ID A0A3N4LFN6_9PEZI Unreviewed; 360 AA.
AC A0A3N4LFN6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Pre-mRNA-splicing factor CWC24 {ECO:0000256|RuleBase:RU367110};
GN ORFNames=L211DRAFT_841934 {ECO:0000313|EMBL:RPB20252.1};
OS Terfezia boudieri ATCC MYA-4762.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pezizaceae; Terfezia.
OX NCBI_TaxID=1051890 {ECO:0000313|EMBL:RPB20252.1, ECO:0000313|Proteomes:UP000267821};
RN [1] {ECO:0000313|EMBL:RPB20252.1, ECO:0000313|Proteomes:UP000267821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4762 {ECO:0000313|EMBL:RPB20252.1,
RC ECO:0000313|Proteomes:UP000267821};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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; ML121575; RPB20252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4LFN6; -.
DR STRING; 1051890.A0A3N4LFN6; -.
DR InParanoid; A0A3N4LFN6; -.
DR Proteomes; UP000267821; 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; 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; 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:UP000267821};
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 184..212
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 272..310
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 184..212
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 39664 MW; 94452B6E21A37E7D CRC64;
MSPLPTDTPT SDSTPHAAPA VPFFRRNNKS KSSIRKRPAT PPPAPASDDS DSDSDSNDDR
AHRRVKRQKQ SGISDASTVI TGRGGRGADD EIVPSGFSVK SKAIISTNDA TASTSYHNEN
ESEYLARKNQ KSPSPAAAAD LSNTGTYKGA SSYSSFIKRS EDAPKKPTGP LKAPTNIRTI
TVTDFAPDVC KDYKQTGFCG FGDSCKFLHA REDYAQGWQL DRDWEIKKKN PNAKTHYKTL
DNAANPLRPK QGQIEGDGDE VDKELEKIPF ACVICKKEYK NPIVTKCGHY FCEACAIQRY
RKKNPSCAIC GGRTDGVFNT AKGLQKKLDE KKRRIEVKEK EEAERKRLEE EAGPLIQGGW
//
