ID A0A150V7L2_9PEZI Unreviewed; 680 AA.
AC A0A150V7L2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=PWI domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_133777 {ECO:0000313|EMBL:KYG46526.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG46526.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG46526.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG46526.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG46526.1}.
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DR EMBL; JPDO01000112; KYG46526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V7L2; -.
DR STRING; 766039.A0A150V7L2; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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; IPR036483; PWI_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR18806; RBM25 PROTEIN; 1.
DR PANTHER; PTHR18806:SF4; RNA-BINDING PROTEIN 25; 1.
DR Pfam; PF01480; PWI; 1.
DR SMART; SM00311; PWI; 1.
DR SUPFAM; SSF101233; PWI domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51025; PWI; 1.
DR PROSITE; PS50102; RRM; 1.
PE 4: Predicted;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 73..156
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 588..680
FT /note="PWI"
FT /evidence="ECO:0000259|PROSITE:PS51025"
FT REGION 281..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 76499 MW; D54DE6E148C5F584 CRC64;
MAYQHAPPPG FDFSAPVIRL GAIPGEVSSR PPRAGLGSYA EPIGSVRNLE RDRAAVRESM
MALQPPTREE VARTIFIGGL SEDAIDDEAI ESVLRCAGKL RRWTRAKDAD DIKCKFGFAE
YEDVESLEAA AEIFGGGLEV PMVKNGVVLK SEEGEAKKMK LLVVVDEQSR NYIDEWKSRR
REDDDARQFR IDGCKEDLRQ CLASIENAMA FRANQAAATA VDNDGDTTMM NGLNKDGDIV
TIPISTNIED ELSDIPAEQR ATVAAEIRAF RERSTKRDIE RLRREEEMEQ AERRRMAASP
PRASAASGPN GAPVGPRGQV PAGPKGFRGV QIPSDYADGV TFVNSNREDE DAEESDEELE
RRRRAKKSEE DQRLYQDAER RWLNRERTRA AAQQRERERE EREAAATEKE NSAIAKRLRE
WDDAEEERLG HEEYYYNHSE WLRRRAAYRE REEAEDKRDR IAEEHEKADE RRRAGEAQGQ
AENFLDQMGA EMGNRPRKQP GDVGGGFKIS LGSAAARTRA SAAQPGPKRA FADVEGLLED
EEDAAASGKK RPELKPLTDL STIPTDLSDE EKAAARQSLV SEIPTDPEPL FAWPIRWSYL
TPDITRKEIR PFVEKKVVEY LGVQEDLLVD AVMDGLRDRK DAAEITRDLE AVLEDEAMLL
VKKVWRMVVF WSEAGARGLV
//
