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B0Y9E7

- MANF_ASPFC

UniProt

B0Y9E7 - MANF_ASPFC

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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

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
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: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-KW
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MHPLPSVALL SAIGAVAAQV GPWGQCGGRS YTGETSCVSG WSCVLFNEWY
60 70 80 90 100
SQCQPATTTS TSSVSATAAP SSTSSSKESV PSATTSKKPV PTGSSSFVKA
110 120 130 140 150
DGLKFNIDGE TKYFAGTNAY WLPFLTNDAD VDSVMDNLQK AGLKILRTWG
160 170 180 190 200
FNDVNSKPSS GTVYFQLHDP STGTTTINTG ADGLQRLDYV VSAAEKRGIK
210 220 230 240 250
LLIPLVNNWD DYGGMNAYVK AYGGSKTEWY TNSKIQSVYQ AYIKAVVSRY
260 270 280 290 300
RDSPAIMAWE LSNEARCQGC STDVIYNWTA KTSAYIKSLD PNHMVATGDE
310 320 330 340 350
GMGVTVDSDG SYPYSTYEGS DFAKNLAAPD IDFGVFHLYT EDWGIKDNSW
360 370 380 390 400
GNGWVTSHAK VCKAAGKPCL FEEYGLKDDH CSASLTWQKT SVSSGMAADL
410 420 430
FWQYGQTLST GPSPNDHFTI YYGTSDWQCG VADHLSTL
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 29, 2014
This is version 34 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