DR111_ARATH
ID DR111_ARATH Reviewed; 387 AA.
AC P42698; Q9S9Q1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=DNA-damage-repair/toleration protein DRT111, chloroplastic {ECO:0000303|PubMed:8479917};
DE AltName: Full=REQUIRED FOR SNC4-1D protein 2 {ECO:0000303|PubMed:25267732};
DE Flags: Precursor;
GN Name=DRT111 {ECO:0000312|EMBL:AAA73382.1};
GN Synonyms=RSN2 {ECO:0000303|PubMed:25267732};
GN OrderedLocusNames=At1g30480 {ECO:0000312|Araport:AT1G30480};
GN ORFNames=F26G16.10 {ECO:0000312|EMBL:AAF19751.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8479917; DOI=10.1093/nar/21.7.1647;
RA Pang Q., Hays J.B., Rajagopal I.;
RT "Two cDNAs from the plant Arabidopsis thaliana that partially restore
RT recombination proficiency and DNA-damage resistance to E. coli mutants
RT lacking recombination-intermediate-resolution activities.";
RL Nucleic Acids Res. 21:1647-1653(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION.
RX PubMed=25267732; DOI=10.1093/mp/ssu103;
RA Zhang Z., Liu Y., Ding P., Li Y., Kong Q., Zhang Y.;
RT "Splicing of receptor-like kinase-encoding SNC4 and CERK1 is regulated by
RT two conserved splicing factors that are required for plant immunity.";
RL Mol. Plant 7:1766-1775(2014).
CC -!- FUNCTION: Seems to be involved in the resistance to UV light and
CC chemical DNA-damaging agents (PubMed:8479917). Regulates the splicing
CC of the receptor-like kinase SNC4/LRKL-2.6 (PubMed:25267732).
CC {ECO:0000269|PubMed:25267732, ECO:0000269|PubMed:8479917}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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DR EMBL; M98455; AAA73382.1; -; mRNA.
DR EMBL; AC009917; AAF19751.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31231.1; -; Genomic_DNA.
DR EMBL; AY045859; AAK76533.1; -; mRNA.
DR EMBL; AY091399; AAM14338.1; -; mRNA.
DR PIR; G86429; G86429.
DR PIR; S33706; S33706.
DR RefSeq; NP_174336.1; NM_102784.3.
DR AlphaFoldDB; P42698; -.
DR SMR; P42698; -.
DR BioGRID; 25162; 6.
DR IntAct; P42698; 1.
DR STRING; 3702.AT1G30480.1; -.
DR iPTMnet; P42698; -.
DR PaxDb; P42698; -.
DR PRIDE; P42698; -.
DR ProteomicsDB; 241256; -.
DR EnsemblPlants; AT1G30480.1; AT1G30480.1; AT1G30480.
DR GeneID; 839927; -.
DR Gramene; AT1G30480.1; AT1G30480.1; AT1G30480.
DR KEGG; ath:AT1G30480; -.
DR Araport; AT1G30480; -.
DR TAIR; locus:2028130; AT1G30480.
DR eggNOG; KOG1996; Eukaryota.
DR HOGENOM; CLU_044888_1_0_1; -.
DR InParanoid; P42698; -.
DR OMA; EERFGNN; -.
DR OrthoDB; 1101846at2759; -.
DR PhylomeDB; P42698; -.
DR PRO; PR:P42698; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42698; baseline and differential.
DR Genevisible; P42698; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR CDD; cd12647; RRM_UHM_SPF45; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR040052; RBM17.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR034653; SPF45_RRM.
DR PANTHER; PTHR13288; PTHR13288; 1.
DR Pfam; PF01585; G-patch; 1.
DR PIRSF; PIRSF031066; Splicing_factor_SPF45; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Chloroplast; DNA damage; DNA repair; mRNA processing; mRNA splicing;
KW Plastid; Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..387
FT /note="DNA-damage-repair/toleration protein DRT111,
FT chloroplastic"
FT /id="PRO_0000031017"
FT DOMAIN 214..260
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 283..369
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 28
FT /note="S -> R (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..70
FT /note="Missing (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..138
FT /note="EDE -> VYP (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="K -> M (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..151
FT /note="KE -> R (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..163
FT /note="DNSDPSRLN -> EITVILSVD (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..190
FT /note="AWKRRAAMSGGGSGGKGRSSSP -> RGRDPARVVVEVLGREDPRLL (in
FT Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..204
FT /note="ET -> KP (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> P (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="A -> P (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="T -> P (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="G -> A (in Ref. 1; AAA73382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42318 MW; 94FFFCA8ABA03C5E CRC64;
MLGGLYGDLP PPTDDEKPSG NSSSVWSSST KMAPPTLRKP PAFAPPQTIL RPLNKPKPIV
SAPYKPPPPS NSSQSVLIPA NESAPSHQPA LVGVTSSVIE EYDPARPNDY EEYKREKKRK
ATEAEMKREM DKRRQEDEER DKREREEREK ERERDNSDPS RLNISGEEAW KRRAAMSGGG
SGGKGRSSSP PGNVDGFSIG KSETSGLGVG AGGQMTAAQR MMAKMGWKQG QGLGKSEQGI
TTPLMAKKTD RRAGVIVNAS ENKSSSAEKK VVKSVNINGE PTRVLLLRNM VGPGQVDDEL
EDEVGGECGK YGTVTRVLIF EITEPNFPVH EAVRIFVQFS RPEETTKALV DLDGRYFGGR
TVRATFYDEE KFSKNELAPV PGEIPGY
