ID   CWC22_XENLA             Reviewed;         803 AA.
AC   Q52KN9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Pre-mRNA-splicing factor CWC22 homolog;
DE   AltName: Full=Nucampholin homolog;
GN   Name=cwc22;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC       spliceosome. Promotes exon-junction complex (EJC) assembly.
CC       {ECO:0000250|UniProtKB:Q9HCG8}.
CC   -!- SUBUNIT: Component of the pre-catalytic spliceosome B and the catalytic
CC       spliceosome C complexes. {ECO:0000250|UniProtKB:Q9HCG8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HCG8}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q9HCG8}. Note=Concentrates around
CC       speckles, which are sites of pre-mRNA synthesis and processing, where
CC       it colocalizes with EJC core proteins. {ECO:0000250|UniProtKB:Q9HCG8}.
CC   -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000305}.
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DR   EMBL; BC094259; AAH94259.1; -; mRNA.
DR   RefSeq; NP_001089418.1; NM_001095949.1.
DR   AlphaFoldDB; Q52KN9; -.
DR   SMR; Q52KN9; -.
DR   PRIDE; Q52KN9; -.
DR   DNASU; 734468; -.
DR   GeneID; 734468; -.
DR   KEGG; xla:734468; -.
DR   CTD; 734468; -.
DR   Xenbase; XB-GENE-1010542; cwc22.S.
DR   OMA; NIFKFDA; -.
DR   OrthoDB; 996017at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 734468; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   Pfam; PF02847; MA3; 1.
DR   SMART; SM00544; MA3; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51366; MI; 1.
PE   2: Evidence at transcript level;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Spliceosome.
FT   CHAIN           1..803
FT                   /note="Pre-mRNA-splicing factor CWC22 homolog"
FT                   /id="PRO_0000302010"
FT   DOMAIN          210..393
FT                   /note="MIF4G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT   DOMAIN          501..617
FT                   /note="MI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT   REGION          1..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..803
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        16..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..482
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..764
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..803
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  92719 MW;  E69CE223437AE781 CRC64;
     MKSSVAQVRG SNYDKVDTRS SSERSSSPED SNEERSPSPR DRGYSNRSRD YSDRDRYEDR
     SRSGRYDRSD ESRRRERERS TSPRDRGYTD RRRGYSDRDG YGNDRSRNGR YDRSEDNRER
     EKRQNYQDRD YEKRSPPARR RSPPARRSEE QTEEQNQTEP PVKKKKEELD PILTRTGGAY
     IPPARLRMMQ EQITDKSSMA YQRMSWEALK KSINGLVNKV NVSNIGNIIQ ELLQENIVRG
     RGLLARSVLQ AQSASPIFTH VYAALVSIIN SKFPHIGELI LKRLILNFRK GYRRNDKQLC
     LTSSKFVAHL INQNVAHEVL ALEMLTLLLE RPNDDSVEVA IGFLKESGLK LTQVTPRGIN
     AIFERLRNIL HESEIDKRVQ YMIEVMFAVR KDGFKDHPVI PEGLDLVEEE DQFTHMLPLE
     DDYNQEDVLN VFKMDPDFLE NEEKYKAIKK EILDEGDSDS EGDANEGSED ESEEEEEDGQ
     EAGTEGEKMT IHDKTEVNLV AFRRTIYLAI QSSLDFEECA HKLIKMDFPE SQTKELCNMI
     LDCCAQQRTY EKFFGLLAGR FCLLKKEYLE AFENIFKEQF ETIHRLETNK LRNVAKMFAH
     LLYTDSLPWS VLECMNLSEE TTTSSSRIFV KIFFQELCEY MGLPKLNARL KDVTLQPFFQ
     GLLPMDNPKN TRFAINFFTS IGLGGLTDEL REHLKNAPKM IMTQKQNVES SDSSSDSSSG
     SESSSDSDSS SSSSSESSSS SSDSDSSRRK KHSQKKKKSR EAHKAASKKQ APDDRRKEAP
     KHKHQKEKYD DKQSRKSKRD SKN