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Protein

T-complex protein 1 subunit eta

Gene

MAL3P3.6

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • unfolded protein binding Source: GeneDB

GO - Biological processi

  • protein folding Source: GeneDB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-PFA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit eta
Short name:
TCP-1-eta
Alternative name(s):
CCT-eta
Gene namesi
ORF Names:MAL3P3.6, PFC0350c
OrganismiPlasmodium falciparum (isolate 3D7)
Taxonomic identifieri36329 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
Proteomesi
  • UP000001450 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_0308200.

Subcellular locationi

GO - Cellular componenti

  • chaperonin-containing T-complex Source: GeneDB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539T-complex protein 1 subunit etaPRO_0000128368Add
BLAST

Proteomic databases

PRIDEiO77323.

PTM databases

SwissPalmiO77323.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.By similarity

GO - Molecular functioni

  • unfolded protein binding Source: GeneDB

Protein-protein interaction databases

BioGridi1209650. 4 interactions.
IntActiO77323. 4 interactions.
MINTiMINT-1586847.

Structurei

3D structure databases

ProteinModelPortaliO77323.
SMRiO77323. Positions 9-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

HOGENOMiHOG000226730.
InParanoidiO77323.
KOiK09499.
OMAiMLELKVI.
PhylomeDBiO77323.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012720. Chap_CCT_eta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PANTHERiPTHR11353:SF22. PTHR11353:SF22. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02345. chap_CCT_eta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O77323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHLMSLPIV LLKEGTDTAQ GRSQIIRNIN ACQIIVDIVK TTLGPRGMDK
60 70 80 90 100
LIYTERDVTI TNDGATVMNL LNISHPAASI LVDIAKSQDD EVGDGTTSVV
110 120 130 140 150
VVAGELLNEA KGLLNDGIEP NMIIDGFRNA CNVAINKLNE LSLNFSNKNE
160 170 180 190 200
EEKRSILLKC AQTALNSKLV SNHKEFFGEL VVNAVYKLGD NLDKSNIGIK
210 220 230 240 250
KVTGGSCLDT QLIYGVAFKK TFSYAGFEQQ PKKFINPKIL LLNVELELKA
260 270 280 290 300
EKENAEVRIE NPNEYNSIVQ AEWDIIFKKL NLIKDCGANI VLSKLPIGDI
310 320 330 340 350
ATQFFADHDI FCAGRVEDAD LKRTANATGA LVQTSLFNLN DDVLGTCGVF
360 370 380 390 400
EEVQIGNERY NIFKECLKTK SVTIILRGGA KQFIEEVERS INDAIMIVLR
410 420 430 440 450
CITNSEIVPG AGSIEMQLSK YLRIYSRSIC NKEQIVLFSF AKALESIPRH
460 470 480 490 500
LSHNAGYDST DILNKLRKKH SEQTSDIWYG VDCMEGDIIN AYDNCIFEVT
510 520 530
KIKRNVIYSA TEAACLILSI DETIKNPSSA AGTQRSPYS
Length:539
Mass (Da):59,577
Last modified:November 1, 1998 - v1
Checksum:i51A18D81698AAE6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL844502 Genomic DNA. Translation: CAB11107.1.
PIRiT18430.
RefSeqiXP_001351157.1. XM_001351121.1.

Genome annotation databases

EnsemblProtistsiPFC0350c:mRNA; PFC0350c:pep; PFC0350c.
GeneDBiPF3D7_0308200.1:pep.
GeneIDi814399.
KEGGipfa:PFC0350c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL844502 Genomic DNA. Translation: CAB11107.1.
PIRiT18430.
RefSeqiXP_001351157.1. XM_001351121.1.

3D structure databases

ProteinModelPortaliO77323.
SMRiO77323. Positions 9-527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1209650. 4 interactions.
IntActiO77323. 4 interactions.
MINTiMINT-1586847.

PTM databases

SwissPalmiO77323.

Proteomic databases

PRIDEiO77323.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiPFC0350c:mRNA; PFC0350c:pep; PFC0350c.
GeneDBiPF3D7_0308200.1:pep.
GeneIDi814399.
KEGGipfa:PFC0350c.

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_0308200.

Phylogenomic databases

HOGENOMiHOG000226730.
InParanoidiO77323.
KOiK09499.
OMAiMLELKVI.
PhylomeDBiO77323.

Enzyme and pathway databases

ReactomeiR-PFA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012720. Chap_CCT_eta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PANTHERiPTHR11353:SF22. PTHR11353:SF22. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02345. chap_CCT_eta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTCPH_PLAF7
AccessioniPrimary (citable) accession number: O77323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: November 1, 1998
Last modified: September 7, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.