Reviewed,
UniProtKB/Swiss-Prot P50719 (TBA_HAECO)
Last modified
January 19, 2010.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (1) |
 Third-party data |
 Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Tubulin alpha chain |
| Organism | Haemonchus contortus (Barber pole worm) |
| Taxonomic identifier | 6289 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Strongylida › Trichostrongyloidea › Haemonchidae › Haemonchinae › Haemonchus |
Protein attributes
| Sequence length | 450 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain. |
| Subunit structure | Dimer of alpha and beta chains. |
| Post-translational modification | Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively By similarity. |
| Sequence similarities | Belongs to the tubulin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Microtubule |
| Ligand | GTP-binding Nucleotide-binding |
| Gene Ontology (GO) | |
| Biological process | microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerizationInferred from electronic annotation. Source: InterPro |
| Cellular component | microtubule Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activityInferred from electronic annotation. Source: InterPro structural molecule activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning of a cDNA encoding alpha-tubulin from Haemonchus contortus." Klein R.D., Nulf S.C., Alexander-Bowman S.J., Mainone C.B., Geary T.G. Mol. Biochem. Parasitol. 56:345-348(1992) [PubMed: 1484557] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L02108 mRNA. Translation: AAA29167.1. |
| PIR | A48466. |
3D structure databases | |
| SMR | P50719. Positions 1-440. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR002452. Alpha_tubulin. IPR008280. Tub_FtsZ_C. IPR000217. Tubulin. IPR018316. Tubulin/FtsZ_2-layer-sand-dom. IPR017975. Tubulin_CS. IPR003008. Tubulin_FtsZ_GTPase. IPR019746. Tubulin_FtsZ_N. [Graphical view] |
| Gene3D | G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit. G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit. |
| PANTHER | PTHR11588:SF10. Alpha_tubulin. 1 hit. PTHR11588. Tubulin. 1 hit. |
| Pfam | PF00091. Tubulin. 1 hit. PF03953. Tubulin_C. 1 hit. [Graphical view] |
| PRINTS | PR01162. ALPHATUBULIN. PR01161. TUBULIN. |
| SMART | SM00865. Tubulin_C. 1 hit. [Graphical view] |
| PROSITE | PS00227. TUBULIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00518. Albendazole. DB00643. Mebendazole. |
Entry information
| Entry name | TBA_HAECO | ||||||||
| Accession | Primary (citable) accession number: P50719 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
