Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytochrome c peroxidase, mitochondrial

Gene

CCP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O.

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei115Transition state stabilizer1
Active sitei119Proton acceptor1
Metal bindingi242Iron (heme axial ligand)1
Active sitei258Tryptophan radical intermediate1

GO - Molecular functioni

  • cytochrome-c peroxidase activity Source: SGD
  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to oxidative stress Source: SGD
  • hydrogen peroxide catabolic process Source: GO_Central
  • response to reactive oxygen species Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YKR066C-MONOMER.
BRENDAi1.11.1.5. 984.
SABIO-RKP00431.

Protein family/group databases

PeroxiBasei2361. SceCcP01.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c peroxidase, mitochondrial (EC:1.11.1.5)
Short name:
CCP
Gene namesi
Name:CCP1
Synonyms:CCP, CPO
Ordered Locus Names:YKR066C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR066C.
SGDiS000001774. CCP1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial intermembrane space Source: SGD
  • mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi258W → F: Substantially diminished activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 67Mitochondrion1 PublicationAdd BLAST67
ChainiPRO_000002363468 – 361Cytochrome c peroxidase, mitochondrialAdd BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei220PhosphotyrosineCombined sources1

Keywords - PTMi

Organic radical, Phosphoprotein

Proteomic databases

MaxQBiP00431.
PRIDEiP00431.

PTM databases

iPTMnetiP00431.

Miscellaneous databases

PMAP-CutDBP00431.

Interactioni

Subunit structurei

Forms a one-to-one complex with cytochrome c.

Binary interactionsi

WithEntry#Exp.IntActNotes
CYC1P000443EBI-4389,EBI-5393

Protein-protein interaction databases

BioGridi34197. 23 interactors.
DIPiDIP-6251N.
IntActiP00431. 5 interactors.
MINTiMINT-598890.

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi83 – 99Combined sources17
Turni100 – 102Combined sources3
Helixi103 – 106Combined sources4
Helixi110 – 121Combined sources12
Turni126 – 128Combined sources3
Beta strandi131 – 133Combined sources3
Helixi137 – 139Combined sources3
Helixi141 – 144Combined sources4
Helixi147 – 149Combined sources3
Turni150 – 152Combined sources3
Helixi153 – 165Combined sources13
Beta strandi167 – 169Combined sources3
Helixi171 – 185Combined sources15
Helixi202 – 204Combined sources3
Turni208 – 210Combined sources3
Helixi218 – 226Combined sources9
Turni227 – 229Combined sources3
Helixi232 – 239Combined sources8
Helixi240 – 243Combined sources4
Beta strandi244 – 247Combined sources4
Helixi249 – 252Combined sources4
Beta strandi256 – 260Combined sources5
Beta strandi262 – 264Combined sources3
Helixi268 – 275Combined sources8
Beta strandi278 – 282Combined sources5
Beta strandi284 – 286Combined sources3
Beta strandi288 – 292Combined sources5
Turni293 – 295Combined sources3
Beta strandi296 – 298Combined sources3
Helixi300 – 307Combined sources8
Helixi309 – 319Combined sources11
Helixi322 – 338Combined sources17
Beta strandi345 – 347Combined sources3
Helixi356 – 359Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2FX-ray2.10A71-361[»]
1A2GX-ray2.10A71-361[»]
1AA4X-ray2.10A71-361[»]
1AC4X-ray2.10A71-361[»]
1AC8X-ray2.10A71-361[»]
1AEBX-ray2.10A71-361[»]
1AEDX-ray2.10A71-361[»]
1AEEX-ray2.10A71-361[»]
1AEFX-ray2.10A71-361[»]
1AEGX-ray2.10A71-361[»]
1AEHX-ray2.10A71-361[»]
1AEJX-ray2.10A71-361[»]
1AEKX-ray2.10A71-361[»]
1AEMX-ray2.10A71-361[»]
1AENX-ray2.10A71-361[»]
1AEOX-ray2.10A71-361[»]
1AEQX-ray2.10A71-361[»]
1AESX-ray2.10A71-361[»]
1AETX-ray2.10A71-361[»]
1AEUX-ray2.10A71-361[»]
1AEVX-ray2.10A71-361[»]
1BEJX-ray2.40A71-361[»]
1BEKX-ray2.20A71-361[»]
1BEMX-ray2.20A71-361[»]
1BEPX-ray2.20A71-361[»]
1BEQX-ray2.16A71-361[»]
1BESX-ray2.00A71-361[»]
1BJ9X-ray2.20A71-361[»]
1BVAX-ray1.89A71-361[»]
1CCAX-ray1.80A68-361[»]
1CCBX-ray2.10A68-361[»]
1CCCX-ray2.00A68-361[»]
1CCEX-ray2.30A71-361[»]
1CCGX-ray2.10A71-361[»]
1CCIX-ray2.40A71-361[»]
1CCJX-ray2.10A71-361[»]
1CCKX-ray2.10A71-361[»]
1CCLX-ray2.00A71-361[»]
1CCPX-ray2.20A68-361[»]
1CMPX-ray1.90A71-361[»]
1CMQX-ray2.30A71-361[»]
1CMTX-ray2.10A71-361[»]
1CMUX-ray2.10A71-361[»]
1CPDX-ray2.20A68-361[»]
1CPEX-ray2.20A68-361[»]
1CPFX-ray2.20A68-361[»]
1CPGX-ray2.20A71-361[»]
1CYFX-ray2.35A68-361[»]
1DCCX-ray2.20A68-361[»]
1DJ1X-ray1.93A71-361[»]
1DJ5X-ray1.93A71-361[»]
1DS4X-ray2.02A71-361[»]
1DSEX-ray2.00A71-361[»]
1DSGX-ray2.56A71-361[»]
1DSOX-ray2.03A71-361[»]
1DSPX-ray2.03A71-361[»]
1EBEX-ray2.20A68-361[»]
1JCIX-ray1.90A68-361[»]
1JDRX-ray1.50A68-361[»]
1KOKX-ray1.70A68-361[»]
1KRJX-ray2.00A68-361[»]
1KXMX-ray1.74A71-361[»]
1KXNX-ray1.80A71-361[»]
1MK8X-ray1.65A68-361[»]
1MKQX-ray1.64A68-361[»]
1MKRX-ray1.58A68-361[»]
1ML2X-ray1.65A68-361[»]
1RYCX-ray1.80A71-361[»]
1S6VX-ray1.88A/C68-361[»]
1S73X-ray1.53A68-361[»]
1SBMX-ray1.69A68-361[»]
1SDQX-ray1.69A68-361[»]
1SOGX-ray1.85A68-361[»]
1STQX-ray1.82A68-361[»]
1U74X-ray2.40A/C68-361[»]
1U75X-ray2.55A/C68-361[»]
1Z53X-ray1.13A68-361[»]
1ZBYX-ray1.20A68-361[»]
1ZBZX-ray1.29A68-361[»]
2ANZX-ray1.75A71-361[»]
2AQDX-ray1.35A71-361[»]
2AS1X-ray1.55A71-361[»]
2AS2X-ray1.45A71-361[»]
2AS3X-ray1.40A71-361[»]
2AS4X-ray1.30A71-361[»]
2AS6X-ray1.45A71-361[»]
2B0ZX-ray2.70A68-361[»]
2B10X-ray2.80A/C68-361[»]
2B11X-ray2.30A/C68-361[»]
2B12X-ray3.02A68-361[»]
2BCNX-ray1.70A/C68-361[»]
2CCPX-ray2.20A68-361[»]
2CEPX-ray2.20A68-361[»]
2CYPX-ray1.70A68-361[»]
2EUNX-ray1.70A71-361[»]
2EUOX-ray1.45A71-361[»]
2EUPX-ray1.40A71-361[»]
2EUQX-ray1.30A71-361[»]
2EURX-ray1.39A71-361[»]
2EUSX-ray1.55A71-361[»]
2EUTX-ray1.12A71-361[»]
2EUUX-ray1.45A71-361[»]
2GB8NMR-A68-361[»]
2IA8X-ray1.48A71-361[»]
2ICVX-ray1.60A71-361[»]
2JTINMR-A68-361[»]
2N18NMR-A68-361[»]
2PCBX-ray2.80A/C68-361[»]
2PCCX-ray2.30A/C68-361[»]
2RBTX-ray1.24X71-361[»]
2RBUX-ray1.80X71-361[»]
2RBVX-ray1.39X71-361[»]
2RBWX-ray1.50X71-361[»]
2RBXX-ray1.50X71-361[»]
2RBYX-ray1.50X71-361[»]
2RBZX-ray1.80X71-361[»]
2RC0X-ray1.50X71-361[»]
2RC1X-ray2.49X71-361[»]
2RC2X-ray1.50X71-361[»]
2V23X-ray1.80A68-361[»]
2V2EX-ray1.68A71-361[»]
2X07X-ray1.86A69-361[»]
2X08X-ray2.01A69-361[»]
2XILX-ray1.68A71-361[»]
2XJ5X-ray1.69A71-361[»]
2XJ8X-ray1.69A71-361[»]
2Y5AX-ray1.25A71-361[»]
2YCGX-ray1.81A68-361[»]
3CCPX-ray2.20A68-361[»]
3CCXX-ray2.30A71-361[»]
3E2NX-ray1.30A68-96[»]
A110-361[»]
3E2OX-ray1.06A68-361[»]
3EXBX-ray1.60A68-361[»]
3M23X-ray1.40A71-361[»]
3M25X-ray1.40A71-361[»]
3M26X-ray1.40A71-361[»]
3M27X-ray1.40A71-361[»]
3M28X-ray1.40A71-361[»]
3M29X-ray1.40A71-361[»]
3M2AX-ray1.40A71-361[»]
3M2BX-ray1.40A71-361[»]
3M2CX-ray1.40A71-361[»]
3M2DX-ray1.40A71-361[»]
3M2EX-ray1.40A71-361[»]
3M2FX-ray1.40A71-361[»]
3M2GX-ray1.40A71-361[»]
3M2HX-ray1.40A71-361[»]
3M2IX-ray1.40A71-361[»]
3R98Other2.40A69-361[»]
3R99Other2.40A69-361[»]
4A6ZX-ray1.61A68-361[»]
4A71X-ray1.61A68-361[»]
4A78X-ray2.01A68-361[»]
4A7MX-ray1.71A68-361[»]
4CCPX-ray2.20A68-361[»]
4CCXX-ray1.90A71-361[»]
4CVIOther2.10A70-361[»]
4CVJOther2.18A71-361[»]
4JB4X-ray2.39A/C68-361[»]
4NFGX-ray2.11A71-361[»]
4P4QX-ray2.01A/C68-361[»]
4XV4X-ray1.69A71-361[»]
4XV5X-ray1.65A71-361[»]
4XV6X-ray1.55A71-361[»]
4XV7X-ray1.62A71-361[»]
4XV8X-ray1.57A71-361[»]
4XVAX-ray2.66A/C/E/G69-361[»]
5CCPX-ray2.20A68-361[»]
5CIBX-ray3.01A/C68-361[»]
5CICX-ray2.10A/C68-361[»]
5CIDX-ray2.76A/C68-361[»]
5CIEX-ray2.60A/C68-361[»]
5CIFX-ray2.01A/C68-361[»]
5CIGX-ray2.06A/C68-361[»]
5CIHX-ray2.60A/C68-361[»]
5D6MX-ray1.65A71-361[»]
5EJTX-ray1.55A68-361[»]
5EJXX-ray1.50A68-361[»]
6CCPX-ray2.20A68-361[»]
7CCPX-ray2.20A68-361[»]
ProteinModelPortaliP00431.
SMRiP00431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00431.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000189824.
InParanoidiP00431.
KOiK00428.
OMAiVCAIQEM.
OrthoDBiEOG092C3FU5.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00431-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTAVRLLPS LGRTAHKRSL YLFSAAAAAA AAATFAYSQS QKRSSSSPGG
60 70 80 90 100
GSNHGWNNWG KAAALASTTP LVHVASVEKG RSYEDFQKVY NAIALKLRED
110 120 130 140 150
DEYDNYIGYG PVLVRLAWHT SGTWDKHDNT GGSYGGTYRF KKEFNDPSNA
160 170 180 190 200
GLQNGFKFLE PIHKEFPWIS SGDLFSLGGV TAVQEMQGPK IPWRCGRVDT
210 220 230 240 250
PEDTTPDNGR LPDADKDADY VRTFFQRLNM NDREVVALMG AHALGKTHLK
260 270 280 290 300
NSGYEGPWGA ANNVFTNEFY LNLLNEDWKL EKNDANNEQW DSKSGYMMLP
310 320 330 340 350
TDYSLIQDPK YLSIVKEYAN DQDKFFKDFS KAFEKLLENG ITFPKDAPSP
360
FIFKTLEEQG L
Length:361
Mass (Da):40,353
Last modified:June 1, 1994 - v2
Checksum:iA5D26385DA6F0A0B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41Q → H in AAA88709 (PubMed:8196765).Curated1
Sequence conflicti62A → P in AAA88709 (PubMed:8196765).Curated1
Sequence conflicti145 – 146ND → DN AA sequence (PubMed:6257176).Curated2
Sequence conflicti231Missing AA sequence (PubMed:6257176).Curated1
Sequence conflicti273L → M in AAS56247 (PubMed:17322287).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti33A → AA in allele 2. 1
Natural varianti120T → I in allele 2. 1
Natural varianti219D → G in allele 2. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS19064. OPBYC.
RefSeqiNP_012992.1. NM_001179856.1.

Genome annotation databases

EnsemblFungiiYKR066C; YKR066C; YKR066C.
GeneIDi853940.
KEGGisce:YKR066C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS19064. OPBYC.
RefSeqiNP_012992.1. NM_001179856.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2FX-ray2.10A71-361[»]
1A2GX-ray2.10A71-361[»]
1AA4X-ray2.10A71-361[»]
1AC4X-ray2.10A71-361[»]
1AC8X-ray2.10A71-361[»]
1AEBX-ray2.10A71-361[»]
1AEDX-ray2.10A71-361[»]
1AEEX-ray2.10A71-361[»]
1AEFX-ray2.10A71-361[»]
1AEGX-ray2.10A71-361[»]
1AEHX-ray2.10A71-361[»]
1AEJX-ray2.10A71-361[»]
1AEKX-ray2.10A71-361[»]
1AEMX-ray2.10A71-361[»]
1AENX-ray2.10A71-361[»]
1AEOX-ray2.10A71-361[»]
1AEQX-ray2.10A71-361[»]
1AESX-ray2.10A71-361[»]
1AETX-ray2.10A71-361[»]
1AEUX-ray2.10A71-361[»]
1AEVX-ray2.10A71-361[»]
1BEJX-ray2.40A71-361[»]
1BEKX-ray2.20A71-361[»]
1BEMX-ray2.20A71-361[»]
1BEPX-ray2.20A71-361[»]
1BEQX-ray2.16A71-361[»]
1BESX-ray2.00A71-361[»]
1BJ9X-ray2.20A71-361[»]
1BVAX-ray1.89A71-361[»]
1CCAX-ray1.80A68-361[»]
1CCBX-ray2.10A68-361[»]
1CCCX-ray2.00A68-361[»]
1CCEX-ray2.30A71-361[»]
1CCGX-ray2.10A71-361[»]
1CCIX-ray2.40A71-361[»]
1CCJX-ray2.10A71-361[»]
1CCKX-ray2.10A71-361[»]
1CCLX-ray2.00A71-361[»]
1CCPX-ray2.20A68-361[»]
1CMPX-ray1.90A71-361[»]
1CMQX-ray2.30A71-361[»]
1CMTX-ray2.10A71-361[»]
1CMUX-ray2.10A71-361[»]
1CPDX-ray2.20A68-361[»]
1CPEX-ray2.20A68-361[»]
1CPFX-ray2.20A68-361[»]
1CPGX-ray2.20A71-361[»]
1CYFX-ray2.35A68-361[»]
1DCCX-ray2.20A68-361[»]
1DJ1X-ray1.93A71-361[»]
1DJ5X-ray1.93A71-361[»]
1DS4X-ray2.02A71-361[»]
1DSEX-ray2.00A71-361[»]
1DSGX-ray2.56A71-361[»]
1DSOX-ray2.03A71-361[»]
1DSPX-ray2.03A71-361[»]
1EBEX-ray2.20A68-361[»]
1JCIX-ray1.90A68-361[»]
1JDRX-ray1.50A68-361[»]
1KOKX-ray1.70A68-361[»]
1KRJX-ray2.00A68-361[»]
1KXMX-ray1.74A71-361[»]
1KXNX-ray1.80A71-361[»]
1MK8X-ray1.65A68-361[»]
1MKQX-ray1.64A68-361[»]
1MKRX-ray1.58A68-361[»]
1ML2X-ray1.65A68-361[»]
1RYCX-ray1.80A71-361[»]
1S6VX-ray1.88A/C68-361[»]
1S73X-ray1.53A68-361[»]
1SBMX-ray1.69A68-361[»]
1SDQX-ray1.69A68-361[»]
1SOGX-ray1.85A68-361[»]
1STQX-ray1.82A68-361[»]
1U74X-ray2.40A/C68-361[»]
1U75X-ray2.55A/C68-361[»]
1Z53X-ray1.13A68-361[»]
1ZBYX-ray1.20A68-361[»]
1ZBZX-ray1.29A68-361[»]
2ANZX-ray1.75A71-361[»]
2AQDX-ray1.35A71-361[»]
2AS1X-ray1.55A71-361[»]
2AS2X-ray1.45A71-361[»]
2AS3X-ray1.40A71-361[»]
2AS4X-ray1.30A71-361[»]
2AS6X-ray1.45A71-361[»]
2B0ZX-ray2.70A68-361[»]
2B10X-ray2.80A/C68-361[»]
2B11X-ray2.30A/C68-361[»]
2B12X-ray3.02A68-361[»]
2BCNX-ray1.70A/C68-361[»]
2CCPX-ray2.20A68-361[»]
2CEPX-ray2.20A68-361[»]
2CYPX-ray1.70A68-361[»]
2EUNX-ray1.70A71-361[»]
2EUOX-ray1.45A71-361[»]
2EUPX-ray1.40A71-361[»]
2EUQX-ray1.30A71-361[»]
2EURX-ray1.39A71-361[»]
2EUSX-ray1.55A71-361[»]
2EUTX-ray1.12A71-361[»]
2EUUX-ray1.45A71-361[»]
2GB8NMR-A68-361[»]
2IA8X-ray1.48A71-361[»]
2ICVX-ray1.60A71-361[»]
2JTINMR-A68-361[»]
2N18NMR-A68-361[»]
2PCBX-ray2.80A/C68-361[»]
2PCCX-ray2.30A/C68-361[»]
2RBTX-ray1.24X71-361[»]
2RBUX-ray1.80X71-361[»]
2RBVX-ray1.39X71-361[»]
2RBWX-ray1.50X71-361[»]
2RBXX-ray1.50X71-361[»]
2RBYX-ray1.50X71-361[»]
2RBZX-ray1.80X71-361[»]
2RC0X-ray1.50X71-361[»]
2RC1X-ray2.49X71-361[»]
2RC2X-ray1.50X71-361[»]
2V23X-ray1.80A68-361[»]
2V2EX-ray1.68A71-361[»]
2X07X-ray1.86A69-361[»]
2X08X-ray2.01A69-361[»]
2XILX-ray1.68A71-361[»]
2XJ5X-ray1.69A71-361[»]
2XJ8X-ray1.69A71-361[»]
2Y5AX-ray1.25A71-361[»]
2YCGX-ray1.81A68-361[»]
3CCPX-ray2.20A68-361[»]
3CCXX-ray2.30A71-361[»]
3E2NX-ray1.30A68-96[»]
A110-361[»]
3E2OX-ray1.06A68-361[»]
3EXBX-ray1.60A68-361[»]
3M23X-ray1.40A71-361[»]
3M25X-ray1.40A71-361[»]
3M26X-ray1.40A71-361[»]
3M27X-ray1.40A71-361[»]
3M28X-ray1.40A71-361[»]
3M29X-ray1.40A71-361[»]
3M2AX-ray1.40A71-361[»]
3M2BX-ray1.40A71-361[»]
3M2CX-ray1.40A71-361[»]
3M2DX-ray1.40A71-361[»]
3M2EX-ray1.40A71-361[»]
3M2FX-ray1.40A71-361[»]
3M2GX-ray1.40A71-361[»]
3M2HX-ray1.40A71-361[»]
3M2IX-ray1.40A71-361[»]
3R98Other2.40A69-361[»]
3R99Other2.40A69-361[»]
4A6ZX-ray1.61A68-361[»]
4A71X-ray1.61A68-361[»]
4A78X-ray2.01A68-361[»]
4A7MX-ray1.71A68-361[»]
4CCPX-ray2.20A68-361[»]
4CCXX-ray1.90A71-361[»]
4CVIOther2.10A70-361[»]
4CVJOther2.18A71-361[»]
4JB4X-ray2.39A/C68-361[»]
4NFGX-ray2.11A71-361[»]
4P4QX-ray2.01A/C68-361[»]
4XV4X-ray1.69A71-361[»]
4XV5X-ray1.65A71-361[»]
4XV6X-ray1.55A71-361[»]
4XV7X-ray1.62A71-361[»]
4XV8X-ray1.57A71-361[»]
4XVAX-ray2.66A/C/E/G69-361[»]
5CCPX-ray2.20A68-361[»]
5CIBX-ray3.01A/C68-361[»]
5CICX-ray2.10A/C68-361[»]
5CIDX-ray2.76A/C68-361[»]
5CIEX-ray2.60A/C68-361[»]
5CIFX-ray2.01A/C68-361[»]
5CIGX-ray2.06A/C68-361[»]
5CIHX-ray2.60A/C68-361[»]
5D6MX-ray1.65A71-361[»]
5EJTX-ray1.55A68-361[»]
5EJXX-ray1.50A68-361[»]
6CCPX-ray2.20A68-361[»]
7CCPX-ray2.20A68-361[»]
ProteinModelPortaliP00431.
SMRiP00431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34197. 23 interactors.
DIPiDIP-6251N.
IntActiP00431. 5 interactors.
MINTiMINT-598890.

Protein family/group databases

PeroxiBasei2361. SceCcP01.

PTM databases

iPTMnetiP00431.

Proteomic databases

MaxQBiP00431.
PRIDEiP00431.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR066C; YKR066C; YKR066C.
GeneIDi853940.
KEGGisce:YKR066C.

Organism-specific databases

EuPathDBiFungiDB:YKR066C.
SGDiS000001774. CCP1.

Phylogenomic databases

HOGENOMiHOG000189824.
InParanoidiP00431.
KOiK00428.
OMAiVCAIQEM.
OrthoDBiEOG092C3FU5.

Enzyme and pathway databases

BioCyciYEAST:YKR066C-MONOMER.
BRENDAi1.11.1.5. 984.
SABIO-RKP00431.

Miscellaneous databases

EvolutionaryTraceiP00431.
PMAP-CutDBP00431.
PROiP00431.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCCPR_YEAST
AccessioniPrimary (citable) accession number: P00431
Secondary accession number(s): D6VXC7, Q6Q5M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 185 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6730 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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.