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A1DBV1

- MANF_NEOFI

UniProt

A1DBV1 - MANF_NEOFI

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Protein

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

Gene
manF, NFIA_099770
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

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 donor By similarity
Active sitei390 – 3901Nucleophile By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 456438Probable mannan endo-1,4-beta-mannosidase FPRO_0000393718Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA1DBV1.
SMRiA1DBV1. Positions 20-54, 112-456.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 5436CBM1Add
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

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: May 14, 2014
This is version 41 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

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