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RFA3A_ARATH
ID   RFA3A_ARATH             Reviewed;         107 AA.
AC   Q9LXK1;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Replication protein A 14 kDa subunit A;
DE            Short=AtRPA14A;
DE   AltName: Full=Replication factor A protein 3A;
DE   AltName: Full=Replication protein A 3A;
GN   Name=RPA3A; Synonyms=RAFA3A, RPA14A; OrderedLocusNames=At3g52630;
GN   ORFNames=F3C22.30;
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=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).
CC   -!- FUNCTION: As part of the replication protein A (RPA/RP-A), a single-
CC       stranded DNA-binding heterotrimeric complex, may play an essential role
CC       in DNA replication, recombination and repair. Binds and stabilizes
CC       single-stranded DNA intermediates, preventing complementary DNA
CC       reannealing and recruiting different proteins involved in DNA
CC       metabolism (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC       A complex (RPA). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AL353912; CAB89224.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78971.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78972.1; -; Genomic_DNA.
DR   PIR; T49016; T49016.
DR   RefSeq; NP_001078273.1; NM_001084804.2.
DR   RefSeq; NP_190831.1; NM_115123.2.
DR   AlphaFoldDB; Q9LXK1; -.
DR   SMR; Q9LXK1; -.
DR   BioGRID; 9747; 1.
DR   IntAct; Q9LXK1; 1.
DR   STRING; 3702.AT3G52630.2; -.
DR   PaxDb; Q9LXK1; -.
DR   PRIDE; Q9LXK1; -.
DR   ProteomicsDB; 236995; -.
DR   EnsemblPlants; AT3G52630.1; AT3G52630.1; AT3G52630.
DR   EnsemblPlants; AT3G52630.2; AT3G52630.2; AT3G52630.
DR   GeneID; 824429; -.
DR   Gramene; AT3G52630.1; AT3G52630.1; AT3G52630.
DR   Gramene; AT3G52630.2; AT3G52630.2; AT3G52630.
DR   KEGG; ath:AT3G52630; -.
DR   Araport; AT3G52630; -.
DR   TAIR; locus:2083198; AT3G52630.
DR   eggNOG; ENOG502S57Y; Eukaryota.
DR   HOGENOM; CLU_141922_3_0_1; -.
DR   InParanoid; Q9LXK1; -.
DR   OMA; GYNGAAH; -.
DR   OrthoDB; 1594928at2759; -.
DR   PhylomeDB; Q9LXK1; -.
DR   PRO; PR:Q9LXK1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LXK1; baseline and differential.
DR   GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013970; Rfa2.
DR   Pfam; PF08661; Rep_fac-A_3; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
KW   Acetylation; DNA damage; DNA recombination; DNA repair; DNA replication;
KW   DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..107
FT                   /note="Replication protein A 14 kDa subunit A"
FT                   /id="PRO_0000422626"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NLG7"
SQ   SEQUENCE   107 AA;  11653 MW;  50AE1ED8C79DD78A CRC64;
     MDTSSPSAFV NGALLRRFIG QKVRTVIQVT GSEIGSVVGK STDDLQIVVR GSSPPSPLTT
     YLEVIGIAES DNAIRAETWT NFGNTFDTQN YNELCKLANG EFKHLFI
 
 
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