ID A0A024G3G0_9STRA Unreviewed; 1067 AA.
AC A0A024G3G0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=RRM domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN9_018810 {ECO:0000313|EMBL:CCI41097.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI41097.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI41097.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI41097.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCI41097.1}.
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DR EMBL; CAIX01000014; CCI41097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024G3G0; -.
DR STRING; 65357.A0A024G3G0; -.
DR InParanoid; A0A024G3G0; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd03759; proteasome_beta_type_3; 1.
DR CDD; cd12223; RRM_SR140; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 1.10.10.790; Surp module; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR033811; Proteasome_beta_3.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR035009; SR140_RRM.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR PANTHER; PTHR23140; RNA PROCESSING PROTEIN LD23810P; 1.
DR PANTHER; PTHR23140:SF0; U2 SNRNP-ASSOCIATED SURP MOTIF-CONTAINING PROTEIN; 1.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SMART; SM00648; SWAP; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF109905; Surp module (SWAP domain); 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50128; SURP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 356..437
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 489..538
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 759..919
FT /note="CID"
FT /evidence="ECO:0000259|PROSITE:PS51391"
FT REGION 233..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1067
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 119108 MW; 172343777C1D063C CRC64;
MSILSYNGSA IIAMAGKDCV GIACDTRLGL QAQTISTNFQ KVFRVSDKIF LGLAGLATDV
QTVSQLLKFK VNMYKMNEER DLKPETLSSY LSAMMYKKRF GPWFIEPVIA GLTADNQPFL
SSMDCLGCEM KTKDFVVAGT MEEALYGMCE SMYRPDMESE DLFETLSQCL LSACNRDALS
GWGAEREERE AKKIKADEEA AAIYAQFVAS FEHIENDQAP MFVQAKSDVK SGHNDSVQTL
GFSSDTNASN KQRGTKRAFL SAHELQVQSA SSNEASVGSK RASKRSEMDK MLEEMKQNDL
ERQHRKEQYH QQQKQTKRRQ IDDFLQEIKE REPLPPNIEE LGPTKGSFDN GDPCTTNLYV
GNLAPSITEQ LLEEEFGKFG QVYSVKIMWP RTEDERLRRR ICGFVSFFTR EDADEARVAL
NNRELNGQEI VVGWGKAVRI DPNARHLRAI QRANADAVPP ILSTIVPPIS RREQRIIVTI
PSEERLRERV DILARFVARN GACFETQLAL REASNPDFAF LSESMDSTTA ASPLYLYYRW
RVYSFAVGDT SSQWLDEPFR MIADGPIWVP PEIPNLDLDT EANGIILTNI RVVEVAQVRV
GEVIVAVGVG VGAKVGAKVE AEAESGAGAG AGAKVEAEAE AKVEAEAKVE AEAKVEALVV
AKINTAVVKD HQMPGEGVVI ELIRNKVVKV ASKRLVKEDS RVDHHPYLDL VRHHDRHHDR
HQVAANQIVR NTVASHQMMT GQQLAKARDR ERGRDREKLP REQYEEFKVI LGALTLDRAS
IKKAMGFALD HSEYAVDIVQ VLYKSFQQEE APSNADLAGG NTVPADSAVH KVAYFFVASD
ILHNSSAAVK NASLFRTTFQ ELLPSIMDIL RSCHRRIVGR MSANAMKEKV LNVLTAWESW
SLFPPMFLVG LNATFLRKVD EDEPTLCVRD ESVVLNESEE EAIRKRCKQS GILASGSSMQ
MLARLRWLKE YTAPQKCPAS VPQQNASSLD AKSLVDQVKR DLDALRKDAT LEMAIRSKNA
RDTQEDDDDD DLDGEPLDEQ QPIGEHGEGD SDDEDLDGEP LDSDNEE
//
