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P37698

- GUNF_CLOCE

UniProt

P37698 - GUNF_CLOCE

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Protein

Endoglucanase F

Gene

celCCF

Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Probable endoglucanase involved in the degradation of cellulose or related beta-glucans.

Catalytic activityi

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

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciCCEL394503:GJET-750-MONOMER.

Protein family/group databases

CAZyiGH48. Glycoside Hydrolase Family 48.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase F (EC:3.2.1.4)
Alternative name(s):
Cellulase F
EGCCF
Endo-1,4-beta-glucanase F
Gene namesi
Name:celCCF
Ordered Locus Names:Ccel_0729
OrganismiClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Taxonomic identifieri394503 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001349: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 722693Endoglucanase FPRO_0000008026Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi394503.Ccel_0729.

Structurei

Secondary structure

1
722
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 5015Combined sources
Helixi52 – 543Combined sources
Beta strandi65 – 673Combined sources
Beta strandi73 – 775Combined sources
Beta strandi80 – 823Combined sources
Helixi83 – 10018Combined sources
Helixi104 – 11613Combined sources
Turni121 – 1233Combined sources
Helixi126 – 1294Combined sources
Helixi147 – 1493Combined sources
Beta strandi151 – 1533Combined sources
Helixi166 – 1738Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi202 – 2076Combined sources
Helixi217 – 2193Combined sources
Beta strandi223 – 2275Combined sources
Beta strandi229 – 2335Combined sources
Helixi238 – 2403Combined sources
Beta strandi251 – 2566Combined sources
Helixi258 – 27619Combined sources
Turni277 – 2793Combined sources
Helixi283 – 29513Combined sources
Helixi296 – 3005Combined sources
Beta strandi310 – 3145Combined sources
Helixi318 – 3203Combined sources
Beta strandi330 – 3378Combined sources
Beta strandi340 – 3434Combined sources
Beta strandi346 – 3494Combined sources
Helixi350 – 3523Combined sources
Helixi355 – 3639Combined sources
Helixi365 – 3673Combined sources
Beta strandi370 – 3734Combined sources
Helixi374 – 39118Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi402 – 4076Combined sources
Turni408 – 4114Combined sources
Beta strandi424 – 4296Combined sources
Turni433 – 4386Combined sources
Helixi442 – 45817Combined sources
Helixi461 – 47515Combined sources
Beta strandi486 – 49611Combined sources
Turni503 – 5053Combined sources
Beta strandi514 – 5218Combined sources
Helixi524 – 54118Combined sources
Helixi544 – 56017Combined sources
Beta strandi561 – 5633Combined sources
Beta strandi570 – 5723Combined sources
Turni574 – 5774Combined sources
Helixi578 – 5814Combined sources
Helixi606 – 6094Combined sources
Helixi611 – 6155Combined sources
Helixi619 – 6279Combined sources
Beta strandi633 – 6353Combined sources
Helixi639 – 65517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F9DX-ray2.30A30-658[»]
1F9OX-ray2.50A30-658[»]
1FAEX-ray2.00A30-658[»]
1FBOX-ray2.30A30-658[»]
1FBWX-ray2.00A30-658[»]
1FCEX-ray2.00A30-658[»]
1G9GX-ray1.90A30-658[»]
1G9JX-ray1.90A30-658[»]
2QNOX-ray2.00A30-658[»]
ProteinModelPortaliP37698.
SMRiP37698. Positions 30-658.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37698.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati667 – 690241Add
BLAST
Repeati699 – 722242Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni667 – 722562 X 24 AA approximate repeatsAdd
BLAST

Domaini

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG10655.
HOGENOMiHOG000020369.
OMAiTYHRFWS.
OrthoDBiEOG64V28H.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
[Graphical view]
PfamiPF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P37698-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKNFKRVGA VAVAAAMSLS IMATTSINAA SSPANKVYQD RFESMYSKIK
60 70 80 90 100
DPANGYFSEQ GIPYHSIETL MVEAPDYGHV TTSEAMSYYM WLEAMHGRFS
110 120 130 140 150
GDFTGFDKSW SVTEQYLIPT EKDQPNTSMS RYDANKPATY APEFQDPSKY
160 170 180 190 200
PSPLDTSQPV GRDPINSQLT SAYGTSMLYG MHWILDVDNW YGFGARADGT
210 220 230 240 250
SKPSYINTFQ RGEQESTWET IPQPCWDEHK FGGQYGFLDL FTKDTGTPAK
260 270 280 290 300
QFKYTNAPDA DARAVQATYW ADQWAKEQGK SVSTSVGKAT KMGDYLRYSF
310 320 330 340 350
FDKYFRKIGQ PSQAGTGYDA AHYLLSWYYA WGGGIDSTWS WIIGSSHNHF
360 370 380 390 400
GYQNPFAAWV LSTDANFKPK SSNGASDWAK SLDRQLEFYQ WLQSAEGAIA
410 420 430 440 450
GGATNSWNGR YEAVPSGTST FYGMGYVENP VYADPGSNTW FGMQVWSMQR
460 470 480 490 500
VAELYYKTGD ARAKKLLDKW AKWINGEIKF NADGTFQIPS TIDWEGQPDT
510 520 530 540 550
WNPTQGYTGN ANLHVKVVNY GTDLGCASSL ANTLTYYAAK SGDETSRQNA
560 570 580 590 600
QKLLDAMWNN YSDSKGISTV EQRGDYHRFL DQEVFVPAGW TGKMPNGDVI
610 620 630 640 650
KSGVKFIDIR SKYKQDPEWQ TMVAALQAGQ VPTQRLHRFW AQSEFAVANG
660 670 680 690 700
VYAILFPDQG PEKLLGDVNG DETVDAIDLA ILKKYLLNSS TTINTANADM
710 720
NSDNAIDAID YALLKKALLS IQ
Length:722
Mass (Da):80,544
Last modified:October 1, 1996 - v2
Checksum:i5E48F85319D70AE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30321 Genomic DNA. Translation: AAB41452.1.
CP001348 Genomic DNA. Translation: ACL75108.1.
M87018 Genomic DNA. Translation: AAA73866.1.
PIRiPC1139.
RefSeqiWP_015924275.1. NC_011898.1.
YP_002505088.1. NC_011898.1.

Genome annotation databases

EnsemblBacteriaiACL75108; ACL75108; Ccel_0729.
GeneIDi7309583.
KEGGicce:Ccel_0729.
PATRICi19432255. VBICloCel57783_0754.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30321 Genomic DNA. Translation: AAB41452.1 .
CP001348 Genomic DNA. Translation: ACL75108.1 .
M87018 Genomic DNA. Translation: AAA73866.1 .
PIRi PC1139.
RefSeqi WP_015924275.1. NC_011898.1.
YP_002505088.1. NC_011898.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F9D X-ray 2.30 A 30-658 [» ]
1F9O X-ray 2.50 A 30-658 [» ]
1FAE X-ray 2.00 A 30-658 [» ]
1FBO X-ray 2.30 A 30-658 [» ]
1FBW X-ray 2.00 A 30-658 [» ]
1FCE X-ray 2.00 A 30-658 [» ]
1G9G X-ray 1.90 A 30-658 [» ]
1G9J X-ray 1.90 A 30-658 [» ]
2QNO X-ray 2.00 A 30-658 [» ]
ProteinModelPortali P37698.
SMRi P37698. Positions 30-658.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 394503.Ccel_0729.

Protein family/group databases

CAZyi GH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL75108 ; ACL75108 ; Ccel_0729 .
GeneIDi 7309583.
KEGGi cce:Ccel_0729.
PATRICi 19432255. VBICloCel57783_0754.

Phylogenomic databases

eggNOGi NOG10655.
HOGENOMi HOG000020369.
OMAi TYHRFWS.
OrthoDBi EOG64V28H.

Enzyme and pathway databases

BioCyci CCEL394503:GJET-750-MONOMER.

Miscellaneous databases

EvolutionaryTracei P37698.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
[Graphical view ]
Pfami PF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view ]
PRINTSi PR00844. GLHYDRLASE48.
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular study and overexpression of the Clostridium cellulolyticum celF cellulase gene in Escherichia coli."
    Reverbel-Leroy C., Belaich A., Bernadac A., Gaudin C., Belaich J.-P., Tardif C.
    Microbiology 142:1013-1023(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
  3. "Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum."
    Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., Belaich J.-P.
    Gene 119:17-28(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 387-722.

Entry informationi

Entry nameiGUNF_CLOCE
AccessioniPrimary (citable) accession number: P37698
Secondary accession number(s): B8I7V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3