ID CCPR_CRYNE Reviewed; 377 AA. AC Q5KIK5; Q55TT2; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 04-NOV-2008, entry version 34. DE RecName: Full=Cytochrome c peroxidase, mitochondrial; DE Short=CCP; DE EC=1.11.1.5; DE Flags: Precursor; GN Name=CCP1; OrderedLocusNames=CND02630, CNBD3710; OS Cryptococcus neoformans (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella; OC Filobasidiella/Cryptococcus neoformans species complex. OX NCBI_TaxID=5207; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-3501A, and JEC21; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., RA D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., RA Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., RA Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., RA Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., RA Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., RA Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., RA Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., RA Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen RT Cryptococcus neoformans."; RL Science 307:1321-1324(2005). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems (By similarity). CC -!- CATALYTIC ACTIVITY: 2 ferrocytochrome c + H(2)O(2) = 2 CC ferricytochrome c + 2 H(2)O. CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per CC subunit (By similarity). CC -!- SUBUNIT: Forms a one-to-one complex with cytochrome c (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c CC peroxidase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017344; AAW42936.1; -; Genomic_DNA. DR EMBL; AAEY01000020; EAL21317.1; -; Genomic_DNA. DR RefSeq; XP_570243.1; -. DR RefSeq; XP_775964.1; -. DR UniGene; Fne.3348; -. DR PeroxiBase; 2357; CnCcP01_JEC21. DR GeneID; 3257130; -. DR GeneID; 4935760; -. DR GenomeReviews; AE017344_GR; CND02630. DR KEGG; cnb:CNBD3710; -. DR KEGG; cne:CND02630; -. DR HOGENOM; Q5KIK5; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:EC. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002207; Asc_perxdse. DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00459; ASPEROXIDASE. DR PRINTS; PR00458; PEROXIDASE. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 3: Inferred from homology; KW Complete proteome; Heme; Iron; Metal-binding; Mitochondrion; KW Oxidoreductase; Peroxidase; Transit peptide. FT TRANSIT 1 17 Mitochondrion (Potential). FT CHAIN 18 377 Cytochrome c peroxidase, mitochondrial. FT /FTId=PRO_0000045289. FT ACT_SITE 138 138 Proton acceptor (By similarity). FT ACT_SITE 277 277 Tryptophan radical intermediate (By FT similarity). FT METAL 261 261 Iron (heme axial ligand). FT SITE 134 134 Transition state stabilizer (By FT similarity). SQ SEQUENCE 377 AA; 42112 MW; 23FFFFF4EF188CB4 CRC64; MSFRAPNLIR SAAGRRASQT LNLRSQVIRR RFATEGGPEI TKPSSPRSSN TRYLLAGVGI AAVGAAYYFY GTGRTAHDSA NKADTVVRGA VATVEAKTGL RRGKDEYQKV YNRIAETLEK EGYDDGSLAP VLLRLAWHSS GTYNKEDGTG GSNFATMRFK PEAEHSANNG LHVAREHMEK IKQEFPWISY GDLWTLGGVC AVQESGGPTI PWRPGRIDGF EAQVTPDGRL PDASQAQDHL RFIFNRMGFN DQEIVALSGA HAMGRCHTNR SGFEGPWTFS PVTFSNQYFA LLRDEPWQWK KWTGPAQYED KNTKTLMMLP TDMALLKDKS FKKYVDIYAD NEEKFFSDFA KAFSKLIELG VPERQWAGEP WTLGTSD //