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Protein

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

Gene

manF

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei281Proton donorBy similarity1
Active sitei390NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

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 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Taxonomic identifieri331117 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006702 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:NFIA_099770.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000039371819 – 456Probable mannan endo-1,4-beta-mannosidase FAdd BLAST438

Structurei

3D structure databases

ProteinModelPortaliA1DBV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 54CBM1PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni79 – 113Ser-rich linkerAdd BLAST35
Regioni114 – 456CatalyticAdd BLAST343

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.
KOiK19355.
OMAiQWIQDHA.
OrthoDBiEOG092C2KMO.

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

« Hide

        10         20         30         40         50
MRPLSSAALL SAIGAVAAQV GPWGQCGGQS YTGGTSCVSG WACVFLNDWY
60 70 80 90 100
SQCQPGAEYT PPLCGRNDNP NIFQATTTST SVSATAPPSS TSSSTASVSS
110 120 130 140 150
STSSTPIPTS SGSFVKAEGL KFNIDGETKY FAGTNAYWLP FLTNNADVDS
160 170 180 190 200
VFDHLQQTGL KILRTWGFND VNSVPNPGTV YFQLHDPSTS TTTINTGADG
210 220 230 240 250
LQRLDYVVSA AEKHGIKLLI PLVNNWDDYG GMNAYIKAYG GSKTEWYTNS
260 270 280 290 300
KIQSVYQAYI KAVVSRYRDS PAIMAWELSN EARCQGCSTD VIYNWATKTS
310 320 330 340 350
AYIKSLDPNH MVATGEEGMG LTVDSDGSYP YSTYEGSDFE KNLAIPHIDF
360 370 380 390 400
GVFHLYTADW GITDNSWGNR WVTSHAKLCE AAGKPCLFEE YGLKDDHCSA
410 420 430 440 450
AVVWQKTSLT TAGMAADLFW QYGQTLSTGQ SPNDRYTIYY GTSDWQCAVI

DHVSRI
Length:456
Mass (Da):49,510
Last modified:January 23, 2007 - v1
Checksum:iD595CF3348D597DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
DS027694 Genomic DNA. Translation: EAW20341.1.
RefSeqiXP_001262238.1. XM_001262237.1.

3D structure databases

ProteinModelPortaliA1DBV1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:NFIA_099770.

Phylogenomic databases

HOGENOMiHOG000169951.
KOiK19355.
OMAiQWIQDHA.
OrthoDBiEOG092C2KMO.

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]
ProtoNetiSearch...

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 5, 2016
This is version 56 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.