ID   YRA2_YEASZ              Reviewed;         203 AA.
AC   E7QH16;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=RNA annealing protein YRA2;
GN   Name=YRA2; ORFNames=VL3_2771;
OS   Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zymaflore VL3;
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that characterize
RT   the genome of industrial strains of Saccharomyces cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
CC   -!- FUNCTION: Involved in export of poly(A) mRNAs from the nucleus.
CC       Recruited to the coding sequences as well as poly-A sites of active
CC       genes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Associates with mRNPs. Interacts with YRA1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the YRA1 family. {ECO:0000305}.
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DR   EMBL; AEJS01000044; EGA86054.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7QH16; -.
DR   SMR; E7QH16; -.
DR   EnsemblFungi; EGA86054; EGA86054; VL3_2771.
DR   HOGENOM; CLU_111217_0_0_1; -.
DR   GO; GO:0005634; C:nucleus; 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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   CDD; cd12295; RRM_YRA2; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR025715; FoP_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034396; Yra2_RRM.
DR   Pfam; PF13865; FoP_duplication; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Acetylation; DNA-binding; mRNA transport; Nucleus; RNA-binding; Transport.
FT   CHAIN           1..203
FT                   /note="RNA annealing protein YRA2"
FT                   /id="PRO_0000409550"
FT   DOMAIN          64..138
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P36036"
SQ   SEQUENCE   203 AA;  23797 MW;  0151E6D6205D496E CRC64;
     MDKAFDEIIG NSHTDSSSNH KVTRYRRRDL RNELGPRLGF APSDAASRSK DRLYREREEP
     PLPKRIRISK IPLDVSDYTL DDMIKEFGSP IFSKIFDNKE DRTCIYEFED PEVLEKIVER
     YNGHELHNAK IEVEIYQPQR KHSRMNAHNR RKQTAQEQGR GRPGSHYRQR PNRVSKKNKG
     REKNNTPTSV EALDAELDAY MKG