ID   PPIL2_CRYNJ             Reviewed;         573 AA.
AC   P0CP90; Q55KK3; Q5KAW8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000305};
DE            Short=PPIase;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13356};
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:Q08752};
DE   AltName: Full=Cyclophilin-60;
DE   AltName: Full=Cyclophilin-like protein Cyp-60;
DE   AltName: Full=RING-type E3 ubiquitin transferase isomerase-like 2 {ECO:0000305};
DE   AltName: Full=Rotamase;
GN   Name=CYP8; OrderedLocusNames=CNJ00200;
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: May catalyze the cis-trans isomerization of proline imidic
CC       peptide bonds in oligopeptides thereby assisting the folding of
CC       proteins. May also function as a chaperone, playing a role in
CC       intracellular transport of proteins. May also have a protein ubiquitin
CC       ligase activity acting as an E3 ubiquitin protein ligase or as a
CC       ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on
CC       proteins. {ECO:0000250|UniProtKB:Q08752, ECO:0000250|UniProtKB:Q13356}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q13356};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q13356}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q09928,
CC       ECO:0000250|UniProtKB:Q13356}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE017350; AAW45760.1; -; Genomic_DNA.
DR   RefSeq; XP_567277.1; XM_567277.1.
DR   AlphaFoldDB; P0CP90; -.
DR   SMR; P0CP90; -.
DR   STRING; 5207.AAW45760; -.
DR   PaxDb; P0CP90; -.
DR   EnsemblFungi; AAW45760; AAW45760; CNJ00200.
DR   GeneID; 3254174; -.
DR   KEGG; cne:CNJ00200; -.
DR   VEuPathDB; FungiDB:CNJ00200; -.
DR   eggNOG; KOG0883; Eukaryota.
DR   HOGENOM; CLU_012062_7_0_1; -.
DR   InParanoid; P0CP90; -.
DR   OMA; NFIKHCA; -.
DR   OrthoDB; 1392223at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002149; Chromosome 10.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   CDD; cd16663; RING-Ubox_PPIL2; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 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   InterPro; IPR026951; PPIL2_U-box_dom.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Isomerase; Nucleus; Reference proteome; Rotamase; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..573
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 2"
FT                   /id="PRO_0000232984"
FT   DOMAIN          37..119
FT                   /note="U-box"
FT   DOMAIN          312..469
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          223..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  63562 MW;  2921176BE24684D0 CRC64;
     MGHNSDKLYV THSEHAAGSH TASSFGKRQE TGKSEFQRLP FDCCALSLQP FKNPVAVISE
     TKAGEAPRAD VFDLLNIVPY IRKFKSNPVT GKPLETSQLI KLNFSRNAEG NLHDPITYKV
     FSPHIHIVFL KNTGNVFDMA SLQLLAIKPK TWRDLVNDEP FKRKDIITIQ DPENLAARDL
     REYDYVKKDL KVSEDELAGD PLRGINVDAA GGASKVLKMI AEKNKSGQSP APTPSKIDDG
     KGQEKKEGVV AKRKVEQMAY NASNYSSGRA AASLTSTSLM PETKSERAMF DEEEYMFEEL
     SRPTKDKERQ KSKAYATITT NFGPLNVELH GDRAPKTVYN FVQLAKAGKY DNVVFHRLIP
     GFMVQGGDPT GTGRGGESYW GEPFRDEHGE KGAYKHDSRG VLSMANSGPR TNGSQFFFTF
     RPTPHLDGKH TVFGKLVGGE ETLDKIERVN VRPGGDRPVR DIVIQGVTVL QDPFEAYQAR
     LQARLARQDQ SDAALKRRAE AQKEREKDRT TWLGTKLGEK GAVGKRRMEE DVGVGKYLKV
     GGEAGQRTTL DVVDYGVEKK KKKAGGFGDF SGW