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Q3J5G0 (Q3J5G0_RHOS4) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. RuleBase RU004024

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O. RuleBase RU004024

Cofactor

Copper A By similarity. RuleBase RU004024

Subcellular location

Membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding961Cadmium; via pros nitrogen PDB 3OMA PDB 3OMI PDB 3OMN PDB 3OM3
Metal binding1011Cadmium PDB 3OMA PDB 3OMI PDB 3OMN PDB 3OM3
Metal binding2521Copper PDB 3OMA PDB 3OMI
Metal binding2541Copper; via carbonyl oxygen PDB 3OMA PDB 3OMI
Metal binding2561Copper PDB 3OMA PDB 3OMI
Metal binding2601Copper; via pros nitrogen PDB 3OMA PDB 3OMI

Sequences

Sequence LengthMass (Da)Tools
Q3J5G0 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 2F363ADA39EFEBF8

FASTA30332,931
        10         20         30         40         50         60 
MRHSTTLTGC ATGAAGLLAA TAAAAQQQSL EIIGRPQPGG TGFQPSASPV ATQIHWLDGF 

        70         80         90        100        110        120 
ILVIIAAITI FVTLLILYAV WRFHEKRNKV PARFTHNSPL EIAWTIVPIV ILVAIGAFSL 

       130        140        150        160        170        180 
PVLFNQQEIP EADVTVKVTG YQWYWGYEYP DEEISFESYM IGSPATGGDN RMSPEVEQQL 

       190        200        210        220        230        240 
IEAGYSRDEF LLATDTAMVV PVNKTVVVQV TGADVIHSWT VPAFGVKQDA VPGRLAQLWF 

       250        260        270        280        290        300 
RAEREGIFFG QCSELCGISH AYMPITVKVV SEEAYAAWLE QARGGTYELS SVLPATPAGV 


SVE 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[2]"Crystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pump."
Liu J., Qin L., Ferguson-Miller S.
Proc. Natl. Acad. Sci. U.S.A. 108:1284-1289(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 30-281 IN COMPLEX WITH CADMIUM AND COPPER.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000143 Genomic DNA. Translation: ABA77974.1.
RefSeqYP_351875.1. NC_007493.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OM3X-ray2.60B/D30-281[»]
3OMAX-ray2.30B/D30-281[»]
3OMIX-ray2.15B/D30-281[»]
3OMNX-ray2.15B/D30-281[»]
ProteinModelPortalQ3J5G0.
SMRQ3J5G0. Positions 30-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272943.RSP_1826.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA77974; ABA77974; RSP_1826.
GeneID3719073.
KEGGrsp:RSP_1826.
PATRIC23150624. VBIRhoSph57909_0712.

Phylogenomic databases

eggNOGCOG1622.
HOGENOMHOG000264988.
KOK02275.
OMAFMPIAIR.
OrthoDBEOG68SVXT.
ProtClustDBCLSK934044.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-419-MONOMER.

Family and domain databases

Gene3D1.10.287.90. 1 hit.
2.60.40.420. 2 hits.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
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.
TIGRFAMsTIGR02866. CoxB. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ3J5G0.

Entry information

Entry nameQ3J5G0_RHOS4
AccessionPrimary (citable) accession number: Q3J5G0
Entry history
Integrated into UniProtKB/TrEMBL: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)