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Q12624

- GUN3_HUMIN

UniProt

Q12624 - GUN3_HUMIN

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Protein

Endoglucanase 3

Gene
CMC3
Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein 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 sitei215 – 2151Proton donor By similarity
Active sitei322 – 3221Nucleophile By similarity

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.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPiEGL5C_HUMGT.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase 3 (EC:3.2.1.4)
Alternative name(s):
Cellulase 3
Endo-1,4-beta-glucanase 3
Gene namesi
Name:CMC3
OrganismiHumicola insolens (Soft-rot fungus)
Taxonomic identifieri34413 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Biotechnological usei

Used as a detergent cellulase. Sold under the name Celluzyme by Novozymes. This special enzyme has three effects: colour brightening, softening and removal of particulate soil. The overall effect is that it helps to preserve the nice appearance of new fabric and restores old fabric so that it looks new again.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed predictionAdd
BLAST
Chaini17 – 388372Endoglucanase 3PRO_0000007863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 41 By similarity
Disulfide bondi35 ↔ 51 By similarity
Glycosylationi92 – 921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi155 – 1551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi259 – 2591N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ12624.
SMRiQ12624. Positions 19-52, 86-387.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 5236CBM1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 9139LinkerAdd
BLAST
Regioni92 – 388297CatalyticAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

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]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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.

Q12624-1 [UniParc]FASTAAdd to Basket

« Hide

MKHSVLAGLF ATGALAQGGA WQQCGGVGFS GSTSCVSGYT CVYLNDWYSQ    50
CQPQPTTLRT TTTPGATSTT RSAPAATSTT PAKGKFKWFG INQSCAEFGK 100
GEYPGLWGKH FTFPSTSSIQ THINDGFNMF RVAFSMERLA PNQLNAAFDA 150
NYLRNLTETV NFITGKGKYA MLDPHNFGRY YERIITDKAA FASFFTKLAT 200
HFASNPLVVF DTNNEYHDMD QQLVFDLNQA AIDAIRAAGA TSQYIMVEGN 250
SWTGAWTWNV TNNNLAALRD PENKLVYQMH QYLDSDGSGT STACVSTQVG 300
LQRVIGATNW LRQNGKVGLL GEFAGGANSV CQQAIEGMLT HLQENSDVWT 350
GALWWAGGPW WGDYIYSFEP PSGIGYTYYN SLLKKYVP 388
Length:388
Mass (Da):42,564
Last modified:November 1, 1996 - v1
Checksum:iC7CF349DACC10690
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81G → S in BAA12676. 1 Publication
Sequence conflicti340 – 3401T → N in BAA12676. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76046 Genomic DNA. Translation: CAA53631.1.
D84470 Genomic DNA. Translation: BAA12676.1.
PIRiJC5461.
S43920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76046 Genomic DNA. Translation: CAA53631.1 .
D84470 Genomic DNA. Translation: BAA12676.1 .
PIRi JC5461.
S43920.

3D structure databases

ProteinModelPortali Q12624.
SMRi Q12624. Positions 19-52, 86-387.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPi EGL5C_HUMGT.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 ]
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
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

  1. "A novel method for efficient expression cloning of fungal enzyme genes."
    Dalboege H., Hansen H.P.H.
    Mol. Gen. Genet. 243:253-260(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning, sequencing, and expression of a thermostable cellulase gene of Humicola grisea."
    Takashima S., Nakamura A., Masaki H., Uozumi T.
    Biosci. Biotechnol. Biochem. 61:245-250(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: IFO 9854.

Entry informationi

Entry nameiGUN3_HUMIN
AccessioniPrimary (citable) accession number: Q12624
Secondary accession number(s): Q12620
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 78 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

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