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Protein

Beta carbonic anhydrase 1, chloroplastic

Gene

BCA1

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

Functioni

Reversible hydration of carbon dioxide. Required for photosynthesis in cotyledons. Binds salicylic acid. Together with BCA4, involved in the CO2 signaling pathway which controls gas-exchange between plants and the atmosphere by modulating stomatal development and movements. Promotes water use efficiency.4 Publications

Catalytic activityi

H2CO3 = CO2 + H2O.UniRule annotation

GO - Molecular functioni

  • carbonate dehydratase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • carbon utilization Source: InterPro
  • defense response to bacterium Source: TAIR
  • defense response to fungus, incompatible interaction Source: TAIR
  • negative regulation of stomatal complex development Source: TAIR
  • photosynthesis Source: UniProtKB
  • regulation of stomatal movement Source: TAIR
  • response to carbon dioxide Source: TAIR
  • response to cold Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Zinc

Enzyme and pathway databases

BioCyciARA:AT3G01500-MONOMER.
ARA:GQT-476-MONOMER.
ARA:GQT-483-MONOMER.
MetaCyc:AT3G01500-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta carbonic anhydrase 1, chloroplastic1 Publication (EC:4.2.1.1UniRule annotation)
Short name:
AtbCA1
Short name:
AtbetaCA1
Alternative name(s):
Beta carbonate dehydratase 1
Protein SALICYLIC ACID-BINDING PROTEIN 3
Short name:
AtSABP3
Gene namesi
Name:BCA11 Publication
Synonyms:CA11 Publication, SABP3
Ordered Locus Names:At3g01500Imported
ORF Names:F4P13.5Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G01500.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: UniProtKB
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • chloroplast thylakoid membrane Source: TAIR
  • membrane Source: TAIR
  • plasma membrane Source: UniProtKB
  • stromule Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Chloroplast, Membrane, Plastid

Pathology & Biotechi

Disruption phenotypei

Reduced levels of seedling establishment associated with altered cotyledon photosynthetic performance at the onset of phototrophic growth and prior to the development of true leaves. These phenotypes are reversed in high CO2 or sucrose supplemented conditions. Decreased resistance against avirulent bacteria. In plants lacking both BCA1 and BCA4, impaired CO(2)-regulation of stomatal movements associated with reduced beta carbonic anhydrase activity in guard cells, and increased stomatal density.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi280 – 2801C → S: Loss of nitrosylation and decreased carbonic anhydrase activity, but no effect on salicylic acid binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 113113ChloroplastCombined sourcesCuratedAdd
BLAST
Chaini114 – 347234Beta carbonic anhydrase 1, chloroplasticPRO_0000004267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141N-acetylalanineCombined sources
Modified residuei175 – 1751PhosphoserineBy similarity
Modified residuei203 – 2031PhosphotyrosineCombined sources
Modified residuei266 – 2661PhosphoserineCombined sources
Modified residuei280 – 2801S-nitrosocysteine1 Publication

Post-translational modificationi

S-nitrosylation at Cys-280 is up-regulated during nitrosative burst and suppresses both binding of salicylic acid and carbonic anhydrase activity. S-nitrosylated in response to an avirulent but not to a virulent bacterial strain.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP27140.
PRIDEiP27140.

2D gel databases

SWISS-2DPAGEP27140.

Expressioni

Tissue specificityi

Strongly expressed in aerial tissues including leaves, stems, flowers and siliques. Accumulates in both guard cells and mesophyll cells.2 Publications

Inductioni

Expression reduced by 70% under dark conditions.

Gene expression databases

ExpressionAtlasiP27140. baseline and differential.
GenevisibleiP27140. AT.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi6467. 15 interactions.
IntActiP27140. 2 interactions.
STRINGi3702.AT3G01500.2.

Structurei

3D structure databases

ProteinModelPortaliP27140.
SMRiP27140. Positions 100-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 5012Poly-SerAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1578. Eukaryota.
COG0288. LUCA.
HOGENOMiHOG000125183.
InParanoidiP27140.
KOiK01673.
OMAiCLPAKAK.
PhylomeDBiP27140.

Family and domain databases

Gene3Di3.40.1050.10. 1 hit.
InterProiIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERiPTHR11002. PTHR11002. 1 hit.
PfamiPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTiSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMiSSF53056. SSF53056. 1 hit.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P27140-1) [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
MSTAPLSGFF LTSLSPSQSS LQKLSLRTSS TVACLPPASS SSSSSSSSSS
60 70 80 90 100
RSVPTLIRNE PVFAAPAPII APYWSEEMGT EAYDEAIEAL KKLLIEKEEL
110 120 130 140 150
KTVAAAKVEQ ITAALQTGTS SDKKAFDPVE TIKQGFIKFK KEKYETNPAL
160 170 180 190 200
YGELAKGQSP KYMVFACSDS RVCPSHVLDF QPGDAFVVRN IANMVPPFDK
210 220 230 240 250
VKYGGVGAAI EYAVLHLKVE NIVVIGHSAC GGIKGLMSFP LDGNNSTDFI
260 270 280 290 300
EDWVKICLPA KSKVISELGD SAFEDQCGRC EREAVNVSLA NLLTYPFVRE
310 320 330 340
GLVKGTLALK GGYYDFVKGA FELWGLEFGL SETSSVKDVA TILHWKL
Length:347
Mass (Da):37,450
Last modified:November 21, 2003 - v2
Checksum:i9061FF3EF64CAFD7
GO
Isoform 2 (identifier: P27140-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     337-347: Missing.

Show »
Length:336
Mass (Da):36,144
Checksum:iF1DAEA0AF21D96B0
GO
Isoform 3 (identifier: P27140-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.

Note: No experimental confirmation available.
Show »
Length:270
Mass (Da):29,504
Checksum:i4A5DED1347C40124
GO

Sequence cautioni

The sequence BAD94771.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7777Missing in isoform 3. 1 PublicationVSP_009003Add
BLAST
Alternative sequencei337 – 34711Missing in isoform 2. 4 PublicationsVSP_009004Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65541 mRNA. Translation: CAA46508.1.
AC009325 Genomic DNA. Translation: AAF01535.1.
CP002686 Genomic DNA. Translation: AEE73675.1.
CP002686 Genomic DNA. Translation: AEE73676.1.
CP002686 Genomic DNA. Translation: AEE73677.1.
AF428284 mRNA. Translation: AAL16116.1.
AF428459 mRNA. Translation: AAL16228.1.
AY056175 mRNA. Translation: AAL07024.1.
AY062785 mRNA. Translation: AAL32863.1.
AY081658 mRNA. Translation: AAM10220.1.
AY091066 mRNA. Translation: AAM13886.1.
AK226447 mRNA. Translation: BAE98589.1.
AK222039 mRNA. Translation: BAD94771.1. Different initiation.
PIRiS28412.
RefSeqiNP_186799.2. NM_111016.3. [P27140-1]
NP_850490.1. NM_180159.2. [P27140-3]
NP_850491.1. NM_180160.3. [P27140-2]
UniGeneiAt.21999.

Genome annotation databases

EnsemblPlantsiAT3G01500.2; AT3G01500.2; AT3G01500. [P27140-1]
GeneIDi821134.
KEGGiath:AT3G01500.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65541 mRNA. Translation: CAA46508.1.
AC009325 Genomic DNA. Translation: AAF01535.1.
CP002686 Genomic DNA. Translation: AEE73675.1.
CP002686 Genomic DNA. Translation: AEE73676.1.
CP002686 Genomic DNA. Translation: AEE73677.1.
AF428284 mRNA. Translation: AAL16116.1.
AF428459 mRNA. Translation: AAL16228.1.
AY056175 mRNA. Translation: AAL07024.1.
AY062785 mRNA. Translation: AAL32863.1.
AY081658 mRNA. Translation: AAM10220.1.
AY091066 mRNA. Translation: AAM13886.1.
AK226447 mRNA. Translation: BAE98589.1.
AK222039 mRNA. Translation: BAD94771.1. Different initiation.
PIRiS28412.
RefSeqiNP_186799.2. NM_111016.3. [P27140-1]
NP_850490.1. NM_180159.2. [P27140-3]
NP_850491.1. NM_180160.3. [P27140-2]
UniGeneiAt.21999.

3D structure databases

ProteinModelPortaliP27140.
SMRiP27140. Positions 100-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi6467. 15 interactions.
IntActiP27140. 2 interactions.
STRINGi3702.AT3G01500.2.

2D gel databases

SWISS-2DPAGEP27140.

Proteomic databases

PaxDbiP27140.
PRIDEiP27140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G01500.2; AT3G01500.2; AT3G01500. [P27140-1]
GeneIDi821134.
KEGGiath:AT3G01500.

Organism-specific databases

TAIRiAT3G01500.

Phylogenomic databases

eggNOGiKOG1578. Eukaryota.
COG0288. LUCA.
HOGENOMiHOG000125183.
InParanoidiP27140.
KOiK01673.
OMAiCLPAKAK.
PhylomeDBiP27140.

Enzyme and pathway databases

BioCyciARA:AT3G01500-MONOMER.
ARA:GQT-476-MONOMER.
ARA:GQT-483-MONOMER.
MetaCyc:AT3G01500-MONOMER.

Miscellaneous databases

PROiP27140.

Gene expression databases

ExpressionAtlasiP27140. baseline and differential.
GenevisibleiP27140. AT.

Family and domain databases

Gene3Di3.40.1050.10. 1 hit.
InterProiIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERiPTHR11002. PTHR11002. 1 hit.
PfamiPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTiSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMiSSF53056. SSF53056. 1 hit.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis thaliana carbonic anhydrase: cDNA sequence and effect of CO2 on mRNA levels."
    Raines C., Horsnell P.R., Holder C., Lloyd J.C.
    Plant Mol. Biol. 20:1143-1148(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: cv. C24.
    Tissue: Leaf.
  2. "Characterization and expression of two cDNAs encoding carbonic anhydrase in Arabidopsis thaliana."
    Fett J.P., Coleman J.R.
    Plant Physiol. 105:707-713(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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] (ISOFORMS 1; 2 AND 3).
    Strain: cv. Columbia.
  6. "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] (ISOFORM 2).
    Strain: cv. Columbia.
  7. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: cv. Wassilewskija.
  8. "Characterization and expression analysis of genes encoding alpha and beta carbonic anhydrases in Arabidopsis."
    Fabre N., Reiter I.M., Becuwe-Linka N., Genty B., Rumeau D.
    Plant Cell Environ. 30:617-629(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  9. "Reduction of plastid-localized carbonic anhydrase activity results in reduced Arabidopsis seedling survivorship."
    Ferreira F.J., Guo C., Coleman J.R.
    Plant Physiol. 147:585-594(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. Cited for: FUNCTION, S-NITROSYLATION AT CYS-280, 3D-STRUCTURE MODELING, MUTAGENESIS OF CYS-280, SALICYLIC ACID-BINDING, DISRUPTION PHENOTYPE.
  11. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Carbonic anhydrases are upstream regulators of CO2-controlled stomatal movements in guard cells."
    Hu H., Boisson-Dernier A., Israelsson-Nordstrom M., Bohmer M., Xue S., Ries A., Godoski J., Kuhn J.M., Schroeder J.I.
    Nat. Cell Biol. 12:87-93(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  13. "Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry."
    Aryal U.K., Krochko J.E., Ross A.R.
    J. Proteome Res. 11:425-437(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203 AND SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-114, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Carbonic anhydrases, EPF2 and a novel protease mediate CO2 control of stomatal development."
    Engineer C.B., Ghassemian M., Anderson J.C., Peck S.C., Hu H., Schroeder J.I.
    Nature 513:246-250(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiBCA1_ARATH
AccessioniPrimary (citable) accession number: P27140
Secondary accession number(s): Q0WWA9
, Q56WK1, Q8RWW2, Q93VR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 21, 2003
Last modified: January 20, 2016
This is version 135 of the entry and version 2 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.