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Protein

Glucanase

Gene

celM

Organism
[Clostridium] cellulolyticum
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521ZincCombined sources
Metal bindingi68 – 681ZincCombined sources
Metal bindingi69 – 691Zinc; via pros nitrogenCombined sources
Metal bindingi85 – 851Zinc; via tele nitrogenCombined sources
Metal bindingi238 – 2381CalciumCombined sources
Metal bindingi241 – 2411CalciumCombined sources
Metal bindingi242 – 2421CalciumCombined sources
Metal bindingi287 – 2871Calcium; via carbonyl oxygenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources, ZincCombined sources

Protein family/group databases

CAZyiGH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
GlucanaseUniRule annotation (EC:3.2.1.-UniRule annotation)
Gene namesi
Name:celMImported
Organismi[Clostridium] cellulolyticumImported
Taxonomic identifieri1521 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030UniRule annotationAdd
BLAST
Chaini31 – 526496GlucanaseUniRule annotationPRO_5005144774Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi394503.Ccel_0737.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IA6X-ray1.80A31-471[»]
1IA7X-ray2.00A31-471[»]
ProteinModelPortaliQ9EYQ2.
SMRiQ9EYQ2. Positions 31-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9EYQ2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini467 – 52660DockerinInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 9 (cellulase E) family.UniRule annotation

Keywords - Domaini

SignalUniRule annotation

Phylogenomic databases

eggNOGiENOG4108KBB. Bacteria.
ENOG410XPC9. LUCA.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
[Graphical view]
PfamiPF00404. Dockerin_1. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS51766. DOCKERIN. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EYQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSKLIKLSA IIISGVMLTT SFVNTGTAFA AGTHDYSTAL KDSIIFFDAN
60 70 80 90 100
KCGPQAGENN VFDWRGACHT TDGSDVGVDL TGGYHDAGDH VKFGLPQGYS
110 120 130 140 150
AAILGWSLYE FKESFDATGN TTKMLQQLKY FTDYFLKSHP NSTTFYYQVG
160 170 180 190 200
EGNADHTYWG APEEQTGQRP SLYKADPSSP ASDILSETSA ALTLMYLNYK
210 220 230 240 250
NIDSAYATKC LNAAKELYAM GKANQGVGNG QSFYQATSFG DDLAWAATWL
260 270 280 290 300
YTATNDSTYI TDAEQFITLG NTMNENKMQD KWTMCWDDMY VPAALRLAQI
310 320 330 340 350
TGKQIYKDAI EINFNYWKTQ VTTTPGGLKW LSNWGVLRYA AAESMVMLVY
360 370 380 390 400
CKQNPDQSLL DLAKKQVDYI LGDNPANMSY IIGYGSNWCI HPHHRAANGY
410 420 430 440 450
TYANGDNAKP AKHLLTGALV GGPDQNDKFL DDANQYQYTE VALDYNAGLV
460 470 480 490 500
GVLAGAIKFF GGTIVNPPVK KGDLNNDTFI DAIDLALCKN YILTQNGNID
510 520
KNNADMNGDG SIDAIDFSLL KKAILG
Length:526
Mass (Da):57,631
Last modified:March 1, 2001 - v1
Checksum:i526CDF064C5AAC9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF316823 Genomic DNA. Translation: AAG45160.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF316823 Genomic DNA. Translation: AAG45160.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IA6X-ray1.80A31-471[»]
1IA7X-ray2.00A31-471[»]
ProteinModelPortaliQ9EYQ2.
SMRiQ9EYQ2. Positions 31-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi394503.Ccel_0737.

Protein family/group databases

CAZyiGH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108KBB. Bacteria.
ENOG410XPC9. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ9EYQ2.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
[Graphical view]
PfamiPF00404. Dockerin_1. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS51766. DOCKERIN. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases."
    Parsiegla G., Belaich A., Belaich J.P., Haser R.
    Biochemistry 41:11134-11142(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 31-471 IN COMPLEX WITH CALCIUM AND ZINC.
  2. "Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome."
    Belaich A., Parsiegla G., Gal L., Villard C., Haser R., Belaich J.P.
    J. Bacteriol. 184:1378-1384(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ9EYQ2_9FIRM
AccessioniPrimary (citable) accession number: Q9EYQ2
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.