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A1C8U0

- MANF_ASPCL

UniProt

A1C8U0 - MANF_ASPCL

Protein

Mannan endo-1,4-beta-mannosidase F

Gene

manF

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 39 (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 sitei261 – 2611Proton donorBy similarity
    Active sitei370 – 3701NucleophileBy 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:
    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:ACLA_044470
    OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
    Taxonomic identifieri344612 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006701: 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 – 436418Mannan endo-1,4-beta-mannosidase FPRO_0000393712Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliA1C8U0.
    SMRiA1C8U0. Positions 20-54, 92-436.
    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 – 436323CatalyticAdd
    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.
    PROSITEiPS51164. CBM1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    A1C8U0-1 [UniParc]FASTAAdd to Basket

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    MRSLSSVALL SAIGAASAQA GPWGQCAGIS HTGPTTCESG WSCVYLNDWY    50
    SQCQPGAATS SSTTVSSTKQ PSSTVAAPSS TTSAHTLPTG SGSFAKTDGL 100
    KFNIDGKTKY FAGTNAYWLP FLTNNADVDA VFDHLQQTGL KILRTWGFND 150
    VNTIPGSGTV YFQLHDKATG TSTINTGANG LQRLDYVISA AEKHGIKLII 200
    PFVNNWDDYG GMNAYINAYG GSKTEWYTNE KIQSVYQAYI KAIVSRYRDS 250
    PAIFAWELGN EPRCKGCSTD VIYNWVAKTS AYIKSLDPNH MVTTGEEGMG 300
    LTVDSDGSYP YSKDEGSDFA RNLAAPDIDF GVYHLYVADW GVSDNAWGNR 350
    WIKSHAKVCE AAGKPCLFEE YGIKDDHCGD SLKWQKTSLT TTANSADLFW 400
    QYGQQLSTGA SPNDHYTIYY GTDDWKCAVI DHISQI 436
    Length:436
    Mass (Da):47,428
    Last modified:January 23, 2007 - v1
    Checksum:i5183B090F2AF6246
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027046 Genomic DNA. Translation: EAW13727.1.
    RefSeqiXP_001275153.1. XM_001275152.1.

    Genome annotation databases

    EnsemblFungiiCADACLAT00004242; CADACLAP00004144; CADACLAG00004242.
    GeneIDi4707278.
    KEGGiact:ACLA_044470.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027046 Genomic DNA. Translation: EAW13727.1 .
    RefSeqi XP_001275153.1. XM_001275152.1.

    3D structure databases

    ProteinModelPortali A1C8U0.
    SMRi A1C8U0. Positions 20-54, 92-436.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADACLAT00004242 ; CADACLAP00004144 ; CADACLAG00004242 .
    GeneIDi 4707278.
    KEGGi act:ACLA_044470.

    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 PS51164. CBM1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

    Entry informationi

    Entry nameiMANF_ASPCL
    AccessioniPrimary (citable) accession number: A1C8U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 39 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, Reference 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