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B8NIV9

- MANF_ASPFN

UniProt

B8NIV9 - MANF_ASPFN

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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

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
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: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-KW
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MRSLSSIALL SVVGAASAQA GPWAQCGGKS FSGSSECASG WKCQELNEWF
60 70 80 90 100
SQCVPGAEST TPTVSSTPTP TDAPSVSITA SATTGINKSI SVSSASKSTP
110 120 130 140 150
LPSSSSASPS PRPTGSGSFA KADGLQFSID GETKYFAGTN AYWLPFQMND
160 170 180 190 200
ADIDSVFDHL EQAGLKILRV WGFNDVNTAP SPGTVYFQLH DKEKSTSTIN
210 220 230 240 250
TGKDGLQRLD YVVAAAEKHG VKLIIPFVNS WDDYGGYNAY VKAYGGSKTE
260 270 280 290 300
WFTNEKIQSV YQAYIKAVVS RYRDSPAIFA WELGNEPRCS GCSTDVIHGW
310 320 330 340 350
ATKISAYIKS LDPNHMVALG DEGMGLTIGS DQSYPYGTSE GNDFEKNLAI
360 370 380 390 400
PDIDFGTLHL YTTDWGIKDN AWGNGWVENH AKACKAAGKP CLFEEYGMKG
410 420 430 440 450
NHCTDELKWQ KTSLSSGTAA DLIWQYGQQL STGESPKDAY SIFYGTDEWK
460
CAVMDHMENV NKN
Length:463
Mass (Da):49,994
Last modified:March 3, 2009 - v1
Checksum:i9DBA89743B6D4063
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 29, 2014
This is version 32 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