Cytochrome c oxidase subunit 2 - Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast)

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A9RAG1 (COX2_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 41. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome c oxidase subunit 2
EC=1.9.3.1

Alternative name(s):
Cytochrome c oxidase polypeptide II

Gene names

Name:

COX2

Encoded on

Mitochondrion

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces ›

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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.
Catalytic activity	4 ferrocytochrome c + O₂ + 4 H⁺ = 4 ferricytochrome c + 2 H₂O.
Cofactor	Copper A By similarity.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the cytochrome c oxidase subunit 2 family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 246

246

Cytochrome c oxidase subunit 2

PRO_0000355032

Regions

Transmembrane

31 – 51

Helical; Potential

Transmembrane

72 – 92

Helical; Potential

Sites

Metal binding

175

Copper A By similarity

Metal binding

210

Copper A By similarity

Metal binding

214

Copper A By similarity

Metal binding

218

Copper A By similarity

Natural variations

Natural variant

M → V in strain: CBS 789 and CLIB 381. Ref.2 Ref.3

Natural variant

M → L in strain: CLIB 660. Ref.3

Natural variant

M → I in strain: CBS 789 and CLIB 381. Ref.2 Ref.3

Natural variant

106

V → I in strain: CBS 789 and CLIB 381. Ref.2 Ref.3

Natural variant

179

M → I in strain: CBS 789 and CLIB 381. Ref.2 Ref.3

Experimental info

Sequence conflict

223

I → T in ABU80664. Ref.2

Sequence conflict

223

I → T in ABU80663. Ref.2

Sequence conflict

223

I → T in CAQ51421. Ref.3

Sequence conflict

223

I → T in CAQ51422. Ref.3

Sequence conflict

223

I → T in CAQ51423. Ref.3

Sequence conflict

223

I → T in CAQ51424. Ref.3

Sequence conflict

223

I → T in CAQ51428. Ref.3

Sequence conflict

223

I → T in CAQ51429. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

A9RAG1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8F8982C0B23935B4
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FASTA

246

28,359

        10         20         30         40         50         60 
MIWTDVPTPW GMRFQDAATP NAEGMHELYD HMMYYLALML GLVSYMLYVM MKDYKNNTFA 

        70         80         90        100        110        120 
YKYIKHGQTL EIMWTMFPAV MLLLMAFPSF MLLYLCDEVL TPAMTVKVVG LQWYWKYEYS 

       130        140        150        160        170        180 
DFVSETGETV EYESYVMPED MLEEGQLRLL DTDTSMVVPV DTHVRFMVTA NDVLHCFTMP 

       190        200        210        220        230        240 
SLGIKVDACP GRLNQVSALM QRTGVYYGQC SELCGVNHGL MPIKTECVPI GDFVEWLGEQ 


ENVYVA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Promiscuous DNA in the nuclear genomes of hemiascomycetous yeasts." Sacerdot C., Casaregola S., Lafontaine I., Tekaia F., Dujon B., Ozier-Kalogeropoulos O. FEMS Yeast Res. 8:846-857(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.
[2]	"Re-examining the phylogeny of clinically relevant Candida species and allied genera based on multigene analyses." Tsui C.K.M., Daniel H.-M., Robert V., Meyer W. FEMS Yeast Res. 8:651-659(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-246, VARIANTS VAL-39; ILE-51; ILE-106 AND ILE-179. Strain: ATCC 20278 / CBS 789 / IFO 0015 / JCM 2104 / WM 66 and ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.
[3]	"Differentiation of Candida famata and Debaryomyces hansenii by rDNA intergenic spacer fingerprinting and revaluation of phylogenetic relationships between D.hansenii, C.famata, D.fabryi and C.flareri. Description of D.vietnamensis sp. nov." Nguyen H.V., Gaillardin C., Neuveglise C. Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-223, VARIANTS VAL-39; LEU-46; ILE-51; ILE-106 AND ILE-179. Strain: ATCC 20278 / CBS 789 / IFO 0015 / JCM 2104 / WM 66, CBS 1961, CBS 766, CLIB 381, CLIB 660 and Kam473.
[4]	"Amplification and sequencing of cytochrome c oxidase subunit II gene for phylogenetic analysis of yeast mitochondria." Nakagawa Y. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-189. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	YP_001621413.1. NC_010166.1.
3D structure databases
ProteinModelPortal	A9RAG1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5845854.
KEGG	dha:cox2.
Phylogenomic databases
eggNOG	COG1622.
KO	K02261.
OrthoDB	EOG4ZW8M5.
Family and domain databases
Gene3D	1.10.287.90. 1 hit. 2.60.40.420. 1 hit.
InterPro	IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR014222. Cyt_c_oxidase_su2. IPR002429. Cyt_c_oxidase_su2_C. IPR011759. Cyt_c_oxidase_su2_TM_dom. [Graphical view]
Pfam	PF00116. COX2. 1 hit. PF02790. COX2_TM. 1 hit. [Graphical view]
SUPFAM	SSF49503. Cupredoxin. 1 hit. SSF81464. Cyt_c_oxidase_II-like_TM. 1 hit.
TIGRFAMs	TIGR02866. CoxB. 1 hit.
PROSITE	PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS50999. COX2_TM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX2_DEBHA

Accession

Primary (citable) accession number: A9RAG1
Secondary accession number(s): B0LCE8

Q34322

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents