ID   PPIL2_USTMA             Reviewed;         582 AA.
AC   Q4P555; A0A0D1DS35;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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; ORFNames=UMAG_04758;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003156; KIS66696.1; -; Genomic_DNA.
DR   RefSeq; XP_011391633.1; XM_011393331.1.
DR   AlphaFoldDB; Q4P555; -.
DR   SMR; Q4P555; -.
DR   STRING; 5270.UM04758P0; -.
DR   EnsemblFungi; KIS66696; KIS66696; UMAG_04758.
DR   GeneID; 23564837; -.
DR   KEGG; uma:UMAG_04758; -.
DR   VEuPathDB; FungiDB:UMAG_04758; -.
DR   eggNOG; KOG0883; Eukaryota.
DR   HOGENOM; CLU_012062_7_0_1; -.
DR   InParanoid; Q4P555; -.
DR   OMA; NFIKHCA; -.
DR   OrthoDB; 1392223at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000561; Chromosome 17.
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   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; 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   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..582
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 2"
FT                   /id="PRO_0000232988"
FT   DOMAIN          39..114
FT                   /note="U-box"
FT   DOMAIN          291..450
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          221..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   582 AA;  64534 MW;  1833F83DB6BD7280 CRC64;
     MGHGKSDRPF LSAAEHSGVY GAHSASSGKA GALEQASFHP VSYDCCAISF QPWSVPVCSP
     DCGIAFELTN LIPFLRKFSS VHPVTGKRFD LDNVVRLNLH KNQHGRFHDP VSFKEFGQHS
     HLVAIRQSGN VFLWDTVQRL NLKPKYMKDL VTDQAFTKSD IITVQDPEHP EHRNPSEMHH
     VKNALKLTQA DKGIDSSQQI NMGAIGSTHK LLSTLRETTQ PDMHTASASS STSASKHTTT
     AYSRNKASGS STGMTAASFT SSSLTPRTAI ERVILDDEEV MFSHIKSRPS SKAYVRLSTN
     FGALNLELHC GKAPKTCFNF LQLCKHGKYD DTLFHRNIPG FMIQGGDPTG TGRGGSSIWN
     SNFRDEFNEP GAFKHDTRGV LSMANKGKDT NASQFFITYR GVPHLDGKHT VFGRLVDGDK
     DATLTKMEQV PSEQGTDRPL KKIQIQDVLV TEDPFEQYQL RQKQSAKAND PTDPEYQRRM
     EKRKRRQNDR TTWLGTELPT NHPEAQQKQS ETKIDNLLVG SWSVGKYLNS TGRPRTKTIQ
     AHPARKEHDE SAAKKTKTNT NAIAIANANA NANAGFGDFS AW