CWC27_CRYNJ
ID CWC27_CRYNJ Reviewed; 491 AA.
AC P0CP92; Q55L68; Q5KAB3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Peptidyl-prolyl isomerase CWC27;
DE Short=PPIase CWC27;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase CWC27;
GN Name=CWC27; OrderedLocusNames=CNJ02320;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017350; AAW45928.1; -; Genomic_DNA.
DR RefSeq; XP_567445.1; XM_567445.1.
DR AlphaFoldDB; P0CP92; -.
DR SMR; P0CP92; -.
DR STRING; 5207.AAW45928; -.
DR PaxDb; P0CP92; -.
DR EnsemblFungi; AAW45928; AAW45928; CNJ02320.
DR GeneID; 3254127; -.
DR KEGG; cne:CNJ02320; -.
DR VEuPathDB; FungiDB:CNJ02320; -.
DR eggNOG; KOG0885; Eukaryota.
DR HOGENOM; CLU_012062_14_4_1; -.
DR InParanoid; P0CP92; -.
DR OMA; DDWYDVY; -.
DR OrthoDB; 1392223at2759; -.
DR Proteomes; UP000002149; Chromosome 10.
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: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; 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; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Rotamase; Spliceosome.
FT CHAIN 1..491
FT /note="Peptidyl-prolyl isomerase CWC27"
FT /id="PRO_0000064182"
FT DOMAIN 11..167
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 186..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 277..327
FT /evidence="ECO:0000255"
FT COMPBIAS 186..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 55194 MW; 70251B0DC9BD42D2 CRC64;
MSNLYATEPA TNGKVIIDTT AGEIEVELWG KECPKAVRNF LALTMEGYYD GVIFHRVVPG
FIIQSGDPTG TGMGGESFYG EPFEDEIHGR LKFNRRGLLG MANNGSRNSN TSQFFITLDA
APELTNKHTM FGKIVGNTIF NVLNIGNLDT DKEERPLIPP KIRRIHIIEN PFDDIVPRIT
AEEKKAQQKA KLEAKKDMEQ RERRAKAKKN TGLLSFGDSE EIPEEEVTVK KKSMTRQDLV
DPSEAEHTKS KTSKMTETFV NIPPSLKDLG KSRENEASEE KKAVDLKNIR AQHEREKAGG
SAARQAEIKR MEEDLRRLKK RSGSVSDSES DSSSRARRKG PSYLEQELAK YASKRGRAAM
KAGNKRGRRD EEEDVLTEMR KFSKRVMQAG DEPEEEQAEE IEEGEAKEEG TGIGAAMAEE
EGGIEVDDDV GWLTHKLKFQ VDDKELTRRA EDEYAVIDPR AKARDLLGKP DKKKLKGNPN
RRTVRNSGRN R
