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A1DBV1

- MANF_NEOFI

UniProt

A1DBV1 - MANF_NEOFI

Protein

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

Gene

manF

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      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 sitei281 – 2811Proton donorBy similarity
    Active sitei390 – 3901NucleophileBy 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:NFIA_099770
    OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
    Taxonomic identifieri331117 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
    ProteomesiUP000006702: 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 – 456438Probable mannan endo-1,4-beta-mannosidase FPRO_0000393718Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliA1DBV1.
    SMRiA1DBV1. Positions 20-54, 112-456.
    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
    Regioni79 – 11335Ser-rich linkerAdd
    BLAST
    Regioni114 – 456343CatalyticAdd
    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

    eggNOGiCOG3934.
    HOGENOMiHOG000169951.
    OMAiEKNLAIP.
    OrthoDBiEOG7M3J90.

    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]
    ProDomiPD001821. CBD_fun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    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.

    A1DBV1-1 [UniParc]FASTAAdd to Basket

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    MRPLSSAALL SAIGAVAAQV GPWGQCGGQS YTGGTSCVSG WACVFLNDWY    50
    SQCQPGAEYT PPLCGRNDNP NIFQATTTST SVSATAPPSS TSSSTASVSS 100
    STSSTPIPTS SGSFVKAEGL KFNIDGETKY FAGTNAYWLP FLTNNADVDS 150
    VFDHLQQTGL KILRTWGFND VNSVPNPGTV YFQLHDPSTS TTTINTGADG 200
    LQRLDYVVSA AEKHGIKLLI PLVNNWDDYG GMNAYIKAYG GSKTEWYTNS 250
    KIQSVYQAYI KAVVSRYRDS PAIMAWELSN EARCQGCSTD VIYNWATKTS 300
    AYIKSLDPNH MVATGEEGMG LTVDSDGSYP YSTYEGSDFE KNLAIPHIDF 350
    GVFHLYTADW GITDNSWGNR WVTSHAKLCE AAGKPCLFEE YGLKDDHCSA 400
    AVVWQKTSLT TAGMAADLFW QYGQTLSTGQ SPNDRYTIYY GTSDWQCAVI 450
    DHVSRI 456
    Length:456
    Mass (Da):49,510
    Last modified:January 23, 2007 - v1
    Checksum:iD595CF3348D597DF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027694 Genomic DNA. Translation: EAW20341.1.
    RefSeqiXP_001262238.1. XM_001262237.1.

    Genome annotation databases

    EnsemblFungiiCADNFIAT00009414; CADNFIAP00009200; CADNFIAG00009414.
    GeneIDi4588382.
    KEGGinfi:NFIA_099770.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027694 Genomic DNA. Translation: EAW20341.1 .
    RefSeqi XP_001262238.1. XM_001262237.1.

    3D structure databases

    ProteinModelPortali A1DBV1.
    SMRi A1DBV1. Positions 20-54, 112-456.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADNFIAT00009414 ; CADNFIAP00009200 ; CADNFIAG00009414 .
    GeneIDi 4588382.
    KEGGi nfi:NFIA_099770.

    Phylogenomic databases

    eggNOGi COG3934.
    HOGENOMi HOG000169951.
    OMAi EKNLAIP.
    OrthoDBi EOG7M3J90.

    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 ]
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    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: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

    Entry informationi

    Entry nameiMANF_NEOFI
    AccessioniPrimary (citable) accession number: A1DBV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 42 of the entry and version 1 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