ID A0A2J6TPC4_9HELO Unreviewed; 391 AA.
AC A0A2J6TPC4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Pre-mRNA-splicing factor CWC2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=K444DRAFT_520458 {ECO:0000313|EMBL:PMD64864.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD64864.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD64864.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD64864.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-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; KZ613747; PMD64864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6TPC4; -.
DR STRING; 1095630.A0A2J6TPC4; -.
DR InParanoid; A0A2J6TPC4; -.
DR OrthoDB; 929875at2759; -.
DR Proteomes; UP000235371; 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: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:UP000235371};
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 114..140
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 176..250
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 114..140
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43408 MW; 2855B8E191D9D98A CRC64;
MADVETATPP TMAPQDMGGE EASTALTTTS NEVSAPSERK VKKIIRKKKR AARPQVDPST
MKSEPPPQTG TIFNIWYNKW SGGDREDKYL SKTAAAGRCN IAKDTGYTKA DKVPGSYFCL
FFARGICPKG QECEYLHRLP GIHDMFNPNV DVFGRDKHSD YRDDMGGVGS FMRQNRTIYV
GRIHVSDDIE EVVARHFAEW GQVERIRVLN TRGVAFITYS NEANAQFAKE AMAHQSLDHS
EILNVRWATA DPNPMAQKRE VRRIEEQAAE AVRRALPAEF VAEIEGRDLE ARKRKRIEGG
FGLAEYEAPD DIYFARGVNA VNPVGRQGLT LEEEQRLMIE ADQVEKEEAE ETGIFSSSTL
AALKGAQASV APRSKTKAPS GPLVAYDSDS D
//
