ID S3DH12_GLAL2 Unreviewed; 719 AA.
AC S3DH12;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=RNA-binding, RBD {ECO:0000313|EMBL:EPE31296.1};
GN ORFNames=GLAREA_12599 {ECO:0000313|EMBL:EPE31296.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE31296.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE31296.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
CC -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
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DR EMBL; KE145362; EPE31296.1; -; Genomic_DNA.
DR RefSeq; XP_008081571.1; XM_008083380.1.
DR AlphaFoldDB; S3DH12; -.
DR STRING; 1116229.S3DH12; -.
DR GeneID; 19471639; -.
DR KEGG; glz:GLAREA_12599; -.
DR eggNOG; KOG2135; Eukaryota.
DR HOGENOM; CLU_017928_1_0_1; -.
DR OMA; ITYDSHA; -.
DR OrthoDB; 5406435at2759; -.
DR Proteomes; UP000016922; 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 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 InterPro; IPR036855; Znf_CCCH_sf.
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; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 225..253
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 332..404
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 225..253
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 125..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..531
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 296..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 79076 MW; F0D9F1BC96D5E293 CRC64;
MLFPEEDSEH LKQWLVTRLG QTSDADADVL ADYVLALLSN DGDTETVRNL CMAEIPDFVQ
DNPTQFISDL FDAIHYKSYL PGAPAPPQRQ TSMPFAPPTG PSSMPPFGVH YGGQNGNRKR
AFNERGDGDV QDRGMGMENG RVYKQPRRGM PGRGGYGDFN GRGGFNGRPP HGNGPSIEQS
LLPAIDPNNP PDPMALMMAI QNMGQSMGFP ITAPLPGQGP PAQKAPRRGR CRDYEQKGFC
ARGNTCMYEH GENSIWVPPG QTPDEYDPSN ATLMTGVEGN GMGSPGAFNN YRGNDRGRGR
GARGDRGHGN AGRRGGRAEF SSDRPNFDRA KTTIVVENIP EESFSEEAVR EFFSQFGEIV
DVSMRPYKRL SIVKYDSWDA AQAAYGSPKV IFDNRFVKVY WYTTPDALPQ PPASATSANG
APKRETNSQG PVPARDTDEP MIDPEEFARK QEEAQKVHDE KAKKKLEMEA ARKELEKRQE
ELNRVRAEET RKLKEKLEAK AKLNGDAGAP TDAKTSQTEA LKAQLAKLEA EAASLGLPGL
DQPLPDEGYG YRGRGGRGRG YRGRGTFAPR GFRGGRGRGG APFVGGGAYK LDNRPKKIAV
SGVDFTEMGS DEALRSHLLG IGDFTSLDPT PSTTTITFKD RFTAEKFMNS AHDEIPGVGK
VEMKWVTEPL PTPVKREEGE VDMKDVGAER VREREIKREE REREENLDYE VAGDEDYIG
//
