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Protein

Pentatricopeptide repeat-containing protein ELI1, chloroplastic

Gene

ELI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Plays a major role in single RNA editing events in chloroplasts. Acts as a site-recognition transacting factor involved in the edition of the site 5 of ndhB1 and ndhB2 (ndhB1-5 and ndhB2-5 sites corresponding to cytidine-830), which are plastid-encoded subunits of the NADH-plastoquinone oxidoreductase. May provide the catalytic activity for editing site conversion.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 zinc ions per subunit.1 Publication

GO - Molecular functioni

  • RNA binding Source: UniProtKB-KW
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • chloroplast RNA modification Source: UniProtKB
  • mRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT4G37830-MONOMER.
ARA:GQT-2007-MONOMER.
MetaCyc:AT4G37830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pentatricopeptide repeat-containing protein ELI1, chloroplasticCurated
Alternative name(s):
Protein EDITING LACKING INSERTIONAL MUTANT 11 Publication
Gene namesi
Name:ELI11 Publication
Synonyms:PCMP-H48
Ordered Locus Names:At4g37380
ORF Names:F6G17.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G37380.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919ChloroplastSequence analysisAdd
BLAST
Chaini20 – 632613Pentatricopeptide repeat-containing protein ELI1, chloroplasticPRO_0000363471Add
BLAST

Proteomic databases

PaxDbiQ9SZT8.
PRIDEiQ9SZT8.

Expressioni

Gene expression databases

GenevisibleiQ9SZT8. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G37380.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SZT8.
SMRiQ9SZT8. Positions 91-502.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati94 – 12835PPR 1Add
BLAST
Repeati129 – 15931PPR 2Add
BLAST
Repeati160 – 19435PPR 3Add
BLAST
Repeati196 – 22126PPR 4Add
BLAST
Repeati222 – 25635PPR 5Add
BLAST
Repeati258 – 29235PPR 6Add
BLAST
Repeati293 – 32331PPR 7Add
BLAST
Repeati324 – 35431PPR 8Add
BLAST
Repeati360 – 39536PPR 9Add
BLAST
Repeati396 – 42631PPR 10Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni431 – 50676Type E motifAdd
BLAST
Regioni497 – 51216Required for function in RNA editing1 PublicationAdd
BLAST
Regioni507 – 53731Type E(+) motifAdd
BLAST
Regioni538 – 63295Type DYW motifAdd
BLAST

Sequence similaritiesi

Belongs to the PPR family. PCMP-H subfamily.Curated
Contains 10 PPR (pentatricopeptide) repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG4197. Eukaryota.
ENOG410Z7Z7. LUCA.
HOGENOMiHOG000237569.
InParanoidiQ9SZT8.
OMAiCWNAMID.
PhylomeDBiQ9SZT8.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR032867. DYW_dom.
IPR002885. Pentatricopeptide_repeat.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF14432. DYW_deaminase. 1 hit.
PF01535. PPR. 5 hits.
PF13041. PPR_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00756. PPR. 3 hits.
PROSITEiPS51375. PPR. 10 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9SZT8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSPLLATS LPQNQLSTTA TARFRLPPPE KLAVLIDKSQ SVDEVLQIHA
60 70 80 90 100
AILRHNLLLH PRYPVLNLKL HRAYASHGKI RHSLALFHQT IDPDLFLFTA
110 120 130 140 150
AINTASINGL KDQAFLLYVQ LLSSEINPNE FTFSSLLKSC STKSGKLIHT
160 170 180 190 200
HVLKFGLGID PYVATGLVDV YAKGGDVVSA QKVFDRMPER SLVSSTAMIT
210 220 230 240 250
CYAKQGNVEA ARALFDSMCE RDIVSWNVMI DGYAQHGFPN DALMLFQKLL
260 270 280 290 300
AEGKPKPDEI TVVAALSACS QIGALETGRW IHVFVKSSRI RLNVKVCTGL
310 320 330 340 350
IDMYSKCGSL EEAVLVFNDT PRKDIVAWNA MIAGYAMHGY SQDALRLFNE
360 370 380 390 400
MQGITGLQPT DITFIGTLQA CAHAGLVNEG IRIFESMGQE YGIKPKIEHY
410 420 430 440 450
GCLVSLLGRA GQLKRAYETI KNMNMDADSV LWSSVLGSCK LHGDFVLGKE
460 470 480 490 500
IAEYLIGLNI KNSGIYVLLS NIYASVGDYE GVAKVRNLMK EKGIVKEPGI
510 520 530 540 550
STIEIENKVH EFRAGDREHS KSKEIYTMLR KISERIKSHG YVPNTNTVLQ
560 570 580 590 600
DLEETEKEQS LQVHSERLAI AYGLISTKPG SPLKIFKNLR VCSDCHTVTK
610 620 630
LISKITGRKI VMRDRNRFHH FTDGSCSCGD FW
Length:632
Mass (Da):70,096
Last modified:May 1, 2000 - v1
Checksum:i5EF31B3BD1633AC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035601 Genomic DNA. Translation: CAB38205.1.
AL161591 Genomic DNA. Translation: CAB80403.1.
CP002687 Genomic DNA. Translation: AEE86786.1.
PIRiT04732.
RefSeqiNP_195454.1. NM_119901.1.
UniGeneiAt.65465.

Genome annotation databases

EnsemblPlantsiAT4G37380.1; AT4G37380.1; AT4G37380.
GeneIDi829892.
GrameneiAT4G37380.1; AT4G37380.1; AT4G37380.
KEGGiath:AT4G37380.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Web resourcesi

Arabidopsis PPR Protein Database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035601 Genomic DNA. Translation: CAB38205.1.
AL161591 Genomic DNA. Translation: CAB80403.1.
CP002687 Genomic DNA. Translation: AEE86786.1.
PIRiT04732.
RefSeqiNP_195454.1. NM_119901.1.
UniGeneiAt.65465.

3D structure databases

ProteinModelPortaliQ9SZT8.
SMRiQ9SZT8. Positions 91-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G37380.1.

Proteomic databases

PaxDbiQ9SZT8.
PRIDEiQ9SZT8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G37380.1; AT4G37380.1; AT4G37380.
GeneIDi829892.
GrameneiAT4G37380.1; AT4G37380.1; AT4G37380.
KEGGiath:AT4G37380.

Organism-specific databases

TAIRiAT4G37380.

Phylogenomic databases

eggNOGiKOG4197. Eukaryota.
ENOG410Z7Z7. LUCA.
HOGENOMiHOG000237569.
InParanoidiQ9SZT8.
OMAiCWNAMID.
PhylomeDBiQ9SZT8.

Enzyme and pathway databases

BioCyciARA:AT4G37830-MONOMER.
ARA:GQT-2007-MONOMER.
MetaCyc:AT4G37830-MONOMER.

Miscellaneous databases

PROiQ9SZT8.

Gene expression databases

GenevisibleiQ9SZT8. AT.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR032867. DYW_dom.
IPR002885. Pentatricopeptide_repeat.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF14432. DYW_deaminase. 1 hit.
PF01535. PPR. 5 hits.
PF13041. PPR_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00756. PPR. 3 hits.
PROSITEiPS51375. PPR. 10 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "In Arabidopsis thaliana, 1% of the genome codes for a novel protein family unique to plants."
    Aubourg S., Boudet N., Kreis M., Lecharny A.
    Plant Mol. Biol. 42:603-613(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  4. "Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis."
    Lurin C., Andres C., Aubourg S., Bellaoui M., Bitton F., Bruyere C., Caboche M., Debast C., Gualberto J., Hoffmann B., Lecharny A., Le Ret M., Martin-Magniette M.-L., Mireau H., Peeters N., Renou J.-P., Szurek B., Taconnat L., Small I.
    Plant Cell 16:2089-2103(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  5. "Identification of two pentatricopeptide repeat genes required for RNA editing and zinc binding by C-terminal cytidine deaminase-like domains."
    Hayes M.L., Giang K., Berhane B., Mulligan R.M.
    J. Biol. Chem. 288:36519-36529(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.

Entry informationi

Entry nameiPP354_ARATH
AccessioniPrimary (citable) accession number: Q9SZT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 93 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.