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Protein

Exoglucanase 1

Gene

cbh-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase 1 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase 1
Exocellobiohydrolase 1
Gene namesi
Name:cbh-1
ORF Names:NCU07340
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 4, Linkage Group IV

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 521504Exoglucanase 1PRO_0000270622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi493 ↔ 510By similarity
Disulfide bondi504 ↔ 520By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ7SA23.

Interactioni

Protein-protein interaction databases

STRINGi5141.NCU07340.1.

Structurei

3D structure databases

ProteinModelPortaliQ7SA23.
SMRiQ7SA23. Positions 24-449, 487-521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini485 – 52137CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 450433CatalyticBy similarityAdd
BLAST
Regioni451 – 48535LinkerBy similarityAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85664.
HOGENOMiHOG000182210.
InParanoidiQ7SA23.
OMAiNWSKCTS.
OrthoDBiEOG7ZGXCF.

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.

Q7SA23-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAKFAALAA LVASANAQAV CSLTAETHPS LNWSKCTSSG CTNVAGSITV
60 70 80 90 100
DANWRWTHIT SGSTNCYSGN EWDTSLCSTN TDCATKCCVD GAEYSSTYGI
110 120 130 140 150
QTSGNSLSLQ FVTKGSYSTN IGSRTYLMNG ADAYQGFELL GNEFTFDVDV
160 170 180 190 200
SGTGCGLNGA LYFVSMDLDG GKAKYTNNKA GAKYGTGYCD AQCPRDLKYI
210 220 230 240 250
NGIANVEGWT PSTNDANAGI GDHGTCCSEM DIWEANKVST AFTPHPCTTI
260 270 280 290 300
EQHMCEGDSC GGTYSDDRYG GTCDADGCDF NSYRMGNTTF YGEGKTVDTS
310 320 330 340 350
SKFTVVTQFI KDSAGDLAEI KRFYVQNGKV IENSQSNVDG VSGNSITQSF
360 370 380 390 400
CNAQKTAFGD IDDFNKKGGL KQMGKALAKP MVLVMSIWDD HAANMLWLDS
410 420 430 440 450
TYPVEGGPGA YRGECPTTSG VPAEVEANAP NSKVIFSNIK FGPIGSTFSG
460 470 480 490 500
GSSGTPPSNP SSSVKPVTST AKPSSTSTAS NPSGTGAAHW AQCGGIGFSG
510 520
PTTCQSPYTC QKINDYYSQC V
Length:521
Mass (Da):54,741
Last modified:December 15, 2003 - v1
Checksum:i230B7A488120B272
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002239 Genomic DNA. Translation: EAA33262.1.
RefSeqiXP_962498.1. XM_957405.1.
UniGeneiNcr.24831.

Genome annotation databases

EnsemblFungiiEFNCRT00000007127; EFNCRP00000007117; EFNCRG00000007115.
GeneIDi3878646.
KEGGincr:NCU07340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002239 Genomic DNA. Translation: EAA33262.1.
RefSeqiXP_962498.1. XM_957405.1.
UniGeneiNcr.24831.

3D structure databases

ProteinModelPortaliQ7SA23.
SMRiQ7SA23. Positions 24-449, 487-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.NCU07340.1.

Proteomic databases

PRIDEiQ7SA23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000007127; EFNCRP00000007117; EFNCRG00000007115.
GeneIDi3878646.
KEGGincr:NCU07340.

Phylogenomic databases

eggNOGiNOG85664.
HOGENOMiHOG000182210.
InParanoidiQ7SA23.
OMAiNWSKCTS.
OrthoDBiEOG7ZGXCF.

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]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiGUX1A_NEUCR
AccessioniPrimary (citable) accession number: Q7SA23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 15, 2003
Last modified: January 7, 2015
This is version 77 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.