ID A0A395MBS3_9HYPO Unreviewed; 692 AA.
AC A0A395MBS3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RFN45270.1};
GN ORFNames=FIE12Z_10487 {ECO:0000313|EMBL:RFN45270.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN45270.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN45270.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN45270.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
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:RFN45270.1}.
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DR EMBL; PXXK01000361; RFN45270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MBS3; -.
DR STRING; 2594813.A0A395MBS3; -.
DR OrthoDB; 5406435at2759; -.
DR Proteomes; UP000265631; 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 Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
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:UP000265631};
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 207..235
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 305..377
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 207..235
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 125..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 77529 MW; BDF940DE3F77C910 CRC64;
MLFPEEHAPL LKAWIVKRIE DTSDADADVL AEYVIALLKH DGDADAVRKL CEQEIPDFLS
EDPKAFLDDV FQAITHKSYL PGAPPAPKIG AEPETINQQS IETAQPNGSK KRGYHDREEY
DPQYGYEAFN QDGRVQKQAR RSGRGGRGDD MRGGQAGGFM HSLPPRPDMP FDPKVMEAFL
QMGAMGMPYS GMPNFPQQSF SGGKSQSRKR GRCRDFDTKG FCSRGSTCPY DHGNEPILMP
QGSDEYDPND PFAMLANAQN PMNPWSFPSD TSRGGRGGRR GRGSKKGGAK APFSADGPNY
DRSKSTIVVE NIPEENFDEE QVREFFSQFG KILEISMQPY KHLAIVKYDK WGSANAAYQS
PKVIFDNRFV KVFWYKNKTD DLPPSAPMQG GIWSDDPMAT EEDELEPEID MEEFQRKQEE
EQKKHQEREA KRAEIEQKRQ EIEKQQHELL ARHREENEKL QARLADLRGE QGEGTSSGTN
MLRAKLAALE QEAKLLGLDP NAEEEASSSW PPRGGYRGRA GYRGRGFAPR GRGSYRGRGG
GGNMHAAYAQ YSIDNRPKKI AIKGVDFTAP DKDEMLRHFL LNLGEFESVE TAPETTHVSF
QDRKTAERFY YSLHGKELPG VEGSLDLAWV STPLPPVKTT SIDDAPGDGG DDKEDDAMAG
FDDQPGRERS AEPQQEDRAV NMDYEVAEED AW
//
