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Protein
Submitted name:

Cytochrome c

Gene

LMJF_16_1310

Organism
Leishmania major
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281Heme (covalent)Combined sources
Metal bindingi29 – 291Iron (heme axial ligand); via tele nitrogenCombined sources
Metal bindingi91 – 911Iron (heme axial ligand)Combined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chainUniRule annotation, Transport

Keywords - Ligandi

HemeUniRule annotationCombined sources, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Cytochrome cImported
Submitted name:
Putative cytochrome cImported
Gene namesi
ORF Names:LMJF_16_1310Imported, LMJF_16_1320Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
Proteomesi
  • UP000000542 Componenti: Chromosome 16

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

MitochondrionUniRule annotation

PTM / Processingi

Post-translational modificationi

Binds 1 heme group per subunit.UniRule annotation

Interactioni

Protein-protein interaction databases

DIPiDIP-60329N.
STRINGi5664.LmjF.16.1320.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DY9X-ray2.08A1-113[»]
4GEDX-ray1.84B1-113[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 113102Cytochrome cInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cytochrome c family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3453. Eukaryota.
COG3474. LUCA.
HOGENOMiHOG000009762.
KOiK08738.
OMAiHEYLRNP.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
[Graphical view]
PANTHERiPTHR11961. PTHR11961. 1 hit.
PfamiPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSiPR00604. CYTCHRMECIAB.
SUPFAMiSSF46626. SSF46626. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4QEN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKARAPLP PGDVERGEKL FKGRAAQCHT ATKGGSNGVG PNLFGIVNRP
60 70 80 90 100
SGKVEGFTYS KANAESGVIW TPEVLDVYLE NPKKFMPGTK MSFAGIKKPQ
110
ERADVIAYLE TLK
Length:113
Mass (Da):12,188
Last modified:July 19, 2005 - v1
Checksum:iBC43840926FF0405
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY971584 mRNA. Translation: AAY40864.1.
FR796412 Genomic DNA. Translation: CAJ04011.1.
FR796412 Genomic DNA. Translation: CAJ04013.1.
RefSeqiXP_001682212.1. XM_001682160.1.
XP_001682213.1. XM_001682161.1.

Genome annotation databases

EnsemblProtistsiLmjF.16.1310:mRNA; LmjF.16.1310:pep; LmjF.16.1310.
LmjF.16.1320:mRNA; LmjF.16.1320:pep; LmjF.16.1320.
GeneIDi5650682.
5650683.
KEGGilma:LMJF_16_1310.
lma:LMJF_16_1320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY971584 mRNA. Translation: AAY40864.1.
FR796412 Genomic DNA. Translation: CAJ04011.1.
FR796412 Genomic DNA. Translation: CAJ04013.1.
RefSeqiXP_001682212.1. XM_001682160.1.
XP_001682213.1. XM_001682161.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DY9X-ray2.08A1-113[»]
4GEDX-ray1.84B1-113[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60329N.
STRINGi5664.LmjF.16.1320.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiLmjF.16.1310:mRNA; LmjF.16.1310:pep; LmjF.16.1310.
LmjF.16.1320:mRNA; LmjF.16.1320:pep; LmjF.16.1320.
GeneIDi5650682.
5650683.
KEGGilma:LMJF_16_1310.
lma:LMJF_16_1320.

Phylogenomic databases

eggNOGiKOG3453. Eukaryota.
COG3474. LUCA.
HOGENOMiHOG000009762.
KOiK08738.
OMAiHEYLRNP.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
[Graphical view]
PANTHERiPTHR11961. PTHR11961. 1 hit.
PfamiPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSiPR00604. CYTCHRMECIAB.
SUPFAMiSSF46626. SSF46626. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the kinetoplastid parasite, Leishmania major."
    Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G.
    , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., Myler P.J.
    Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FriedlinImported and MHOM/IL/81/FriedlinImported.
  2. "Identification of excreted/secreted proteins of Leishmania major."
    Chenik M., Lakhal S., Louzir H., Dellagi K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FriedlinImported and MHOM/IL/81/FriedlinImported.
  4. Zhao B.P., Ren Z.A., Li C.D.
    Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FriedlinImported.
  5. "Leishmania major peroxidase is a cytochrome c peroxidase."
    Jasion V.S., Poulos T.L.
    Biochemistry 51:2453-2460(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) IN COMPLEX WITH HEME.
  6. "Crystal structure of the Leishmania major peroxidase-cytochrome c complex."
    Jasion V.S., Doukov T., Pineda S.H., Li H., Poulos T.L.
    Proc. Natl. Acad. Sci. U.S.A. 109:18390-18394(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH HEME.

Entry informationi

Entry nameiQ4QEN5_LEIMA
AccessioniPrimary (citable) accession number: Q4QEN5
Secondary accession number(s): A0PJ38
Entry historyi
Integrated into UniProtKB/TrEMBL: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 16, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.