PPIL4_CRYNJ
ID PPIL4_CRYNJ Reviewed; 504 AA.
AC P0CP88; Q55ZM2; Q5KNY5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=CNA04870;
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 (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}.
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DR EMBL; AE017341; AAW41108.1; -; Genomic_DNA.
DR RefSeq; XP_566927.1; XM_566927.1.
DR AlphaFoldDB; P0CP88; -.
DR SMR; P0CP88; -.
DR STRING; 5207.AAW41108; -.
DR PaxDb; P0CP88; -.
DR EnsemblFungi; AAW41108; AAW41108; CNA04870.
DR VEuPathDB; FungiDB:CNA04870; -.
DR eggNOG; KOG0415; Eukaryota.
DR HOGENOM; CLU_018791_2_1_1; -.
DR InParanoid; P0CP88; -.
DR OMA; APKCCEN; -.
DR OrthoDB; 1392223at2759; -.
DR Proteomes; UP000002149; Chromosome 1.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
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; Reference proteome; RNA-binding; Rotamase.
FT CHAIN 1..504
FT /note="Peptidyl-prolyl cis-trans isomerase-like 4"
FT /id="PRO_0000232976"
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