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UniProtKB/Swiss-Prot entry Q2LCQ6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COX1_DICCI
Primary accession number Q2LCQ6
Secondary accession numbers None
Integrated into Swiss-Prot on December 4, 2007
Sequence was last modified on February 21, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 21)
Name and origin of the protein
Protein name Cytochrome c oxidase subunit 1+2
Synonyms EC 1.9.3.1
Cytochrome c oxidase polypeptide I+II
Gene name
Name: cox1/2
From
Dictyostelium citrinum (Slime mold) [TaxID: 361072] 
Encoded on Mitochondrion.
Taxonomy Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/molbev/msn088; PubMed=18413355 [NCBI, ExPASy, EBI, Israel, Japan]
Heidel A.J., Gloeckner G.;
"Mitochondrial genome evolution in the social amoebae.";
Mol. Biol. Evol. 25:1440-1450(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
DQ336395; ABC60387.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_492636.1; -.
3D structure databases
ModBase Q2LCQ6.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005746; Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0004129; Molecular function: cytochrome-c oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0009060; Biological process: aerobic respiration (inferred from electronic annotation from InterPro).
GO:0022904; Biological process: respiratory electron transport chain (inferred from electronic annotation from InterPro).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001505; Copper_CuA.
IPR000883; COX1.
IPR014222; COX2.
IPR002429; COX2_C.
IPR008972; Cupredoxin.
IPR011759; Cyt_c_oxidase_II_TM.
Graphical view of domain structure.
Gene3D G3DSA:1.20.210.10; COX1; 1.
G3DSA:1.10.287.90; COX2_TM; 1.
G3DSA:2.60.40.420; Cupredoxin; 1.
PANTHER PTHR10422; COX1; 1.
Pfam PF00115; COX1; 1.
PF00116; COX2; 1.
PF02790; COX2_TM; 1.
Pfam graphical view of domain structure.
PRINTS PR01165; CYCOXIDASEI.
PR01166; CYCOXIDASEII.
ProDom PD000131; Copper_CuA; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02866; CoxB; 1.
PROSITE PS50855; COX1; 1.
PS00078; COX2; 1.
PS50857; COX2_CUA; 1.
PS50999; COX2_TM; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 3912629; -.
Other
ProtoNet Q2LCQ6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Respiratory chain; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   773  773     Cytochrome c oxidase subunit 1+2. PRO_0000312386
TRANSMEM   41    61  21     Potential. 
TRANSMEM   87   111  25     Potential. 
TRANSMEM   130   150  21     Potential. 
TRANSMEM   173   193  21     Potential. 
TRANSMEM   211   231  21     Potential. 
TRANSMEM   262   278  17     Potential. 
TRANSMEM   290   310  21     Potential. 
TRANSMEM   335   355  21     Potential. 
TRANSMEM   362   382  21     Potential. 
TRANSMEM   396   416  21     Potential. 
TRANSMEM   444   464  21     Potential. 
TRANSMEM   483   503  21     Potential. 
TRANSMEM   555   575  21     Potential. 
TRANSMEM   604   624  21     Potential. 
REGION   1   491  491     COX1. 
REGION   492   773  282     COX2. 
METAL   85    85        Iron (heme A axial ligand) (By similarity). 
METAL   264   264        Copper B (By similarity). 
METAL   268   268        Copper B (By similarity). 
METAL   314   314        Copper B (By similarity). 
METAL   315   315        Copper B (By similarity). 
METAL   400   400        Iron (heme A3 axial ligand) (By similarity). 
METAL   402   402        Iron (heme A axial ligand) (By similarity). 
METAL   709   709        Copper A (By similarity). 
METAL   744   744        Copper A (By similarity). 
METAL   748   748        Copper A (By similarity). 
METAL   752   752        Copper A (By similarity). 
CROSSLNK   264   268        1'-histidyl-3'-tyrosine (His-Tyr) (By similarity). 
Sequence information
Length: 773 AA [This is the length of the unprocessed precursor] Molecular weight: 86778 Da [This is the MW of the unprocessed precursor] CRC64: DBAB29E1527D1BD4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLLEIYDKQ LVEQEEGGFR AILTRYLNKW IFTVDHKLIG TMYITFSIFA GIIGTLLSLV 

        70         80         90        100        110        120 
IPMELSTGNM LEGDSQQYNV IVTAHGLIMI FFVVMYCSMP AMLGGFANWF LPIMVGAPDV 

       130        140        150        160        170        180 
AFPRLNNISL WLIVVSFGLL LTSSCVGIGA GTGWTVYPPL SMMEYHPGHA VDVGILSLHI 

       190        200        210        220        230        240 
AGASSLVGAI NFLTTVFNMK IAGLSWPKVS LFVWSVVITA VLLVLSLPVL AGGLTMLITD 

       250        260        270        280        290        300 
RNFETTFFDP IGGGDPILYQ HLFHPEVYIL ILPGFGIISI IISRYSNKGI FGVKGMISAM 

       310        320        330        340        350        360 
SAIGFLGFLV WAYHHMYTVG LDVDTRAYFT AATMIIAIPT GIKIFSWLAT LWGGVIKITT 

       370        380        390        400        410        420 
PMLFVIGFLV LFTIGGLTGV VLANGGLDIS LHDTYYVVAH FHYVLSMGAI FAIFAGYYYY 

       430        440        450        460        470        480 
YAIMNSNRIL GIVRYNEQLG RIHFWTMFIG VNVTFFPMHF LGLAGMPRRI GDYPDAYIGW 

       490        500        510        520        530        540 
NLIASYGSLI TAFGLLFFFV NIFTPYFKKK ALISKKFQRG AMILMGLDFS RDWQIGFQDP 

       550        560        570        580        590        600 
ATPIMEGIID LHNYIFFYLI VVAVFIGWVM GRILWRFAYK WSYPTIGDIE IFKNFTAYNQ 

       610        620        630        640        650        660 
IIHGTVIEIV WTLIPTVILY LIAIPSFTLL YAMDEIINPT VTIKIIGHQW YWSYEYGDNS 

       670        680        690        700        710        720 
SNLVEFDSYM VYERDLNEGQ LRLLEVDNSM IVPVKTHIRL IITSGDVLHS WAVPSFGIKV 

       730        740        750        760        770 
DAVPGRLNQI GLYVKREGTF YGQCSELCGV DHGFMPIKVE AVKVQEYLGR LYK 

Q2LCQ6 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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NPSA logo NPSA Sequence analysis tools

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