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P46238

- GUXC_FUSOX

UniProt

P46238 - GUXC_FUSOX

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Protein

Putative exoglucanase type C

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

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei229 – 2291NucleophileBy similarity
Active sitei234 – 2341Proton donorBy similarity

GO - Molecular functioni

  1. cellulose 1,4-beta-cellobiosidase 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.
GH7. Glycoside Hydrolase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative exoglucanase type C (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Beta-glucancellobiohydrolase
Exocellobiohydrolase I
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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 514497Putative exoglucanase type CPRO_0000007913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi486 ↔ 503By similarity
Glycosylationi490 – 4901N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi497 ↔ 513By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP46238.
SMRiP46238. Positions 18-455, 480-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini478 – 51437CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 439422CatalyticAdd
BLAST
Regioni440 – 48243LinkerAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 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.

P46238-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYRIVATASA LIAAARAQQV CSLNTETKPA LTWSKCTSSG CSDVKGSVVI
60 70 80 90 100
DANWRWTHQT SGSTNCYTGN KWDTSICTDG KTCAEKCCLD GADYSGTYGI
110 120 130 140 150
TSSGNQLSLG FVTNGPYSKN IGSRTYLMEN ENTYQMFQLL GNEFTFDVDV
160 170 180 190 200
SGIGCGLNGA PHFVSMDEDG GKAKYSGNKA GAKYGTGYCD AQCPRDVKFI
210 220 230 240 250
NGVANSEGWK PSDSDVNAGV GNLGTCCPEM DIWEANSIST AFTPHPCTKL
260 270 280 290 300
TQHSCTGDSC GGTYSSDRYG GTCDADGCDF NAYRQGNKTF YGPGSNFNID
310 320 330 340 350
TTKKMTVVTQ FHKGSNGRLS EITRLYVQNG KVIANSESKI AGNPGSSLTS
360 370 380 390 400
DFCSKQKSVF GDIDDFSKKG GWNGMSDALS APMVLVMSLW HDHHSNMLWL
410 420 430 440 450
DSTYPTDSTK VGSQRGSCAT TSGKPSDLER DVPNSKVSFS NIKFGPIGST
460 470 480 490 500
YKSDGTTPNP PASSSTTGSS TPTNPPAGSV DQWGQCGGQN YSGPTTCKSP
510
FTCKKINDFY SQCQ
Length:514
Mass (Da):54,704
Last modified:November 1, 1995 - v1
Checksum:i6A4617323A46E062
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29379 mRNA. Translation: AAA65587.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29379 mRNA. Translation: AAA65587.1 .

3D structure databases

ProteinModelPortali P46238.
SMRi P46238. Positions 18-455, 480-514.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.70.100.10. 1 hit.
InterProi IPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view ]
PRINTSi PR00734. GLHYDRLASE7.
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_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 nameiGUXC_FUSOX
AccessioniPrimary (citable) accession number: P46238
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 76 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