ID F8PWL2_SERL3 Unreviewed; 341 AA.
AC F8PWL2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Pre-mRNA-splicing factor CWC24 {ECO:0000256|RuleBase:RU367110};
GN ORFNames=SERLA73DRAFT_180881 {ECO:0000313|EMBL:EGO00336.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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; GL945479; EGO00336.1; -; Genomic_DNA.
DR AlphaFoldDB; F8PWL2; -.
DR STRING; 936435.F8PWL2; -.
DR eggNOG; KOG1813; Eukaryota.
DR HOGENOM; CLU_050460_1_1_1; -.
DR InParanoid; F8PWL2; -.
DR OMA; RCGHYYC; -.
DR OrthoDB; 21858at2759; -.
DR Proteomes; UP000008063; 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 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:UP000008063};
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 172..200
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 236..273
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 172..200
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..341
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 37286 MW; F3DC5841FFA72E5A CRC64;
MASTGEVIVP FFKKGKSRPT TSRLRATSPP PAPLNVPVSS SSKSEVVLPS RKANGNLLSA
GTKRTSSQRH EIDDQDVPER EGPDIKWTAS GSHVNAALDI LAGDEAAELL AKRQRKEKAE
KGDEDEDIPD DGLYRGQKAY RSHIKKNQEV PKAMRVGPQR STNTIRTVTI VDYQPDVCKD
YKETGYCGFG DTCKFLHDRG TYLAGWQLDN LAANPKKNVE DVSDSDSDDE DIPFACLICR
KHYTEPIVTR CGHYFCSACA IKRFAKTPKC LACGAPTGGI FNRADKVMDK INKKRKEKEE
EEGEDAGNAG ADVKIEGLIE QGSDAEGDSD ESDDSANGDQ D
//
