Unreviewed, UniProtKB/TrEMBL Q9EYQ2 (Q9EYQ2_CLOCE)

Names and origin

Protein names

Submitted name:
    Cellulase Cel9-M EMBL AAG45160.1

Gene names

Name:

celM EMBL AAG45160.1

Organism

Clostridium cellulolyticum EMBL AAG45160.1

Taxonomic identifier

1521 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Ontologies

Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9EYQ2-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 526CDF064C5AAC9E	FASTA	526	57,631
	10 20 30 40 50 60 MKSKLIKLSA IIISGVMLTT SFVNTGTAFA AGTHDYSTAL KDSIIFFDAN KCGPQAGENN 70 80 90 100 110 120 VFDWRGACHT TDGSDVGVDL TGGYHDAGDH VKFGLPQGYS AAILGWSLYE FKESFDATGN 130 140 150 160 170 180 TTKMLQQLKY FTDYFLKSHP NSTTFYYQVG EGNADHTYWG APEEQTGQRP SLYKADPSSP 190 200 210 220 230 240 ASDILSETSA ALTLMYLNYK NIDSAYATKC LNAAKELYAM GKANQGVGNG QSFYQATSFG 250 260 270 280 290 300 DDLAWAATWL YTATNDSTYI TDAEQFITLG NTMNENKMQD KWTMCWDDMY VPAALRLAQI 310 320 330 340 350 360 TGKQIYKDAI EINFNYWKTQ VTTTPGGLKW LSNWGVLRYA AAESMVMLVY CKQNPDQSLL 370 380 390 400 410 420 DLAKKQVDYI LGDNPANMSY IIGYGSNWCI HPHHRAANGY TYANGDNAKP AKHLLTGALV 430 440 450 460 470 480 GGPDQNDKFL DDANQYQYTE VALDYNAGLV GVLAGAIKFF GGTIVNPPVK KGDLNNDTFI 490 500 510 520 DAIDLALCKN YILTQNGNID KNNADMNGDG SIDAIDFSLL KKAILG

References

[1]	"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: 11844767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"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: 12220178] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-471.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF316823 Genomic DNA. Translation: AAG45160.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR012341. 6hp_glycosidase. IPR016134. Cellulos_enz_dockerin_1. IPR002105. Cellulos_enz_dockerin_1_Ca-bd. IPR002048. EF_hand_Ca_bd. IPR001701. Glyco_hydro_9. [Graphical view]
Gene3D	G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit. G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit.
PANTHER	PTHR22298:SF3. Glyco_hydro_9. 1 hit.
Pfam	PF00404. Dockerin_1. 2 hits. PF00759. Glyco_hydro_9. 1 hit. [Graphical view]
PROSITE	PS00448. CLOS_CELLULOSOME_RPT. 1 hit. PS00018. EF_HAND_1. 1 hit. Uncertain. PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit. [Graphical view]

Entry information

Entry name

Q9EYQ2_CLOCE

Accession

Primary (citable) accession number: Q9EYQ2

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2001
Last sequence update:	March 1, 2001
Last modified:	November 25, 2008
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)