P35315 (ATC_TRYBB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 79.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable calcium-transporting ATPase EC=3.6.3.8 Alternative name(s): Calcium pump | ||
| Gene names |
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| Organism | Trypanosoma brucei brucei | ||
| Taxonomic identifier | 5702 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma |
Protein attributes
| Sequence length | 1011 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium By similarity. |
| Catalytic activity | ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]. |
| Subcellular location | Flagellar pocket. Cell membrane; Multi-pass membrane protein. Note: May be located in the flagellar pocket of the membrane. |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. [View classification] |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calcium transport Ion transport Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | ATP-binding Calcium Magnesium Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | ATP biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | flagellar pocket Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1011 | 1011 | Probable calcium-transporting ATPase | PRO_0000046228 | |||||
Regions | |||||||||
| Topological domain | 1 – 65 | 65 | Cytoplasmic Potential | ||||||
| Transmembrane | 66 – 84 | 19 | Helical; Potential | ||||||
| Topological domain | 85 – 90 | 6 | Extracellular Potential | ||||||
| Transmembrane | 91 – 110 | 20 | Helical; Potential | ||||||
| Topological domain | 111 – 258 | 148 | Cytoplasmic Potential | ||||||
| Transmembrane | 259 – 278 | 20 | Helical; Potential | ||||||
| Topological domain | 279 – 303 | 25 | Extracellular Potential | ||||||
| Transmembrane | 304 – 321 | 18 | Helical; Potential | ||||||
| Topological domain | 322 – 770 | 449 | Cytoplasmic Potential | ||||||
| Transmembrane | 771 – 794 | 24 | Helical; Potential | ||||||
| Topological domain | 795 – 835 | 41 | Extracellular Potential | ||||||
| Transmembrane | 836 – 856 | 21 | Helical; Potential | ||||||
| Topological domain | 857 – 885 | 29 | Cytoplasmic Potential | ||||||
| Transmembrane | 886 – 905 | 20 | Helical; Potential | ||||||
| Topological domain | 906 – 922 | 17 | Extracellular Potential | ||||||
| Transmembrane | 923 – 942 | 20 | Helical; Potential | ||||||
| Topological domain | 943 – 1011 | 69 | Cytoplasmic Potential | ||||||
Sites | |||||||||
| Active site | 357 | 1 | 4-aspartylphosphate intermediate By similarity | ||||||
| Binding site | 514 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Structure and transcription of a P-ATPase gene from Trypanosoma brucei." Revelard P., Pays E. Mol. Biochem. Parasitol. 46:241-251(1991) [PubMed: 1833643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M73769 Genomic DNA. Translation: AAA30227.1. |
3D structure databases | |
| ProteinModelPortal | P35315. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR005782. ATPase_P-typ_Ca-transp. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view] |
| Gene3D | G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits. |
| Pfam | PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view] |
| PRINTS | PR00119. CATATPASE. |
| SMART | SM00831. Cation_ATPase_N. 1 hit. [Graphical view] |
| SUPFAM | SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit. |
| TIGRFAMs | TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 2 hits. |
| PROSITE | PS00154. ATPASE_E1_E2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATC_TRYBB | ||||||||
| Accession | Primary (citable) accession number: P35315 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with