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Database: UniProt
Entry: T0M377_COLGC
LinkDB: T0M377_COLGC
Original site: T0M377_COLGC 
ID   T0M377_COLGC            Unreviewed;       650 AA.
AC   T0M377;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=RRM domain-containing protein {ECO:0000259|PROSITE:PS50102};
GN   ORFNames=CGLO_01815 {ECO:0000313|EMBL:EQB57996.1};
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:EQB57996.1, 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   -!- SIMILARITY: Belongs to the RENT3 family.
CC       {ECO:0000256|ARBA:ARBA00005991}.
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:EQB57996.1}.
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DR   EMBL; AMYD01000380; EQB57996.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0M377; -.
DR   STRING; 1237896.T0M377; -.
DR   eggNOG; KOG1295; Eukaryota.
DR   HOGENOM; CLU_018549_0_0_1; -.
DR   OMA; DWFQYKP; -.
DR   OrthoDB; 77197at2759; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR   CDD; cd12455; RRM_like_Smg4_UPF3; 1.
DR   CDD; cd00590; RRM_SF; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR039722; Upf3.
DR   InterPro; IPR005120; UPF3_dom.
DR   PANTHER; PTHR13112:SF0; FI21285P1; 1.
DR   PANTHER; PTHR13112; UPF3 REGULATOR OF NONSENSE TRANSCRIPTS-LIKE PROTEIN; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF03467; Smg4_UPF3; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT   DOMAIN          486..562
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   650 AA;  67364 MW;  30EBE890B0DDE6B5 CRC64;
     MATSGSQGAS RKTNGVLPVT GQQTAADTPK SNKSRAAVEG HKVVIRRLPP GLTEQELWNK
     LGDVWKAGQG LVSWHNFEAG KISQDAAKPS RPARVYLNVL KREDLNTLSN LIQARSWEDA
     KMTSNSPSLV GPPVLEMASY NKIPSGKKRT DPRQGTIDQD PEFMAFLQDL TNPEQNKETE
     GSESKDAADE SKPDAKVTTT PLIEFLKEKK ANKAKEAAAA KSAKQARQES QNAKGKASAS
     TEDSKKGKKD SKAERSAEKP KETVKILTKK ATADAVKAAE AVASQITQSS SAAQEAPKSR
     RAGIAAAARI LQRDLGISPG SAHRRARLDA AKAEAEAKAA TPKEPAQPAA EVPAAAAPPA
     PPAQSSSNAA QSSERNAAPS APKSGRTRRG GGGKNAAASE GKGKSNDTGG SSNTPAPTKT
     PVVLLKKRDE KKNEEKTERA EKAEKEASSS QPAPAKANPP TGPKGSGKGS NSKKGASSVA
     VTPGATRGFV KHANPSQGVT ENLLKQAMEA FGTVIFVEID KRKGFAYVDF SDHDGLAKAI
     AASPVTVAQG TVQVLERKEK KPAASNAAST NNSGNAASSS NAPAASSSAS SANKEKDANA
     TNNPDKPEEQ RHKRTRRGRG GGKAAANKDA QQQAAAAAAA PAADKAAGAG
//
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