ID   SNU71_ASHGO             Reviewed;         586 AA.
AC   Q750D5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=U1 small nuclear ribonucleoprotein component SNU71;
GN   Name=SNU71; OrderedLocusNames=AGR020C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 492; 500 AND 503-505.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Component of the U1 snRNP particle, which recognizes and
CC       binds the 5'-splice site of pre-mRNA. Together with other non-snRNP
CC       factors, U1 snRNP forms the spliceosomal commitment complex, that
CC       targets pre-mRNA to the splicing pathway (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the U1 snRNP particle, a subcomplex of the
CC       spliceosome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNU71 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016820; AAS54509.2; -; Genomic_DNA.
DR   RefSeq; NP_986685.2; NM_211747.2.
DR   AlphaFoldDB; Q750D5; -.
DR   SMR; Q750D5; -.
DR   STRING; 33169.AAS54509; -.
DR   PRIDE; Q750D5; -.
DR   EnsemblFungi; AAS54509; AAS54509; AGOS_AGR020C.
DR   GeneID; 4622984; -.
DR   KEGG; ago:AGOS_AGR020C; -.
DR   eggNOG; KOG2253; Eukaryota.
DR   HOGENOM; CLU_031562_0_0_1; -.
DR   InParanoid; Q750D5; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005685; C:U1 snRNP; IEA:EnsemblFungi.
DR   GO; GO:0071004; C:U2-type prespliceosome; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:EnsemblFungi.
DR   InterPro; IPR002483; PWI_dom.
DR   SMART; SM00311; PWI; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome.
FT   CHAIN           1..586
FT                   /note="U1 small nuclear ribonucleoprotein component SNU71"
FT                   /id="PRO_0000333454"
FT   REGION          276..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          274..356
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        276..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..327
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..424
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  66570 MW;  21585AF340FA95AE CRC64;
     MGDIVFVSAA LYLANSPNWK SKVLKPGFSP IPSNELYNFE QTLKSTSQEP VSSTAVSKAP
     EKSALDAEDG GLRLDYKGPK YQELRLFLPI SLTQQLHTLV IQNIPESATK TADFIQWLEQ
     ATTKHFSTKT DGTKVEDLVE NWSSVIASTL ESTQDIFIRM YPLTEFAQVV LYWIEWFSKA
     TDSVTTVHID ENTARYIDDI VPSSYTPDVT EEELVALRTQ IADLKSSVSE SSTENAAMVA
     YEVDMSTLSD LPKSSLNQLV KDIIEFRTRV LTMEREKRTQ EALEEGRRRR SQLKRVMEQI
     RKSKGSSVPA TEPEEDEDEY EDEDGEEDWA IERRRLEKEK ESAQQSYNAL LSHLNGTVMP
     DLRARKQRLI LLKDYEAKLQ RERAFFLKEL LHLGNSDYYD HRREFKEEEE QQDDVDRRAQ
     NEQRIQAPKD AVLQASASAS RSPDTSAAHS APVQEPVAKE QKIKLALKRV FDTRAQEAES
     DSEPEADIPA TAVSASTPAP TADLPDRLPF QGPELAARMA ELRQSRLVDE LVNEYLGVYE
     DELVDYILDN IVENASRGQL LLELQETFDD DSVRIVDAIW AKLLKH