Exo-beta-1,4-glucanase precursor - Cellulomonas fimi

Contribute

Unreviewed, UniProtKB/TrEMBL Q59277 (Q59277_CELFI)

Last modified November 25, 2008. Version 47. History...

Clusters with 100%, 90%, 50% identity |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein names

Submitted name:
Exo-beta-1,4-glucanase EMBL AAA56792.1
EC=3.2.1.91

Gene names

Name:

cex EMBL AAA56792.1

Organism

Cellulomonas fimi EMBL AAA56792.1

Taxonomic identifier

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family. RuleBase RU003432V0

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase RuleBase RU003432V0 Hydrolase
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro cellulose 1,4-beta-cellobiosidase activity Inferred from electronic annotation. Source: EC polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

42

Potential EMBL AAA56792.1

Chain

443

beta-1,4-xylanase EMBL AAA56792.1

PRO_5000142097

Sequences

Sequence

Length

Mass (Da)

Tools

Q59277-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1E0BFD54C0B95A27
Show »

485

51,209

        10         20         30         40         50         60 
MPRTTPAPGH PARGARTALR TTLAAAAATL VVGATVVLPA QAATTLKEAA DGAGRDFGFA 

        70         80         90        100        110        120 
LDPNRLSEAQ YKAIADSEFN LVVAENAMKW DATEPSQNSF SFGAGDRVAS YAADTGKELY 

       130        140        150        160        170        180 
GHTLVWHSQL PDWAKNLNGS AFESAMVNHV TKVADHFEGK VASWDVVNEA FADGGGRRQD 

       190        200        210        220        230        240 
SAFQQKLGNG YIETAFRAAR AADPTAKLCI NDYNVEGINA KSNSLYDLVK DFKARGVPLD 

       250        260        270        280        290        300 
CVGFQSHLIV GQVPGDFRQN LQRFADLGVD VRITELDIRM RTPSDATKLA TQAADYKKVV 

       310        320        330        340        350        360 
QACMQVTRCQ GVTVWGITDK YSWVPDVFPG EGAALVWDAS YAKKPAYAAV MEAFGASPTP 

       370        380        390        400        410        420 
TPTTPTPTPT TPTPTPTSGP AGCQVLWGVN QWNTGFTANV TVKNTSSAPV DGWTLTFSFP 

       430        440        450        460        470        480 
SGQQVTQAWS STVTQSGSAV TVRNAPWNGS IPAGGTAQFG FNGSHTGTNA APTAFSLNGT 


PCTVG

References

[1]	"Structure of the gene encoding the exoglucanase of Cellulomonas fimi." O'Neill G., Goh S.H., Warren R.A.J., Kilburn D.G., Miller R.C. Jr. Gene 44:325-330(1986) [PubMed: 3096818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Revision to the Cellulomonas fimi Cex gene sequence encoding an exo-beta-1,4-glucanse and beta-1,4-xylanase." Ramirez C., MacLeod A.M., Gilkes N.R. Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Detailed structural analysis of glycosidase/inhibitor interactions: complexes of Cex from Cellulomonas fimi with xylobiose-derived aza-sugars." Notenboom V., Williams S.J., Hoos R., Withers S.G., Rose D.R. Biochemistry 39:11553-11563(2000) [PubMed: 10995222] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 43-354.

Cross-references

Sequence databases

L11080 Genomic DNA. Translation: AAA56792.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FH7	X-ray	1.82	A	43-354	[»]
1FH8	X-ray	1.95	A	43-354	[»]
1FH9	X-ray	1.72	A	43-354	[»]
1FHD	X-ray	1.90	A	43-354	[»]

SMR

Q59277. Positions 377-485.

ModBase

Family and domain databases

InterPro

IPR001919. CBD_bac.
IPR012291. CBD_carb_bd.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sub_cat.
IPR017909. Twin_arg_translocation_Tat.
[Graphical view]

Gene3D

G3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00553. CBM_2. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]

PROSITE

PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Entry information

Entry name

Q59277_CELFI

Accession

Primary (citable) accession number: Q59277

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information