ID D5GI91_TUBMM Unreviewed; 540 AA.
AC D5GI91;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Splicing factor U2AF subunit {ECO:0000256|RuleBase:RU364135};
DE AltName: Full=U2 snRNP auxiliary factor large subunit {ECO:0000256|RuleBase:RU364135};
GN ORFNames=GSTUM_00008345001 {ECO:0000313|EMBL:CAZ84234.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ84234.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ84234.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ84234.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA.
CC {ECO:0000256|RuleBase:RU364135}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364135}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family.
CC {ECO:0000256|RuleBase:RU364135}.
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DR EMBL; FN430324; CAZ84234.1; -; Genomic_DNA.
DR RefSeq; XP_002840043.1; XM_002839997.1.
DR AlphaFoldDB; D5GI91; -.
DR STRING; 656061.D5GI91; -.
DR EnsemblFungi; CAZ84234; CAZ84234; GSTUM_00008345001.
DR GeneID; 9181952; -.
DR KEGG; tml:GSTUM_00008345001; -.
DR eggNOG; KOG0120; Eukaryota.
DR HOGENOM; CLU_021795_2_0_1; -.
DR InParanoid; D5GI91; -.
DR OMA; MTQWDIK; -.
DR OrthoDB; 101932at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0000243; C:commitment complex; IEA:EnsemblFungi.
DR GO; GO:0071004; C:U2-type prespliceosome; IEA:EnsemblFungi.
DR GO; GO:0089701; C:U2AF complex; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:EnsemblFungi.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:EnsemblFungi.
DR CDD; cd12231; RRM2_U2AF65; 1.
DR CDD; cd12232; RRM3_U2AF65; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR006529; U2AF_lg.
DR NCBIfam; TIGR01642; U2AF_lg; 1.
DR PANTHER; PTHR23139; RNA-BINDING PROTEIN; 1.
DR PANTHER; PTHR23139:SF9; SPLICING FACTOR U2AF 65 KDA SUBUNIT; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50102; RRM; 3.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU364135};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU364135};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364135};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 224..306
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 333..411
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 441..532
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60647 MW; F1D81E3E611FF595 CRC64;
MNGDSYSSRG GDRHGYGRDY HGTDHRRERD RDRNDRDRGD RDRERAGRRD RSRSPHRGRS
HRDDYFETDR ADRYRERDRD TDRYAGRDRD YERERRRGGG GDRRGERNPR YDEPRGGRST
AAADAYPVRK RSATPPVKKR EPTPDLTDVT PINERRRRMT MWDIKPQGYE NVTAEQAKLS
GMFPLPGAPR QAPMDPTRLH AFMTQPSNVA TASTLKPTNS RQAKRLLMSN IPPGTDEESL
LQFFNQTLSS LNVTTGGPDP ITSVQLSGSK ILGLLEFKNT NDATVCLALS GIEFNGGNIE
IKRPRDYIVP IVPEDHRHQE PGVISSDVPD TPNKILISEI PEYLQDEQVI ELLKSFGDLK
AFVLVKDVTD ETSKGIAFCE YLDPGTTEIA VEGLNAMEIA DNTLRVRRAS IGMKQAAGVE
MGVNAMAMMA GTTSVDLEAS RVLQLLNMVT ADELLDPEEY DEICEDIRDE CQKFGSLVDM
KVPRPSGGSR QAAGVGKIFV RFETQESASN ALRSLAGRKF ADRTVVCTYF SEENYEVGAF
//
