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AATPC_ARATH
ID   AATPC_ARATH             Reviewed;         451 AA.
AC   Q147F9; Q8GZ01; Q9SVK5;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=AAA-ATPase At3g50940;
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:Q9FLD5};
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g50940 {ECO:0000312|EMBL:AEE78729.1};
GN   ORFNames=F18B3.220 {ECO:0000312|EMBL:CAB42923.1};
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 {ECO:0000312|EMBL:ABG48490.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INDUCTION BY SALT.
RC   STRAIN=cv. Columbia;
RX   PubMed=16510518; DOI=10.1093/jxb/erj098;
RA   Ma S., Gong Q., Bohnert H.J.;
RT   "Dissecting salt stress pathways.";
RL   J. Exp. Bot. 57:1097-1107(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC   -!- INDUCTION: Induced in roots by salt stress.
CC       {ECO:0000269|PubMed:16510518}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB42923.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL049862; CAB42923.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE78729.1; -; Genomic_DNA.
DR   EMBL; AK117288; BAC41960.2; -; mRNA.
DR   EMBL; BT026134; ABG48490.1; -; mRNA.
DR   PIR; T08415; T08415.
DR   RefSeq; NP_190663.2; NM_114954.4.
DR   AlphaFoldDB; Q147F9; -.
DR   SMR; Q147F9; -.
DR   IntAct; Q147F9; 1.
DR   STRING; 3702.AT3G50940.1; -.
DR   PaxDb; Q147F9; -.
DR   PRIDE; Q147F9; -.
DR   ProteomicsDB; 245125; -.
DR   EnsemblPlants; AT3G50940.1; AT3G50940.1; AT3G50940.
DR   GeneID; 824258; -.
DR   Gramene; AT3G50940.1; AT3G50940.1; AT3G50940.
DR   KEGG; ath:AT3G50940; -.
DR   Araport; AT3G50940; -.
DR   TAIR; locus:2078007; AT3G50940.
DR   eggNOG; KOG0743; Eukaryota.
DR   HOGENOM; CLU_010189_0_1_1; -.
DR   InParanoid; Q147F9; -.
DR   OMA; ANEQHIN; -.
DR   OrthoDB; 532729at2759; -.
DR   PhylomeDB; Q147F9; -.
DR   PRO; PR:Q147F9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q147F9; baseline and differential.
DR   Genevisible; Q147F9; AT.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR025753; AAA_N_dom.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF14363; AAA_assoc; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Magnesium; Nucleotide-binding; Reference proteome;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..451
FT                   /note="AAA-ATPase At3g50940"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434714"
FT   BINDING         254..261
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        417
FT                   /note="A -> S (in Ref. 3; BAC41960)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   451 AA;  51470 MW;  4AA9712D3B12B04B CRC64;
     MSSSSESHLA TAKTALTAVA SVAAAAILAR SVVQDYMPNE VHEYISHGFR RFFSYFSYQM
     TAVIEEFGGF EHNQVFEAAE AYLSTKISNS TRRIKVNKLE KQSNYSVTVE RDEEVVDIFD
     GVKLSWILVC RHVDKKDFRN PRDLNSTLKS EVRSYELSFR KKFKNMVLES YLPFVVEQAA
     SIKQKFKTLK IFTVDSYSVE WTSVTLDHPS TFRTLALDPE VKKNLVEDLD RFVQRKGFYG
     RVGKAWKRGY LLYGPPGTGK SSLIAAIANH LNFDIYDLDL TSLNNNAELR RLLMSTANRS
     ILVVEDIDCS IELKDRSTDQ ENNDPLHKTV TLSGLLNFVD GLWSSCGNER IIVFTTNYRE
     KLDPALLRPG RMDMHIHMSY CTPAAFKVLA SNYLEIQDHI LFEQIEEFIR EIEVTPAEVA
     EQLMRSDSVD KVLQGLVEFL KAKKQIDNSK A
 
 
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