PPIL2_CRYNB
ID PPIL2_CRYNB Reviewed; 573 AA.
AC P0CP91; Q55KK3; Q5KAW8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=CNBJ3300;
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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL18407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAEY01000050; EAL18407.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_773054.1; XM_767961.1.
DR AlphaFoldDB; P0CP91; -.
DR SMR; P0CP91; -.
DR EnsemblFungi; AAW45760; AAW45760; CNJ00200.
DR EnsemblFungi; EAL18407; EAL18407; CNBJ3300.
DR GeneID; 4938677; -.
DR KEGG; cnb:CNBJ3300; -.
DR HOGENOM; CLU_012062_7_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001435; Chromosome 10.
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:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
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; Rotamase; Transferase; Ubl conjugation pathway.
FT CHAIN 1..573
FT /note="Peptidyl-prolyl cis-trans isomerase-like 2"
FT /id="PRO_0000410205"
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