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Protein

Divalent-cation tolerance protein CutA

Gene

cutA

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in resistance toward heavy metals.

Cofactori

Cu cationCuratedNote: Binds 1 copper ion in the interface between two trimers.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi48Copper1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Divalent-cation tolerance protein CutA
Gene namesi
Name:cutA
Ordered Locus Names:PH0992
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001571291 – 102Divalent-cation tolerance protein CutAAdd BLAST102

Interactioni

Subunit structurei

Homotrimer. The binding of the copper ion probably leads to oligomerization.

Protein-protein interaction databases

STRINGi70601.PH0992.

Structurei

Secondary structure

1102
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Helixi11 – 23Combined sources13
Beta strandi28 – 41Combined sources14
Beta strandi44 – 57Combined sources14
Helixi59 – 61Combined sources3
Helixi62 – 72Combined sources11
Beta strandi74 – 77Combined sources4
Beta strandi81 – 84Combined sources4
Beta strandi86 – 88Combined sources3
Helixi90 – 99Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J2VX-ray2.00A1-102[»]
1UKUX-ray1.45A1-102[»]
1UMJX-ray1.60A/B1-102[»]
2E66X-ray2.00A/B/C1-102[»]
4NYOX-ray1.80A/B/C/D/E/F1-102[»]
4NYPX-ray2.00A/B/C/D/E/F1-102[»]
ProteinModelPortaliO58720.
SMRiO58720.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58720.

Family & Domainsi

Sequence similaritiesi

Belongs to the CutA family.Curated

Phylogenomic databases

eggNOGiarCOG04231. Archaea.
COG1324. LUCA.
HOGENOMiHOG000222826.
KOiK03926.
OMAiPGMQSVY.

Family and domain databases

InterProiIPR004323. Ion_tolerance_CutA.
IPR011322. N-reg_PII-like_a/b.
[Graphical view]
PANTHERiPTHR23419. PTHR23419. 1 hit.
PfamiPF03091. CutA1. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.

Sequencei

Sequence statusi: Complete.

O58720-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIVYTTFPD WESAEKVVKT LLKERLIACA NLREHRAFYW WEGKIEEDKE
60 70 80 90 100
VGAILKTRED LWEELKERIK ELHPYDVPAI IRIDVDDVNE DYLKWLIEET

KK
Length:102
Mass (Da):12,348
Last modified:August 1, 1998 - v1
Checksum:iDC17341ECFDD8401
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30089.1.
PIRiC71091.
RefSeqiWP_010885081.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30089; BAA30089; BAA30089.
GeneIDi1443316.
KEGGipho:PH0992.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30089.1.
PIRiC71091.
RefSeqiWP_010885081.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J2VX-ray2.00A1-102[»]
1UKUX-ray1.45A1-102[»]
1UMJX-ray1.60A/B1-102[»]
2E66X-ray2.00A/B/C1-102[»]
4NYOX-ray1.80A/B/C/D/E/F1-102[»]
4NYPX-ray2.00A/B/C/D/E/F1-102[»]
ProteinModelPortaliO58720.
SMRiO58720.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0992.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30089; BAA30089; BAA30089.
GeneIDi1443316.
KEGGipho:PH0992.

Phylogenomic databases

eggNOGiarCOG04231. Archaea.
COG1324. LUCA.
HOGENOMiHOG000222826.
KOiK03926.
OMAiPGMQSVY.

Miscellaneous databases

EvolutionaryTraceiO58720.

Family and domain databases

InterProiIPR004323. Ion_tolerance_CutA.
IPR011322. N-reg_PII-like_a/b.
[Graphical view]
PANTHERiPTHR23419. PTHR23419. 1 hit.
PfamiPF03091. CutA1. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCUTA_PYRHO
AccessioniPrimary (citable) accession number: O58720
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.