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Q9SVJ4 (GUN22_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase 22
EC=3.2.1.4
Alternative name(s):
Endo-1,4-beta glucanase 22
Glycosyl hydrolase 9B16
Gene names
Name:GH9B16
Ordered Locus Names:At4g38990
ORF Names:F19H22.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Subcellular location

Secreted By similarity.

Sequence similarities

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

Caution

The conserved 'Asp-464' active site is replaced by a Gly residue.

Sequence caution

The sequence AEE87005.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 494473Endoglucanase 22
PRO_0000249274

Sites

Active site4131 By similarity
Active site4731 By similarity

Amino acid modifications

Glycosylation4681N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SVJ4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FF242EA53A8070A4

FASTA49455,019
        10         20         30         40         50         60 
MKPLVCSFIV ILLILLPTTI SHDYSDALTK SILFFEGQRS GYLPREQRMT WRHNSALNDG 

        70         80         90        100        110        120 
KNLNVDLVGG YYDAGDNIKF HFPMAFTTTM LAWSAIDFGS YMSPADLRDN LVALRWGSNY 

       130        140        150        160        170        180 
LLKTVSQLPN RIFVQVGEPT PDHQCWERPE DMDTPRTAYA LEAPKPASDL AGEIAAALAA 

       190        200        210        220        230        240 
ASIAFKRFDP RYSKLLLDNA LRTFEYADSH RGSYTNNPET KLAVCPFYCS VNGYEDELLW 

       250        260        270        280        290        300 
GAAWLRRATG KDSYIKYLVE NRQSFGSDSN YFEFGWDNKV GGVNVLVAKE VFEKNVAAIA 

       310        320        330        340        350        360 
PYKDTAEKLM CSFFLETPGA HMSYSPGGLL YKPGSSQLQN TVALSFLLLT YANYLSKSSQ 

       370        380        390        400        410        420 
QPLQILSTTP LWYLTQRIAN IVGFEKVDYI LGDNPMKMSY MIGYGNRYPR QIHHRGASSP 

       430        440        450        460        470        480 
SITTHPTPVK CSEGWNSFSS PNPDPNVLVG AVIGGPNIDD KFVGGRTNAS ETEPTTYINA 

       490 
PFVGLLAYFK ANPV

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Phylogenetic analysis of the plant endo-beta-1,4-glucanase gene family."
Libertini E., Li Y., McQueen-Mason S.J.
J. Mol. Evol. 58:506-515(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL035679 Genomic DNA. Translation: CAB38819.1.
AL161594 Genomic DNA. Translation: CAB80562.1.
CP002687 Genomic DNA. Translation: AEE87005.1. Sequence problems.
IPIIPI00536910.
IPI01020163.
PIRT06059.
RefSeqNP_195610.3. NM_120059.3.
UniGeneAt.74494.

3D structure databases

HSSPHSSP built from PDB template 1TF4 based on UniProtKB P26221.
ProteinModelPortalQ9SVJ4.
SMRQ9SVJ4. Positions 20-491.
ModBaseSearch...

Protein family/group databases

CAZyGH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID830054.
KEGGath:AT4G38990.

Organism-specific databases

TAIRAt4g38990.

Phylogenomic databases

eggNOGeuNOG01127.

Gene expression databases

GenevestigatorQ9SVJ4.
GermOnlineAT4G38990. Arabidopsis thaliana.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR001701. Glyco_hydro_9.
[Graphical view]
PfamPF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMSSF48208. Glyco_trans_6hp. 1 hit.
PROSITEPS00592. GLYCOSYL_HYDROL_F9_1. False negative.
PS00698. GLYCOSYL_HYDROL_F9_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN22_ARATH
AccessionPrimary (citable) accession number: Q9SVJ4
Secondary accession number(s): F4JUJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents