ID D0NGW9_PHYIT Unreviewed; 265 AA.
AC D0NGW9;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
GN ORFNames=PITG_10711 {ECO:0000313|EMBL:EEY58608.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY58608.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
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 Evidence={ECO:0000256|RuleBase:RU363014};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; DS028137; EEY58608.1; -; Genomic_DNA.
DR RefSeq; XP_002901552.1; XM_002901506.1.
DR AlphaFoldDB; D0NGW9; -.
DR STRING; 403677.D0NGW9; -.
DR EnsemblProtists; PITG_10711T0; PITG_10711T0; PITG_10711.
DR GeneID; 9470204; -.
DR KEGG; pif:PITG_10711; -.
DR VEuPathDB; FungiDB:PITG_10711; -.
DR eggNOG; KOG2017; Eukaryota.
DR eggNOG; KOG3258; Eukaryota.
DR HOGENOM; CLU_1051559_0_0_1; -.
DR InParanoid; D0NGW9; -.
DR OMA; MAHTIIA; -.
DR OrthoDB; 700at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.50.40; -; 2.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR PANTHER; PTHR43629; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR43629:SF2; RHODANESE-LIKE_PPIC DOMAIN-CONTAINING PROTEIN 12, CHLOROPLASTIC; 1.
DR Pfam; PF13616; Rotamase_3; 2.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000256|RuleBase:RU363014}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000256|RuleBase:RU363014}; Signal {ECO:0000256|RuleBase:RU363014};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU363014"
FT CHAIN 23..265
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363014"
FT /id="PRO_5003013348"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..121
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 165..257
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT COILED 174..201
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 265 AA; 28831 MW; B743A18DC4D4F2B2 CRC64;
MAPKVLALLA TVLLCCIASV AGQDAAPVAI QAHASHILVD TEAEADDLSV QLGEASNLFL
KFAQLAKEHS KCPSSRKGGD LGTFDRGQMV PEFDKVAFEG EIGVVHKVKT QFGWHLVLIS
RRLDGTEEPD KYRDLKQALL KIMPFLGPII LIFIMAYGAR GSKGGPRARA FHILVKSEDE
ADKLFKEIDA AEDKKTKLSE LAGKHSTCPS GKKGGDLGMF GRGEMVPQFD KVVFEGEVGE
LAKVQTQFGW HVLLCTERLG DKKSK
//
