O58720 (CUTA_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Divalent-cation tolerance protein CutA

Gene names

Name:	cutA
Ordered Locus Names:	PH0992

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	102 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in resistance toward heavy metals.
Cofactor	Binds 1 copper ion in the interface between two trimers Probable.
Subunit structure	Homotrimer. The binding of the copper ion probably leads to oligomerization.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the CutA family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	response to metal ion Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 102

102

Divalent-cation tolerance protein CutA

PRO_0000157129

Sites

Metal binding

48

1

Copper

Secondary structure

1

.

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102

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Helix

11 – 23

13

Beta strand

28 – 41

14

Beta strand

44 – 57

14

Helix

59 – 61

3

Helix

62 – 72

11

Beta strand

74 – 77

4

Beta strand

81 – 84

4

Beta strand

86 – 88

3

Helix

90 – 99

10

Sequences

	Sequence		Length	Mass (Da)
	O58720 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: DC17341ECFDD8401	FASTA	102	12,348
	10 20 30 40 50 60 MIIVYTTFPD WESAEKVVKT LLKERLIACA NLREHRAFYW WEGKIEEDKE VGAILKTRED 70 80 90 100 LWEELKERIK ELHPYDVPAI IRIDVDDVNE DYLKWLIEET KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] 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: 15351719] [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: 14706845] [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: 14741340] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30089.1.

PIR

C71091.

RefSeq

NP_142908.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J2V	X-ray	2.00	A	1-102	[»]
1UKU	X-ray	1.45	A	1-102	[»]
1UMJ	X-ray	1.60	A/B	1-102	[»]
1V99	X-ray	1.80	A/B/C/D/E/F	1-102	[»]
1V9B	X-ray	2.00	A/B/C/D/E/F	1-102	[»]
2E66	X-ray	2.00	A/B/C	1-102	[»]

ProteinModelPortal

O58720.

SMR

O58720. Positions 1-102.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000000180; EBPYRP00000000180; EBPYRG00000000180.

GeneID

1443316.

GenomeReviews

Gene locus PH0992 in contig BA000001_GR.

KEGG

pho:PH0992.

NMPDR

fig|70601.1.peg.969.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000023384.

HOGENOM

HBG715543.

OMA

ILCTAPD.

PhylomeDB

O58720.

ProtClustDB

CLSK785533.

Enzyme and pathway databases

BioCyc

PHOR70601:PH0992-MONOMER.

Family and domain databases

InterPro

IPR004323. Ion_tolerance_CutA.
IPR011322. N-reg_PII-like_a/b.
[Graphical view]

Gene3D

G3DSA:3.30.70.830. Ion_tolerance_CutA1. 1 hit.

KO

K03926.

PANTHER

PTHR23419. Ion_tolerance_CutA1. 1 hit.

Pfam

PF03091. CutA1. 1 hit.
[Graphical view]

SUPFAM

SSF54913. N-reg_PII-like_a/b. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00536. Guanidine.

Entry information

Entry name

CUTA_PYRHO

Accession

Primary (citable) accession number: O58720

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program