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Protein

Peroxidase

Gene

CIP1

Organism
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei71Transition state stabilizer1
Active sitei75Proton acceptor1
Metal bindingi76Calcium 11
Metal bindingi94Calcium 1; via carbonyl oxygen1
Metal bindingi96Calcium 11
Metal bindingi98Calcium 11
Metal bindingi203Iron (heme axial ligand)1
Metal bindingi204Calcium 21
Metal bindingi221Calcium 21
Metal bindingi223Calcium 21
Metal bindingi226Calcium 2; via carbonyl oxygen1
Metal bindingi228Calcium 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
mycoCLAPiPRX2A_COPCI.
PeroxiBasei2403. CcinCIIBA.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase (EC:1.11.1.7)
Gene namesi
Name:CIP1
OrganismiCoprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
Taxonomic identifieri5346 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000002366721 – 363PeroxidaseAdd BLAST343

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Pyrrolidone carboxylic acid1
Disulfide bondi31 ↔ 43
Disulfide bondi42 ↔ 312
Disulfide bondi62 ↔ 148
Glycosylationi162N-linked (GlcNAc...) (high mannose)1 Publication1
Disulfide bondi276 ↔ 341
Glycosylationi358O-linked (Man...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP28314.

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 39Combined sources4
Helixi40 – 42Combined sources3
Helixi45 – 54Combined sources10
Turni55 – 60Combined sources6
Helixi64 – 77Combined sources14
Helixi82 – 86Combined sources5
Beta strandi94 – 96Combined sources3
Helixi98 – 101Combined sources4
Helixi103 – 106Combined sources4
Helixi110 – 112Combined sources3
Helixi116 – 129Combined sources14
Helixi133 – 146Combined sources14
Helixi179 – 189Combined sources11
Helixi193 – 199Combined sources7
Helixi200 – 205Combined sources6
Beta strandi207 – 211Combined sources5
Helixi213 – 215Combined sources3
Beta strandi218 – 222Combined sources5
Helixi230 – 235Combined sources6
Beta strandi244 – 246Combined sources3
Beta strandi254 – 256Combined sources3
Helixi263 – 270Combined sources8
Turni272 – 274Combined sources3
Helixi275 – 280Combined sources6
Helixi285 – 300Combined sources16
Turni301 – 303Combined sources3
Helixi306 – 308Combined sources3
Beta strandi309 – 311Combined sources3
Helixi313 – 315Combined sources3
Helixi334 – 336Combined sources3
Beta strandi342 – 344Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H3JX-ray2.00A/B22-363[»]
1LY8X-ray2.05A/B21-363[»]
1LY9X-ray2.00A/B21-363[»]
1LYCX-ray1.57A/B21-363[»]
1LYKX-ray2.00A/B21-363[»]
ProteinModelPortaliP28314.
SMRiP28314.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28314.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.

Family and domain databases

CDDicd00692. ligninase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
PF11895. Peroxidase_ext. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
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.

P28314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSLLSTFA AVIIGALALP QGPGGGGSVT CPGGQSTSNS QCCVWFDVLD
60 70 80 90 100
DLQTNFYQGS KCESPVRKIL RIVFHDAIGF SPALTAAGQF GGGGADGSII
110 120 130 140 150
AHSNIELAFP ANGGLTDTVE ALRAVGINHG VSFGDLIQFA TAVGMSNCPG
160 170 180 190 200
SPRLEFLTGR SNSSQPSPPS LIPGPGNTVT AILDRMGDAG FSPDEVVDLL
210 220 230 240 250
AAHSLASQEG LNSAIFRSPL DSTPQVFDTQ FYIETLLKGT TQPGPSLGFA
260 270 280 290 300
EELSPFPGEF RMRSDALLAR DSRTACRWQS MTSSNEVMGQ RYRAAMAKMS
310 320 330 340 350
VLGFDRNALT DCSDVIPSAV SNNAAPVIPG GLTVDDIEVS CPSEPFPEIA
360
TASGPLPSLA PAP
Length:363
Mass (Da):37,640
Last modified:July 1, 1993 - v2
Checksum:iE56EB53B963C3DB5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti119V → I in CAA50060 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti99I → V.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69457 mRNA. Translation: CAA49216.1.
X70789 Genomic DNA. Translation: CAA50060.1.
PIRiS31780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69457 mRNA. Translation: CAA49216.1.
X70789 Genomic DNA. Translation: CAA50060.1.
PIRiS31780.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H3JX-ray2.00A/B22-363[»]
1LY8X-ray2.05A/B21-363[»]
1LY9X-ray2.00A/B21-363[»]
1LYCX-ray1.57A/B21-363[»]
1LYKX-ray2.00A/B21-363[»]
ProteinModelPortaliP28314.
SMRiP28314.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
mycoCLAPiPRX2A_COPCI.
PeroxiBasei2403. CcinCIIBA.

Proteomic databases

PRIDEiP28314.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.

Miscellaneous databases

EvolutionaryTraceiP28314.

Family and domain databases

CDDicd00692. ligninase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
PF11895. Peroxidase_ext. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
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 nameiPER_COPCI
AccessioniPrimary (citable) accession number: P28314
Secondary accession number(s): P28315, Q12575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.