ID A0A318ZSD4_9EURO Unreviewed; 369 AA.
AC A0A318ZSD4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pre-mRNA-splicing factor CWC2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BP01DRAFT_375803 {ECO:0000313|EMBL:PYH42988.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH42988.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH42988.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH42988.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RRM CWC2 family.
CC {ECO:0000256|ARBA:ARBA00008024}.
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DR EMBL; KZ821247; PYH42988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZSD4; -.
DR STRING; 1450539.A0A318ZSD4; -.
DR OrthoDB; 929875at2759; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12360; RRM_cwf2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR034181; Cwc2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR032297; Torus.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14089:SF2; PRE-MRNA-SPLICING FACTOR CWC2; 1.
DR PANTHER; PTHR14089; PRE-MRNA-SPLICING FACTOR RBM22; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF16131; Torus; 1.
DR SMART; SM00360; RRM; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Spliceosome {ECO:0000256|ARBA:ARBA00022728};
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 99..126
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 162..232
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 99..126
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 41309 MW; 32F9D695D293EB14 CRC64;
MADTTPPSTT ETTPADPSPQ PDAVVKKRII RKKRRPARVQ VEADKAKEIQ AQFQPQSGTT
YNIYYNKWAG GDREDSSQAA AQTRCNLARD SGYTKADAQP GAHICLHFAR GLCHRGQDCE
YLHRRPTIHD ITPPQMDVFG REKFNDYRDD MGGVGSFLRQ NRTIYVGKIH VREVVARHFA
EWGEIDRIRV LTSRGVAFVT YKTEAMAQFA KEAMAHQSLD HNEILNVRWA TQDPNPLAQK
REARRIEEQA AEAIRRALPA EFIAQIEGKD AHAKRQKTNY DLEGYDEPDQ VRFAVGLRKT
EHSQQEQLAL PAAEDHRQQE EPSQPQIEQG GIFSSSTLAA LGAARASVSA KPQQAAPAGP
LVAYDSDDE
//
