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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Copper

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-986-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 102102Divalent-cation tolerance protein CutAPRO_0000157129Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi70601.PH0992.

Structurei

Secondary structure

1
102
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi11 – 2313Combined sources
Beta strandi28 – 4114Combined sources
Beta strandi44 – 5714Combined sources
Helixi59 – 613Combined sources
Helixi62 – 7211Combined sources
Beta strandi74 – 774Combined sources
Beta strandi81 – 844Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 9910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58720.

Family & Domainsi

Sequence similaritiesi

Belongs to the CutA family.Curated

Phylogenomic databases

eggNOGiarCOG04231. Archaea.
COG1324. LUCA.
HOGENOMiHOG000222826.
KOiK03926.
OMAiRAAACVN.

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
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. Positions 1-102.
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.
OMAiRAAACVN.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-986-MONOMER.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. "Structural evidence for guanidine-protein side chain interactions: crystal structure of CutA from Pyrococcus horikoshii in 3 M guanidine hydrochloride."
    Tanaka Y., Tsumoto K., Umetsu M., Nakanishi T., Yasutake Y., Sakai N., Yao M., Tanaka I., Arakawa T., Kumagai I.
    Biochem. Biophys. Res. Commun. 323:185-191(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  3. "Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA."
    Tanaka Y., Tsumoto K., Nakanishi T., Yasutake Y., Sakai N., Yao M., Tanaka I., Kumagai I.
    FEBS Lett. 556:167-174(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
  4. "Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins."
    Umetsu M., Tsumoto K., Ashish K., Nitta S., Tanaka Y., Adschiri T., Kumagai I.
    FEBS Lett. 557:49-56(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

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 11, 2015
This is version 92 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.