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Database: UniProt
Entry: A0A225X2R5_9STRA
LinkDB: A0A225X2R5_9STRA
Original site: A0A225X2R5_9STRA 
ID   A0A225X2R5_9STRA        Unreviewed;       478 AA.
AC   A0A225X2R5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN   ORFNames=PHMEG_0001608 {ECO:0000313|EMBL:OWZ23509.1};
OS   Phytophthora megakarya.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ23509.1, ECO:0000313|Proteomes:UP000198211};
RN   [1] {ECO:0000313|Proteomes:UP000198211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA   Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA   Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT   "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT   of cacao black pod achieved similar genome size and gene model numbers by
RT   different mechanisms.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC         ProRule:PRU00277};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWZ23509.1}.
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DR   EMBL; NBNE01000059; OWZ23509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225X2R5; -.
DR   STRING; 4795.A0A225X2R5; -.
DR   EnsemblProtists; OWZ23509; OWZ23509; PHMEG_0001608.
DR   OrthoDB; 25281at2759; -.
DR   Proteomes; UP000198211; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd01926; cyclophilin_ABH_like; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}; Reference proteome {ECO:0000313|Proteomes:UP000198211};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}; TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          34..122
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REPEAT          189..222
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          311..475
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   478 AA;  52180 MW;  9C6A982F69B72BF2 CRC64;
     MTDATKNEPV DLSGDGGVLK ETYVEGSGEC PPAGDEIRAH YTGTLLDGTK FDSSRDRNSE
     FKFVLGKGNV IKAWDLAFAS MKVGEKAVLT CKPEYAYGAS GSPPKIPANA TLKFDVELLG
     FSPKAKEMWE MDAEEKIVEA TKLKAKGTEQ FKAKQFAAAA ATYNQAASYM EDMYDVADED
     KKTMKSLQTT CFLNAAMALL KVEDYAEAVS VATKALNNDP SSVKALYRRG VGRMHMNDLE
     RAKEDLLAAG KLDPANREVR RELEALKKKM KDARQKEKAV FGGLFGKVSM YDDKSAVEGE
     PELDPNNPKV FFDLKIGDED AGKVVMQLYK DVCPKTAENF RALCTGEKGN CSTGQPLHYK
     GSSFHRVIKS FMIQGGDFTR GDGTGGESIY GEKFPDENFR LKHTEPGLLS MANAGPGTNG
     SQFFITTVAT PHLDGKHVVF GKVVEGFDVI KRVEALDTDK GDKPTQAVVI ADCGMYEE
//
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