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Q5AR04

- MANF_EMENI

UniProt

Q5AR04 - MANF_EMENI

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Protein

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

Gene

manF

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei256 – 2561Proton donorBy similarity
Active sitei364 – 3641NucleophileBy 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:AN9276
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VIII

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 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 433414Probable mannan endo-1,4-beta-mannosidase FPRO_0000393717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5AR04.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 5334CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 8227Thr-rich linkerAdd
BLAST
Regioni83 – 433351CatalyticAdd
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.
InParanoidiQ5AR04.
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.

Q5AR04-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRQALTLIP LLGAAAAQSG PYGQCGGNDW SGATTCVSGY VCVYQNEWYS
60 70 80 90 100
QCVPGTATSS STTLTTTTSA TTRTTTTTTS TTSVPSSTNF PSASGLNFTI
110 120 130 140 150
DGVTDYFAGS NSYWISMLTN DADVDLVLDH IASSGHKILR IWGFNDVNTE
160 170 180 190 200
PSTGQVWFQK HQGGVSTINT GQYGLQRLDA VVSSAEKRGI KLIINFVNNW
210 220 230 240 250
DDYGGMSAYL NAYGGSTKTD WYTSATIQAA YRTYIKAVID RFIDSPAIFA
260 270 280 290 300
WELANEPRCN GCDTSILYDW IADTSAYIKS LDPLHMVCIG DEGFGLDEGS
310 320 330 340 350
DGSYPFSYNE GLDFAANLAI DTIDFGTFHL YPGSWGVSYD WGNLWAITHG
360 370 380 390 400
AACATAGKPC LFEEYGAPSD HCAIEVPWQT TAVSSTGIAG DLFWQWGDTL
410 420 430
STGQTHNDGN TIYYGSDEYT CMVTEHMERI AAR
Length:433
Mass (Da):46,869
Last modified:April 20, 2010 - v2
Checksum:iA4CBD63B0AF37C79
GO

Sequence cautioni

The sequence CBF87312.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence EAA66343.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACD01000172 Genomic DNA. Translation: EAA66343.1. Sequence problems.
BN001308 Genomic DNA. Translation: CBF87312.1. Sequence problems.
RefSeqiXP_682545.1. XM_677453.1.

Genome annotation databases

EnsemblFungiiCADANIAT00001054; CADANIAP00001054; CADANIAG00001054.
GeneIDi2867914.
KEGGiani:AN9276.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACD01000172 Genomic DNA. Translation: EAA66343.1 . Sequence problems.
BN001308 Genomic DNA. Translation: CBF87312.1 . Sequence problems.
RefSeqi XP_682545.1. XM_677453.1.

3D structure databases

ProteinModelPortali Q5AR04.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00001054 ; CADANIAP00001054 ; CADANIAG00001054 .
GeneIDi 2867914.
KEGGi ani:AN9276.2.

Phylogenomic databases

eggNOGi COG3934.
HOGENOMi HOG000169951.
InParanoidi Q5AR04.
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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiMANF_EMENI
AccessioniPrimary (citable) accession number: Q5AR04
Secondary accession number(s): C8VQC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: October 29, 2014
This is version 57 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, 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