ID T0L5A9_COLGC Unreviewed; 253 AA.
AC T0L5A9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RRM domain-containing protein {ECO:0000259|PROSITE:PS50102};
GN ORFNames=CGLO_17928 {ECO:0000313|EMBL:EQB43415.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB43415.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB43415.1}.
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DR EMBL; AMYD01004289; EQB43415.1; -; Genomic_DNA.
DR AlphaFoldDB; T0L5A9; -.
DR STRING; 1237896.T0L5A9; -.
DR eggNOG; KOG0533; Eukaryota.
DR HOGENOM; CLU_052367_2_0_1; -.
DR OMA; GIARVWF; -.
DR OrthoDB; 1367875at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR19965:SF96; POLYMERASE DELTA-INTERACTING PROTEIN 3; 1.
DR PANTHER; PTHR19965; RNA AND EXPORT FACTOR BINDING PROTEIN; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM01218; FoP_duplication; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 70..148
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 26612 MW; 9F6D27031D8C2AEA CRC64;
MSGKLDQSLD EILSTQRRSS GGPRRRSQRR STGRPAAAAP VGGVQKTSKP ARAAANKPNA
AKPSQGSGDS KVIVSNLPKD VSEQQIKEYF LTSVGPIKRV EISYGPNSVS RGIANITFRD
ADGASKAFQK LNGLLVDNRP IKIEIVVSAS QAANVIPPSK TLAERTSQPK AQPKSAAINK
RNANANKGPA AGNAQAGKKP RRARSGRPAK KTQEELDSEM ADYFESGNAN NENAAAPAPA
ATNGDAAMEE DIM
//
