ID   CWC27_NEUCR             Reviewed;         541 AA.
AC   Q7SBX8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Peptidyl-prolyl isomerase cwc-27;
DE            Short=PPIase cwc-27;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase cwc-27;
GN   Name=cwc-27; ORFNames=B18P7.140, NCU08514;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Involved in pre-mRNA splicing (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM002237; EAA33928.1; -; Genomic_DNA.
DR   EMBL; BX842594; CAE75687.1; -; Genomic_DNA.
DR   RefSeq; XP_963164.1; XM_958071.2.
DR   AlphaFoldDB; Q7SBX8; -.
DR   SMR; Q7SBX8; -.
DR   STRING; 5141.EFNCRP00000008494; -.
DR   EnsemblFungi; EAA33928; EAA33928; NCU08514.
DR   GeneID; 3879312; -.
DR   KEGG; ncr:NCU08514; -.
DR   VEuPathDB; FungiDB:NCU08514; -.
DR   HOGENOM; CLU_012062_14_5_1; -.
DR   InParanoid; Q7SBX8; -.
DR   OMA; GTYGSQF; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Rotamase; Spliceosome.
FT   CHAIN           1..541
FT                   /note="Peptidyl-prolyl isomerase cwc-27"
FT                   /id="PRO_0000064186"
FT   DOMAIN          11..193
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          199..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  60296 MW;  6BAC7ECAB92D1664 CRC64;
     MSAIYNLEPQ PTASAIIHTT QGEIAVELFA KQTPLTCRNF LQLALDGYYD NTIFHRLIPG
     FIVQGGDPSG TGHGGESIYD NGALSGDLDP WPMDQRRGKN AGPHGVNFKD EFHSRLKFNR
     RGLLGMANEG APDTNSSQFF FTLGKADELT GKNTMFGRVA GDTIYNLAKI GEAEVEEGGE
     RPLYPIKITR IEILINPFDD MQKREKKPRP QQISRPTPAE KKQKKRKGGK QLLSFGDEVG
     DEDGEELPLP KKPKFDTRIV ADLDQDDSSK QSASKKSSAK RDAKPVANDV PKREEKPEPK
     PVKESRRSPS PQPVAQKKEQ PPKKHYSEHS SPEPEEPKKK SLLEKTNEEI AALKASMKRT
     IHSEPVKQEK KKSALEQLIP DTAIRGRKRR PGASSNPTRE EQEALDLLKS FKAKIETAPP
     EKNAAQPAVN PDVEDGEQDG QADEEKVCDL HFIANCQSCK AWDKVEDNED SGDEGWMSHK
     LSFAADKLGK DLSYRKKAEE ELVVIDPLAK ARTLKEEKKA TRDAKTGGSS RAWDRGRRDR
     H