ID D5G8U5_TUBMM Unreviewed; 336 AA.
AC D5G8U5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Pre-mRNA-splicing factor CWC24 {ECO:0000256|RuleBase:RU367110};
GN ORFNames=GSTUM_00004845001 {ECO:0000313|EMBL:CAZ80938.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ80938.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ80938.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ80938.1};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- FUNCTION: Involved in pre-mRNA splicing.
CC {ECO:0000256|RuleBase:RU367110}.
CC -!- SUBUNIT: Associated with the spliceosome.
CC {ECO:0000256|RuleBase:RU367110}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367110}.
CC -!- SIMILARITY: Belongs to the CWC24 family.
CC {ECO:0000256|ARBA:ARBA00009161, ECO:0000256|RuleBase:RU367110}.
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DR EMBL; FN430053; CAZ80938.1; -; Genomic_DNA.
DR RefSeq; XP_002836747.1; XM_002836701.1.
DR AlphaFoldDB; D5G8U5; -.
DR STRING; 656061.D5G8U5; -.
DR EnsemblFungi; CAZ80938; CAZ80938; GSTUM_00004845001.
DR GeneID; 9186447; -.
DR KEGG; tml:GSTUM_00004845001; -.
DR eggNOG; KOG1813; Eukaryota.
DR HOGENOM; CLU_050460_0_0_1; -.
DR InParanoid; D5G8U5; -.
DR OMA; ANFRKKP; -.
DR OrthoDB; 21858at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd16539; RING-HC_RNF113A_B; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039971; CWC24-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12930; ZINC FINGER PROTEIN 183; 1.
DR PANTHER; PTHR12930:SF0; ZINC FINGER PROTEIN 183; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|RuleBase:RU367110};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; mRNA processing {ECO:0000256|RuleBase:RU367110};
KW mRNA splicing {ECO:0000256|RuleBase:RU367110};
KW Nucleus {ECO:0000256|RuleBase:RU367110};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Spliceosome {ECO:0000256|RuleBase:RU367110};
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 183..211
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 257..294
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 183..211
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..336
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 37537 MW; 6A3FC0F5FAF239E6 CRC64;
MTEPVPQSDT PATTVPAPTV TFFKRSTKNR SSIRKRPATP PPTTTSDSSD AYSSSDEKAT
GTRCVKKRRK NKSVVTTKTT SKPSSATLGN SEDVKRRYTD VSSELTNAND ATKTNWHNHG
DNETSSLSSK KNTAEGEGEP IVGGAYKGTS SYTSFIKKSE NAPARSVGPM KAPSNIRTIT
ITDYAPDVCK DYKQTGFCGF GDTCKFLHAR EDYAQGWKLD RDWEIDQKTG KAKNKKGDDS
KGEDEEEREL KDIPFKCVIC KDDYKSPIVT KCKHYFCETC AIARYKKTPN CEICGKRTDG
AFSMAKELRK KLERKVVREE ERRKKEEAEA MMMESN
//
