WHY2_SOLTU
ID WHY2_SOLTU Reviewed; 238 AA.
AC D9J034; E0CX05;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Single-stranded DNA-binding protein WHY2, mitochondrial;
DE AltName: Full=Protein WHIRLY 2;
DE Short=StWHY2;
DE Flags: Precursor;
GN Name=WHY2;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18997341; DOI=10.1107/s1744309108032399;
RA Cappadocia L., Sygusch J., Brisson N.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of the Whirly domain of StWhy2 in complex with single-stranded DNA.";
RL Acta Crystallogr. F 64:1056-1059(2008).
RN [2]
RP GENE FAMILY.
RX PubMed=15708347; DOI=10.1016/j.tplants.2004.12.008;
RA Desveaux D., Marechal A., Brisson N.;
RT "Whirly transcription factors: defense gene regulation and beyond.";
RL Trends Plant Sci. 10:95-102(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 48-216 IN COMPLEX WITH
RP SINGLE-STRANDED DNA.
RX PubMed=20551348; DOI=10.1105/tpc.109.071399;
RA Cappadocia L., Marechal A., Parent J.S., Lepage E., Sygusch J., Brisson N.;
RT "Crystal structures of DNA-Whirly complexes and their role in Arabidopsis
RT organelle genome repair.";
RL Plant Cell 22:1849-1867(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 48-216 IN COMPLEX WITH
RP SINGLE-STRANDED DNA, FUNCTION, SUBUNIT, AND MUTAGENESIS OF LYS-67.
RX PubMed=21911368; DOI=10.1093/nar/gkr740;
RA Cappadocia L., Parent J.S., Zampini E., Lepage E., Sygusch J., Brisson N.;
RT "A conserved lysine residue of plant Whirly proteins is necessary for
RT higher order protein assembly and protection against DNA damage.";
RL Nucleic Acids Res. 40:258-269(2012).
CC -!- FUNCTION: Single-stranded DNA-binding protein that may be involved in
CC the maintenance of mitochondrial genome stability by preventing break-
CC induced DNA rearrangements. {ECO:0000269|PubMed:21911368}.
CC -!- SUBUNIT: Homotetramer. Assembles into hexamers of homotetramers upon
CC binding long DNA. {ECO:0000269|PubMed:20551348,
CC ECO:0000269|PubMed:21911368}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Whirly family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HM234504; ADI77438.1; -; mRNA.
DR RefSeq; NP_001275393.1; NM_001288464.1.
DR PDB; 3N1H; X-ray; 2.20 A; A=48-218.
DR PDB; 3N1I; X-ray; 2.20 A; A=48-218.
DR PDB; 3N1J; X-ray; 2.65 A; A=48-218.
DR PDB; 3N1K; X-ray; 2.70 A; A=48-218.
DR PDB; 3N1L; X-ray; 2.35 A; A=48-218.
DR PDB; 3R9Y; X-ray; 2.35 A; A=48-216.
DR PDB; 3R9Z; X-ray; 1.76 A; A=48-216.
DR PDB; 3RA0; X-ray; 2.45 A; A=48-216.
DR PDBsum; 3N1H; -.
DR PDBsum; 3N1I; -.
DR PDBsum; 3N1J; -.
DR PDBsum; 3N1K; -.
DR PDBsum; 3N1L; -.
DR PDBsum; 3R9Y; -.
DR PDBsum; 3R9Z; -.
DR PDBsum; 3RA0; -.
DR AlphaFoldDB; D9J034; -.
DR SMR; D9J034; -.
DR STRING; 4113.PGSC0003DMT400059032; -.
DR EnsemblPlants; RHC11H1G1630.2.1; RHC11H1G1630.2.1; RHC11H1G1630.2.
DR GeneID; 102577630; -.
DR Gramene; RHC11H1G1630.2.1; RHC11H1G1630.2.1; RHC11H1G1630.2.
DR KEGG; sot:102577630; -.
DR eggNOG; ENOG502QRRY; Eukaryota.
DR InParanoid; D9J034; -.
DR OrthoDB; 1637760at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; D9J034; baseline.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.30.31.10; -; 1.
DR InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR InterPro; IPR013742; Whirly.
DR PANTHER; PTHR31745; PTHR31745; 1.
DR Pfam; PF08536; Whirly; 1.
DR SUPFAM; SSF54447; SSF54447; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..238
FT /note="Single-stranded DNA-binding protein WHY2,
FT mitochondrial"
FT /id="PRO_0000420451"
FT REGION 65..70
FT /note="Required for ssDNA binding"
FT /evidence="ECO:0000250"
FT MUTAGEN 67
FT /note="K->A: No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:21911368"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3R9Z"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:3R9Z"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3R9Z"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3R9Z"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:3R9Z"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3R9Z"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3R9Z"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:3R9Z"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3R9Z"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:3N1I"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:3N1I"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:3R9Z"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:3R9Z"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:3R9Z"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:3R9Z"
FT HELIX 189..206
FT /evidence="ECO:0007829|PDB:3R9Z"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3R9Z"
SQ SEQUENCE 238 AA; 26594 MW; CB3AD1B2BEF42572 CRC64;
MLKVSRLLHP RNQLLHKKLP GECVKGSIWQ HAINTFAGFS TVRQNVVADA GKREGRVFAP
YSVFKGKAAL SAEPRLPTFN RLDSGGVKLN RRGVIMLTFW PSVGERKYDW EKRQLFALSA
TEVGSLISMG TRDSSEFFHD PSMLSSNAGQ VRKSLSIKPN ADGSGYFISL SVVNNNLKTN
DRFTVPVTTA EFAVMRTAFS FALPHIMGWD RFTNRPSESI SQSPSKVVPQ LMEAEWDR
