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B8NIV9

- MANF_ASPFN

UniProt

B8NIV9 - MANF_ASPFN

Protein

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

Gene

manF

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 31 (01 Oct 2014)
      Sequence version 1 (03 Mar 2009)
      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 sitei286 – 2861Proton donorBy similarity
    Active sitei395 – 3951NucleophileBy 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:AFLA_069870
    OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
    Taxonomic identifieri332952 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001875: 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 – 463445Probable mannan endo-1,4-beta-mannosidase FPRO_0000393714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliB8NIV9.
    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
    Regioni75 – 11844Ser-rich linkerAdd
    BLAST
    Regioni119 – 463345CatalyticAdd
    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]
    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.

    B8NIV9-1 [UniParc]FASTAAdd to Basket

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    MRSLSSIALL SVVGAASAQA GPWAQCGGKS FSGSSECASG WKCQELNEWF    50
    SQCVPGAEST TPTVSSTPTP TDAPSVSITA SATTGINKSI SVSSASKSTP 100
    LPSSSSASPS PRPTGSGSFA KADGLQFSID GETKYFAGTN AYWLPFQMND 150
    ADIDSVFDHL EQAGLKILRV WGFNDVNTAP SPGTVYFQLH DKEKSTSTIN 200
    TGKDGLQRLD YVVAAAEKHG VKLIIPFVNS WDDYGGYNAY VKAYGGSKTE 250
    WFTNEKIQSV YQAYIKAVVS RYRDSPAIFA WELGNEPRCS GCSTDVIHGW 300
    ATKISAYIKS LDPNHMVALG DEGMGLTIGS DQSYPYGTSE GNDFEKNLAI 350
    PDIDFGTLHL YTTDWGIKDN AWGNGWVENH AKACKAAGKP CLFEEYGMKG 400
    NHCTDELKWQ KTSLSSGTAA DLIWQYGQQL STGESPKDAY SIFYGTDEWK 450
    CAVMDHMENV NKN 463
    Length:463
    Mass (Da):49,994
    Last modified:March 3, 2009 - v1
    Checksum:i9DBA89743B6D4063
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EQ963479 Genomic DNA. Translation: EED50165.1.
    RefSeqiXP_002380546.1. XM_002380505.1.

    Genome annotation databases

    EnsemblFungiiCADAFLAT00008411; CADAFLAP00008411; CADAFLAG00008411.
    GeneIDi7914152.
    KEGGiafv:AFLA_069870.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EQ963479 Genomic DNA. Translation: EED50165.1 .
    RefSeqi XP_002380546.1. XM_002380505.1.

    3D structure databases

    ProteinModelPortali B8NIV9.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFLAT00008411 ; CADAFLAP00008411 ; CADAFLAG00008411 .
    GeneIDi 7914152.
    KEGGi afv:AFLA_069870.

    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 ]
    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. "Genome sequence of Aspergillus flavus strain NRRL 3357."
      Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
      Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

    Entry informationi

    Entry nameiMANF_ASPFN
    AccessioniPrimary (citable) accession number: B8NIV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 31 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