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C7PG38 (C7PG38_CHIPD) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B) By similarity.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Cofactor

Copper A By similarity.

Subcellular location

Membrane; Multi-pass membrane protein By similarity RuleBase RU000456.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family. RuleBase RU000456

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential EMBL ACU58021.1
Chain25 – 353329 Potential EMBL ACU58021.1
PRO_5000509123

Sequences

Sequence LengthMass (Da)Tools
C7PG38 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 1A723DD29626A6E1

FASTA35339,587
        10         20         30         40         50         60 
MSGYLAVLVV VLIFVVIFQI AKASEYVSIL KGEKKARQQS NRVNGFLLII FLILGLVGVY 

        70         80         90        100        110        120 
YCNDALKGKI FFEAASEQGE GIDNMIKWTL WITGIVFIIT QILLFWFSFK YQEKEGQQAF 

       130        140        150        160        170        180 
YFPHNNKLEL IWTVIPAIAL TILVAIGLRH WFRITSDAPK DAAVVEITGK QFNWLIRYPG 

       190        200        210        220        230        240 
KDGQLGRKFF KNINDANNPV GQDWDDQLNK DDFMATEMHL VVGKPVKLII GSRDVIHDVG 

       250        260        270        280        290        300 
LSHFRLKMDA VPGIPTTLWF TPKYTTTEMK DKTGNPDFVY EISCDQMCGS GHYSMKANIV 

       310        320        330        340        350 
VETQEEFDAW TAKQVAQYGV AHPAEAPVAK PAEAPAAATD TTQKVVAANE VKP 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001699 Genomic DNA. Translation: ACU58021.1.
RefSeqYP_003120222.1. NC_013132.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING485918.Cpin_0523.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACU58021; ACU58021; Cpin_0523.
GeneID8356629.
KEGGcpi:Cpin_0523.
PATRIC21349663. VBIChiPin99107_0518.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1622.
HOGENOMHOG000023391.
KOK02275.
OMARAKMDMI.
OrthoDBEOG68SVXT.

Enzyme and pathway databases

BioCycCPIN485918:GHYR-532-MONOMER.

Family and domain databases

Gene3D1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProIPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
PROSITEPS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC7PG38_CHIPD
AccessionPrimary (citable) accession number: C7PG38
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: April 16, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)