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Protein

Chaperone protein ClpC1, chloroplastic

Gene

CLPC1

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

Functioni

Molecular chaperone that hydrolyzes ATP and is associated with the chloroplast protein import apparatus. May function as the motor for chloroplast protein translocation, as translocation requires ATP hydrolysis in the stroma. May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast. Involved in the regulation of chlorophyll b biosynthesis through the destabilization of chlorophyllide a oxygenase (CAO) protein in response to the accumulation of chlorophyll b. Involved in leaf iron homeostasis.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi302 – 3098ATPSequence analysis
Nucleotide bindingi645 – 6528ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent peptidase activity Source: TAIR

GO - Biological processi

  • chloroplast organization Source: TAIR
  • protein import into chloroplast stroma Source: TAIR
  • protein targeting to chloroplast Source: TAIR
  • regulation of chlorophyll biosynthetic process Source: TAIR
  • response to cytokinin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G50920-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 ClpC1, chloroplastic1 Publication
Alternative name(s):
ATP-dependent Clp protease ATP-binding subunit ClpC homolog 1
Casein lytic proteinase C1
Protein DE-REGULATED CAO ACCUMULATION 1
Protein IRON-RESCUED MUTANT 1
Gene namesi
Name:CLPC11 Publication
Synonyms:DCA1, HSP93-V1 Publication, IRM1
Ordered Locus Names:At5g50920Imported
ORF Names:K3K7.7Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G50920.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast inner membrane Source: TAIR
  • chloroplast stroma Source: TAIR
  • chloroplast thylakoid membrane Source: TAIR
  • mitochondrion Source: TAIR
  • plastid Source: TAIR
  • plastid stroma Source: TAIR
  • Tic complex Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid

Pathology & Biotechi

Disruption phenotypei

Small plants with chlorotic leaves, aberrant chloroplast biogenesis and inefficient chloroplast import of both photosynthetic and non-photosynthetic preproteins (PubMed:15516497, PubMed:15563614, Ref. 11, PubMed:15659100, PubMed:17376159, PubMed:17291312, PubMed:20382967). Clpc1 and clpc2 double mutants are embryo lethal when homozygous (PubMed:17376159).7 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi773 – 7731G → R in irm1; iron deficiency chlorosis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838ChloroplastSequence analysisAdd
BLAST
Chaini39 – 929891Chaperone protein ClpC1, chloroplasticPRO_0000412575Add
BLAST

Proteomic databases

PaxDbiQ9FI56.
PRIDEiQ9FI56.

Expressioni

Tissue specificityi

Highly expressed in rosette leaves. Expressed in roots, stems and inflorescences (PubMed:11982939, PubMed:15659100, PubMed:20382967). Expressed in photosynthetic green tissues with high levels in young, developing leaf tissues (PubMed:23898032).4 Publications

Inductioni

By cold and salt stresses. Not induced by heat stress.2 Publications

Gene expression databases

GenevisibleiQ9FI56. AT.

Interactioni

Subunit structurei

Homodimer (PubMed:14593120). May form hexamer and interact with Clp core (PubMed:14593120). Interacts (via N-terminus) with CLPS1 (PubMed:23898032).2 Publications

Protein-protein interaction databases

BioGridi20411. 2 interactions.
IntActiQ9FI56. 1 interaction.
STRINGi3702.AT5G50920.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FI56.
SMRiQ9FI56. Positions 92-905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini511 – 54636UVRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni257 – 504248IBy similarityAdd
BLAST
Regioni571 – 762192IIBy similarityAdd
BLAST

Domaini

The N-terminal domain (91-234) is important for membrane association and is essential for the in vivo functions, but not for the ATPase activity.1 Publication

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.
InParanoidiQ9FI56.
KOiK03696.
OMAiDEKQRTY.
PhylomeDBiQ9FI56.

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.

Q9FI56-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMATRVLAQ STPPSLACYQ RNVPSRGSGR SRRSVKMMCS QLQVSGLRMQ
60 70 80 90 100
GFMGLRGNNA LDTLGKSRQD FHSKVRQAMN VPKGKASRFT VKAMFERFTE
110 120 130 140 150
KAIKVIMLAQ EEARRLGHNF VGTEQILLGL IGEGTGIAAK VLKSMGINLK
160 170 180 190 200
DARVEVEKII GRGSGFVAVE IPFTPRAKRV LELSLEEARQ LGHNYIGSEH
210 220 230 240 250
LLLGLLREGE GVAARVLENL GADPSNIRTQ VIRMVGENNE VTANVGGGSS
260 270 280 290 300
SNKMPTLEEY GTNLTKLAEE GKLDPVVGRQ PQIERVVQIL GRRTKNNPCL
310 320 330 340 350
IGEPGVGKTA IAEGLAQRIA SGDVPETIEG KKVITLDMGL LVAGTKYRGE
360 370 380 390 400
FEERLKKLME EIRQSDEIIL FIDEVHTLIG AGAAEGAIDA ANILKPALAR
410 420 430 440 450
GELQCIGATT LDEYRKHIEK DPALERRFQP VKVPEPTVDE TIQILKGLRE
460 470 480 490 500
RYEIHHKLRY TDESLVAAAQ LSYQYISDRF LPDKAIDLID EAGSRVRLRH
510 520 530 540 550
AQVPEEAREL EKELRQITKE KNEAVRGQDF EKAGTLRDRE IELRAEVSAI
560 570 580 590 600
QAKGKEMSKA ESETGEEGPM VTESDIQHIV SSWTGIPVEK VSTDESDRLL
610 620 630 640 650
KMEETLHKRI IGQDEAVKAI SRAIRRARVG LKNPNRPIAS FIFSGPTGVG
660 670 680 690 700
KSELAKALAA YYFGSEEAMI RLDMSEFMER HTVSKLIGSP PGYVGYTEGG
710 720 730 740 750
QLTEAVRRRP YTVVLFDEIE KAHPDVFNMM LQILEDGRLT DSKGRTVDFK
760 770 780 790 800
NTLLIMTSNV GSSVIEKGGR RIGFDLDYDE KDSSYNRIKS LVTEELKQYF
810 820 830 840 850
RPEFLNRLDE MIVFRQLTKL EVKEIADILL KEVFERLKKK EIELQVTERF
860 870 880 890 900
KERVVDEGYN PSYGARPLRR AIMRLLEDSM AEKMLAREIK EGDSVIVDVD
910 920
AEGNVTVLNG GSGTPTTSLE EQEDSLPVA
Length:929
Mass (Da):103,453
Last modified:March 1, 2001 - v1
Checksum:i438DEA514125F0BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 489SQLQVSGLR → IIFNVWLP in AAC04687 (PubMed:11982939).Curated
Sequence conflicti187 – 1882EA → AT in AAC04687 (PubMed:11982939).Curated
Sequence conflicti507 – 5071A → V in AAC04687 (PubMed:11982939).Curated
Sequence conflicti685 – 6851K → T in AAC04687 (PubMed:11982939).Curated
Sequence conflicti690 – 6901P → L in AAC04687 (PubMed:11982939).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022909 mRNA. Translation: AAC04687.1.
AB017063 Genomic DNA. Translation: BAB08738.1.
CP002688 Genomic DNA. Translation: AED96011.1.
AY102125 mRNA. Translation: AAM26692.1.
AK227173 mRNA. Translation: BAE99213.1.
PIRiT52292.
RefSeqiNP_568746.1. NM_124471.3.
UniGeneiAt.24774.
At.74761.
At.74764.
At.75059.

Genome annotation databases

EnsemblPlantsiAT5G50920.1; AT5G50920.1; AT5G50920.
GeneIDi835165.
GrameneiAT5G50920.1; AT5G50920.1; AT5G50920.
KEGGiath:AT5G50920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022909 mRNA. Translation: AAC04687.1.
AB017063 Genomic DNA. Translation: BAB08738.1.
CP002688 Genomic DNA. Translation: AED96011.1.
AY102125 mRNA. Translation: AAM26692.1.
AK227173 mRNA. Translation: BAE99213.1.
PIRiT52292.
RefSeqiNP_568746.1. NM_124471.3.
UniGeneiAt.24774.
At.74761.
At.74764.
At.75059.

3D structure databases

ProteinModelPortaliQ9FI56.
SMRiQ9FI56. Positions 92-905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20411. 2 interactions.
IntActiQ9FI56. 1 interaction.
STRINGi3702.AT5G50920.1.

Protein family/group databases

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

Proteomic databases

PaxDbiQ9FI56.
PRIDEiQ9FI56.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G50920.1; AT5G50920.1; AT5G50920.
GeneIDi835165.
GrameneiAT5G50920.1; AT5G50920.1; AT5G50920.
KEGGiath:AT5G50920.

Organism-specific databases

TAIRiAT5G50920.

Phylogenomic databases

eggNOGiKOG1051. Eukaryota.
COG0542. LUCA.
HOGENOMiHOG000218210.
InParanoidiQ9FI56.
KOiK03696.
OMAiDEKQRTY.
PhylomeDBiQ9FI56.

Enzyme and pathway databases

BioCyciARA:AT5G50920-MONOMER.

Miscellaneous databases

PROiQ9FI56.

Gene expression databases

GenevisibleiQ9FI56. 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. "Characterization of chloroplast Clp proteins in Arabidopsis: localization, tissue specificity and stress responses."
    Zheng B., Halperin T., Hruskova-Heidingsfeldova O., Adam Z., Clarke A.K.
    Physiol. Plantarum 114:92-101(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones."
    Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.
    DNA Res. 6:183-195(1999) [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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. Cited for: GENE FAMILY, NOMENCLATURE.
  7. "Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications."
    Peltier J.-B., Ripoll D.R., Friso G., Rudella A., Cai Y., Ytterberg J., Giacomelli L., Pillardy J., van Wijk K.J.
    J. Biol. Chem. 279:4768-4781(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis."
    Constan D., Froehlich J.E., Rangarajan S., Keegstra K.
    Plant Physiol. 136:3605-3615(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content."
    Sjoegren L.L., MacDonald T.M., Sutinen S., Clarke A.K.
    Plant Physiol. 136:4114-4126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "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.
  11. "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, DISRUPTION PHENOTYPE.
  12. "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: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  13. "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.
  14. "Clp protease controls chlorophyll b synthesis by regulating the level of chlorophyllide a oxygenase."
    Nakagawara E., Sakuraba Y., Yamasato A., Tanaka R., Tanaka A.
    Plant J. 49:800-809(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  15. "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.
  16. "ClpC1, an ATP-dependent Clp protease in plastids, is involved in iron homeostasis in Arabidopsis leaves."
    Wu H., Ji Y., Du J., Kong D., Liang H., Ling H.Q.
    Ann. Bot. 105:823-833(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-773.
  17. "The amino-terminal domain of chloroplast Hsp93 is important for its membrane association and functions in vivo."
    Chu C.C., Li H.M.
    Plant Physiol. 158:1656-1665(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  18. "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.
  19. "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.
  20. "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 nameiCLPC1_ARATH
AccessioniPrimary (citable) accession number: Q9FI56
Secondary accession number(s): O48931
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 104 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.