PIN4_GIBZE
ID PIN4_GIBZE Reviewed; 133 AA.
AC Q4I665; A0A0E0SEN8; I1S8D4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase PIN4;
DE Short=PPIase PIN4;
DE EC=5.2.1.8;
DE AltName: Full=Parvulin-14;
DE Short=Par14;
GN Name=PIN4; ORFNames=FGRRES_16807, FGSG_13112;
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 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).
RN [4]
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: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ESU13529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231666; ESU13529.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970335; CEF84901.1; -; Genomic_DNA.
DR RefSeq; XP_011327036.1; XM_011328734.1.
DR AlphaFoldDB; Q4I665; -.
DR SMR; Q4I665; -.
DR STRING; 229533.Q4I665; -.
DR EnsemblFungi; ESU13529; ESU13529; FGSG_13112.
DR GeneID; 23559919; -.
DR KEGG; fgr:FGSG_13112; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G24445; -.
DR HOGENOM; CLU_3125195_0_0_1; -.
DR InParanoid; Q4I665; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR043323; PIN4.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR PANTHER; PTHR45995; PTHR45995; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..133
FT /note="Peptidyl-prolyl cis-trans isomerase PIN4"
FT /id="PRO_0000232934"
FT DOMAIN 39..131
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 133 AA; 14288 MW; 8D9A783E402AA3F0 CRC64;
MGKNDKKGAD KGGKAKGGDK GKDAKDTKDS GSGGKAKGAQ SINVRHILCE KHAKKEEALA
KLNDGVKFDE VAREYSEDKA RQGGSLGWKT KGSLDPKFEE VAFALETSTT NSPKFVEVKT
GFGYHIIMVE GRK
