Reviewed, UniProtKB/Swiss-Prot Q5KIK5 (CCPR_CRYNE)

Names and origin

Protein names

Recommended name:
    Cytochrome c peroxidase, mitochondrial
      Short name=CCP
    EC=1.11.1.5

Gene names

Name:	CCP1
Ordered Locus Names:	CND02630, CNBD3710

Organism

Cryptococcus neoformans (Filobasidiella neoformans) [Complete proteome]

Taxonomic identifier

5207 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity.
Catalytic activity	2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.
Subunit structure	Forms a one-to-one complex with cytochrome c By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytochrome-c peroxidase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 17	17	Mitochondrion Potential
	Chain	18 – 377	360	Cytochrome c peroxidase, mitochondrial		PRO_0000045289
Sites
	Active site	138	1	Proton acceptor By similarity
	Active site	277	1	Tryptophan radical intermediate By similarity
	Metal binding	261	1	Iron (heme axial ligand)
	Site	134	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5KIK5-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 23FFFFF4EF188CB4	FASTA	377	42,112
	10 20 30 40 50 60 MSFRAPNLIR SAAGRRASQT LNLRSQVIRR RFATEGGPEI TKPSSPRSSN TRYLLAGVGI 70 80 90 100 110 120 AAVGAAYYFY GTGRTAHDSA NKADTVVRGA VATVEAKTGL RRGKDEYQKV YNRIAETLEK 130 140 150 160 170 180 EGYDDGSLAP VLLRLAWHSS GTYNKEDGTG GSNFATMRFK PEAEHSANNG LHVAREHMEK 190 200 210 220 230 240 IKQEFPWISY GDLWTLGGVC AVQESGGPTI PWRPGRIDGF EAQVTPDGRL PDASQAQDHL 250 260 270 280 290 300 RFIFNRMGFN DQEIVALSGA HAMGRCHTNR SGFEGPWTFS PVTFSNQYFA LLRDEPWQWK 310 320 330 340 350 360 KWTGPAQYED KNTKTLMMLP TDMALLKDKS FKKYVDIYAD NEEKFFSDFA KAFSKLIELG 370 VPERQWAGEP WTLGTSD

References

[1]

"The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans." Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S. , Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W. Science 307:1321-1324(2005) [PubMed: 15653466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B-3501A and JEC21.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017344 Genomic DNA. Translation: AAW42936.1. AAEY01000020 Genomic DNA. Translation: EAL21317.1.
RefSeq	XP_570243.1. XP_775964.1.
UniGene	Fne.3348
3D structure databases
SMR	Q5KIK5. Positions 91-377.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5KIK5.
Protein family/group databases
PeroxiBase	2357. CnCcP01_JEC21.
Genome annotation databases
GeneID	3257130. 4935760.
GenomeReviews	Gene locus CND02630 in contig AE017344_GR.
KEGG	cnb:CNBD3710. cne:CND02630.
Phylogenomic databases
eggNOG	fuNOG05104.
HOGENOM	HBG597790.
OMA	ATMRFAP.
OrthoDB	EOG92JQ7X.
PhylomeDB	Q5KIK5.
Enzyme and pathway databases
BRENDA	1.11.1.5. 2772.
Family and domain databases
InterPro	IPR002207. Asc_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CCPR_CRYNE

Accession

Primary (citable) accession number: Q5KIK5
Secondary accession number(s): Q55TT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	February 15, 2005
Last modified:	February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)