PPIL2_RHIO9
ID PPIL2_RHIO9 Reviewed; 533 AA.
AC P0C1J1; I1CHY2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=cyp14; ORFNames=RO3G_12773;
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=16995943; DOI=10.1186/1471-2164-7-244;
RA Pemberton T.J.;
RT "Identification and comparative analysis of sixteen fungal peptidyl-prolyl
RT cis/trans isomerase repertoires.";
RL BMC Genomics 7:244-244(2006).
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=EIE88062.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476742; EIE88062.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P0C1J1; -.
DR SMR; P0C1J1; -.
DR STRING; 936053.P0C1J1; -.
DR EnsemblFungi; EIE88062; EIE88062; RO3G_12773.
DR eggNOG; KOG0883; Eukaryota.
DR InParanoid; P0C1J1; -.
DR OrthoDB; 1392223at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
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 Coiled coil; Isomerase; Nucleus; Reference proteome; Rotamase; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..533
FT /note="Peptidyl-prolyl cis-trans isomerase-like 2"
FT /id="PRO_0000244724"
FT DOMAIN 38..111
FT /note="U-box"
FT DOMAIN 284..438
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 454..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..519
FT /evidence="ECO:0000255"
FT COMPBIAS 454..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 61062 MW; C5006A9A243CDF52 CRC64;
MGKWTDKLYI THSEWSGEVG QHSASSGITG RNSSGGFKRL PFYCCSLSLQ PFEHPVCTPD
GIIFDLMNII PYIKKYGTNP VTGEKLETKN LIKLHFHKND KDEYFCPVTY KVFSDHTTIA
AIKTTGNVFA YDTLEKLNIK AKHWKDLLTD EPFTRKDIIM LQDPHNLEKK DMSKFDYLKN
NKPEELEKRK PINNINVAGM GNTKKVFDEL QKKNSNEDDN KAIEKKEEIP TSFHKKRETL
PYNAAHYTTG EAAESFTSTV VNAYTASTRA LIDEDEFMYK KIKKKSYARI ITNYGNINVE
LFSDKKPKTC HNFIELAKTG YYNDVIFHRN IKKFMIQGGD PTGTGKGGES IWKRYFPDEI
KTTLKHDARG VLSMANRGKD TNGSQFFITY AAAPHLDGLH TVFGKVVGGL DVLSKLESIP
VDEKDRPERE IKIKQIQMFV DPFEEYQRRL KNKLTHEANA ERENEEMRKR REKEEKMGWF
GPSVPKIQTS GGGGVGKYLQ STKRDNSEIS NEGEELQKKQ KITKTTFGNF DNF
