Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell division protein FtsZ homolog 1, chloroplastic

Gene

FTSZ1

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

Functioni

Exhibits GTPase activity. Component of the plastid division machinery that forms a contractile ring at the division site. Required for plastid division in a dose-dependent manner. Involved in blue light-induced chloroplast movements. May regulate thylakoid development.9 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei201 – 2011GTPBy similarity
Binding sitei205 – 2051GTPBy similarity
Binding sitei249 – 2491GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi83 – 875GTPBy similarity
Nucleotide bindingi170 – 1723GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein self-association Source: UniProtKB

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • chloroplast fission Source: TAIR
  • chloroplast organization Source: UniProtKB
  • chloroplast relocation Source: UniProtKB
  • microtubule-based process Source: InterPro
  • plastid fission Source: TAIR
  • response to blue light Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZ homolog 1, chloroplastic
Short name:
AtFtsZ1
Short name:
AtFtsZ1-1
Short name:
Chloroplast FtsZ
Short name:
CpFtsZ
Alternative name(s):
Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 10
Protein PLASTID MOVEMENT IMPAIRED4
Gene namesi
Name:FTSZ1
Synonyms:ARC10, FTSZ1-1, PMI4
Ordered Locus Names:At5g55280
ORF Names:MCO15.23
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G55280.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: UniProtKB
  • chloroplast thylakoid membrane Source: UniProtKB-SubCell
  • microtubule Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Highly heterogeneous chloroplast population with giant chloroplasts and some smaller. Impaired chloroplast division, some green cells with one single big chloroplast. Abnormal thylakoids.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi159 – 1591D → N: Forms long filaments with impaired midplastidial localization, heterogeneous chloroplast population, one greatly enlarged with numerous smaller chloroplasts per cell. 1 Publication
Mutagenesisi267 – 2671G → R in pmi4; reduced accumulation with impaired midplastidial localization in rings and filaments, giant chloroplasts, and altered chloroplast movements in response to blue light. 2 Publications
Mutagenesisi275 – 2751D → A: Impaired GTPase activity. 1 Publication
Mutagenesisi298 – 2981R → Q: Reduced accumulation, heterogeneous chloroplast population. 1 Publication
Mutagenesisi366 – 3661G → A in arc10; forms long filaments, heterogeneous chloroplast population, one greatly enlarged with numerous smaller chloroplasts per cell. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6666ChloroplastCombined sourcesAdd
BLAST
Chaini67 – 433367Cell division protein FtsZ homolog 1, chloroplasticPRO_0000010306Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ42545.
PRIDEiQ42545.

Expressioni

Tissue specificityi

In pollen grain, restricted to plastids of vegetative cells. Also present in pollen tubes plastids.1 Publication

Gene expression databases

GenevisibleiQ42545. AT.

Interactioni

Subunit structurei

Aggregates to form a contractile ring-like structure. This aggregation is regulated in midchloroplast stroma by MIND1 (repressor) and MINE1 (promoter). Self-interacts and binds to FTSZ2-1 in heteropolymers to form two morphologically distinct types of filaments, termed type-I (smooth filaments) and type-II (rough filaments), in a GTP-dependent manner. Interacts with ARC3. Part of a complex made of ARC3, ARC6, FTSZ1 and FTSZ2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-2131124,EBI-2131124
ARC6Q9FIG92EBI-2131124,EBI-2000800
FTSZ2-2Q9LXJ06EBI-2131124,EBI-2430270

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi20865. 5 interactions.
IntActiQ42545. 5 interactions.
MINTiMINT-4507116.
STRINGi3702.AT5G55280.1.

Structurei

3D structure databases

ProteinModelPortaliQ42545.
SMRiQ42545. Positions 91-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IEJ4. Eukaryota.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiQ42545.
KOiK03531.
OMAiGMAMMGI.
PhylomeDBiQ42545.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ.
InterProiIPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PfamiPF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR00423. CELLDVISFTSZ.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsiTIGR00065. ftsZ. 1 hit.
PROSITEiPS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q42545-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIIPLAQLN ELTISSSSSS FLTKSISSHS LHSSCICASS RISQFRGGFS
60 70 80 90 100
KRRSDSTRSK SMRLRCSFSP MESARIKVIG VGGGGNNAVN RMISSGLQSV
110 120 130 140 150
DFYAINTDSQ ALLQSSAENP LQIGELLTRG LGTGGNPLLG EQAAEESKDA
160 170 180 190 200
IANALKGSDL VFITAGMGGG TGSGAAPVVA QISKDAGYLT VGVVTYPFSF
210 220 230 240 250
EGRKRSLQAL EAIEKLQKNV DTLIVIPNDR LLDIADEQTP LQDAFLLADD
260 270 280 290 300
VLRQGVQGIS DIITIPGLVN VDFADVKAVM KDSGTAMLGV GVSSSKNRAE
310 320 330 340 350
EAAEQATLAP LIGSSIQSAT GVVYNITGGK DITLQEVNRV SQVVTSLADP
360 370 380 390 400
SANIIFGAVV DDRYTGEIHV TIIATGFSQS FQKTLLTDPR AAKLLDKMGS
410 420 430
SGQQENKGMS LPHQKQSPST ISTKSSSPRR LFF
Length:433
Mass (Da):45,565
Last modified:July 11, 2002 - v2
Checksum:i82C942D597171EDB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151S → F in AAA82068 (PubMed:7637778).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39877 mRNA. Translation: AAA82068.1.
AB010071 Genomic DNA. Translation: BAB08597.1.
CP002688 Genomic DNA. Translation: AED96609.1.
AY034992 mRNA. Translation: AAK59497.1.
AY113896 mRNA. Translation: AAM44944.1.
RefSeqiNP_200339.1. NM_124910.5.
UniGeneiAt.1538.

Genome annotation databases

EnsemblPlantsiAT5G55280.1; AT5G55280.1; AT5G55280.
GeneIDi835621.
GrameneiAT5G55280.1; AT5G55280.1; AT5G55280.
KEGGiath:AT5G55280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39877 mRNA. Translation: AAA82068.1.
AB010071 Genomic DNA. Translation: BAB08597.1.
CP002688 Genomic DNA. Translation: AED96609.1.
AY034992 mRNA. Translation: AAK59497.1.
AY113896 mRNA. Translation: AAM44944.1.
RefSeqiNP_200339.1. NM_124910.5.
UniGeneiAt.1538.

3D structure databases

ProteinModelPortaliQ42545.
SMRiQ42545. Positions 91-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20865. 5 interactions.
IntActiQ42545. 5 interactions.
MINTiMINT-4507116.
STRINGi3702.AT5G55280.1.

Proteomic databases

PaxDbiQ42545.
PRIDEiQ42545.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G55280.1; AT5G55280.1; AT5G55280.
GeneIDi835621.
GrameneiAT5G55280.1; AT5G55280.1; AT5G55280.
KEGGiath:AT5G55280.

Organism-specific databases

TAIRiAT5G55280.

Phylogenomic databases

eggNOGiENOG410IEJ4. Eukaryota.
COG0206. LUCA.
HOGENOMiHOG000049094.
InParanoidiQ42545.
KOiK03531.
OMAiGMAMMGI.
PhylomeDBiQ42545.

Miscellaneous databases

PROiQ42545.

Gene expression databases

GenevisibleiQ42545. AT.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ.
InterProiIPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PfamiPF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR00423. CELLDVISFTSZ.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsiTIGR00065. ftsZ. 1 hit.
PROSITEiPS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Conserved cell and organelle division."
    Osteryoung K.W., Vierling E.
    Nature 376:473-474(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
    Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:41-54(1998) [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. "Chloroplast division in higher plants requires members of two functionally divergent gene families with homology to bacterial ftsZ."
    Osteryoung K.W., Stokes K.D., Rutherford S.M., Percival A.L., Lee W.Y.
    Plant Cell 10:1991-2004(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: cv. Columbia.
  6. "Plastid division and development."
    Pyke K.A.
    Plant Cell 11:549-556(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-366.
  7. "Chloroplast division and morphology are differentially affected by overexpression of FtsZ1 and FtsZ2 genes in Arabidopsis."
    Stokes K.D., McAndrew R.S., Figueroa R., Vitha S., Osteryoung K.W.
    Plant Physiol. 124:1668-1677(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "FtsZ ring formation at the chloroplast division site in plants."
    Vitha S., McAndrew R.S., Osteryoung K.W.
    J. Cell Biol. 153:111-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  9. "Colocalization of plastid division proteins in the chloroplast stromal compartment establishes a new functional relationship between FtsZ1 and FtsZ2 in higher plants."
    McAndrew R.S., Froehlich J.E., Vitha S., Stokes K.D., Osteryoung K.W.
    Plant Physiol. 127:1656-1666(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
    Strain: cv. Columbia.
  10. "Plastid division is mediated by combinatorial assembly of plastid division proteins."
    Maple J., Aldridge C., Moeller S.G.
    Plant J. 43:811-823(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSZ2-1, SELF-INTERACTION.
  11. "A plant-specific protein essential for blue-light-induced chloroplast movements."
    DeBlasio S.L., Luesse D.L., Hangarter R.P.
    Plant Physiol. 139:101-114(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-267.
  12. "ARC3 is a stromal Z-ring accessory protein essential for plastid division."
    Maple J., Vojta L., Soll J., Moeller S.G.
    EMBO Rep. 8:293-299(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARC3.
  13. "Effects of mutations in Arabidopsis FtsZ1 on plastid division, FtsZ ring formation and positioning, and FtsZ filament morphology in vivo."
    Yoder D.W., Kadirjan-Kalbach D., Olson B.J.S.C., Miyagishima S.-Y., Deblasio S.L., Hangarter R.P., Osteryoung K.W.
    Plant Cell Physiol. 48:775-791(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-159; GLY-267; ARG-298 AND GLY-366, SUBCELLULAR LOCATION.
    Strain: cv. Columbia and cv. Wassilewskija-2.
  14. "Developmentally regulated association of plastid division protein FtsZ1 with thylakoid membranes in Arabidopsis thaliana."
    El-Kafafi E.-S., Karamoko M., Pignot-Paintrand I., Grunwald D., Mandaron P., Lerbs-Mache S., Falconet D.
    Biochem. J. 409:87-94(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
    Strain: cv. Wassilewskija.
  15. "In vivo quantitative relationship between plastid division proteins FtsZ1 and FtsZ2 and identification of ARC6 and ARC3 in a native FtsZ complex."
    McAndrew R.S., Olson B.J., Kadirjan-Kalbach D.K., Chi-Ham C.L., Vitha S., Froehlich J.E., Osteryoung K.W.
    Biochem. J. 412:367-378(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  16. "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
    Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
    PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  17. "The assembly of the FtsZ ring at the mid-chloroplast division site depends on a balance between the activities of AtMinE1 and ARC11/AtMinD1."
    Fujiwara M.T., Hashimoto H., Kazama Y., Abe T., Yoshida S., Sato N., Itoh R.D.
    Plant Cell Physiol. 49:345-361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  18. "Live imaging of chloroplast FtsZ1 filaments, rings, spirals, and motile dot structures in the AtMinE1 mutant and overexpressor of Arabidopsis thaliana."
    Fujiwara M.T., Sekine K., Yamamoto Y.Y., Abe T., Sato N., Itoh R.D.
    Plant Cell Physiol. 50:1116-1126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  19. "Plant FtsZ1 and FtsZ2 expressed in a eukaryotic host: GTPase activity and self-assembly."
    Smith A.G., Johnson C.B., Vitha S., Holzenburg A.
    FEBS Lett. 584:166-172(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  20. "GTP-dependent heteropolymer formation and bundling of chloroplast FtsZ1 and FtsZ2."
    Olson B.J.S.C., Wang Q., Osteryoung K.W.
    J. Biol. Chem. 285:20634-20643(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS GTPASE, SUBUNIT, MUTAGENESIS OF ASP-275.
  21. "AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins."
    Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N.
    Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  22. "Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering."
    Olinares P.D., Ponnala L., van Wijk K.J.
    Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  23. "Dynamic morphologies of pollen plastids visualised by vegetative-specific FtsZ1-GFP in Arabidopsis thaliana."
    Fujiwara M.T., Hashimoto H., Kazama Y., Hirano T., Yoshioka Y., Aoki S., Sato N., Itoh R.D., Abe T.
    Protoplasma 242:19-33(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT.
    Strain: cv. Columbia and cv. Landsberg erecta.
  24. "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 SER-67, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER CYS-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFTSZ1_ARATH
AccessioniPrimary (citable) accession number: Q42545
Secondary accession number(s): Q9FLN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2002
Last modified: February 17, 2016
This is version 127 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.