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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 donorBy similarity
Active sitei322 – 3221NucleophileBy 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 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 388372Endoglucanase 3PRO_0000007863Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 5236CBM1PROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

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

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

        10         20         30         40         50
MKHSVLAGLF ATGALAQGGA WQQCGGVGFS GSTSCVSGYT CVYLNDWYSQ
60 70 80 90 100
CQPQPTTLRT TTTPGATSTT RSAPAATSTT PAKGKFKWFG INQSCAEFGK
110 120 130 140 150
GEYPGLWGKH FTFPSTSSIQ THINDGFNMF RVAFSMERLA PNQLNAAFDA
160 170 180 190 200
NYLRNLTETV NFITGKGKYA MLDPHNFGRY YERIITDKAA FASFFTKLAT
210 220 230 240 250
HFASNPLVVF DTNNEYHDMD QQLVFDLNQA AIDAIRAAGA TSQYIMVEGN
260 270 280 290 300
SWTGAWTWNV TNNNLAALRD PENKLVYQMH QYLDSDGSGT STACVSTQVG
310 320 330 340 350
LQRVIGATNW LRQNGKVGLL GEFAGGANSV CQQAIEGMLT HLQENSDVWT
360 370 380
GALWWAGGPW WGDYIYSFEP PSGIGYTYYN SLLKKYVP
Length:388
Mass (Da):42,564
Last modified:November 1, 1996 - v1
Checksum:iC7CF349DACC10690
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81G → S in BAA12676. (PubMed:9058960)Curated
Sequence conflicti340 – 3401T → N in BAA12676. (PubMed:9058960)Curated

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: October 1, 2014
This is version 79 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