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Protein

Cellulase 1

Gene

cel1

Organism
Streptomyces reticuli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This endoglucanase acts only on crystalline cellulose.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei669PROSITE-ProRule annotation1
Active sitei717PROSITE-ProRule annotation1
Active sitei726PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulase 1 (EC:3.2.1.4)
Alternative name(s):
Avicelase
Endo-1,4-beta-glucanase
Endoglucanase
Gene namesi
Name:cel1
OrganismiStreptomyces reticuli
Taxonomic identifieri1926 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi


    Note: Exists in both mycelium-associated and extracellular forms.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000000795830 – 746Cellulase 1Add BLAST717

Structurei

3D structure databases

ProteinModelPortaliQ05156.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 170CBM-cenCAdd BLAST126

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni171 – 211LinkerAdd BLAST41
Regioni212 – 746CatalyticAdd BLAST535

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

CDDicd02850. E_set_Cellulase_N. 1 hit.
Gene3Di1.50.10.10. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR004197. Cellulase_Ig-like.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF02018. CBM_4_9. 1 hit.
PF02927. CelD_N. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q05156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRRTTAVLT LTALLGTALT ALPVQQAGAE EVEQVRNGTF DTTTDPWWTS
60 70 80 90 100
NVTAGLSDGR LCADVPGGTT NRWDSAIGQN DITLVKGETY RFSFHASGIP
110 120 130 140 150
EGHVVRAVVG LAVSPYDTWQ EASPVLTEAD GSYSYTFTAP VDTTQGQVAF
160 170 180 190 200
QVGGSTDAWR FCVDDVSLLG GVPPEVYEPD TGPRVRVNQV AYLPAGPKNA
210 220 230 240 250
TLVTDATARL PWQLRNAQGT TVARGLTVPR GVDASSGQNV HSIDFGSYRG
260 270 280 290 300
RGTGYTLVAD GETSHPFDID AAAYRPLRLD SVKYYYTQRS GIAIRDDLRP
310 320 330 340 350
GYGRAAGHLN VAPNQGDANV PCQPGVCDYT LDVTGGWYDA GDHGKYVVNG
360 370 380 390 400
GIATWELLST YERSLTARTG HPAALGDGTL ALPESGNKVP DVLDEARWEL
410 420 430 440 450
EFLLKMQVPA GQPLAGMAHH KLHDEQWTGL PLLPDQDPQK RELHPPTTAA
460 470 480 490 500
TLNLAATAAQ AARLYRPFDK AFAARALTAA RTAWQAALAH PDLLADPNDG
510 520 530 540 550
TGGGAYNDDD VTDEFYWAAA ELYLTTGERQ FADHVLDSPV HTADIFGPTG
560 570 580 590 600
FDWGHTAAAG RLDLALVPSR LPGRDQVRRS VIKAADTYLA TLTAHPYGMP
610 620 630 640 650
YAPAGNRYDW GSSHQVLNNG VVLASAYDLT GAAKYRDGAL QGMDYVLGRN
660 670 680 690 700
ALNMSYVTGY GEVSSHNQHS RWYAHQLDPT LPNPPSGTLA GGPNSSIQDP
710 720 730 740
YAQSKLTGCV GQFCYIDDIQ SWSTNETAIN WNAALARMAS FAADQG
Length:746
Mass (Da):80,000
Last modified:June 1, 1994 - v1
Checksum:iFDF1ADB4714A35FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65616 Genomic DNA. Translation: CAA46570.1.
PIRiS27985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65616 Genomic DNA. Translation: CAA46570.1.
PIRiS27985.

3D structure databases

ProteinModelPortaliQ05156.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd02850. E_set_Cellulase_N. 1 hit.
Gene3Di1.50.10.10. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR004197. Cellulase_Ig-like.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF02018. CBM_4_9. 1 hit.
PF02927. CelD_N. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUN1_STRRE
AccessioniPrimary (citable) accession number: Q05156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 5, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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.