ID   PPIL4_CRYNB             Reviewed;         504 AA.
AC   P0CP89; Q55ZM2; Q5KNY5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 4;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   Name=CYP6; OrderedLocusNames=CNBA4680;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
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 (By similarity). {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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL23123.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AAEY01000003; EAL23123.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_777770.1; XM_772677.1.
DR   AlphaFoldDB; P0CP89; -.
DR   SMR; P0CP89; -.
DR   PRIDE; P0CP89; -.
DR   EnsemblFungi; AAW41108; AAW41108; CNA04870.
DR   EnsemblFungi; EAL23123; EAL23123; CNBA4680.
DR   GeneID; 4933730; -.
DR   KEGG; cnb:CNBA4680; -.
DR   HOGENOM; CLU_018791_2_1_1; -.
DR   Proteomes; UP000001435; Chromosome 1.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   CDD; cd01921; cyclophilin_RRM; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR035542; CRIP.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR035538; Cyclophilin_PPIL4.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR45843; PTHR45843; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Isomerase; Nucleus; RNA-binding; Rotamase.
FT   CHAIN           1..504
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 4"
FT                   /id="PRO_0000410204"
FT   DOMAIN          1..169
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   DOMAIN          246..324
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          330..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  57871 MW;  5A3EDE73927DB07C CRC64;
     MSVMLETSLG DLIIDLEVDK CPRTCENFIK LCKLKYYALN AFFNVSKNFI AQSGDPTATG
     TGGESLASYV YSQSPSGPRP PRYFTPEILN SLKHTHKGTL SMAVAPINPP GCGSQFFITL
     ADNIDYLDGK HAVFGHVIEG LDTLDKINDA FTDKEGRPLQ NIRIRHVEIL EDPFPDPDNF
     MPIPQSPIRP PDDLSKVRIA DTEDPNAVIP EEEAEELRRR TEAASSALTL EMIGDLPFAA
     VRPPENILFV CKLNPVTQDE DLELIFSRFG KILSCEVVRD KKSGDSLQYA FIEFDEREAA
     EQAYFKMQNV LVDDRRIWVD FSQSVAKMNR SMLSSSNPTG RGGRGGRGGR GGNYSGRRDG
     DRDRDRDSGW SSRRDAPDSR RPPPPPVPMS SSRDVGGTEG YGLVFDDRSA PSSRGSKRDR
     ERSPKRERDR ERERDRSPRR DRDRERDRSP RRDRDRERDD HDRRDRDRNG RDRERNGDRE
     RYRERSRERE NERYRERDDR DRRR