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Q12622

- GUN1_HUMGT

UniProt

Q12622 - GUN1_HUMGT

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Protein

Endoglucanase EG-1

Gene

EG-1

Organism
Humicola grisea var. thermoidea
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

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 sitei217 – 2171NucleophileBy similarity
Active sitei222 – 2221Proton donorBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

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

CAZyiGH7. Glycoside Hydrolase Family 7.
mycoCLAPiEGL7A_HUMGT.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase EG-1 (EC:3.2.1.4)
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:EG-1
OrganismiHumicola grisea var. thermoidea
Taxonomic identifieri5528 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 435415Endoglucanase EG-1PRO_0000007916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acidBy similarity
Disulfide bondi38 ↔ 44By similarity
Disulfide bondi71 ↔ 93By similarity
Disulfide bondi83 ↔ 89By similarity
Glycosylationi109 – 1091N-linked (GlcNAc...)By similarity
Disulfide bondi160 ↔ 385By similarity
Disulfide bondi192 ↔ 215By similarity
Disulfide bondi196 ↔ 214By similarity
Disulfide bondi235 ↔ 254By similarity
Disulfide bondi243 ↔ 248By similarity
Disulfide bondi259 ↔ 335By similarity
Glycosylationi267 – 2671N-linked (GlcNAc...)By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

3D structure databases

ProteinModelPortaliQ12622.
SMRiQ12622. Positions 21-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12622-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARGTALLGL TSLLLGLVNG QKPGETKEVH PQLTTFRCTK KGGCKPATNY
60 70 80 90 100
IVLDSLSHPI HRAEGLGWGN CGDWGNPPPK DVCPDVESCA KNCIMEGIPD
110 120 130 140 150
YSQYGVTTNG TSLRLQHILP DGRVPSPRVY LLDKTERRYE MLHLTGFEFT
160 170 180 190 200
FDVDATKLPC GMNSALYLSE MHPTGAKSKH NPGGAYYGTG YCDAQCFVTP
210 220 230 240 250
FINGLGNIEG KGSCCNEMDI WEANSRASHV APHVCNKKGL YLCEGEECAF
260 270 280 290 300
EGVCDKNGCG WNPYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRKGKL
310 320 330 340 350
EKIHRFYVQD GKIIESFYTN KEGIPYTNMI EDEFCAATGS RKYMELGATQ
360 370 380 390 400
GMGEALTRGM VLAMSIWWDQ GGNMEWLDHG EAGPCAKGEG APSNVVQVEP
410 420 430
FPEVTYTNLR WGEIGSTYQE VQKPKPKPGP GPRSD
Length:435
Mass (Da):47,890
Last modified:November 1, 1996 - v1
Checksum:i25EB3D62D96B65FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63516 Genomic DNA. Translation: BAA09786.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63516 Genomic DNA. Translation: BAA09786.1 .

3D structure databases

ProteinModelPortali Q12622.
SMRi Q12622. Positions 21-418.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH7. Glycoside Hydrolase Family 7.
mycoCLAPi EGL7A_HUMGT.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.70.100.10. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view ]
Pfami PF00840. Glyco_hydro_7. 1 hit.
[Graphical view ]
PRINTSi PR00734. GLHYDRLASE7.
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Takashima S., Nakamura A., Hidaka M., Masaki H., Uozumi T.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: IFO 9854.

Entry informationi

Entry nameiGUN1_HUMGT
AccessioniPrimary (citable) accession number: Q12622
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 73 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