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Protein

Cytochrome c oxidase subunit 2

Gene

COX2

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Cu cationBy similarityNote: Binds a copper A center.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi175Copper ABy similarity1
Metal bindingi210Copper ABy similarity1
Metal bindingi214Copper ABy similarity1
Metal bindingi218Copper ABy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 2 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene namesi
Name:COX2
Encoded oniMitochondrion
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
Proteomesi
  • UP000000599 Componenti: Mitochondrion

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei31 – 51HelicalSequence analysisAdd BLAST21
Transmembranei72 – 92HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003550321 – 246Cytochrome c oxidase subunit 2Add BLAST246

Structurei

3D structure databases

ProteinModelPortaliA9RAG1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiA9RAG1.
KOiK02261.
OrthoDBiEOG092C40RV.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9RAG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIWTDVPTPW GMRFQDAATP NAEGMHELYD HMMYYLALML GLVSYMLYVM
60 70 80 90 100
MKDYKNNTFA YKYIKHGQTL EIMWTMFPAV MLLLMAFPSF MLLYLCDEVL
110 120 130 140 150
TPAMTVKVVG LQWYWKYEYS DFVSETGETV EYESYVMPED MLEEGQLRLL
160 170 180 190 200
DTDTSMVVPV DTHVRFMVTA NDVLHCFTMP SLGIKVDACP GRLNQVSALM
210 220 230 240
QRTGVYYGQC SELCGVNHGL MPIKTECVPI GDFVEWLGEQ ENVYVA
Length:246
Mass (Da):28,359
Last modified:February 5, 2008 - v1
Checksum:i8F8982C0B23935B4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti223I → T in ABU80664 (PubMed:18248416).Curated1
Sequence conflicti223I → T in ABU80663 (PubMed:18248416).Curated1
Sequence conflicti223I → T in CAQ51421 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51422 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51423 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51424 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51428 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51429 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti39M → V in strain: CBS 789 and CLIB 381. 2 Publications1
Natural varianti46M → L in strain: CLIB 660. 1 Publication1
Natural varianti51M → I in strain: CBS 789 and CLIB 381. 2 Publications1
Natural varianti106V → I in strain: CBS 789 and CLIB 381. 2 Publications1
Natural varianti179M → I in strain: CBS 789 and CLIB 381. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ508940 Genomic DNA. Translation: ABF58062.1.
EF599377 Genomic DNA. Translation: ABU80663.1.
EF599378 Genomic DNA. Translation: ABU80664.1.
AM991984 Genomic DNA. Translation: CAQ51421.1.
AM991986 Genomic DNA. Translation: CAQ51423.1.
AM991987 Genomic DNA. Translation: CAQ51424.1.
AM991985 Genomic DNA. Translation: CAQ51422.1.
AM991991 Genomic DNA. Translation: CAQ51428.1.
AM991992 Genomic DNA. Translation: CAQ51429.1.
D55727 Genomic DNA. Translation: BAA09541.1.
RefSeqiYP_001621413.1. NC_010166.1.

Genome annotation databases

GeneIDi5845854.
KEGGidha:cox2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ508940 Genomic DNA. Translation: ABF58062.1.
EF599377 Genomic DNA. Translation: ABU80663.1.
EF599378 Genomic DNA. Translation: ABU80664.1.
AM991984 Genomic DNA. Translation: CAQ51421.1.
AM991986 Genomic DNA. Translation: CAQ51423.1.
AM991987 Genomic DNA. Translation: CAQ51424.1.
AM991985 Genomic DNA. Translation: CAQ51422.1.
AM991991 Genomic DNA. Translation: CAQ51428.1.
AM991992 Genomic DNA. Translation: CAQ51429.1.
D55727 Genomic DNA. Translation: BAA09541.1.
RefSeqiYP_001621413.1. NC_010166.1.

3D structure databases

ProteinModelPortaliA9RAG1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5845854.
KEGGidha:cox2.

Phylogenomic databases

InParanoidiA9RAG1.
KOiK02261.
OrthoDBiEOG092C40RV.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOX2_DEBHA
AccessioniPrimary (citable) accession number: A9RAG1
Secondary accession number(s): B0LCE8
, B0LCE9, B4F4K1, B4F4K2, B4F4K4, B4F4K8, Q34322
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 5, 2008
Last modified: September 7, 2016
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.