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Protein

Cytochrome c oxidase subunit 2

Gene

coxII-1

Organism
Petunia hybrida (Petunia)
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

Cofactori

Cu cationUniRule annotationNote: Binds a copper A center.UniRule annotation

GO - Molecular functioni

Keywordsi

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 annotation
Gene namesi
Name:coxII-1Imported
Encoded oniMitochondrionImported
OrganismiPetunia hybrida (Petunia)Imported
Taxonomic identifieri4102 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaePetunioideaePetunia

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 annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_500432301317 – 258Cytochrome c oxidase subunit 2Sequence analysisAdd BLAST242

Structurei

3D structure databases

ProteinModelPortaliQ99029
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 111COX2_TMInterPro annotationAdd BLAST96
Domaini113 – 251COX2_CUAInterPro annotationAdd BLAST139

Sequence similaritiesi

Belongs to the cytochrome c oxidase subunit 2 family.UniRule 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
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
PS50857 COX2_CUA, 1 hit
PS50999 COX2_TM, 1 hit

Sequencei

Sequence statusi: Complete.

Q99029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVLEWLFLT IAPCDAAEPW QLGSQDAATP IMQGITDLHH DVFFFVILIL
60 70 80 90 100
VFVSWILGRA LWHFHYKKNP IPQRIVHGTT IEILRTIFPS IIPMFIAIPS
110 120 130 140 150
FALLYSMDEV VVDPAITIKA IGHQWYRTYE YSDYNSSDEQ SLTFDSYTIP
160 170 180 190 200
EDDPELGQSR LLEVDNRVVV PAKSYIRFIV TSADVPDSWA VPSLGVKCDA
210 220 230 240 250
VPGRLNQTSI SVQREGVYYG QCSEICGTNH AFMPIVVEAV PRKDYGSRVS

NQLIQTEA
Length:258
Mass (Da):29,126
Last modified:November 1, 1996 - v1
Checksum:i5549FA7B566B0084
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17394 Genomic DNA Translation: CAA35255.1
PIRiS19533

Similar proteinsi

Entry informationi

Entry nameiQ99029_PETHY
AccessioniPrimary (citable) accession number: Q99029
Entry historyiIntegrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 96 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