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Protein

Chaperone protein ClpC2, chloroplastic

Gene

CLPC2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone (PubMed:15304652, PubMed:21737456, PubMed:24599948). May act as a suppressor of FtsH-mediated thylakoid membrane biogenesis and may enhance photoinhibition (PubMed:15304652). Seems not involved in chloroplastic protein import (PubMed:15304652). Probable component of the TIC-associated stromal import motor involved in inner membrane translocation (PubMed:17376159). Has an ATPase activity, but no ADPase activity (PubMed:21737456). Interacts with transit peptides with a positional preference (PubMed:21737456, PubMed:22545953). Localization of the signal sequence at the N-terminal end of a protein seems mandatory for interaction to take place (PubMed:22545953).5 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=1.42 mM for ATP1 Publication
  1. Vmax=0.62 nmol/min/µg enzyme1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi323 – 3308ATPSequence analysis
Nucleotide bindingi666 – 6738ATPSequence analysis

GO - Molecular functioni

  • ATPase activity Source: TAIR
  • ATP binding Source: UniProtKB-KW
  • protein homodimerization activity Source: TAIR

GO - Biological processi

  • chloroplast organization Source: TAIR
  • protein hexamerization Source: TAIR
  • protein import into chloroplast stroma Source: TAIR
  • protein metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G48870-MONOMER.
ARA:GQT-2605-MONOMER.

Protein family/group databases

TCDBi3.A.9.1.2. the chloroplast envelope protein translocase (cept or tic-toc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein ClpC2, chloroplastic1 Publication (EC:3.6.1.31 Publication)
Alternative name(s):
ATP-dependent Clp protease ATP-binding subunit ClpC homolog 2
AtClpC
Casein lytic proteinase C2
Gene namesi
Name:CLPC21 Publication
Synonyms:HSP93-III1 Publication
Ordered Locus Names:At3g48870Imported
ORF Names:T21J18.140Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G48870.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast membrane Source: UniProtKB-SubCell
  • chloroplast stroma Source: TAIR
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • plastid Source: TAIR
  • plastid stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype (PubMed:17376159). Clpc1 and clpc2 double mutants are embryo lethal when homozygous (PubMed:17376159).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545ChloroplastSequence analysisAdd
BLAST
Chaini46 – 952907Chaperone protein ClpC2, chloroplasticPRO_0000412576Add
BLAST

Proteomic databases

PaxDbiQ9SXJ7.
PRIDEiQ9SXJ7.

PTM databases

SwissPalmiQ9SXJ7.

Expressioni

Tissue specificityi

Expressed at low levels in roots and inflorescences (PubMed:15659100). Expressed at very low levels in rosette leaves (PubMed:15659100). Expressed in photosynthetic green tissues with high levels in young, developing leaf tissues (PubMed:23898032).2 Publications

Inductioni

By senescence. Not induced by heat stress.2 Publications

Gene expression databases

ExpressionAtlasiQ9SXJ7. baseline.
GenevisibleiQ9SXJ7. AT.

Interactioni

Subunit structurei

Homodimer and homohexamer (PubMed:21737456). Hexamerization upon addition of ATP (PubMed:21737456). Interacts with CLPT1 (PubMed:25149061). Interacts with CLPS1 (PubMed:23898032). Stably associated with the import machinery (PubMed:21737456).3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi9366. 3 interactions.
IntActiQ9SXJ7. 2 interactions.
STRINGi3702.AT3G48870.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SXJ7.
SMRiQ9SXJ7. Positions 112-928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini532 – 56736UVRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 525248IBy similarityAdd
BLAST
Regioni592 – 783192IIBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the ClpA/ClpB family. ClpC subfamily.Curated
Contains 1 UVR domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG1051. Eukaryota.
COG0542. LUCA.
HOGENOMiHOG000218210.
InParanoidiQ9SXJ7.
OMAiHNNSEAV.
PhylomeDBiQ9SXJ7.

Family and domain databases

Gene3Di1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
IPR027417. P-loop_NTPase.
IPR001943. UVR_dom.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
PF02151. UVR. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF81923. SSF81923. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SXJ7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAWSIALLTP PFFGPGRHVQ AKEYREPRGC VMKMSSLKAP VLRIQATEYR
60 70 80 90 100
EPRGRVKMMS SLQAPLLTIQ SFSGLRAPSA LDYLGRPSPG FLVKYKLAKS
110 120 130 140 150
SGREKASRCV PKAMFERFTE KAIKVIMLSQ EEARRLGHNF VGTEQILLGL
160 170 180 190 200
IGEGTGIAAK VLKSMGINLK DSRVEVEKII GRGSGFVAVE IPFTPRAKRV
210 220 230 240 250
LELSLEEARQ LGHNYIGSEH LLLGLLREGE GVAARVLENL GADPSNIRTQ
260 270 280 290 300
VIRMVGENNE VTASVGGGSS GNSKMPTLEE YGTNLTKLAE EGKLDPVVGR
310 320 330 340 350
QPQIERVVQI LARRTKNNPC LIGEPGVGKT AIAEGLAQRI ASGDVPETIE
360 370 380 390 400
GKTVITLDMG LLVAGTKYRG EFEERLKKLM EEIRQSDEII LFIDEVHTLI
410 420 430 440 450
GAGAAEGAID AANILKPALA RGELQCIGAT TIDEYRKHIE KDPALERRFQ
460 470 480 490 500
PVKVPEPTVE EAIQILQGLR ERYEIHHKLR YTDEALVAAA QLSHQYISDR
510 520 530 540 550
FLPDKAIDLI DEAGSRVRLR HAQLPEEARE LEKQLRQITK EKNEAVRSQD
560 570 580 590 600
FEMAGSHRDR EIELKAEIAN VLSRGKEVAK AENEAEEGGP TVTESDIQHI
610 620 630 640 650
VATWTGIPVE KVSSDESSRL LQMEQTLHTR VIGQDEAVKA ISRAIRRARV
660 670 680 690 700
GLKNPNRPIA SFIFSGPTGV GKSELAKALA AYYFGSEEAM IRLDMSEFME
710 720 730 740 750
RHTVSKLIGS PPGYVGYTEG GQLTEAVRRR PYTLVLFDEI EKAHPDVFNM
760 770 780 790 800
MLQILEDGRL TDSKGRTVDF KNTLLIMTSN VGSSVIEKGG RRIGFDLDHD
810 820 830 840 850
EKDSSYNRIK SLVTEELKQY FRPEFLNRLD EMIVFRQLTK LEVKEIADIM
860 870 880 890 900
LKEVVARLEV KEIELQVTER FKERVVDEGF DPSYGARPLR RAIMRLLEDS
910 920 930 940 950
MAEKMLSRDI KEGDSVIVDV DAEGSVVVLS GTTGRVGGFA AEEAMEDPIP

IL
Length:952
Mass (Da):105,739
Last modified:May 1, 2000 - v1
Checksum:iF6BD9C64FE6A6F87
GO

Sequence cautioni

The sequence AAL10478.1 differs from that shown. Reason: Frameshift at position 548. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti307 – 3071V → M in CAB87915 (PubMed:11130713).Curated
Sequence conflicti461 – 4611E → G in AAL10478 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022324 mRNA. Translation: BAA82062.1.
AL132963 Genomic DNA. Translation: CAB87915.1.
CP002686 Genomic DNA. Translation: AEE78466.1.
AY056787 mRNA. Translation: AAL10478.1. Frameshift.
PIRiT49283.
T52456.
RefSeqiNP_566912.2. NM_114746.4. [Q9SXJ7-1]
UniGeneiAt.23421.

Genome annotation databases

EnsemblPlantsiAT3G48870.1; AT3G48870.1; AT3G48870. [Q9SXJ7-1]
GeneIDi824048.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022324 mRNA. Translation: BAA82062.1.
AL132963 Genomic DNA. Translation: CAB87915.1.
CP002686 Genomic DNA. Translation: AEE78466.1.
AY056787 mRNA. Translation: AAL10478.1. Frameshift.
PIRiT49283.
T52456.
RefSeqiNP_566912.2. NM_114746.4. [Q9SXJ7-1]
UniGeneiAt.23421.

3D structure databases

ProteinModelPortaliQ9SXJ7.
SMRiQ9SXJ7. Positions 112-928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9366. 3 interactions.
IntActiQ9SXJ7. 2 interactions.
STRINGi3702.AT3G48870.1.

Protein family/group databases

TCDBi3.A.9.1.2. the chloroplast envelope protein translocase (cept or tic-toc) family.

PTM databases

SwissPalmiQ9SXJ7.

Proteomic databases

PaxDbiQ9SXJ7.
PRIDEiQ9SXJ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G48870.1; AT3G48870.1; AT3G48870. [Q9SXJ7-1]
GeneIDi824048.

Organism-specific databases

TAIRiAT3G48870.

Phylogenomic databases

eggNOGiKOG1051. Eukaryota.
COG0542. LUCA.
HOGENOMiHOG000218210.
InParanoidiQ9SXJ7.
OMAiHNNSEAV.
PhylomeDBiQ9SXJ7.

Enzyme and pathway databases

BioCyciARA:AT3G48870-MONOMER.
ARA:GQT-2605-MONOMER.

Miscellaneous databases

PROiQ9SXJ7.

Gene expression databases

ExpressionAtlasiQ9SXJ7. baseline.
GenevisibleiQ9SXJ7. AT.

Family and domain databases

Gene3Di1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
IPR027417. P-loop_NTPase.
IPR001943. UVR_dom.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
PF02151. UVR. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF81923. SSF81923. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of clp genes expressed in senescing Arabidopsis leaves."
    Nakabayashi K., Ito M., Kiyosue T., Shinozaki K., Watanabe A.
    Plant Cell Physiol. 40:504-514(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION BY SENESCENCE.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. Cited for: GENE FAMILY, NOMENCLATURE.
  6. "Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in thylakoid membrane biogenesis."
    Park S., Rodermel S.R.
    Proc. Natl. Acad. Sci. U.S.A. 101:12765-12770(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The ATP-dependent Clp protease in chloroplasts of higher plants."
    Clarke A.K., MacDonald T.M., Sjoegren L.L.
    Physiol. Plantarum 123:406-412(2005)
    Cited for: NOMENCLATURE.
  8. "In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import."
    Kovacheva S., Bedard J., Patel R., Dudley P., Twell D., Rios G., Koncz C., Jarvis P.
    Plant J. 41:412-428(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import."
    Kovacheva S., Bedard J., Wardle A., Patel R., Jarvis P.
    Plant J. 50:364-379(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress and chloroplast development."
    Lee U., Rioflorido I., Hong S.W., Larkindale J., Waters E.R., Vierling E.
    Plant J. 49:115-127(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Insights into the Clp/HSP100 chaperone system from chloroplasts of Arabidopsis thaliana."
    Rosano G.L., Bruch E.M., Ceccarelli E.A.
    J. Biol. Chem. 286:29671-29680(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  12. "Chloroplastic Hsp100 chaperones ClpC2 and ClpD interact in vitro with a transit peptide only when it is located at the N-terminus of a protein."
    Bruch E.M., Rosano G.L., Ceccarelli E.A.
    BMC Plant Biol. 12:57-57(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The chloroplast ATP-dependent Clp protease in vascular plants - new dimensions and future challenges."
    Clarke A.K.
    Physiol. Plantarum 145:235-244(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  14. "ClpS1 is a conserved substrate selector for the chloroplast Clp protease system in Arabidopsis."
    Nishimura K., Asakura Y., Friso G., Kim J., Oh S.H., Rutschow H., Ponnala L., van Wijk K.J.
    Plant Cell 25:2276-2301(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH CLPS1.
  15. "Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones."
    Colombo C.V., Ceccarelli E.A., Rosano G.L.
    BMC Plant Biol. 14:228-228(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLPT1.
  16. "Quantitative analysis of the chloroplast molecular chaperone ClpC/Hsp93 in Arabidopsis reveals new insights into its localization, interaction with the Clp proteolytic core, and functional importance."
    Sjoegren L.L., Tanabe N., Lymperopoulos P., Khan N.Z., Rodermel S.R., Aronsson H., Clarke A.K.
    J. Biol. Chem. 289:11318-11330(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCLPC2_ARATH
AccessioniPrimary (citable) accession number: Q9SXJ7
Secondary accession number(s): Q93ZM4, Q9M2Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: May 1, 2000
Last modified: April 13, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.