ID A0A0S7DXI1_9EURO Unreviewed; 340 AA.
AC A0A0S7DXI1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Pre-mRNA-splicing factor CWC24 {ECO:0000256|RuleBase:RU367110};
GN ORFNames=ALT_005615 {ECO:0000313|EMBL:GIM41167.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM41167.1};
RN [1] {ECO:0000313|EMBL:GIM41167.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM41167.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
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}.
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:GIM41167.1}.
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DR EMBL; BCLY01000012; GIM41167.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DXI1; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_6763; -.
DR OrthoDB; 21858at2759; -.
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; 4.10.1000.10; Zinc finger, CCCH-type; 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; PF13923; zf-C3HC4_2; 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};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU367110};
KW mRNA splicing {ECO:0000256|RuleBase:RU367110};
KW Nucleus {ECO:0000256|RuleBase:RU367110};
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 ZN_FING 170..198
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 37426 MW; C11B591B70468DA4 CRC64;
MAEETQAADA VPQISFKKRT NKAKANFRKK PDTPPPASGS DSDFTSSDDE EGRRIKRRRK
NVAVTASSAT AGPRRNTVED QPATETAAIP LTSSNDATKH SNWYDEELSE KNLLGTTRAR
PASSTPSAPD GTYKGTANYS SFIQKNPNAP TKQFGPIKAP TNVRTVTVMD FAPDVCKDWK
QTGFCGFGDS CKFLHAREDY KQGWELDREW EIGTKGKQLS GRVVSKRSGD AKTAEDDEDD
DDEELLESIP FACIICKSSY KSPIITKCGH YFCESCALQR YRKNPSCAAC GAGTGGVFNV
AKKLNHLLDK KRERARKLRE QAIAEGEEVS SDEEEGDEES
//
