YRA2_YEAS2
ID YRA2_YEAS2 Reviewed; 203 AA.
AC C7GIZ9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=RNA annealing protein YRA2;
GN Name=YRA2; ORFNames=C1Q_00145;
OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=574961;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAY291;
RX PubMed=19812109; DOI=10.1101/gr.091777.109;
RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA Pereira G.A.G.;
RT "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT bioethanol production.";
RL Genome Res. 19:2258-2270(2009).
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; ACFL01000006; EEU09186.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GIZ9; -.
DR SMR; C7GIZ9; -.
DR Proteomes; UP000008073; 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_0000409543"
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 137..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 COMPBIAS 150..164
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; 23778 MW; 89B7A4B210438652 CRC64;
MDKAFDEIIG NSHTDSSSNH KVTRYRRRDL RNELGPRLGF APSDAASRSK DRLYREREEP
PLPKRIRISK IPLDVSDYTL DDMIKEFGSP IFSKIFDNKE DRTCIYEFED PEVLEKIVER
YNGHELHNAK IEVEIYQPQR KHSRMNAHNR RKQTAQEHGR GRPGSHYRQK PNRVSKKNKG
REKNNTPTSV EALDAELDAY MKG