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P37698

- GUNF_CLOCE

UniProt

P37698 - GUNF_CLOCE

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
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MSKNFKRVGA VAVAAAMSLS IMATTSINAA SSPANKVYQD RFESMYSKIK    50
    DPANGYFSEQ GIPYHSIETL MVEAPDYGHV TTSEAMSYYM WLEAMHGRFS 100
    GDFTGFDKSW SVTEQYLIPT EKDQPNTSMS RYDANKPATY APEFQDPSKY 150
    PSPLDTSQPV GRDPINSQLT SAYGTSMLYG MHWILDVDNW YGFGARADGT 200
    SKPSYINTFQ RGEQESTWET IPQPCWDEHK FGGQYGFLDL FTKDTGTPAK 250
    QFKYTNAPDA DARAVQATYW ADQWAKEQGK SVSTSVGKAT KMGDYLRYSF 300
    FDKYFRKIGQ PSQAGTGYDA AHYLLSWYYA WGGGIDSTWS WIIGSSHNHF 350
    GYQNPFAAWV LSTDANFKPK SSNGASDWAK SLDRQLEFYQ WLQSAEGAIA 400
    GGATNSWNGR YEAVPSGTST FYGMGYVENP VYADPGSNTW FGMQVWSMQR 450
    VAELYYKTGD ARAKKLLDKW AKWINGEIKF NADGTFQIPS TIDWEGQPDT 500
    WNPTQGYTGN ANLHVKVVNY GTDLGCASSL ANTLTYYAAK SGDETSRQNA 550
    QKLLDAMWNN YSDSKGISTV EQRGDYHRFL DQEVFVPAGW TGKMPNGDVI 600
    KSGVKFIDIR SKYKQDPEWQ TMVAALQAGQ VPTQRLHRFW AQSEFAVANG 650
    VYAILFPDQG PEKLLGDVNG DETVDAIDLA ILKKYLLNSS TTINTANADM 700
    NSDNAIDAID YALLKKALLS IQ 722
    Length:722
    Mass (Da):80,544
    Last modified:October 1, 1996 - v2
    Checksum:i5E48F85319D70AE5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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: October 1, 2014
    This is version 98 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