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Protein
Submitted name:

Cellulase

Gene

celG

Organism
Pseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Protein family/group databases

CAZyiCBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Submitted name:
CellulaseImported (EC:3.2.1.4Imported)
Gene namesi
Name:celGImported
OrganismiPseudoalteromonas haloplanktis (Alteromonas haloplanktis)Imported
Taxonomic identifieri228 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence analysisAdd
BLAST
Chaini33 – 494462Sequence analysisPRO_5004160338Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi722419.PH505_cs00040.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TVNX-ray1.41A/B33-325[»]
1TVPX-ray1.60A/B33-325[»]
ProteinModelPortaliO86099.
SMRiO86099. Positions 33-325, 434-494.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO86099.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini447 – 49044Chitin-binding type-3InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 5 (cellulase A) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG4107QWR. Bacteria.
COG2730. LUCA.

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
4.10.1080.10. 1 hit.
InterProiIPR032798. CBM_5_12_2.
IPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR003367. Thrombospondin_3-like_rpt.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PfamiPF14600. CBM_5_12_2. 1 hit.
PF00150. Cellulase. 1 hit.
PF02412. TSP_3. 3 hits.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 1 hit.
SSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O86099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNSSNNHKR KDFKVASLSL ALLLGCSTMA NAAVEKLTVS GNQILAGGEN
60 70 80 90 100
TSFAGPSLFW SNTGWGAEKF YTAETVAKAK TEFNATLIRA AIGHGTSTGG
110 120 130 140 150
SLNFDWEGNM SRLDTVVNAA IAEDMYVIID FHSHEAHTDQ ATAVRFFEDV
160 170 180 190 200
ATKYGQYDNV IYEIYNEPLQ ISWVNDIKPY AETVIDKIRA IDPDNLIVVG
210 220 230 240 250
TPTWSQDVDV ASQNPIDRAN IAYTLHFYAG THGQSYRNKA QTALDNGIAL
260 270 280 290 300
FATEWGTVNA DGNGGVNINE TDAWMAFFKT NNISHANWAL NDKNEGASLF
310 320 330 340 350
TPGGSWNSLT SSGSKVKEII QGWGGGSSNV DLDSDGDGVS DSLDQCNNTP
360 370 380 390 400
AGTTVDSIGC AVTDSDADGI SDNVDQCPNT PVGETVNNVG CVVEVVEPQS
410 420 430 440 450
DADNDGVNDD IDQCPDTPAG TSVDTNGCSV VSSTDCNGIN AYPNWVNKDY
460 470 480 490
SGGPFTHNNT DDKMQYQGNA YSANWYTNSL PGSDASWTLL YTCN
Length:494
Mass (Da):52,873
Last modified:November 1, 1998 - v1
Checksum:i2A32E4EEC1DAB513
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17552 Genomic DNA. Translation: CAA76775.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17552 Genomic DNA. Translation: CAA76775.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TVNX-ray1.41A/B33-325[»]
1TVPX-ray1.60A/B33-325[»]
ProteinModelPortaliO86099.
SMRiO86099. Positions 33-325, 434-494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi722419.PH505_cs00040.

Protein family/group databases

CAZyiCBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QWR. Bacteria.
COG2730. LUCA.

Miscellaneous databases

EvolutionaryTraceiO86099.

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
4.10.1080.10. 1 hit.
InterProiIPR032798. CBM_5_12_2.
IPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR003367. Thrombospondin_3-like_rpt.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PfamiPF14600. CBM_5_12_2. 1 hit.
PF00150. Cellulase. 1 hit.
PF02412. TSP_3. 3 hits.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 1 hit.
SSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Garsoux G., Barras F., Gerday C.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Antarctic A23Imported.
  2. "Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering."
    Violot S., Aghajari N., Czjzek M., Feller G., Sonan G.K., Gouet P., Gerday C., Haser R., Receveur-Brechot V.
    J. Mol. Biol. 348:1211-1224(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 33-325.

Entry informationi

Entry nameiO86099_PSEHA
AccessioniPrimary (citable) accession number: O86099
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: April 13, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.