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Protein

Cytochrome c oxidase subunit 2

Gene

cox2

Organism
Prototheca wickerhamii
Status
Unreviewed-Annotation score: -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.UniRule annotation

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductaseImported
Biological processElectron transport, Respiratory chainUniRule annotationSAAS annotation, Transport
LigandCopperUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 2UniRule annotationSAAS annotation
Gene namesi
Name:cox2Imported
Encoded oniMitochondrionImported
OrganismiPrototheca wickerhamiiImported
Taxonomic identifieri3111 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaTrebouxiophyceaeChlorellalesChlorellaceaePrototheca

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membraneUniRule annotationSAAS annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_500422167817 – 258Cytochrome c oxidase subunit 2Sequence analysisAdd BLAST242

Structurei

3D structure databases

ProteinModelPortaliQ37621
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 114COX2_TMInterPro annotationAdd BLAST96
Domaini115 – 253COX2_CUAInterPro annotationAdd BLAST139

Sequence similaritiesi

Belongs to the cytochrome c oxidase subunit 2 family.UniRule annotationSAAS annotation

Keywords - Domaini

SignalSequence analysis, Transmembrane, Transmembrane helixSAAS annotation

Family and domain databases

CDDicd13912 CcO_II_C, 1 hit
Gene3Di1.10.287.90, 1 hit
2.60.40.420, 1 hit
InterProiView protein in InterPro
IPR002429 CcO_II-like_C
IPR034210 CcO_II_C
IPR001505 Copper_CuA
IPR008972 Cupredoxin
IPR014222 Cyt_c_oxidase_su2
IPR011759 Cyt_c_oxidase_su2_TM_dom
IPR036257 Cyt_c_oxidase_su2_TM_sf
PfamiView protein in Pfam
PF00116 COX2, 1 hit
PF02790 COX2_TM, 1 hit
SUPFAMiSSF49503 SSF49503, 1 hit
SSF81464 SSF81464, 1 hit
TIGRFAMsiTIGR02866 CoxB, 1 hit
PROSITEiView protein in PROSITE
PS00078 COX2, 1 hit
PS50857 COX2_CUA, 1 hit
PS50999 COX2_TM, 1 hit

Sequencei

Sequence statusi: Complete.

Q37621-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLLFAYAL IPFVSFSDAP EAWQIGFQDP ATPIMQGLID LHHDIQFFLI
60 70 80 90 100
AVLVFVVWMV SRALYLFHYT RNPLPEKIIH GTLIEIVWTI TPSLILIFIA
110 120 130 140 150
VPSFALLYSL DEVVDPAVTI KAIGHQWYWS YEYSDYSIAD DQSIAFDSYM
160 170 180 190 200
IPDDDLELGQ YRLLEVDNRV VVPVDTHIRV IITAADVLHS WAIPSLGVKC
210 220 230 240 250
DAVPGRLNQI PMFIKREGVF YGQCSELCGT NHAFMPIVVE AVSLENYISW

VSNKLEEL
Length:258
Mass (Da):29,373
Last modified:November 1, 1996 - v1
Checksum:iAA9A6DDFE5F5551B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02970 Genomic DNA Translation: AAD12642.1
PIRiT11923
RefSeqiNP_042254.1, NC_001613.1

Genome annotation databases

GeneIDi802128

Similar proteinsi

Entry informationi

Entry nameiQ37621_PROWI
AccessioniPrimary (citable) accession number: Q37621
Entry historyiIntegrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health