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B0Y9E7

- MANF_ASPFC

UniProt

B0Y9E7 - MANF_ASPFC

Protein

Probable mannan endo-1,4-beta-mannosidase F

Gene

manF

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 2 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.By similarity

    Catalytic activityi

    Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei264 – 2641Proton donorBy similarity
    Active sitei373 – 3731NucleophileBy similarity

    GO - Molecular functioni

    1. cellulose binding Source: InterPro
    2. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable mannan endo-1,4-beta-mannosidase F (EC:3.2.1.78)
    Alternative name(s):
    Endo-beta-1,4-mannanase F
    Gene namesi
    Name:manF
    ORF Names:AFUB_080770
    OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
    Taxonomic identifieri451804 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001699: Unassembled WGS sequence

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 438420Probable mannan endo-1,4-beta-mannosidase FPRO_0000393713Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliB0Y9E7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 5436CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni60 – 9637Ser-rich linkerAdd
    BLAST
    Regioni97 – 438342CatalyticAdd
    BLAST

    Domaini

    Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-mannanase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

    Sequence similaritiesi

    Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000169951.
    OrthoDBiEOG7M3J90.
    PhylomeDBiB0Y9E7.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR000254. Cellulose-bd_dom_fun.
    IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00734. CBM_1. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SMARTiSM00236. fCBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEiPS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    B0Y9E7-1 [UniParc]FASTAAdd to Basket

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    MHPLPSVALL SAIGAVAAQV GPWGQCGGRS YTGETSCVSG WSCVLFNEWY    50
    SQCQPATTTS TSSVSATAAP SSTSSSKESV PSATTSKKPV PTGSSSFVKA 100
    DGLKFNIDGE TKYFAGTNAY WLPFLTNDAD VDSVMDNLQK AGLKILRTWG 150
    FNDVNSKPSS GTVYFQLHDP STGTTTINTG ADGLQRLDYV VSAAEKRGIK 200
    LLIPLVNNWD DYGGMNAYVK AYGGSKTEWY TNSKIQSVYQ AYIKAVVSRY 250
    RDSPAIMAWE LSNEARCQGC STDVIYNWTA KTSAYIKSLD PNHMVATGDE 300
    GMGVTVDSDG SYPYSTYEGS DFAKNLAAPD IDFGVFHLYT EDWGIKDNSW 350
    GNGWVTSHAK VCKAAGKPCL FEEYGLKDDH CSASLTWQKT SVSSGMAADL 400
    FWQYGQTLST GPSPNDHFTI YYGTSDWQCG VADHLSTL 438
    Length:438
    Mass (Da):47,327
    Last modified:April 20, 2010 - v2
    Checksum:i8E55123506BD7E24
    GO

    Sequence cautioni

    The sequence EDP48640.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499600 Genomic DNA. Translation: EDP48640.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499600 Genomic DNA. Translation: EDP48640.1 . Different initiation.

    3D structure databases

    ProteinModelPortali B0Y9E7.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOGENOMi HOG000169951.
    OrthoDBi EOG7M3J90.
    PhylomeDBi B0Y9E7.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR000254. Cellulose-bd_dom_fun.
    IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CEA10 / CBS 144.89 / FGSC A1163.

    Entry informationi

    Entry nameiMANF_ASPFC
    AccessioniPrimary (citable) accession number: B0Y9E7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 33 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    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