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A1C8U0

- MANF_ASPCL

UniProt

A1C8U0 - MANF_ASPCL

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Protein

Mannan endo-1,4-beta-mannosidase F

Gene

manF

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
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 sitei261 – 2611Proton donorBy similarity
Active sitei370 – 3701NucleophileBy 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:
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:ACLA_044470
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006701: 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 – 436418Mannan endo-1,4-beta-mannosidase FPRO_0000393712Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA1C8U0.
SMRiA1C8U0. Positions 20-54, 92-436.
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
Regioni79 – 11335Ser-rich linkerAdd
BLAST
Regioni114 – 436323CatalyticAdd
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]
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.
PROSITEiPS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A1C8U0-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MRSLSSVALL SAIGAASAQA GPWGQCAGIS HTGPTTCESG WSCVYLNDWY
60 70 80 90 100
SQCQPGAATS SSTTVSSTKQ PSSTVAAPSS TTSAHTLPTG SGSFAKTDGL
110 120 130 140 150
KFNIDGKTKY FAGTNAYWLP FLTNNADVDA VFDHLQQTGL KILRTWGFND
160 170 180 190 200
VNTIPGSGTV YFQLHDKATG TSTINTGANG LQRLDYVISA AEKHGIKLII
210 220 230 240 250
PFVNNWDDYG GMNAYINAYG GSKTEWYTNE KIQSVYQAYI KAIVSRYRDS
260 270 280 290 300
PAIFAWELGN EPRCKGCSTD VIYNWVAKTS AYIKSLDPNH MVTTGEEGMG
310 320 330 340 350
LTVDSDGSYP YSKDEGSDFA RNLAAPDIDF GVYHLYVADW GVSDNAWGNR
360 370 380 390 400
WIKSHAKVCE AAGKPCLFEE YGIKDDHCGD SLKWQKTSLT TTANSADLFW
410 420 430
QYGQQLSTGA SPNDHYTIYY GTDDWKCAVI DHISQI
Length:436
Mass (Da):47,428
Last modified:January 23, 2007 - v1
Checksum:i5183B090F2AF6246
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS027046 Genomic DNA. Translation: EAW13727.1.
RefSeqiXP_001275153.1. XM_001275152.1.

Genome annotation databases

EnsemblFungiiCADACLAT00004242; CADACLAP00004144; CADACLAG00004242.
GeneIDi4707278.
KEGGiact:ACLA_044470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS027046 Genomic DNA. Translation: EAW13727.1 .
RefSeqi XP_001275153.1. XM_001275152.1.

3D structure databases

ProteinModelPortali A1C8U0.
SMRi A1C8U0. Positions 20-54, 92-436.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADACLAT00004242 ; CADACLAP00004144 ; CADACLAG00004242 .
GeneIDi 4707278.
KEGGi act:ACLA_044470.

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 PS51164. CBM1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Entry informationi

Entry nameiMANF_ASPCL
AccessioniPrimary (citable) accession number: A1C8U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 40 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