RO60_DEIRA
ID RO60_DEIRA Reviewed; 531 AA.
AC Q9RUW8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=RNA-binding protein RO60 {ECO:0000250|UniProtKB:P10155};
DE AltName: Full=60 kDa SS-A/Ro ribonucleoprotein homolog {ECO:0000305};
DE AltName: Full=Ro sixty-related protein {ECO:0000303|PubMed:17392270};
GN Name=rsr {ECO:0000303|PubMed:17392270}; OrderedLocusNames=DR_1262;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP CHARACTERIZATION, AND FUNCTION.
RX PubMed=10766734;
RA Chen X., Quinn A.-M., Wolin S.L.;
RT "Ro ribonucleoproteins contribute to the resistance of Deinococcus
RT radiodurans to ultraviolet irradiation.";
RL Genes Dev. 14:777-782(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
RP METAL-BINDING SITES, SUBUNIT, FUNCTION, RNA-BINDING, AND DOMAIN.
RX PubMed=17392270; DOI=10.1074/jbc.m611163200;
RA Ramesh A., Savva C.G., Holzenburg A., Sacchettini J.C.;
RT "Crystal structure of Rsr, an ortholog of the antigenic Ro protein, links
RT conformational flexibility to RNA binding activity.";
RL J. Biol. Chem. 282:14960-14967(2007).
CC -!- FUNCTION: Binds to several small RNAs that accumulate during recovery
CC from UV irradiation (PubMed:17392270). Contributes to the resistance of
CC D.radiodurans to ultraviolet irradiation (PubMed:10766734).
CC {ECO:0000269|PubMed:10766734, ECO:0000269|PubMed:17392270}.
CC -!- SUBUNIT: Forms oligomers upon binding DrY RNA, The multimers are of an
CC average size of 700 kDa and are composed of around 12 molecules of Rsr-
CC DrY RNA. {ECO:0000269|PubMed:17392270}.
CC -!- INTERACTION:
CC Q9RUW8; Q9RSR1: pnp; NbExp=2; IntAct=EBI-15836588, EBI-15836673;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10155}.
CC -!- DOMAIN: The horseshoe-shaped TROVE domain is built with 7 helical HEAT-
CC like repeats, and is closed by the VWFA-like domain giving rise to a
CC ring-shaped monomer. Single-stranded RNA is bound in the positively
CC charged central cavity. {ECO:0000269|PubMed:17392270}.
CC -!- DOMAIN: The MIDAS-like motif in the VWFA-like domain binds divalent
CC metal cations. {ECO:0000269|PubMed:17392270}.
CC -!- SIMILARITY: Belongs to the Ro 60 kDa family. {ECO:0000305}.
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DR EMBL; AE000513; AAF10833.1; -; Genomic_DNA.
DR PIR; C75418; C75418.
DR RefSeq; NP_294986.1; NC_001263.1.
DR RefSeq; WP_010887905.1; NZ_CP015081.1.
DR PDB; 2NVO; X-ray; 1.89 A; A=1-531.
DR PDBsum; 2NVO; -.
DR AlphaFoldDB; Q9RUW8; -.
DR SMR; Q9RUW8; -.
DR DIP; DIP-58600N; -.
DR IntAct; Q9RUW8; 3.
DR STRING; 243230.DR_1262; -.
DR EnsemblBacteria; AAF10833; AAF10833; DR_1262.
DR KEGG; dra:DR_1262; -.
DR PATRIC; fig|243230.17.peg.1457; -.
DR eggNOG; COG2304; Bacteria.
DR HOGENOM; CLU_024421_1_0_0; -.
DR InParanoid; Q9RUW8; -.
DR OMA; WWYEWLK; -.
DR OrthoDB; 912523at2; -.
DR EvolutionaryTrace; Q9RUW8; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR040322; TROVE2.
DR InterPro; IPR008858; TROVE_dom.
DR InterPro; IPR037214; TROVE_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR14202; PTHR14202; 1.
DR Pfam; PF05731; TROVE; 2.
DR SUPFAM; SSF140864; SSF140864; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50988; TROVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Reference proteome;
KW Ribonucleoprotein; RNA-binding.
FT CHAIN 1..531
FT /note="RNA-binding protein RO60"
FT /id="PRO_0000174173"
FT DOMAIN 24..360
FT /note="TROVE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00343"
FT REGION 128..274
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT REGION 352..531
FT /note="VWFA-like domain"
FT /evidence="ECO:0000305"
FT BINDING 369
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:17392270"
FT BINDING 371
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:17392270"
FT BINDING 438
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:2NVO"
FT STRAND 48..59
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:2NVO"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:2NVO"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 338..351
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2NVO"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:2NVO"
FT STRAND 400..414
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:2NVO"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:2NVO"
FT STRAND 455..463
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 472..483
FT /evidence="ECO:0007829|PDB:2NVO"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:2NVO"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:2NVO"
FT HELIX 519..527
FT /evidence="ECO:0007829|PDB:2NVO"
SQ SEQUENCE 531 AA; 57423 MW; D842B351E7CE7B8A CRC64;
MKNLLRAINP LNRPQTERLD ERQVRNNAGG FVYTVSDESR LTRFLVLGVD GGTFYASAQK
HTVQATDFVR ELVQRDAALA LRVTLDVVRG QRAPKADPAL LVLALIAKTA PNAADRKAAW
DALPEVARTG TMLLHFLAFA DALGGWGRLT RRGVANVYET ADVDKLALWA VKYKARDGWS
QADALRKAHP KTDDAARNAV LKFMVDGVLP KVDSPALRVI EGHLKATEAQ TDAAAAALMQ
EYRLPLEAVP THVRGAEVYR AAMQTNGLTW LLRNLGNLGR VGVLTPNDSA TVQAVIERLT
DPAALKRGRI HPLDALKARL VYAQGQGVRG KGTWLPVPRV VDALEEAFTL AFGNVQPANT
RHLLALDVSG SMTCGDVAGV PGLTPNMAAA AMSLIALRTE PDALTMGFAE QFRPLGITPR
DTLESAMQKA QSMSFGGTDC AQPILWAAQE RLDVDTFVVY TDNETWAGQV HPTVALDQYA
QKMGRAPKLI VVGLTATEFS IADPQRRDML DVVGFDAAAP NVMTAFARGE V
