ID   RDM1_CHICK              Reviewed;         277 AA.
AC   Q8JFQ4; Q2L4W7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=RAD52 motif-containing protein 1;
GN   Name=RDM1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, RNA-BINDING, AND DNA-BINDING.
RC   TISSUE=Bursa of Fabricius;
RX   PubMed=15611051; DOI=10.1074/jbc.m412874200;
RA   Hamimes S., Arakawa H., Stasiak A.Z., Kierzek A.M., Hirano S., Yang Y.-G.,
RA   Takata M., Stasiak A., Buerstedde J.M., Van Dyck E.;
RT   "RDM1, a novel RNA recognition motif (RRM)-containing protein involved in
RT   the cell response to cisplatin in vertebrates.";
RL   J. Biol. Chem. 280:9225-9235(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=16916790; DOI=10.1093/nar/gkl469;
RA   Shimada N., Matsudo H., Osano K., Arakawa H., Buerstedde J.-M.,
RA   Matsumoto Y., Chayahara K., Torihata A., Ono M.;
RT   "Activation of the chicken Ig-beta locus by the collaboration of scattered
RT   regulatory regions through changes in chromatin structure.";
RL   Nucleic Acids Res. 34:3794-3802(2006).
RN   [3]
RP   FUNCTION, SUBUNIT, MUTAGENESIS OF 119-LEU--PHE-121, RNA-BINDING, AND
RP   DNA-BINDING.
RX   PubMed=16630539; DOI=10.1016/j.bbrc.2006.03.154;
RA   Hamimes S., Bourgeon D., Stasiak A.Z., Stasiak A., Van Dyck E.;
RT   "Nucleic acid-binding properties of the RRM-containing protein RDM1.";
RL   Biochem. Biophys. Res. Commun. 344:87-94(2006).
CC   -!- FUNCTION: Confers resistance to the antitumor agent cisplatin. Binds
CC       preferentially to sites of DNA modified by cisplatin in vitro. Binds to
CC       double-stranded DNA in a cooperative manner resulting in the formation
CC       of filament-like structures. Binds to single-stranded DNA with no
CC       cooperativity. Binds to RNA. {ECO:0000269|PubMed:15611051,
CC       ECO:0000269|PubMed:16630539}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16630539}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, nucleolus
CC       {ECO:0000250}.
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DR   EMBL; AB080727; BAC02561.1; -; mRNA.
DR   EMBL; AB248100; BAE78658.1; -; Genomic_DNA.
DR   RefSeq; NP_989877.2; NM_204546.2.
DR   AlphaFoldDB; Q8JFQ4; -.
DR   SMR; Q8JFQ4; -.
DR   STRING; 9031.ENSGALP00000000321; -.
DR   PaxDb; Q8JFQ4; -.
DR   GeneID; 395228; -.
DR   KEGG; gga:395228; -.
DR   CTD; 201299; -.
DR   VEuPathDB; HostDB:geneid_395228; -.
DR   eggNOG; ENOG502RXM9; Eukaryota.
DR   InParanoid; Q8JFQ4; -.
DR   OrthoDB; 1475838at2759; -.
DR   PhylomeDB; Q8JFQ4; -.
DR   PRO; PR:Q8JFQ4; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProt.
DR   CDD; cd12364; RRM_RDM1; 1.
DR   Gene3D; 3.30.390.80; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR041247; Rad52_fam.
DR   InterPro; IPR042525; Rad52_Rad59_Rad22_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR040224; RDM1.
DR   InterPro; IPR034200; RDM1_RRM.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR31164; PTHR31164; 1.
DR   Pfam; PF04098; Rad52_Rad22; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..277
FT                   /note="RAD52 motif-containing protein 1"
FT                   /id="PRO_0000299531"
FT   DOMAIN          15..95
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   MUTAGEN         119..121
FT                   /note="LGF->AAA: Inhibits partially single-stranded DNA-
FT                   binding activity but not homodimerization."
FT                   /evidence="ECO:0000269|PubMed:16630539"
FT   CONFLICT        29
FT                   /note="E -> K (in Ref. 2; BAE78658)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="P -> A (in Ref. 2; BAE78658)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="G -> V (in Ref. 2; BAE78658)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   277 AA;  30268 MW;  7DFA47F596CBF4E2 CRC64;
     MAEVLEFRVP AGSAQTLLVW GLEPTVGLEH SLFSVFSKFG LLYSVRVHSN AAVAGPGCYA
     IIKFYSAADA SRAQHACNGQ RLFQNSPLKV CVCTKQKGFQ QQVLALNSNK CQELANHYLG
     FNGWSSRIIT LQNVSGFDDE NEEVGKKRSV RYLCAVEVTL PNHGVRTRGV GLGEADVESG
     EDPLEFGTAT RRVQKLAVGK ALSSAFQKIL LVVLESGKVA VEYNHAAEEP TDSLTEEELE
     GLVQVSELPL EPFDLEEEVL SDLTLDDELP VWEVPSN