Q5G935 (Q5G935_9ARCH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: Carboxylesterase EMBL AAW62260.1 EC=3.1.1.1 EMBL AAW62260.1
Organism	uncultured archaeon EMBL AAW62260.1
Taxonomic identifier	115547 [NCBI]
Taxonomic lineage	cellular organisms › Archaea › environmental samples

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Hydrolase EMBL AAW62260.1
Technical term	3D-structure PDB 2C7B
Gene Ontology (GO)
Molecular_function	carboxylesterase activity Inferred from electronic annotation. Source: EC methyl indole-3-acetate esterase activity Inferred from electronic annotation. Source: EC methyl jasmonate esterase activity Inferred from electronic annotation. Source: EC methyl salicylate esterase activity Inferred from electronic annotation. Source: EC retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q5G935 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: B0F5BC9FA756C15D	FASTA	311	33,785
	10 20 30 40 50 60 MPLDPQIKPI LERIRALSIA ASPQELRRQV EEQSRLLTAA VQEPIAETRD VHIPVSGGSI 70 80 90 100 110 120 RARVYFPKKA AGLPAVLYYH GGGFVFGSIE THDHICRRLS RLSDSVVVSV DYRLAPEYKF 130 140 150 160 170 180 PTAVEDAYAA LKWVADRADE LGVDPDRIAV AGDSAGGNLA AVVSILDRNS GEKLVKKQVL 190 200 210 220 230 240 IYPVVNMTGV PTASLVEFGV AETTSLPIEL MVWFGRQYLK RPEEAYDFKA SPLLADLGGL 250 260 270 280 290 300 PPALVVTAEY DPLRDEGELY AYKMKASGSR AVAVRFAGMV HGFVSFYPFV DAGREALDLA 310 AASIRSGLQP S

References

[1]	Rhee J.-K., Ahn D.-G., Kim Y.-G., Oh J.-W. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"New thermophilic and thermostable esterase with sequence similarity to the hormone-sensitive lipase family, cloned from a metagenomic library." Rhee J.K., Ahn D.G., Kim Y.G., Oh J.W. Appl. Environ. Microbiol. 71:817-825(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties." Byun J.S., Rhee J.K., Kim N.D., Yoon J., Kim D.U., Koh E., Oh J.W., Cho H.S. BMC Struct. Biol. 7:47-47(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY726780 Genomic DNA. Translation: AAW62260.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C7B	X-ray	2.30	A/B	1-311	[»]

ProteinModelPortal

Q5G935.

SMR

Q5G935. Positions 17-310.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR013094. AB_hydrolase_3.
IPR002168. Lipase_GDXG_AS.
[Graphical view]

Pfam

PF07859. Abhydrolase_3. 1 hit.
[Graphical view]

PROSITE

PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5G935.

Entry information

Entry name

Q5G935_9ARCH

Accession

Primary (citable) accession number: Q5G935

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	May 29, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)