ID A0A2A9MFH5_9APIC Unreviewed; 548 AA.
AC A0A2A9MFH5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Pre-mRNA-splicing factor cwc2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BESB_048610 {ECO:0000313|EMBL:PFH36669.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH36669.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH36669.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH36669.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) 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}.
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:PFH36669.1}.
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DR EMBL; NWUJ01000003; PFH36669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9MFH5; -.
DR STRING; 94643.A0A2A9MFH5; -.
DR VEuPathDB; ToxoDB:BESB_048610; -.
DR OrthoDB; 929875at2759; -.
DR Proteomes; UP000224006; Chromosome iii.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039171; Cwc2/Slt11.
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 PANTHER; PTHR14089:SF2; PRE-MRNA-SPLICING FACTOR CWC2; 1.
DR PANTHER; PTHR14089; PRE-MRNA-SPLICING FACTOR RBM22; 1.
DR Pfam; PF16131; Torus; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000224006};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
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 218..240
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 278..360
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 218..240
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60449 MW; 3FF745C6B241A423 CRC64;
MASSTSSNPA EHMADGGNTG GGGSNSPTQT QELGCPTHRQ LSEAHDSVVR PVSNNPGEEV
RSLRPTPSVL TSAAQGVQLD CANASLPTDV LLTENQYALY AAYYQWYYHA AQEARNSLLS
DNMTNRTQLQ EHPPDSKRDI VKKWMKRPAR QQIDQNEASR YSHCEGGTEY NIWYGKYLTD
RYNKPSYLDR ETAPYKCNPK RDAGYTRANT DASGEHFFCI YYAKGGCCLG KNCRFRHSVP
TADDEGHLEW SYDIFGRERF STHKDDMDGV GSFNHDCKTL FVGGFCIDSE IPDGLKKMES
FLLKEFSAWG DVTCIRVIPK KNIAFITYAY RVQAEFAKVA MADQNLGKQA PLLLVKWAHH
DGNANKRRTD EEEEAKRKRQ KELTEIGPSM PSADGVHPGA FPFLPEGSAC RDAAGDAAAV
SATLQGHYNT WQVLSADVPE KADSMSARFS QAAYLHGSFL QDWAALYDGC SEKDVDAAPR
PLAEQMPKPN AESSGGGDPS ASPLISTDEA EEALGRMQHI LNRIDGLDAT AFEVPMHSLS
APVYPQIS
//