ID   CWC27_XENLA             Reviewed;         477 AA.
AC   Q6GLX7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Spliceosome-associated protein CWC27 homolog {ECO:0000305};
DE   AltName: Full=Probable inactive peptidyl-prolyl cis-trans isomerase CWC27 homolog {ECO:0000250|UniProtKB:Q6UX04};
DE            Short=PPIase CWC27 {ECO:0000250|UniProtKB:Q6UX04};
GN   Name=cwc27; Synonyms=sdccag10;
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=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: As part of the spliceosome, plays a role in pre-mRNA
CC       splicing. Probable inactive PPIase with no peptidyl-prolyl cis-trans
CC       isomerase activity. {ECO:0000250|UniProtKB:Q6UX04}.
CC   -!- SUBUNIT: Part of the activated spliceosome B/catalytic step 1
CC       spliceosome, one of the forms of the spliceosome which has a well-
CC       formed active site but still cannot catalyze the branching reaction and
CC       is composed at least of 52 proteins, the U2, U5 and U6 snRNAs and the
CC       pre-mRNA. Recruited during early steps of activated spliceosome B
CC       maturation, it is probably one of the first proteins released from this
CC       complex as he matures to the spliceosome C complex.
CC       {ECO:0000250|UniProtKB:Q6UX04}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UX04}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Despite the fact that it belongs to the cyclophilin-type
CC       PPIase family, it has probably no peptidyl-prolyl cis-trans isomerase
CC       activity. {ECO:0000250|UniProtKB:Q6UX04}.
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DR   EMBL; BC074317; AAH74317.1; -; mRNA.
DR   RefSeq; NP_001086199.1; NM_001092730.1.
DR   AlphaFoldDB; Q6GLX7; -.
DR   SMR; Q6GLX7; -.
DR   DNASU; 444628; -.
DR   GeneID; 444628; -.
DR   KEGG; xla:444628; -.
DR   CTD; 444628; -.
DR   Xenbase; XB-GENE-942799; cwc27.S.
DR   OrthoDB; 1392223at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 444628; Expressed in pancreas and 19 other tissues.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..477
FT                   /note="Spliceosome-associated protein CWC27 homolog"
FT                   /id="PRO_0000313653"
FT   DOMAIN          11..166
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          203..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          308..381
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        218..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..278
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  54875 MW;  AD5032026CE472D2 CRC64;
     MSNIYIQEPP SNGKVLLKTT AGEIDIELWS KEAPKACRNF VQLCLEGYYD NTIFHRVVPE
     FIIQGGDPTG TGTGGESVFG KPFRDEFHSR LRFNRRGLVA MANAGPHDNG SQFFFTLGRA
     DELNNKHTIF GKVTGDTIYN ILRLAEVDIG EDERPVNPHK IKCTEVLFNP FDDIIPRIDK
     KTKKDEEEEG KKSKAKGTKN FNLLSFGEEA EEDEEEVNEV SKVMRGKSKS SHDLLKDDPR
     LSSVPAVERE KDSQSADSDK DEDEMSDDDD EEEDDEMDSD EKHQMKDRIS NKLRKDPSKS
     IKQAENSDEA EERKSSRSEE LRREARQLKR ELKAAKEKKE NNIKESETAK EAENTVANSA
     LEEYLKEKEK YEEVRKKNTN KGVSREQQTL ALLDRFKSKL TQAITEPPKE EEASDVDEEN
     DKGWLSHVLQ FEEKSGKVKD ANMQDEDTFE IYDPRNPVNK RRREESKKIM KQKKERR