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Protein

Exo-beta-D-glucosaminidase

Gene

gls1

Organism
Hypocrea virens (Gliocladium virens) (Trichoderma virens)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has no activity against beta-D-galactoside, beta-D-glucuronide, beta-D-mannoside, chitin, glycol chitosan, cellulose, N,N'-diacetylchitibiose and pNP-GlcNAc (By similarity).By similarity

Catalytic activityi

Hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei462 – 4621Proton donorBy similarity
Active sitei537 – 5371NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Exo-beta-D-glucosaminidaseImported (EC:3.2.1.165)
Gene namesi
Name:gls1Imported
OrganismiHypocrea virens (Gliocladium virens) (Trichoderma virens)
Taxonomic identifieri29875 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

  • Secretedextracellular space By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 268By similarityPRO_0000399049
Chaini27 – 890864Exo-beta-D-glucosaminidaseSequence analysisBy similarityPRO_0000399050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence analysis
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence analysis
Glycosylationi576 – 5761N-linked (GlcNAc...)Sequence analysis
Glycosylationi687 – 6871N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi29875.EHK20158.

Structurei

3D structure databases

ProteinModelPortaliC0LRA7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2230. Eukaryota.
COG3250. LUCA.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR028829. Exo-b-D-glucosamin.
IPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10066:SF66. PTHR10066:SF66. 2 hits.
PfamiPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

C0LRA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAKAVAALL LGSGLASAAG TPLTSKAGDK VPIPDWDLKS SSEVSKDLKG
60 70 80 90 100
LSKPGVDTSA WYHAGTSKCT LMACLLNAGI YKDEDLWYSD NLNHFNWGQF
110 120 130 140 150
SIPWLYRHEF ALAPAKGKHF ILQTNGITSK ADLFFNGQQI ADSEYQAGAY
160 170 180 190 200
AGRTYDITSL AAKDNAFVVQ VHPTDYLYDF ALGYVDWNPY PPDNGTGIWR
210 220 230 240 250
DITVKETGSV SMGPISVVVD IDVPVESSPA KVTIRAEAQN LENVAVVLDA
260 270 280 290 300
EAVVSGNSCS GGPLKQTVKL APGEKKLVEF TKTIAKPKIW WPKQWGDQPL
310 320 330 340 350
YNAKVTFSVN KAVSDTAQTN FGVRKVTSFV NQYNDTQYSV NGHPFQVVGG
360 370 380 390 400
GYGADMFLRW DGDRFTRIVE YMLDMHQNTI RLEGKMEHPE LYEICDKYGL
410 420 430 440 450
MVMPGWECCD KWEAWAYNDE LAIFPPPVWD DNDYQTANYS MIHEASMLQP
460 470 480 490 500
HPSVLTFLVG SDFWPNDEAV VLYVNALKNA GWQTPIIASA SKRGFPALLG
510 520 530 540 550
PGGMKMDGPY DWVPPNYWYD TEPSEDRLGA AFGFGSELGA GVGTPELGSL
560 570 580 590 600
KRFLSQSDLN DLWKNPNKNL YHMSTNVSSF YNRKIYNQGL FKRYGAPTSL
610 620 630 640 650
DDYLLKAQMM DYEATRAQYE GFSSLWTASR PATGNIYWML NNAWPSLHWN
660 670 680 690 700
QFGYYMHPAG SYFGTKVGSR IEHVAYNYQK KEVWVINHSL DQTGPRKVDI
710 720 730 740 750
ELIDTNGKQI AKQSVNINTK ANSGFKAADI SSQIGKLSSV AFLRLILSDS
760 770 780 790 800
KGNVLSRNVY WVTNSIDKLD WDSSTWYYTQ VTSFVDYTPL NKLSAAQISV
810 820 830 840 850
TTGSSRRVAG VPGTQTRTVT LENKPSVPAV FIRLTLVDKS GNDVNPVSWT
860 870 880 890
DNYVTLWPKE KLQLEVGGWD ASGDSIQVSG RNIAATTVKL
Length:890
Mass (Da):98,811
Last modified:May 5, 2009 - v1
Checksum:iCA246878D8B1813A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ754260 mRNA. Translation: ACN62417.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ754260 mRNA. Translation: ACN62417.1.

3D structure databases

ProteinModelPortaliC0LRA7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi29875.EHK20158.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2230. Eukaryota.
COG3250. LUCA.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR028829. Exo-b-D-glucosamin.
IPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10066:SF66. PTHR10066:SF66. 2 hits.
PfamiPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Expressed sequence tags from Trichoderma virens reveal genes encoding for chitin modifying enzymes."
    Abdul Murad A.M., Badrun R., Yang Ahmad Z., Khairuddin F., Mohd Adnan A., Ahmad Zairun M., Kamaruddin S., Priyatno T.P., Quay D.H.X., Zainal Z., Mahadi N.M., Hassan O., Abu Bakar F.D.
    Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiEBDG_HYPVI
AccessioniPrimary (citable) accession number: C0LRA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 5, 2009
Last modified: May 11, 2016
This is version 30 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

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 one 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.