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Q7XFK2 (BGA14_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 64. Feed History...

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

Names and origin

Protein namesRecommended name:
Beta-galactosidase 14

Short name=Lactase 14
EC=3.2.1.23
Gene names
Ordered Locus Names:Os10g0340600, LOC_Os10g19960
ORF Names:OsJ_029934, OSJNBa0050M22.9
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length808 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Subcellular location

Secretedextracellular spaceapoplast Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Contains 1 SUEL-type lectin domain.

Ontologies

Keywords
   Cellular componentApoplast
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 808780Beta-galactosidase 14
PRO_0000294166

Regions

Domain726 – 80883SUEL-type lectin

Sites

Active site1871Proton donor Potential
Active site2591Nucleophile Potential

Amino acid modifications

Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation4321N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Glycosylation5261N-linked (GlcNAc...) Potential
Glycosylation5661N-linked (GlcNAc...) Potential
Glycosylation5951N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q7XFK2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 36ED4F19771A2E0E

FASTA80890,072
        10         20         30         40         50         60 
MAKAMCSLGA CLAVMLVVLA AAVAGVGCSI VSYDGRSLIL DGERRIVISG SIHYPRSTPE 

        70         80         90        100        110        120 
MWPDLIKKAK EGGLNAIETY VFWNGHEPRR REFNFEGNYD VVRFFKEIQN AGMYAILRIG 

       130        140        150        160        170        180 
PYICGEWNYG GLPVWLRDIP GIKFRLHNKP FENGMEAFTT LIVKKMKDAN MFAGQGGPII 

       190        200        210        220        230        240 
LAQIENEYGY TMLQPENIQS AHEYIHWCAD MANKQNVGVP WIMCQQDNDV PPNVVNTCNG 

       250        260        270        280        290        300 
FYCHEWFSNR TSIPKMWTEN WTGWYRDWDQ PEFRRPTEDI AFAVAMFFQM RGSLQNYYMY 

       310        320        330        340        350        360 
HGGTNFGRTA GGPYITTSYD YDAPLDEYGN LRQPKYGHLK ELHSVLMSME KILLHGDYID 

       370        380        390        400        410        420 
TNYGDNVTVT KYTLNATSAC FINNRFDDRD VNVTLDGTTH FLPAWSVSIL PNCKTVAFNS 

       430        440        450        460        470        480 
AKIKTQTTVM VNKTSMVEQQ TEHFKWSWMP ENLRPFMTDE KGNFRKNELL EQIVTTTDQS 

       490        500        510        520        530        540 
DYLWYRTSLE HKGEGSYVLY VNTTGHELYA FVNGKLVGQQ YSPNENFTFQ LKSPNYGGSF 

       550        560        570        580        590        600 
ELLPAGIVGG PVKLIDSSGS AIDLSNNSWS YKAGLAGEYR KIYLDKPGNK WRSHNSTIPI 

       610        620        630        640        650        660 
NRPFTWYKTT FQAPAGEDSV VVDLHGLNKG VAWVNGNSLG RYWPSYVAAD MPGCHHCDYR 

       670        680        690        700        710        720 
GVFKAEVEAQ KCLTGCGEPS QQLYHVPRSF LNKGEPNTLI LFEEAGGDPS EVAVRTVVEG 

       730        740        750        760        770        780 
SVCASAEVGD TVTLSCGAHG RTISSVDVAS FGVARGRCGS YDGGCESKVA YDAFAAACVG 

       790        800 
KESCTVLVTD AFANAGCVSG VLTVQATC 

« Hide

References

[1]"In-depth view of structure, activity, and evolution of rice chromosome 10."
Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H. expand/collapse author list , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.
Science 300:1566-1569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[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. Nipponbare.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC090483 Genomic DNA. Translation: AAK98719.1.
DP000086 Genomic DNA. Translation: AAP53122.1.
CM000147 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalQ7XFK2.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH35. Glycoside Hydrolase Family 35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ7XFK2.

Phylogenomic databases

eggNOGCOG1874.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProIPR008979. Galactose-bd-like.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
IPR000922. Lectin_gal-bd_dom.
[Graphical view]
PANTHERPTHR23421. PTHR23421. 1 hit.
PfamPF02140. Gal_Lectin. 1 hit.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSPR00742. GLHYDRLASE35.
SUPFAMSSF49785. SSF49785. 3 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
PS50228. SUEL_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGA14_ORYSJ
AccessionPrimary (citable) accession number: Q7XFK2
Secondary accession number(s): Q947Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 1, 2003
Last modified: October 16, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries