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Protein
Submitted name:

LCC

Gene
N/A
Organism
uncultured bacterium
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...

Keywords - Molecular functioni

HydrolaseImported

Protein family/group databases

ESTHERi9bact-g9by57. Polyesterase-lipase-cutinase.

Names & Taxonomyi

Protein namesi
Submitted name:
LCCImported (EC:3.1.1.74Imported)
Organismiuncultured bacteriumImported
Taxonomic identifieri77133 [NCBI]
Taxonomic lineageiBacteriaenvironmental samples

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi275 ↔ 292Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EB0X-ray1.50A36-293[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR029059. AB_hydrolase_5.
IPR005065. PAF_acetylhydro.
[Graphical view]
PANTHERiPTHR10272. PTHR10272. 1 hit.
PfamiPF12695. Abhydrolase_5. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

G9BY57-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGVLWRVRT AALMAALLAL AAWALVWASP SVEAQSNPYQ RGPNPTRSAL
60 70 80 90 100
TADGPFSVAT YTVSRLSVSG FGGGVIYYPT GTSLTFGGIA MSPGYTADAS
110 120 130 140 150
SLAWLGRRLA SHGFVVLVIN TNSRFDYPDS RASQLSAALN YLRTSSPSAV
160 170 180 190 200
RARLDANRLA VAGHSMGGGG TLRIAEQNPS LKAAVPLTPW HTDKTFNTSV
210 220 230 240 250
PVLIVGAEAD TVAPVSQHAI PFYQNLPSTT PKVYVELDNA SHFAPNSNNA
260 270 280 290
AISVYTISWM KLWVDNDTRY RQFLCNVNDP ALSDFRTNNR HCQ
Length:293
Mass (Da):31,496
Last modified:February 22, 2012 - v1
Checksum:i202216278CDCEB8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ704839 Genomic DNA. Translation: AEV21261.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ704839 Genomic DNA. Translation: AEV21261.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EB0X-ray1.50A36-293[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERi9bact-g9by57. Polyesterase-lipase-cutinase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR029059. AB_hydrolase_5.
IPR005065. PAF_acetylhydro.
[Graphical view]
PANTHERiPTHR10272. PTHR10272. 1 hit.
PfamiPF12695. Abhydrolase_5. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach."
    Sulaiman S., Yamato S., Kanaya E., Kim J.J., Koga Y., Takano K., Kanaya S.
    Appl. Environ. Microbiol. 78:1556-1562(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of Leaf-branch compost bacterial cutinase homolog."
    Sulaiman S., You D.J., Eiko K., Koga Y., Kanaya S.
    Submitted (MAR-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 36-293, DISULFIDE BONDS.

Entry informationi

Entry nameiG9BY57_9BACT
AccessioniPrimary (citable) accession number: G9BY57
Entry historyi
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: June 24, 2015
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.