ID   CWC27_DANRE             Reviewed;         470 AA.
AC   Q7ZW86;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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; ORFNames=zgc:56702;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2003) 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; BC049533; AAH49533.1; -; mRNA.
DR   RefSeq; NP_957397.1; NM_201103.1.
DR   AlphaFoldDB; Q7ZW86; -.
DR   SMR; Q7ZW86; -.
DR   STRING; 7955.ENSDARP00000064209; -.
DR   PaxDb; Q7ZW86; -.
DR   GeneID; 394078; -.
DR   KEGG; dre:394078; -.
DR   CTD; 10283; -.
DR   ZFIN; ZDB-GENE-040426-1118; cwc27.
DR   eggNOG; KOG0865; Eukaryota.
DR   eggNOG; KOG0885; Eukaryota.
DR   InParanoid; Q7ZW86; -.
DR   OrthoDB; 1392223at2759; -.
DR   PhylomeDB; Q7ZW86; -.
DR   Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q7ZW86; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..470
FT                   /note="Spliceosome-associated protein CWC27 homolog"
FT                   /id="PRO_0000313652"
FT   DOMAIN          11..166
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          172..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          281..332
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        172..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..270
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  53481 MW;  FF8175A7EEA94EE7 CRC64;
     MSNIYIQEPP TNGKVLLKTS AGDIDIELWS KETPKACRNF VQLCMEGYYD GTIFHRMVPE
     FIVQGGDPTG TGTGGESIYG RPFKDEFHSR LRFNRRGLVA MANAGPHDNG SQFFFTLGRA
     DELNNKHTIF GKVTGDTVYN MLRLADVACD GDERPLNPHK IRSTEVLHSP FDDIIPREIK
     GKKEKNKDEA KKSQSKATKN FSLLSFGEEA EEDEEMVNQV SQTMKGKSKS SHDLLKDDPK
     LSSVPVVDRN QGEGDFEDSD DDEDDAEDDS DREAEKAKVR ENIAKKLKKD KTDEEKSSQD
     LVKKTSRSDE LRKEARQLKK ELLAIKQRKE DGVKKEEDVS EVGDSKQNSE AVTEYLESRK
     KYDDMRKQKL KKGSGREAQT LALLESFKSK LSSAISETPS APEEDVEELA EDDDKGWMAH
     VLHFDEQSRK VKDANMQDED TFEIYDPRNP VNKRRREESK KLLKDKKARR