P00431 (CCPR_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	CCP1
Synonyms:	CCP, CPO
Ordered Locus Names:	YKR066C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Catalytic activity	2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subunit structure	Forms a one-to-one complex with cytochrome c.
Subcellular location	Mitochondrion matrix.
Miscellaneous	Present with 6730 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Organic radical Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to oxidative stress Inferred from mutant phenotype PubMed 10589830. Source: SGD hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial intermembrane space Inferred from direct assay PubMed 6290489. Source: SGD mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cytochrome-c peroxidase activity Inferred from direct assay PubMed 17580971PubMed 21334283. Source: SGD heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CYC1	P00044	2	EBI-4389,EBI-5393

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 67

67

Mitochondrion Ref.6

Chain

68 – 361

294

Cytochrome c peroxidase, mitochondrial

PRO_0000023634

Sites

Active site

119

1

Proton acceptor

Active site

258

1

Tryptophan radical intermediate

Metal binding

242

1

Iron (heme axial ligand)

Site

115

1

Transition state stabilizer

Amino acid modifications

Modified residue

220

1

Phosphotyrosine Ref.10

Natural variations

Natural variant

33

1

A → AA in allele 2.

Natural variant

120

1

T → I in allele 2.

Natural variant

219

1

D → G in allele 2.

Experimental info

Mutagenesis

258

1

W → F: Substantially diminished activity. Ref.8

Sequence conflict

41

1

Q → H in AAA88709. Ref.3

Sequence conflict

62

1

A → P in AAA88709. Ref.3

Sequence conflict

145 – 146

2

ND → DN AA sequence Ref.6

Sequence conflict

231

1

Missing AA sequence Ref.6

Sequence conflict

273

1

L → M in AAS56247. Ref.5

Secondary structure

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361

Helix Strand Turn

Details...

Helix

83 – 99

17

Turn

100 – 102

3

Helix

103 – 106

4

Helix

110 – 121

12

Turn

126 – 128

3

Beta strand

131 – 133

3

Helix

137 – 139

3

Helix

141 – 144

4

Helix

147 – 149

3

Turn

150 – 152

3

Helix

153 – 165

13

Beta strand

167 – 169

3

Helix

171 – 185

15

Helix

202 – 204

3

Turn

208 – 210

3

Helix

218 – 226

9

Turn

227 – 229

3

Helix

232 – 239

8

Helix

240 – 243

4

Beta strand

244 – 247

4

Helix

249 – 252

4

Beta strand

256 – 260

5

Beta strand

262 – 264

3

Helix

268 – 275

8

Beta strand

278 – 282

5

Beta strand

284 – 286

3

Beta strand

288 – 292

5

Turn

293 – 295

3

Beta strand

296 – 298

3

Helix

300 – 307

8

Helix

309 – 319

11

Helix

322 – 338

17

Beta strand

345 – 347

3

Helix

356 – 359

4

Sequences

	Sequence		Length	Mass (Da)
	P00431 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: A5D26385DA6F0A0B	FASTA	361	40,353
	10 20 30 40 50 60 MTTAVRLLPS LGRTAHKRSL YLFSAAAAAA AAATFAYSQS QKRSSSSPGG GSNHGWNNWG 70 80 90 100 110 120 KAAALASTTP LVHVASVEKG RSYEDFQKVY NAIALKLRED DEYDNYIGYG PVLVRLAWHT 130 140 150 160 170 180 SGTWDKHDNT GGSYGGTYRF KKEFNDPSNA GLQNGFKFLE PIHKEFPWIS SGDLFSLGGV 190 200 210 220 230 240 TAVQEMQGPK IPWRCGRVDT PEDTTPDNGR LPDADKDADY VRTFFQRLNM NDREVVALMG 250 260 270 280 290 300 AHALGKTHLK NSGYEGPWGA ANNVFTNEFY LNLLNEDWKL EKNDANNEQW DSKSGYMMLP 310 320 330 340 350 360 TDYSLIQDPK YLSIVKEYAN DQDKFFKDFS KAFEKLLENG ITFPKDAPSP FIFKTLEEQG L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre sequence for protein transport into mitochondria." Kaput J., Goltz S., Blobel G. J. Biol. Chem. 257:15054-15058(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation and sequence analysis of a second allele of the yeast nuclear gene cytochrome C peroxidase." Piattoni M., Miyazaki W., Jayaraman K., Kaput J. Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DBY939.
[3]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence." Takio K., Titani K., Ericsson L.H., Yonetani T. Arch. Biochem. Biophys. 203:615-629(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 68-361.
[7]	"Isolation of the yeast nuclear gene encoding the mitochondrial protein, cytochrome c peroxidase." Goltz S., Kaput J., Blobel G. J. Biol. Chem. 257:11186-11190(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-332.
[8]	"Tryptophan-191-->phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation." Mauro J.M., Fishel L.A., Hazzard J.T., Meyer T.E., Tollin G., Cusanovich M.A., Kraut J. Biochemistry 27:6243-6256(1988) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TRP-258.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-220, MASS SPECTROMETRY.
[11]	"Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution." Finzel B.C., Poulos T.L., Kraut J. J. Biol. Chem. 259:13027-13036(1984) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[12]	"X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis." Wang J.M., Mauro M., Edwards S.L., Oatley S.J., Fishel L.A., Ashford V.A., Xuong N.-H., Kraut J. Biochemistry 29:7160-7173(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS.
[13]	"The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme." Goodin D.B., McRee D.E. Biochemistry 32:3313-3324(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[14]	"A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity." Fitzgerald M.M., Musah R.A., McRee D.E., Goodin D.B. Nat. Struct. Biol. 3:626-631(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[15]	"Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase." Hirst J., Goodin D.B. J. Biol. Chem. 275:8582-8591(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
[16]	"Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure." Hirst J., Wilcox S.K., Williams P.A., Blankenship J., McRee D.E., Goodin D.B. Biochemistry 40:1265-1273(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01468 Genomic DNA. Translation: AAA88709.1.
X62422 Genomic DNA. Translation: CAA44288.1.
Z28291 Genomic DNA. Translation: CAA82145.1.
AY557921 Genomic DNA. Translation: AAS56247.1.
J01321 Genomic DNA. Translation: AAA88710.1.
BK006944 Genomic DNA. Translation: DAA09217.1.

PIR

OPBYC. S19064.

RefSeq

NP_012992.1. NM_001179856.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A2F	X-ray	2.10	A	71-361	[»]
1A2G	X-ray	2.10	A	71-361	[»]
1AA4	X-ray	2.10	A	71-361	[»]
1AC4	X-ray	2.10	A	71-361	[»]
1AC8	X-ray	2.10	A	71-361	[»]
1AEB	X-ray	2.10	A	71-361	[»]
1AED	X-ray	2.10	A	71-361	[»]
1AEE	X-ray	2.10	A	71-361	[»]
1AEF	X-ray	2.10	A	71-361	[»]
1AEG	X-ray	2.10	A	71-361	[»]
1AEH	X-ray	2.10	A	71-361	[»]
1AEJ	X-ray	2.10	A	71-361	[»]
1AEK	X-ray	2.10	A	71-361	[»]
1AEM	X-ray	2.10	A	71-361	[»]
1AEN	X-ray	2.10	A	71-361	[»]
1AEO	X-ray	2.10	A	71-361	[»]
1AEQ	X-ray	2.10	A	71-361	[»]
1AES	X-ray	2.10	A	71-361	[»]
1AET	X-ray	2.10	A	71-361	[»]
1AEU	X-ray	2.10	A	71-361	[»]
1AEV	X-ray	2.10	A	71-361	[»]
1BEJ	X-ray	2.40	A	71-361	[»]
1BEK	X-ray	2.20	A	71-361	[»]
1BEM	X-ray	2.20	A	71-361	[»]
1BEP	X-ray	2.20	A	71-361	[»]
1BEQ	X-ray	2.16	A	71-361	[»]
1BES	X-ray	2.00	A	71-361	[»]
1BJ9	X-ray	2.20	A	71-361	[»]
1BVA	X-ray	1.89	A	71-361	[»]
1CCA	X-ray	1.80	A	68-361	[»]
1CCB	X-ray	2.10	A	68-361	[»]
1CCC	X-ray	2.00	A	68-361	[»]
1CCE	X-ray	2.30	A	71-361	[»]
1CCG	X-ray	2.10	A	71-361	[»]
1CCI	X-ray	2.40	A	71-361	[»]
1CCJ	X-ray	2.10	A	71-361	[»]
1CCK	X-ray	2.10	A	71-361	[»]
1CCL	X-ray	2.00	A	71-361	[»]
1CCP	X-ray	2.20	A	68-361	[»]
1CMP	X-ray	1.90	A	71-361	[»]
1CMQ	X-ray	2.30	A	71-361	[»]
1CMT	X-ray	2.10	A	71-361	[»]
1CMU	X-ray	2.10	A	71-361	[»]
1CPD	X-ray	2.20	A	68-361	[»]
1CPE	X-ray	2.20	A	68-361	[»]
1CPF	X-ray	2.20	A	68-361	[»]
1CPG	X-ray	2.20	A	71-361	[»]
1CYF	X-ray	2.35	A	68-361	[»]
1DCC	X-ray	2.20	A	68-361	[»]
1DJ1	X-ray	1.93	A	71-361	[»]
1DJ5	X-ray	1.93	A	71-361	[»]
1DS4	X-ray	2.02	A	71-361	[»]
1DSE	X-ray	2.00	A	71-361	[»]
1DSG	X-ray	2.56	A	71-361	[»]
1DSO	X-ray	2.03	A	71-361	[»]
1DSP	X-ray	2.03	A	71-361	[»]
1EBE	X-ray	2.20	A	68-361	[»]
1JCI	X-ray	1.90	A	68-361	[»]
1JDR	X-ray	1.50	A	68-361	[»]
1KOK	X-ray	1.70	A	68-361	[»]
1KRJ	X-ray	2.00	A	68-361	[»]
1KXM	X-ray	1.74	A	71-361	[»]
1KXN	X-ray	1.80	A	71-361	[»]
1MK8	X-ray	1.65	A	68-361	[»]
1MKQ	X-ray	1.64	A	68-361	[»]
1MKR	X-ray	1.58	A	68-361	[»]
1ML2	X-ray	1.65	A	68-361	[»]
1RYC	X-ray	1.80	A	71-361	[»]
1S6V	X-ray	1.88	A/C	68-361	[»]
1S73	X-ray	1.53	A	68-361	[»]
1SBM	X-ray	1.69	A	68-361	[»]
1SDQ	X-ray	1.69	A	68-361	[»]
1SOG	X-ray	1.85	A	68-361	[»]
1STQ	X-ray	1.82	A	68-361	[»]
1U74	X-ray	2.40	A/C	68-361	[»]
1U75	X-ray	2.55	A/C	68-361	[»]
1Z53	X-ray	1.13	A	68-361	[»]
1ZBY	X-ray	1.20	A	68-361	[»]
1ZBZ	X-ray	1.29	A	68-361	[»]
2ANZ	X-ray	1.75	A	71-361	[»]
2AQD	X-ray	1.35	A	71-361	[»]
2AS1	X-ray	1.55	A	71-361	[»]
2AS2	X-ray	1.45	A	71-361	[»]
2AS3	X-ray	1.40	A	71-361	[»]
2AS4	X-ray	1.30	A	71-361	[»]
2AS6	X-ray	1.45	A	71-361	[»]
2B0Z	X-ray	2.70	A	68-361	[»]
2B10	X-ray	2.80	A/C	68-361	[»]
2B11	X-ray	2.30	A/C	68-361	[»]
2B12	X-ray	3.02	A	68-361	[»]
2BCN	X-ray	1.70	A/C	68-361	[»]
2CCP	X-ray	2.20	A	68-361	[»]
2CEP	X-ray	2.20	A	68-361	[»]
2CYP	X-ray	1.70	A	68-361	[»]
2EUN	X-ray	1.70	A	71-361	[»]
2EUO	X-ray	1.45	A	71-361	[»]
2EUP	X-ray	1.40	A	71-361	[»]
2EUQ	X-ray	1.30	A	71-361	[»]
2EUR	X-ray	1.39	A	71-361	[»]
2EUS	X-ray	1.55	A	71-361	[»]
2EUT	X-ray	1.12	A	71-361	[»]
2EUU	X-ray	1.45	A	71-361	[»]
2GB8	NMR	-	A	68-361	[»]
2IA8	X-ray	1.48	A	71-361	[»]
2ICV	X-ray	1.60	A	71-361	[»]
2JTI	NMR	-	A	68-361	[»]
2PCB	X-ray	2.80	A/C	68-361	[»]
2PCC	X-ray	2.30	A/C	68-361	[»]
2RBT	X-ray	1.24	X	71-361	[»]
2RBU	X-ray	1.80	X	71-361	[»]
2RBV	X-ray	1.39	X	71-361	[»]
2RBW	X-ray	1.50	X	71-361	[»]
2RBX	X-ray	1.50	X	71-361	[»]
2RBY	X-ray	1.50	X	71-361	[»]
2RBZ	X-ray	1.80	X	71-361	[»]
2RC0	X-ray	1.50	X	71-361	[»]
2RC1	X-ray	2.49	X	71-361	[»]
2RC2	X-ray	1.50	X	71-361	[»]
2V23	X-ray	1.80	A	68-361	[»]
2V2E	X-ray	1.68	A	71-361	[»]
2X07	X-ray	1.86	A	69-361	[»]
2X08	X-ray	2.01	A	69-361	[»]
2XIL	X-ray	1.68	A	71-361	[»]
2XJ5	X-ray	1.69	A	71-361	[»]
2XJ8	X-ray	1.69	A	71-361	[»]
2Y5A	X-ray	1.25	A	71-361	[»]
2YCG	X-ray	1.81	A	68-361	[»]
3CCP	X-ray	2.20	A	68-361	[»]
3CCX	X-ray	2.30	A	71-361	[»]
3E2N	X-ray	1.30	A	68-361	[»]
3E2O	X-ray	1.06	A	68-361	[»]
3EXB	X-ray	1.60	A	68-361	[»]
3M23	X-ray	1.40	A	71-361	[»]
3M25	X-ray	1.40	A	71-361	[»]
3M26	X-ray	1.40	A	71-361	[»]
3M27	X-ray	1.40	A	71-361	[»]
3M28	X-ray	1.40	A	71-361	[»]
3M29	X-ray	1.40	A	71-361	[»]
3M2A	X-ray	1.40	A	71-361	[»]
3M2B	X-ray	1.40	A	71-361	[»]
3M2C	X-ray	1.40	A	71-361	[»]
3M2D	X-ray	1.40	A	71-361	[»]
3M2E	X-ray	1.40	A	71-361	[»]
3M2F	X-ray	1.40	A	71-361	[»]
3M2G	X-ray	1.40	A	71-361	[»]
3M2H	X-ray	1.40	A	71-361	[»]
3M2I	X-ray	1.40	A	71-361	[»]
3R98	Other	2.40	A	69-361	[»]
3R99	Other	2.40	A	69-361	[»]
4A6Z	X-ray	1.61	A	68-361	[»]
4A71	X-ray	1.61	A	68-361	[»]
4A78	X-ray	2.01	A	68-361	[»]
4A7M	X-ray	1.71	A	68-361	[»]
4CCP	X-ray	2.20	A	68-361	[»]
4CCX	X-ray	1.90	A	71-361	[»]
5CCP	X-ray	2.20	A	68-361	[»]
6CCP	X-ray	2.20	A	68-361	[»]
7CCP	X-ray	2.20	A	68-361	[»]

ProteinModelPortal

P00431.

SMR

P00431. Positions 43-361.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6251N.

IntAct

P00431. 4 interactions.

MINT

MINT-598890.

STRING

4932.YKR066C.

Protein family/group databases

PeroxiBase

2361. SceCcP01.

Proteomic databases

PaxDb

P00431.

PeptideAtlas

P00431.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YKR066C; YKR066C; YKR066C.

GeneID

853940.

KEGG

sce:YKR066C.

Organism-specific databases

CYGD

YKR066c.

SGD

S000001774. CCP1.

Phylogenomic databases

eggNOG

COG0376.

HOGENOM

HOG000189824.

KO

K00428.

OMA

HALGKTH.

OrthoDB

EOG49GPRM.

Enzyme and pathway databases

SABIO-RK

P00431.

Gene expression databases

Genevestigator

P00431.

GermOnline

YKR066C. Saccharomyces cerevisiae.

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.

SUPFAM

SSF48113. Peroxidase_super. 1 hit.

PROSITE

PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00431.

NextBio

975327.

PMAP-CutDB

P00431.

Entry information

Entry name

CCPR_YEAST

Accession

Primary (citable) accession number: P00431
Secondary accession number(s): D6VXC7, Q6Q5M9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 152 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program