ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/TrEMBL entry Q56J81


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name Q56J81_9BILA
Primary accession number Q56J81
Secondary accession numbers None
Integrated into TrEMBL on May 10, 2005
Sequence was last modified on May 10, 2005 (Sequence version 1)
Annotations were last modified on    May 5, 2009 (Entry version 20)
Name and origin of the protein
Protein name Fba1-like protein [Fragment]
Synonyms None
Gene name None
From
Philodina sp. NPS-2005 [TaxID: 317012] 
Taxonomy Eukaryota; Metazoa; Rotifera; Bdelloidea; Philodinida; Philodinidae; Philodina.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE.
DOI=10.1093/molbev/msi139; PubMed=15788744 [NCBI, ExPASy, EBI, Israel, Japan]
Pouchkina-Stantcheva N.N., Tunnacliffe A.;
"Spliced leader RNA-mediated trans-splicing in phylum Rotifera.";
Mol. Biol. Evol. 22:1482-1489(2005).
Comments
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
AY942840; AAX81538.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q56J81.
Ontologies
GO
GO:0004332; Molecular function: fructose-bisphosphate aldolase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR000771; Ketose_bisP_aldolase_II.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01116; F_bP_aldolase; 1.
Pfam graphical view of domain structure.
ProDom PD002376; K_bP_aldolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00602; ALDOLASE_CLASS_II_1; 1.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
None
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description
NON_TER   168   168         
Sequence information
Length: 168 AA [This is the length of the partial sequence] Molecular weight: 18022 Da [This is the MW of the partial sequence] CRC64: B54934C8DDB4A3E4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGVLDVVPAG VLTGDNVLKL FAYAKEHQFA IPAINVTSSS AANSVLEAAR DAKAPVIIQF 

        70         80         90        100        110        120 
SQGGAQFFAG KGLNNDGQAA SILGSIAGAH HVRTVAKSYG VPVVLHSDHC AKKLEPWFVG 

       130        140        150        160 
MLEADEAYFK AHGEPLFSSH MIDFSEEPKD HNIEACKKYL KRMAPMKN 

Q56J81 in FASTA format

View entry in raw text format (no links)
Request for annotation of this UniProtKB/TrEMBL entry

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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!