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P46236

- GUNB_FUSOX

UniProt

P46236 - GUNB_FUSOX

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Protein

Putative endoglucanase type B

Gene
N/A
Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei190 – 1901PROSITE-ProRule annotation
Active sitei236 – 2361Proton donorPROSITE-ProRule annotation
Active sitei416 – 4161NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative endoglucanase type B (EC:3.2.1.4)
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
OrganismiFusarium oxysporum (Fusarium vascular wilt)
Taxonomic identifieri5507 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium oxysporum species complex

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 462446Putative endoglucanase type BPRO_0000007910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 50By similarity
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi44 ↔ 60By similarity
Disulfide bondi191 ↔ 250By similarity
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi383 ↔ 430By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP46236.

Structurei

3D structure databases

ProteinModelPortaliP46236.
SMRiP46236. Positions 106-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 6137CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 9934LinkerAdd
BLAST
Regioni100 – 462363CatalyticAdd
BLAST

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46236-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAYKLILAAF AATALAAPVE ERQSCSNGVW AQCGGQNWSG TPCCTSGNKC
60 70 80 90 100
VKLNDFYSQC QPGSAEPSST AAGPSSTTAT KTTATGGSST TAGGSVTSAP
110 120 130 140 150
PAASDNPYAG VDLWANNYYR SEVMNLAVPK LSGAKATAAA KVADVPSFQW
160 170 180 190 200
MDTYDHISLM EDTLADIRKA NKAGGKYAGQ FVVYDLPNRD CAAAASNGEY
210 220 230 240 250
SLDKDGANKY KAYIAKIKGI LQNYSDTKVI LVIEPDSLAN LVTNLNVDKC
260 270 280 290 300
AKAESAYKEL TVYAIKELNL PNVSMYLDAG HGGWLGWPAN IGPAAKLYAQ
310 320 330 340 350
IYKDAGKPSR VRGLVTNVSN YNGWKLSTKP DYTESNPNYD EQRYINAFAP
360 370 380 390 400
LLAQEGWSNV KFIVDQGRSG KQPTGQKAQG DWCNAKGTGF GLRPSTNTGD
410 420 430 440 450
ALADAFVWVK PGGESDGTSD TSAARYDYHC GLDDALKPAP EAGTWFQAYF
460
EQLLDNANPS FL
Length:462
Mass (Da):49,208
Last modified:November 1, 1995 - v1
Checksum:iE25B2F5B828B637F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29377 mRNA. Translation: AAA65585.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29377 mRNA. Translation: AAA65585.1 .

3D structure databases

ProteinModelPortali P46236.
SMRi P46236. Positions 106-461.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.

Proteomic databases

PRIDEi P46236.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.40. 1 hit.
InterProi IPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view ]
PIRSFi PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSi PR00733. GLHYDRLASE6.
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The use of conserved cellulase family-specific sequences to clone cellulase homologue cDNAs from Fusarium oxysporum."
    Sheppard P.O., Grant F.J., Oort P.J., Sprecher C.A., Foster D.C., Hagen F.S., Upshall A., McKnight G.L., O'Hara P.J.
    Gene 150:163-167(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiGUNB_FUSOX
AccessioniPrimary (citable) accession number: P46236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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