PPIL2_GIBZE
ID PPIL2_GIBZE Reviewed; 578 AA.
AC Q4IBK5; A0A0E0SLT5; V6R9P8;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
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=FGRRES_17668, FGSG_05403;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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=ESU11358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231665; ESU11358.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970334; CEF87398.1; -; Genomic_DNA.
DR RefSeq; XP_011323934.1; XM_011325632.1.
DR AlphaFoldDB; Q4IBK5; -.
DR SMR; Q4IBK5; -.
DR STRING; 5518.FGSG_05403P0; -.
DR PRIDE; Q4IBK5; -.
DR EnsemblFungi; ESU11358; ESU11358; FGSG_05403.
DR GeneID; 23552587; -.
DR KEGG; fgr:FGSG_05403; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G17827; -.
DR eggNOG; KOG0883; Eukaryota.
DR HOGENOM; CLU_012062_7_0_1; -.
DR InParanoid; Q4IBK5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000070720; Chromosome 3.
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..578
FT /note="Peptidyl-prolyl cis-trans isomerase-like 2"
FT /id="PRO_0000232986"
FT DOMAIN 40..114
FT /note="U-box"
FT DOMAIN 321..475
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 240..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 63755 MW; E8CFFF8ADD8FB88D CRC64;
MGKGTDKLYI THSEWSSADA FSPSIGAGAS RNQQATASFR RLPFNFCAAS LQPFKNPVCT
PDGTIFDVEV IGVWLEKHPN QNPVTGEPLQ KKDLIRLNFA RNSESDSLGA GLSDGKGDLI
DPVTYKVFTD NTHIVAIRHG TYANVFAWDT VDRMNIKAKS WRDLVDDEEF TRADIITLQD
PQNAASRDLN QFKFLKEGHE AQLTKEQEEE RNAGNINAGA LGSMGEKVSR AKAAVEKARK
AREQGGDVNR SSTALTKPTG AGTVVRQSMI NDKKLAVNSA TYTTGKAAAS FTSTGLTPET
SGERALLSDE EYMLKPKRVK ATGFARMETN MGDLTIELYP EFAPKAVWNF IKLSQTGYYK
GVAFHRNIPN FMIQGGDPSG SGRGGQSVWG KYFDDEFDGP MTHNGRGTLS MANKGKNTNS
SQFFFAYKPT PHLDRKHTVF GKVVENINVL SKMENVPTDG SNRPLNKILI KDIVILLDPF
AEFQKQKQAN ELQTKEREKI RLQGGTDDDK TTWTGKRIRS DGSMENTGAG ESVGKYLKTT
TQQSTPTVNE ADLEDVDTWE EPVRKKAKGG GFGNFDNW
