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P29719

- GUNA_PAELA

UniProt

P29719 - GUNA_PAELA

Protein

Endoglucanase A

Gene

celA

Organism
Paenibacillus lautus (Bacillus lautus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei213 – 2131By similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiCBM3. Carbohydrate-Binding Module Family 3.
    GH44. Glycoside Hydrolase Family 44.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase A (EC:3.2.1.4)
    Alternative name(s):
    Cellulase A
    EG-A
    Endo-1,4-beta-glucanase
    Gene namesi
    Name:celA
    OrganismiPaenibacillus lautus (Bacillus lautus)
    Taxonomic identifieri1401 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 700667Endoglucanase APRO_0000008021Add
    BLAST

    Post-translational modificationi

    A short form (EG-A-S) arises from post-translational proteolysis of approximately 150 AA at the C-terminus of EG-A-L.

    Structurei

    3D structure databases

    ProteinModelPortaliP29719.
    SMRiP29719. Positions 33-543.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini550 – 700151CBM3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.710. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR024745. Glyco_hydro_44.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00942. CBM_3. 1 hit.
    PF12891. Glyco_hydro_44. 1 hit.
    [Graphical view]
    SMARTiSM01067. CBM_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51172. CBM3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29719-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTRQRKRLF VSAALAVSLT MTVPMPASVN AAASDVTFTI NTQSERAAIS    50
    PNIYGTNQDL SGTENWSSRR LGGNRLTGYN WENNASSAGR DWLHYSDDFL 100
    CGNGGVPDTD CDKPGAVVTA FHDKSLENGA YSIVTLQMAG YVSRDKNGPV 150
    DESETAPSPR WDKVEFAKNA PFSLQPHLND GQVYMDEEVN FLVNRYGNAS 200
    TSTGIKAYSL DNEPALWSET HPRIHPEQLQ AAELVAKSID LSKAVKNVDP 250
    HAEIFGPALY GFGAYLSLQD APGWPSLQGN YSWFIDYYLD QMKNAHTQNG 300
    KRLLDVLDVH WYPEAQGGGQ RIVFGGAGNI DTQKARVQAP RSLWDPAYQE 350
    DSWIGTWFSS YLPLIPKLQS SIQTYYPGTK LAITESSYGG DNHISGGIAT 400
    ADALGIFGKY GVYAANYWQT EDNTDYTSAA YKLYRNYDGN KSGFGSIKVD 450
    AATSDTENSS VYASVTDEEN SELHLIVLNK NFDDPINATF QLSGDKTYTS 500
    GRVWGFDQTG SDITEQAAIT NINNNQFTYT LPPLSAYHIV LKADSTEPVN 550
    SDLVVQYKDG DRNNATDNQI KPHFNIQNKG TSPVDLSSLT LRYYFTKDSS 600
    AAMNGWIDWA KLGGSNIQIS FGNHNGADSD TYAELGFSSG AGSIAEGGQS 650
    GEIQLRMSKA DWSNFNEAND YSFDGAKTAY IDWDRVTLYQ DGQLVWGIEP 700
    Length:700
    Mass (Da):76,910
    Last modified:April 1, 1993 - v1
    Checksum:i3D5C8CADA53EEE0F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76588 Genomic DNA. Translation: AAA22303.1.
    PIRiB41897.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76588 Genomic DNA. Translation: AAA22303.1 .
    PIRi B41897.

    3D structure databases

    ProteinModelPortali P29719.
    SMRi P29719. Positions 33-543.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM3. Carbohydrate-Binding Module Family 3.
    GH44. Glycoside Hydrolase Family 44.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.40.710. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR024745. Glyco_hydro_44.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00942. CBM_3. 1 hit.
    PF12891. Glyco_hydro_44. 1 hit.
    [Graphical view ]
    SMARTi SM01067. CBM_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51172. CBM3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "celA from Bacillus lautus PL236 encodes a novel cellulose-binding endo-beta-1,4-glucanase."
      Hansen C.K., Diderichsen B., Joergensen P.L.
      J. Bacteriol. 174:3522-3531(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: PL236.

    Entry informationi

    Entry nameiGUNA_PAELA
    AccessioniPrimary (citable) accession number: P29719
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3