ID A0A165ED80_9APHY Unreviewed; 810 AA.
AC A0A165ED80;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LAESUDRAFT_725544 {ECO:0000313|EMBL:KZT06782.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT06782.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT06782.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT06782.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
CC -!- SUBUNIT: Associated with the spliceosome.
CC {ECO:0000256|ARBA:ARBA00011524}.
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DR EMBL; KV427622; KZT06782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ED80; -.
DR STRING; 1314785.A0A165ED80; -.
DR InParanoid; A0A165ED80; -.
DR OrthoDB; 5406435at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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; PF00642; zf-CCCH; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000076871};
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 191..214
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 376..448
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 191..214
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 114..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 86544 MW; 8B8CDBABE1B3A4A9 CRC64;
MLFDPETSSD LKTWLVKNLE PICDAEPGAL AEYILALLKH NAPESELRKE LSGQLEEFLE
KENTPFLDTL FTALRTKSYM PYSAASPTGY PSSNGEDNGI PIPLDALLTS SISTSPSRGL
KRSLDHEDHD SHAPAKGPRT NDGHFSRYGR NDRRSSWGDR GDRGARMGGA GRGDYMDGGM
GRGPSGHGRG ICRDYYNHGY CARGAFCKYS HGDDAVVPSQ LFPMAGPMGV GPLPFVPMLP
GAMPFGISGG SNAAYDPRER MDMRPVQGAG LDVGDRPINA RAPMVPRERG AGSPTAPNLG
ELPAMQDLTG DMGGASGGDM NGSSGMMAMQ GIEMTGAPAL PNGHGRGGYR GGRGGGGRGV
FGGEVQNFRP DRHTDKTLVV EKIPQDKLSL GAVNEWFKRF GNVTNVAVDA ANGKALVSFS
SHAEAHTAWR SKDAVFDNRF VKVYWHKPME GHGQLGARML AASAPLMANI AARETAPTTI
SPESSTTQPA PSTPTPIRKS STPSAAAALA AKQRLLEQQI AEQKSLMAKL GTASSQEKKE
IMARLRKLGE EMKPLATPSP ATPPASAATA KSRGITPSAD EKERLERERL DKELELHHAV
SAAEGEMEEN TEELKATLAK LKAEAASLGI TDVSDGAYSS GTTYRPYRAR GRGRGMRGGY
RGFMRGGPPR GSMKLDLRPK TLLVKNVGAG AEQAVREWYE TMGQVESVDT TDDGDVLVAF
RSRAAAEQGL AKGTNIPSIG QVRISWHNNQ QTGAAAQKTS LQLPEGSSPV EDRMVTEDRP
PSPAETDEAQ YQEESAPAWA GDDADGFRML
//
