[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=YX; PubMed=8215374 [NCBI, ExPASy, EBI, Israel, Japan] Jung E.D., Lao G., Irwin D., Barr B.K., Benjamin A., Wilson D.B.; "DNA sequences and expression in Streptomyces lividans of an exoglucanase gene and an endoglucanase gene from Thermomonospora fusca."; Appl. Environ. Microbiol. 59:3032-3043(1993).
[2]	SEQUENCE REVISION. Wilson D.B.; Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[3]	PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=YX; PubMed=1904434 [NCBI, ExPASy, EBI, Israel, Japan] Lao G., Ghangas G.S., Jung E.D., Wilson D.B.; "DNA sequences of three beta-1,4-endoglucanase genes from Thermomonospora fusca."; J. Bacteriol. 173:3397-3407(1991).
[4]	PROTEIN SEQUENCE OF 47-67. Wilson D.B.; "Cellulases of Thermomonospora fusca."; Methods Enzymol. 160:314-323(1988).
[5]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 47-651. DOI=10.1038/nsb1097-810; PubMed=9334746 [NCBI, ExPASy, EBI, Israel, Japan] Sakon J., Irwin D., Wilson D.B., Karplus P.A.; "Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca."; Nat. Struct. Biol. 4:810-818(1997).

Comments

CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
PATHWAY: Glycan metabolism; cellulose degradation .
SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
SIMILARITY: Contains 1 CBM3 (carbohydrate binding type-3) domain.
SIMILARITY: Contains 1 fibronectin type-III domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L20093; AAB42155.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B42360; B42360.

3D structure databases

PDB

1JS4; X-ray; 2.00 A; A/B=47-651.	[ExPASy / RCSB / EBI]
1TF4; X-ray; 1.90 A; A/B=47-651.	[ExPASy / RCSB / EBI]
3TF4; X-ray; 2.20 A; A/B=47-651.	[ExPASy / RCSB / EBI]
4TF4; X-ray; 2.00 A; A/B=47-651.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JS4; -.
1TF4; -.
3TF4; -.
4TF4; -.

ModBase

P26221.

Ontologies

GO:0030246;	Molecular function: carbohydrate binding (inferred from electronic annotation from InterPro).
GO:0008810;	Molecular function: cellulase activity (inferred from electronic annotation from EC).
GO:0030245;	Biological process: cellulose catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR012341; 6hp_glycosidase.
IPR001956; CBD_3.
IPR001919; CBD_bac.
IPR003961; FN_III.
IPR001701; Glyco_hydro_9.
Graphical view of domain structure.

Gene3D

G3DSA:1.50.10.10; CelA/Cel48F_cat; 1.

PANTHER

PTHR22298:SF3; Glyco_hydro_9; 1.

Pfam

PF00553; CBM_2; 1.
PF00942; CBM_3; 1.
PF00041; fn3; 1.
PF00759; Glyco_hydro_9; 1.
Pfam graphical view of domain structure.

ProDom

PD001947; CBD_3; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00637; CBD_II; 1.
SM00060; FN3; 1.
SMART graphical view of domain structure.

PROSITE

PS51173; CBM2; 1.
PS00561; CBM2_A; 1.
PS51172; CBM3; 1.
PS50853; FN3; 1.
PS00592; GLYCOSYL_HYDROL_F9_1; 1.
PS00698; GLYCOSYL_HYDROL_F9_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

P26221; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 46`	`46`
`CHAIN`	`47 880`	`834`	`Endoglucanase E-4.`	`PRO_0000007959`
`DOMAIN`	`504 652`	`149`	`CBM3.`
`DOMAIN`	`675 766`	`92`	`Fibronectin type-III.`
`DOMAIN`	`771 880`	`110`	`CBM2.`
`ACT_SITE`	`427 427`		`By similarity.`
`ACT_SITE`	`461 461`		`By similarity.`
`ACT_SITE`	`470 470`		`By similarity.`
`HELIX`	`52 65`	`14`
`TURN`	`85 88`	`4`
`HELIX`	`89 91`	`3`
`STRAND`	`102 104`	`3`
`HELIX`	`109 125`	`17`
`HELIX`	`127 132`	`6`
`HELIX`	`136 152`	`17`
`STRAND`	`159 165`	`7`
`HELIX`	`167 171`	`5`
`HELIX`	`177 179`	`3`
`STRAND`	`186 190`	`5`
`HELIX`	`196 213`	`18`
`TURN`	`214 216`	`3`
`HELIX`	`218 237`	`20`
`HELIX`	`242 244`	`3`
`HELIX`	`249 252`	`4`
`HELIX`	`259 273`	`15`
`HELIX`	`276 285`	`10`
`HELIX`	`286 288`	`3`
`STRAND`	`295 298`	`4`
`STRAND`	`305 307`	`3`
`HELIX`	`310 321`	`12`
`HELIX`	`324 336`	`13`
`TURN`	`337 339`	`3`
`STRAND`	`358 360`	`3`
`HELIX`	`361 378`	`18`
`HELIX`	`382 400`	`19`
`STRAND`	`413 416`	`4`
`HELIX`	`424 427`	`4`
`STRAND`	`430 432`	`3`
`STRAND`	`436 439`	`4`
`TURN`	`466 468`	`3`
`HELIX`	`473 475`	`3`
`HELIX`	`477 490`	`14`
`STRAND`	`508 517`	`10`
`STRAND`	`520 531`	`12`
`STRAND`	`542 550`	`9`
`HELIX`	`557 559`	`3`
`STRAND`	`561 563`	`3`
`STRAND`	`567 569`	`3`
`STRAND`	`576 579`	`4`
`STRAND`	`582 588`	`7`
`STRAND`	`596 598`	`3`
`TURN`	`599 602`	`4`
`STRAND`	`603 611`	`9`
`HELIX`	`618 620`	`3`
`HELIX`	`622 624`	`3`
`STRAND`	`637 641`	`5`
`STRAND`	`644 648`	`5`

Sequence information

Length: 880 AA [This is the length of the unprocessed precursor]

Molecular weight: 95203 Da [This is the MW of the unprocessed precursor]

CRC64: 5EA9A6ABF45A4D9A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVTEPPPRR RGRHSRARRF LTSLGATAAL TAGMLGVPLA TGTAHAEPAF NYAEALQKSM 

        70         80         90        100        110        120 
FFYEAQRSGK LPENNRVSWR GDSGLNDGAD VGLDLTGGWY DAGDHVKFGF PMAFTATMLA 

       130        140        150        160        170        180 
WGAIESPEGY IRSGQMPYLK DNLRWVNDYF IKAHPSPNVL YVQVGDGDAD HKWWGPAEVM 

       190        200        210        220        230        240 
PMERPSFKVD PSCPGSDVAA ETAAAMAASS IVFADDDPAY AATLVQHAKQ LYTFADTYRG 

       250        260        270        280        290        300 
VYSDCVPAGA FYNSWSGYQD ELVWGAYWLY KATGDDSYLA KAEYEYDFLS TEQQTDLRSY 

       310        320        330        340        350        360 
RWTIAWDDKS YGTYVLLAKE TGKQKYIDDA NRWLDYWTVG VNGQRVPYSP GGMAVLDTWG 

       370        380        390        400        410        420 
ALRYAANTAF VALVYAKVID DPVRKQRYHD FAVRQINYAL GDNPRNSSYV VGFGNNPPRN 

       430        440        450        460        470        480 
PHHRTAHGSW TDSIASPAEN RHVLYGALVG GPGSPNDAYT DDRQDYVANE VATDYNAGFS 

       490        500        510        520        530        540 
SALAMLVEEY GGTPLADFPP TEEPDGPEIF VEAQINTPGT TFTEIKAMIR NQSGWPARML 

       550        560        570        580        590        600 
DKGTFRYWFT LDEGVDPADI TVSSAYNQCA TPEDVHHVSG DLYYVEIDCT GEKIFPGGQS 

       610        620        630        640        650        660 
EHRREVQFRI AGGPGWDPSN DWSFQGIGNE LAPAPYIVLY DDGVPVWGTA PEEGEEPGGG 

       670        680        690        700        710        720 
EGPGGGEEPG EDVTPPSAPG SPAVRDVTST SAVLTWSASS DTGGSGVAGY DVFLRAGTGQ 

       730        740        750        760        770        780 
EQKVGSTTRT SFTLTGLEPD TTYIAAVVAR DNAGNVSQRS TVSFTTLAEN GGGPDASCTV 

       790        800        810        820        830        840 
GYSTNDWDSG FTASIRITYH GTAPLSSWEL SFTFPAGQQV THGWNATWRQ DGAAVTATPM 

       850        860        870        880 
SWNSSLAPGA TVEVGFNGSW SGSNTPPTDF TLNGEPCALA

P26221 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools