ID   YRA2_YEAS1              Reviewed;         203 AA.
AC   B3LQP5;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=RNA annealing protein YRA2;
GN   Name=YRA2; ORFNames=SCRG_03817;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408051; EDV12898.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LQP5; -.
DR   SMR; B3LQP5; -.
DR   EnsemblFungi; EDV12898; EDV12898; SCRG_03817.
DR   HOGENOM; CLU_111217_0_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
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_0000409542"
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