GenomeNet

Database: UniProt
Entry: W9ILQ1_FUSOX
LinkDB: W9ILQ1_FUSOX
Original site: W9ILQ1_FUSOX 
ID   W9ILQ1_FUSOX            Unreviewed;       684 AA.
AC   W9ILQ1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=RNA-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOYG_04779 {ECO:0000313|EMBL:EWY95868.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY95868.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY95868.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC       (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
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DR   EMBL; JH717841; EWY95868.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9ILQ1; -.
DR   HOGENOM; CLU_017928_1_0_1; -.
DR   OrthoDB; 5406435at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   CDD; cd12257; RRM1_RBM26_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 1.20.1390.10; PWI domain; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR002483; PWI_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR045137; RBM26/27.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR   PANTHER; PTHR14398:SF0; ZINC FINGER PROTEIN SWM; 1.
DR   Pfam; PF01480; PWI; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT   DOMAIN          205..233
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          304..376
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   ZN_FING         205..233
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          87..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..533
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..677
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  76728 MW;  83C80E398B02037E CRC64;
     MLFSEEDAPL LKAWIVKRIE DTSDADADVL AEYVIALLKH DGDADAVRKL CEQEIPDFLS
     EDPKAFLDDV FQAIAYRSYL PGAPPAPKIG VEPVQQPLAD STTPNSSRKR GFYDREEYDP
     QDGYESFNRD GRVQKQPRRG GRGGRGDDMR GGRPGAPTYN LPPRPDMPFD PKVMEAFLQM
     GSMGMPYPGM PNFPQQGFGG GRGQPRRRGR CRDFDTKGFC SRGSTCPYDH GNESIFVPPG
     TDAEYDPSDP FAMLANAPNS MNPWTFPPDG GRGGRGGRRN RGAKKGGSRA PFSAEGPNYD
     RTKSTIVVEN IPEESFSEEQ VREFFSQFGN IQEVSMQPYK HLAIVKYDKW GSANAAYQSP
     KVIFDNRFVK VFWYKDKIDT LPASAPLQAG NWSGDPMAAE DDEVLPEIDM EEFQRKQEEE
     QKKHQEREAQ RAKIEQERQE VVKKHQELLA RHREENEKLQ AKLASQRGED GDANSSGTSM
     LRAKLAALEQ EAKMLGLDPD AGEESNSSWA PRGGYRGRGS FRARGRGRRS FRGRGGGNMH
     AAYAQYSIDN RPKKLAITGV DFTAPDKDEM LRHFLLNLGE FESVDTAPET THVSFQDRKT
     AEKFYYSLNG KELPGIEGRL ELAWVNTPLP PVKTLGNDDA PRHGVEDDAM ADFDDQPRRE
     KSAEPQREER AVNMDYEVAE EDAW
//
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