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A2XYW8 (GUN13_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endoglucanase 13
EC=3.2.1.4
Alternative name(s):
Endo-1,4-beta glucanase 13
OsGLU6
Gene names
Name:GLU6
ORF Names:H0103C06.3, H0403D02.19, OsI_017261
OrganismOryza sativa subsp. indica (Rice)
Taxonomic identifier39946 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza ›

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
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_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

cellulase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Chain35 – 625591Endoglucanase 13
PRO_0000295017

Sites

Active site4271 By similarity
Active site4791 By similarity
Active site4881 By similarity

Amino acid modifications

Glycosylation4401N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2301D → H in EAY96028. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2XYW8 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: D220BF0D009441F1

FASTA62568,381
        10         20         30         40         50         60 
MAATMNKTPA TTFLLIPAAA SLVLLLAAAA SVEASAFDYA GAFDKCLLFF EAQRSGKLPD 

        70         80         90        100        110        120 
DRLVRWRGDS ALTDGFSQGV DLVGGYYDSG DHVKFGLPMA YAVTMLSWGV VEFEKEMVDG 

       130        140        150        160        170        180 
NKLHRVLDAI RWGTNYFVKA HTQHNALWVQ VGDGDSDHLC WERAEDMSTP RTAFKIDINN 

       190        200        210        220        230        240 
PGSEVAGETA AALAAAAKAF KPYDRMYSDL LLLHSKQLFT FADTFRGKYD DSLQSAKKFY 

       250        260        270        280        290        300 
PSASGYQDEL LWAAAWLYEA TGDEQYLRYV SQNAEAFGGT GWAVTEFSWD NKYAGLQVLL 

       310        320        330        340        350        360 
SKVLFEQGGS AAGYADTLKQ YQAKAEFFLC ACLQKNNGHN VKMTPGGLMY VSDWSNMQYV 

       370        380        390        400        410        420 
SSSAFLLTVY ADYLAESRGT LRCPDGEVKP AEILLFARSQ VDYVLGKNPK GMSYMVGYGS 

       430        440        450        460        470        480 
YYPTHVHHRG ASIPSIYAMN ATVGCMEGFD KYYNSKNADP NVLHGALVGG PDANDAYDDD 

       490        500        510        520        530        540 
RCNYQHAEPT LAGNAPMSGV FARLAASPAD NTPEYTPAPN APSPSNGGSP LEFVHTVTNT 

       550        560        570        580        590        600 
WKANGVDYYR HVVTAKNTCG HAITYLKLQI KELSGEIYGV SRTNAKDMYE FPSWMTRLDA 

       610        620 
GAQLTIVYIQ GGPAAKIAVV EYKTA

« Hide

References

[1]"Sequence and analysis of rice chromosome 4."
Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L. expand/collapse author list , Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., Han B.
Nature 420:316-320(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Guang-Lu-Ai No.4.
[2]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. 93-11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL732344 Genomic DNA. Translation: CAH68191.1.
AL732351 Genomic DNA. Translation: CAJ86099.1.
CM000129 Genomic DNA. Translation: EAY96028.1.
UniGeneOs.50125.

3D structure databases

ProteinModelPortalA2XYW8.
ModBaseSearch...

Protein family/group databases

CAZyCBM49. Carbohydrate-Binding Module Family 49.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneA2XYW8.

Phylogenomic databases

eggNOGNOG05134.
HOGENOMHOG000021033.

Gene expression databases

ArrayExpressA2XYW8.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR019028. CBM_49.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamPF09478. CBM49. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTSM01063. CBM49. 1 hit.
[Graphical view]
SUPFAMSSF48208. Glyco_trans_6hp. 1 hit.
PROSITEPS00592. GLYCOSYL_HYDROL_F9_1. False negative.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN13_ORYSI
AccessionPrimary (citable) accession number: A2XYW8
Secondary accession number(s): Q259H9, Q7XQ92
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: April 3, 2013
This is version 34 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

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