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Protein

Frataxin homolog, mitochondrial

Gene

SPCC1183.03c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe2+ to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe2+ to Fe3+. May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization (By similarity).By similarity

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Heme biosynthesis, Ion transport, Iron storage, Iron transport, Transport

Keywords - Ligandi

Iron

Enzyme and pathway databases

ReactomeiR-SPO-1362409. Mitochondrial iron-sulfur cluster biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Frataxin homolog, mitochondrial (EC:1.16.3.1)
Gene namesi
ORF Names:SPCC1183.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1183.03c.
PomBaseiSPCC1183.03c.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 158Frataxin homolog, mitochondrialPRO_0000010134
Transit peptidei1 – ?Mitochondrion

Proteomic databases

MaxQBiO74831.

Interactioni

Subunit structurei

Monomer. Oligomer (By similarity).By similarity

Protein-protein interaction databases

BioGridi275715. 1 interaction.
MINTiMINT-4681082.

Structurei

3D structure databases

ProteinModelPortaliO74831.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the frataxin family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiO74831.
KOiK19054.
OMAiENDYHRV.
OrthoDBiEOG7WDNF7.
PhylomeDBiO74831.

Family and domain databases

Gene3Di3.30.920.10. 1 hit.
HAMAPiMF_00142. CyaY.
InterProiIPR017789. Frataxin.
IPR002908. Frataxin/CyaY.
IPR020895. Frataxin_CS.
[Graphical view]
PANTHERiPTHR16821. PTHR16821. 1 hit.
PfamiPF01491. Frataxin_Cyay. 1 hit.
[Graphical view]
PRINTSiPR00904. FRATAXIN.
SMARTiSM01219. Frataxin_Cyay. 1 hit.
[Graphical view]
SUPFAMiSSF55387. SSF55387. 1 hit.
TIGRFAMsiTIGR03421. FeS_CyaY. 1 hit.
TIGR03422. mito_frataxin. 1 hit.
PROSITEiPS01344. FRATAXIN_1. 1 hit.
PS50810. FRATAXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O74831-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSLRAAFRR RTPIFLKPYE FSTNVFGLRC RYYSQVRHNG ALTDLEYHRV
60 70 80 90 100
ADDTLDVLND TFEDLLEEVG KKDYDIQYAN GVITLMLGEK GTYVINKQPP
110 120 130 140 150
AHQIWLSSPV SGPKHYEYSL KSKTWCSTRD EGTLLGILSS EFSKWFSRPI

EFKKSEDF
Length:158
Mass (Da):18,387
Last modified:November 1, 1998 - v1
Checksum:iF5018ECAB617573E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21083.1.
PIRiT40843.
RefSeqiNP_587886.1. NM_001022878.2.

Genome annotation databases

EnsemblFungiiSPCC1183.03c.1; SPCC1183.03c.1:pep; SPCC1183.03c.
GeneIDi2539143.
KEGGispo:SPCC1183.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21083.1.
PIRiT40843.
RefSeqiNP_587886.1. NM_001022878.2.

3D structure databases

ProteinModelPortaliO74831.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275715. 1 interaction.
MINTiMINT-4681082.

Proteomic databases

MaxQBiO74831.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1183.03c.1; SPCC1183.03c.1:pep; SPCC1183.03c.
GeneIDi2539143.
KEGGispo:SPCC1183.03c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1183.03c.
PomBaseiSPCC1183.03c.

Phylogenomic databases

InParanoidiO74831.
KOiK19054.
OMAiENDYHRV.
OrthoDBiEOG7WDNF7.
PhylomeDBiO74831.

Enzyme and pathway databases

ReactomeiR-SPO-1362409. Mitochondrial iron-sulfur cluster biogenesis.

Miscellaneous databases

NextBioi20800315.
PROiO74831.

Family and domain databases

Gene3Di3.30.920.10. 1 hit.
HAMAPiMF_00142. CyaY.
InterProiIPR017789. Frataxin.
IPR002908. Frataxin/CyaY.
IPR020895. Frataxin_CS.
[Graphical view]
PANTHERiPTHR16821. PTHR16821. 1 hit.
PfamiPF01491. Frataxin_Cyay. 1 hit.
[Graphical view]
PRINTSiPR00904. FRATAXIN.
SMARTiSM01219. Frataxin_Cyay. 1 hit.
[Graphical view]
SUPFAMiSSF55387. SSF55387. 1 hit.
TIGRFAMsiTIGR03421. FeS_CyaY. 1 hit.
TIGR03422. mito_frataxin. 1 hit.
PROSITEiPS01344. FRATAXIN_1. 1 hit.
PS50810. FRATAXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiFRDA_SCHPO
AccessioniPrimary (citable) accession number: O74831
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.