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Protein

Glucanase

Gene

E3

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi180CalciumCombined sources1
Active sitei264UniRule annotation1
Active sitei312Proton donorUniRule annotation1
Metal bindingi457Calcium; via carbonyl oxygenCombined sources1
Active sitei535NucleophileUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradationUniRule annotation, Polysaccharide degradation

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
GlucanaseUniRule annotation (EC:3.2.1.-UniRule annotation)
Gene namesi
Name:E3Imported
OrganismiThermobifida fusca (Thermomonospora fusca)Imported
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33UniRule annotationAdd BLAST33
ChainiPRO_500514382934 – 596GlucanaseUniRule annotationAdd BLAST563

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi265 ↔ 330Combined sources
Disulfide bondi503 ↔ 553Combined sources

Keywords - PTMi

Disulfide bondUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi269800.Tfu_0620.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B4FX-ray2.20A/B177-596[»]
4B4HX-ray1.50A/B177-596[»]
ProteinModelPortaliQ60029.
SMRiQ60029.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 142CBM2 (carbohydrate binding type-2)InterPro annotationAdd BLAST109

Sequence similaritiesi

Belongs to the glycosyl hydrolase family 6.UniRule annotation
Contains 1 CBM2 (carbohydrate binding type-2) domain.UniRule annotation

Keywords - Domaini

SignalUniRule annotation

Phylogenomic databases

eggNOGiENOG41065HY. Bacteria.
COG5297. LUCA.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKVRATNRR SWMRRGLAAA SGLALGASMV AFAAPANAAG CSVDYTVNSW
60 70 80 90 100
GTGFTANVTI TNLGSAINGW TLEWDFPGNQ QVTNLWNGTY TQSGQHVSVS
110 120 130 140 150
NAPYNASIPA NGTVEFGFNG SYSGSNDIPS SFKLNGVTCD GSDDPDPEPS
160 170 180 190 200
PSPSPSPSPT DPDEPGGPTN PPTNPGEKVD NPFEGAKLYV NPVWSAKAAA
210 220 230 240 250
EPGGSAVANE STAVWLDRIG AIEGNDSPTT GSMGLRDHLE EAVRQSGGDP
260 270 280 290 300
LTIQVVIYNL PGRDCAALAS NGELGPDELD RYKSEYIDPI ADIMWDFADY
310 320 330 340 350
ENLRIVAIIE IDSLPNLVTN VGGNGGTELC AYMKQNGGYV NGVGYALRKL
360 370 380 390 400
GEIPNVYNYI DAAHHGWIGW DSNFGPSVDI FYEAANASGS TVDYVHGFIS
410 420 430 440 450
NTANYSATVE PYLDVNGTVN GQLIRQSKWV DWNQYVDELS FVQDLRQALI
460 470 480 490 500
AKGFRSDIGM LIDTSRNGWG GPNRPTGPSS STDLNTYVDE SRIDRRIHPG
510 520 530 540 550
NWCNQAGAGL GERPTVNPAP GVDAYVWVKP PGESDGASEE IPNDEGKGFD
560 570 580 590
RMCDPTYQGN ARNGNNPSGA LPNAPISGHW FSAQFRELLA NAYPPL
Length:596
Mass (Da):63,548
Last modified:November 1, 1996 - v1
Checksum:iB0FA5277FE7721E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18978 Genomic DNA. Translation: AAA62211.1.
PIRiA55976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18978 Genomic DNA. Translation: AAA62211.1.
PIRiA55976.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B4FX-ray2.20A/B177-596[»]
4B4HX-ray1.50A/B177-596[»]
ProteinModelPortaliQ60029.
SMRiQ60029.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269800.Tfu_0620.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG41065HY. Bacteria.
COG5297. LUCA.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ60029_THEFU
AccessioniPrimary (citable) accession number: Q60029
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 88 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.