ID A0A2H3IGQ9_9EURO Unreviewed; 535 AA.
AC A0A2H3IGQ9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Nucleotide-binding, alpha-beta plait {ECO:0000313|EMBL:PCH02746.1};
GN ORFNames=PENO1_036060 {ECO:0000313|EMBL:PCH02746.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH02746.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH02746.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH02746.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCH02746.1}.
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DR EMBL; NPFK01000078; PCH02746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IGQ9; -.
DR STRING; 290292.A0A2H3IGQ9; -.
DR OrthoDB; 3127428at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd12577; RRM1_Hrp1p; 1.
DR CDD; cd12330; RRM2_Hrp1p; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034156; Hrp1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR48031:SF2; RNA-BINDING PROTEIN 4; 1.
DR PANTHER; PTHR48031; SRA STEM-LOOP-INTERACTING RNA-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50102; RRM; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 112..194
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 196..272
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 57890 MW; 5C5AAAD768E97BEE CRC64;
MTEPEELEED LFADLYDGND NNQPTSTGVA DHSAEATTSS AAPQTNDYQN GRGYEPSYEN
SNVHDTYQGQ ETGGIQSYHS MNETSHDVNI HTGDGTQSTD GETQGTGIKE DGKMFIGGLN
WETTDQSLKD YFSQFGEVSE CTVMRDSATG RSRGFGFLTF RDPKTVNTVM VKEHYLDGKI
IDPKRAIPRD EQEKTSKIFV GGVSQEATEQ DFKQFFMQFG RVVDATLMID KDTGRPRGFG
FVTFDSEAAV EATLSRPLEI LGKSIEVKKA QPRGNLRDDG GRRGRDQGMG PDNSQQQGGQ
GPGGMPSGIT PQMMAQYWQR MQQYFAMMQQ QMAAAQGQGM GGMNMAGMNP AMMQQMKQMQ
MAAGQQPGQS PSPGPQGMQN MMNNPAMMQQ MQQMQQMQQM QGQGQGQMGM SGPGYGANRG
GPGYNAHEQL AFEQQKYEQQ QARRGGAYSP YQQGGPTSWE GMYDEVPQPN VPAGPQGRGG
GNMGRGGKPG TPGGSTPPAA PANAPTGPRN AGRPGANYRG GGRGGGHRGF HPYSR
//
