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Protein
Submitted name:

328aa long hypothetical L-asparaginase

Gene

PH0066

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-68-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
328aa long hypothetical L-asparaginaseImported
Gene namesi
Ordered Locus Names:PH0066Imported
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)Imported
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi70601.PH0066.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLSX-ray2.16A/B1-328[»]
1WNFX-ray2.50A/B1-328[»]
ProteinModelPortaliO57797.
SMRiO57797. Positions 1-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO57797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 182181AsparaginaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the asparaginase 1 family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01924. Archaea.
COG0252. LUCA.
HOGENOMiHOG000227974.
KOiK01424.
OMAiLMWILGH.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR006033. AsnASEI.
IPR006034. Asparaginase/glutaminase.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00519. asnASE_I. 1 hit.
PROSITEiPS00917. ASN_GLN_ASE_2. 1 hit.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O57797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRILILGMGG TIASVKGERG YESALSVSKI LKLAGISSEA KIEARDLMNV
60 70 80 90 100
DSTLIQPSDW ERLAKEIEKE VWEYDGIVIT HGTDTMAYSA SMLSFMLRNP
110 120 130 140 150
PIPIVLTGSM LPITEKNSDA PFNLRTALEF VKLGIRGIYI AFNGKVMLGV
160 170 180 190 200
RASKIRSMGF DAFESINYPN VAEIKDDKLR ILHIPDFYGD EFFSDIKYEP
210 220 230 240 250
KVLVIKLIPG LSGDIVREAL RLGYKGIILE GYGVGGIPYR GTDLFEVVSS
260 270 280 290 300
ISKRIPVVLT TQAIYDGVDL QRYKVGRIAL EAGVIPAGDM TKEATITKLM
310 320
WILGHTKNIE EVKQLMGKNI TGELTRVS
Length:328
Mass (Da):36,236
Last modified:August 1, 1998 - v1
Checksum:iF3AEED6E5DC60562
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29135.1.
PIRiH71225.
RefSeqiWP_010884185.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29135; BAA29135; BAA29135.
GeneIDi1443967.
KEGGipho:PH0066.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29135.1.
PIRiH71225.
RefSeqiWP_010884185.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLSX-ray2.16A/B1-328[»]
1WNFX-ray2.50A/B1-328[»]
ProteinModelPortaliO57797.
SMRiO57797. Positions 1-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA29135; BAA29135; BAA29135.
GeneIDi1443967.
KEGGipho:PH0066.

Phylogenomic databases

eggNOGiarCOG01924. Archaea.
COG0252. LUCA.
HOGENOMiHOG000227974.
KOiK01424.
OMAiLMWILGH.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-68-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO57797.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR006033. AsnASEI.
IPR006034. Asparaginase/glutaminase.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00519. asnASE_I. 1 hit.
PROSITEiPS00917. ASN_GLN_ASE_2. 1 hit.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]
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-3Imported.
  2. "Crystal Structure of PH0066 from Pyrococcus horikoshii."
    Ihsanawati, Sekine S., Murayama K., Sugawara M., Shirouzu M., Yokoyama S.
    Submitted (AUG-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
  3. "Structure of the type I L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii at 2.16 angstroms resolution."
    Yao M., Yasutake Y., Morita H., Tanaka I.
    Acta Crystallogr. D 61:294-301(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS).

Entry informationi

Entry nameiO57797_PYRHO
AccessioniPrimary (citable) accession number: O57797
Entry historyi
Integrated into UniProtKB/TrEMBL: August 1, 1998
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

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.