Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Putative exoglucanase type C

Gene
N/A
Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei229NucleophileBy similarity1
Active sitei234Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000000791318 – 514Putative exoglucanase type CAdd BLAST497

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi287N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi486 ↔ 503By similarity
Glycosylationi490N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi497 ↔ 513By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP46238

Structurei

3D structure databases

ProteinModelPortaliP46238
SMRiP46238
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini478 – 514CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni18 – 439CatalyticAdd BLAST422
Regioni440 – 482LinkerAdd BLAST43

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IE3Y Eukaryota
ENOG41101KD LUCA

Family and domain databases

CDDicd07999 GH7_CBH_EG, 1 hit
Gene3Di2.70.100.10, 1 hit
InterProiView protein in InterPro
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR013320 ConA-like_dom_sf
IPR001722 Glyco_hydro_7
IPR037019 Glyco_hydro_7_sf
PANTHERiPTHR33753 PTHR33753, 1 hit
PfamiView protein in Pfam
PF00734 CBM_1, 1 hit
PF00840 Glyco_hydro_7, 1 hit
PRINTSiPR00734 GLHYDRLASE7
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001821 CBD_fun, 1 hit
SMARTiView protein in SMART
SM00236 fCBD, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF57180 SSF57180, 1 hit
PROSITEiView protein in PROSITE
PS00562 CBM1_1, 1 hit
PS51164 CBM1_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiGUXC_FUSOX
AccessioniPrimary (citable) accession number: P46238
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 88 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health