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Protein

RuBisCO large subunit-binding protein subunit alpha, chloroplastic

Gene
N/A
Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This protein binds RuBisCO small and large subunits and is implicated in the assembly of the enzyme oligomer.

Miscellaneous

This protein shows ATPase activity.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processStress response
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RuBisCO large subunit-binding protein subunit alpha, chloroplastic
Alternative name(s):
60 kDa chaperonin subunit alpha
CPN-60 alpha
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000005019? – 580RuBisCO large subunit-binding protein subunit alpha, chloroplastic
Transit peptidei1 – ?ChloroplastSequence analysis

Proteomic databases

PRIDEiQ42694.
ProMEXiQ42694.

Expressioni

Inductioni

By heat shock.

Interactioni

Subunit structurei

Oligomer of probably six alpha and six beta subunits.

Structurei

Secondary structure

1580
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi226 – 229Combined sources4
Helixi235 – 237Combined sources3
Turni241 – 244Combined sources4
Beta strandi245 – 260Combined sources16
Helixi263 – 274Combined sources12
Turni275 – 277Combined sources3
Beta strandi280 – 287Combined sources8
Helixi289 – 300Combined sources12
Beta strandi306 – 310Combined sources5
Beta strandi312 – 314Combined sources3
Helixi315 – 329Combined sources15
Helixi336 – 338Combined sources3
Helixi342 – 344Combined sources3
Helixi347 – 349Combined sources3
Beta strandi351 – 358Combined sources8
Beta strandi363 – 366Combined sources4
Helixi372 – 388Combined sources17
Helixi392 – 405Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5CDJX-ray1.75A/B224-408[»]
ProteinModelPortaliQ42694.
SMRiQ42694.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.

Family and domain databases

CDDicd03344. GroEL. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60. 1 hit.
InterProiView protein in InterPro
IPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR037290. Cpn60/TCP-1_sf.
IPR027409. GroEL-like_apical_dom_sf.
IPR027413. GROEL-like_equatorial_sf.
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiView protein in Pfam
PF00118. Cpn60_TCP1. 1 hit.
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
SSF54849. SSF54849. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiView protein in PROSITE
PS00296. CHAPERONINS_CPN60. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q42694-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQSQLAKGS RQTTGRPFQN KPARAARRLV IRAADAKEIV FDQESRRRLQ
60 70 80 90 100
AGINKVADAV GVTLGPRGRN VVLEQKFGVP QVINDGVSIR RAIELKDPVE
110 120 130 140 150
NAGAQLIKEV AGRTNDAAGD GTTTASVLAR EMIHYGLQSV TAGANPIAVK
160 170 180 190 200
RGLDKTAEYL VAKLKEHAKP VKGRDDIKNV ASISAGNDNA IGEMIADALD
210 220 230 240 250
KVGSNGVLSI ETSNSTETVV EVQEGMEIDR GYISPQFVTN QERLLVEYDN
260 270 280 290 300
CRVLVTDQKI DAIRDIIPIL EQVTRLNAPL LIIAEDVSGE ALATLVVNKL
310 320 330 340 350
RGVLNVCAIK APGFGERRKS LLQDIAIVTG AEFIAKDLGM KVEQAVVEQL
360 370 380 390 400
GVARKVTVAN NTTTLIADAA SKDEIEMRIA QLKKELAETD SVYDTEKLSE
410 420 430 440 450
RIAKLSGGVA VIKVGAATEA ELEDRKLRIE DAKNATFAAV EEGIVPGGGA
460 470 480 490 500
ALLHLSELVP AFKETLTDAE EKLGADIVMK SLRAPCRLIA DNAGVEGEVI
510 520 530 540 550
VQRLLGKPFE VGYNAMIDKV ENLLDAGVID PAKVTRNGLL NSVSIAGIML
560 570 580
TTQAVMVEKH KPSEIPGGMT ASGMPSGMTI
Length:580
Mass (Da):61,863
Last modified:November 1, 1997 - v1
Checksum:i16FD34B115E706F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27472 mRNA. Translation: AAA98642.1.
PIRiS56645.

Similar proteinsi

Entry informationi

Entry nameiRUBA_CHLRE
AccessioniPrimary (citable) accession number: Q42694
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 31, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families