ID   PPIL2_ASPOR             Reviewed;         570 AA.
AC   Q2U5W8;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=AO090120000480;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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   -!- 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; AP007166; BAE63047.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2U5W8; -.
DR   SMR; Q2U5W8; -.
DR   STRING; 510516.Q2U5W8; -.
DR   EnsemblFungi; BAE63047; BAE63047; AO090120000480.
DR   HOGENOM; CLU_012062_7_0_1; -.
DR   OMA; NFIKHCA; -.
DR   Proteomes; UP000006564; Chromosome 5.
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; Reference proteome; Rotamase; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..570
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 2"
FT                   /id="PRO_0000232983"
FT   DOMAIN          37..110
FT                   /note="U-box"
FT   DOMAIN          298..457
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          215..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  62365 MW;  6A4AE867668AD7E2 CRC64;
     MGKGSKQITH SEWASGDSYS ASAGAGGGKG GDNAPFKRLP FNFCSLSLQP FAHPVCTPSG
     TIFDLTNILP WIKKHGKNPV DGTPLKNSDL IKLNIAKNES GDYVDPVTYK VLTDNTHIVA
     LRNTGNVFAW DTVERLNIKG KLWRDLVTDE EFGRKDIITL QDPQNIESRN LSSFNYLKEG
     ESVPGQKEEE SNVNASALGS SAKILKAKEA VAKARSERAQ RADSSAVTKK ADGSTTTSTQ
     SKTASFQSGK PTPYNAAKYT TGMAAASFTS TGLTPHTSAE LALLSDEEYM LKRGRVKQKG
     YARISTTSGD INLELQTEYA PKAVWNFIKL AKKGYYKDVT FHRNIKGFMI QGGDPSGTGR
     GGESIWGKYF NDEFEGPLKH DSRGTLSMAN KGKNTNSSQF FIAYRALPHL NNKHTIFGHV
     IDDPTPSSTT LNNLETHPVN SSTNRPTPDI RITDVTIFVD PFEEFLNQKK AEEASGKNKK
     VDPTEEDRET QQEDDDQVTW TGKRVRGPGS TAAGGDAGSG VGKYLKAALA NQTTQEEDEI
     VEFVDEEPEP EPMRKKFKSR GGFGDFSSWD