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PP354_ARATH
ID   PP354_ARATH             Reviewed;         632 AA.
AC   Q9SZT8;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Pentatricopeptide repeat-containing protein ELI1, chloroplastic {ECO:0000305};
DE   AltName: Full=Protein EDITING LACKING INSERTIONAL MUTANT 1 {ECO:0000303|PubMed:24194514};
DE   Flags: Precursor;
GN   Name=ELI1 {ECO:0000303|PubMed:24194514}; Synonyms=PCMP-H48;
GN   OrderedLocusNames=At4g37380; ORFNames=F6G17.30;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RX   PubMed=10809006; DOI=10.1023/a:1006352315928;
RA   Aubourg S., Boudet N., Kreis M., Lecharny A.;
RT   "In Arabidopsis thaliana, 1% of the genome codes for a novel protein family
RT   unique to plants.";
RL   Plant Mol. Biol. 42:603-613(2000).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=15269332; DOI=10.1105/tpc.104.022236;
RA   Lurin C., Andres C., Aubourg S., Bellaoui M., Bitton F., Bruyere C.,
RA   Caboche M., Debast C., Gualberto J., Hoffmann B., Lecharny A., Le Ret M.,
RA   Martin-Magniette M.-L., Mireau H., Peeters N., Renou J.-P., Szurek B.,
RA   Taconnat L., Small I.;
RT   "Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins
RT   reveals their essential role in organelle biogenesis.";
RL   Plant Cell 16:2089-2103(2004).
RN   [5]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=24194514; DOI=10.1074/jbc.m113.485755;
RA   Hayes M.L., Giang K., Berhane B., Mulligan R.M.;
RT   "Identification of two pentatricopeptide repeat genes required for RNA
RT   editing and zinc binding by C-terminal cytidine deaminase-like domains.";
RL   J. Biol. Chem. 288:36519-36529(2013).
CC   -!- FUNCTION: Plays a major role in single RNA editing events in
CC       chloroplasts. Acts as a site-recognition transacting factor involved in
CC       the edition of the site 5 of ndhB1 and ndhB2 (ndhB1-5 and ndhB2-5 sites
CC       corresponding to cytidine-830), which are plastid-encoded subunits of
CC       the NADH-plastoquinone oxidoreductase. May provide the catalytic
CC       activity for editing site conversion. {ECO:0000269|PubMed:24194514}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:24194514};
CC       Note=Binds 2 zinc ions per subunit. {ECO:0000269|PubMed:24194514};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PPR family. PCMP-H subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC       URL="https://ppr.plantenergy.uwa.edu.au";
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DR   EMBL; AL035601; CAB38205.1; -; Genomic_DNA.
DR   EMBL; AL161591; CAB80403.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86786.1; -; Genomic_DNA.
DR   PIR; T04732; T04732.
DR   RefSeq; NP_195454.1; NM_119901.2.
DR   AlphaFoldDB; Q9SZT8; -.
DR   SMR; Q9SZT8; -.
DR   STRING; 3702.AT4G37380.1; -.
DR   PaxDb; Q9SZT8; -.
DR   PRIDE; Q9SZT8; -.
DR   EnsemblPlants; AT4G37380.1; AT4G37380.1; AT4G37380.
DR   GeneID; 829892; -.
DR   Gramene; AT4G37380.1; AT4G37380.1; AT4G37380.
DR   KEGG; ath:AT4G37380; -.
DR   Araport; AT4G37380; -.
DR   TAIR; locus:2126352; AT4G37380.
DR   eggNOG; KOG4197; Eukaryota.
DR   HOGENOM; CLU_002706_37_2_1; -.
DR   InParanoid; Q9SZT8; -.
DR   OMA; HHPILNF; -.
DR   OrthoDB; 1344243at2759; -.
DR   PhylomeDB; Q9SZT8; -.
DR   BioCyc; ARA:AT4G37830-MON; -.
DR   BioCyc; MetaCyc:AT4G37830-MON; -.
DR   PRO; PR:Q9SZT8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZT8; baseline and differential.
DR   Genevisible; Q9SZT8; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:1900865; P:chloroplast RNA modification; IMP:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 4.
DR   InterPro; IPR032867; DYW_dom.
DR   InterPro; IPR002885; Pentatricopeptide_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF14432; DYW_deaminase; 1.
DR   Pfam; PF01535; PPR; 5.
DR   Pfam; PF13041; PPR_2; 1.
DR   TIGRFAMs; TIGR00756; PPR; 3.
DR   PROSITE; PS51375; PPR; 10.
PE   3: Inferred from homology;
KW   Chloroplast; Metal-binding; mRNA processing; Plastid; Reference proteome;
KW   Repeat; RNA editing; RNA-binding; Transit peptide; Zinc.
FT   TRANSIT         1..19
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..632
FT                   /note="Pentatricopeptide repeat-containing protein ELI1,
FT                   chloroplastic"
FT                   /id="PRO_0000363471"
FT   REPEAT          94..128
FT                   /note="PPR 1"
FT   REPEAT          129..159
FT                   /note="PPR 2"
FT   REPEAT          160..194
FT                   /note="PPR 3"
FT   REPEAT          196..221
FT                   /note="PPR 4"
FT   REPEAT          222..256
FT                   /note="PPR 5"
FT   REPEAT          258..292
FT                   /note="PPR 6"
FT   REPEAT          293..323
FT                   /note="PPR 7"
FT   REPEAT          324..354
FT                   /note="PPR 8"
FT   REPEAT          360..395
FT                   /note="PPR 9"
FT   REPEAT          396..426
FT                   /note="PPR 10"
FT   REGION          431..506
FT                   /note="Type E motif"
FT   REGION          497..512
FT                   /note="Required for function in RNA editing"
FT                   /evidence="ECO:0000269|PubMed:24194514"
FT   REGION          507..537
FT                   /note="Type E(+) motif"
FT   REGION          538..632
FT                   /note="Type DYW motif"
SQ   SEQUENCE   632 AA;  70096 MW;  5EF31B3BD1633AC1 CRC64;
     MASSPLLATS LPQNQLSTTA TARFRLPPPE KLAVLIDKSQ SVDEVLQIHA AILRHNLLLH
     PRYPVLNLKL HRAYASHGKI RHSLALFHQT IDPDLFLFTA AINTASINGL KDQAFLLYVQ
     LLSSEINPNE FTFSSLLKSC STKSGKLIHT HVLKFGLGID PYVATGLVDV YAKGGDVVSA
     QKVFDRMPER SLVSSTAMIT CYAKQGNVEA ARALFDSMCE RDIVSWNVMI DGYAQHGFPN
     DALMLFQKLL AEGKPKPDEI TVVAALSACS QIGALETGRW IHVFVKSSRI RLNVKVCTGL
     IDMYSKCGSL EEAVLVFNDT PRKDIVAWNA MIAGYAMHGY SQDALRLFNE MQGITGLQPT
     DITFIGTLQA CAHAGLVNEG IRIFESMGQE YGIKPKIEHY GCLVSLLGRA GQLKRAYETI
     KNMNMDADSV LWSSVLGSCK LHGDFVLGKE IAEYLIGLNI KNSGIYVLLS NIYASVGDYE
     GVAKVRNLMK EKGIVKEPGI STIEIENKVH EFRAGDREHS KSKEIYTMLR KISERIKSHG
     YVPNTNTVLQ DLEETEKEQS LQVHSERLAI AYGLISTKPG SPLKIFKNLR VCSDCHTVTK
     LISKITGRKI VMRDRNRFHH FTDGSCSCGD FW
 
 
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