Pfam	PF02777. Sod_Fe_C. 1 hit. PF00081. Sod_Fe_N. 1 hit. [Graphical view]
PIRSF	PIRSF000349. SODismutase. 1 hit.
PRINTS	PR01703. MNSODISMTASE.
SUPFAM	SSF46609. SSF46609. 1 hit. SSF54719. SSF54719. 1 hit.
PROSITE	PS00088. SOD_MN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A8JAX1_CHLRE

Accession

Primary (citable) accession number: A8JAX1

Entry history

Integrated into UniProtKB/TrEMBL:	December 4, 2007
Last sequence update:	December 4, 2007
Last modified:	November 13, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)