ID W2QHX7_PHYPN Unreviewed; 627 AA.
AC W2QHX7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=PPTG_22457 {ECO:0000313|EMBL:ETN12149.1};
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN12149.1, ECO:0000313|Proteomes:UP000018817};
RN [1] {ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN12149.1, ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|EMBL:ETN12149.1,
RC ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL Submitted (NOV-2013) 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; Evidence={ECO:0000256|PROSITE-
CC ProRule:PRU00277};
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DR EMBL; KI669577; ETN12149.1; -; Genomic_DNA.
DR RefSeq; XP_008902554.1; XM_008904306.1.
DR AlphaFoldDB; W2QHX7; -.
DR STRING; 761204.W2QHX7; -.
DR EnsemblProtists; ETN12149; ETN12149; PPTG_22457.
DR GeneID; 20191056; -.
DR VEuPathDB; FungiDB:PPTG_22457; -.
DR OMA; YARVHYV; -.
DR OrthoDB; 55622at2759; -.
DR Proteomes; UP000018817; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10891:SF1006; CALCIUM-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR10891; EF-HAND CALCIUM-BINDING DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF13499; EF-hand_7; 3.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00054; EFh; 6.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 6.
DR PROSITE; PS50222; EF_HAND_2; 6.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT DOMAIN 46..80
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 135..170
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 171..206
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 246..281
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 282..317
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 333..368
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 369..404
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 517..607
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 94..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..492
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 99..113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 70862 MW; A7BC5975D473C16F CRC64;
MGEVDATVVE RMEGNVDEVQ EKREQEAAAC LQRMFRCRTA RLRLREMLAS VFEKFYDADS
GLHYYLDKRT GETTWEKPRA LRNDDIDLTA VYDGKEEDTS EAEPTEEESG LQVVDLDNDN
KNEENEEKYL GYSTQDVALA REQFAHYDAD SSGSINANEL HKLFTNLGEQ LTLNNVRELI
KAVDKDGNGE VDFDEFLHLL PVYDGKEEDT SEAEPTEEES GLQVVDLDND NKNEENEEKY
LGYSTQDVAL AREQFAHYDA DSSGSINANE LHKLFTNLGE QLTLNNVREL IKAVDKDGNG
EVDFDEFLHL LRKQQDKNRY SASLTLALLF GPKELTKLKQ QFMILDLDGS GSIDEHELQQ
LVNKLGRRAE EFDLPAMLRE VDGDGSGTIG FNEFLQIVAS MTKSDGGPKS AFAVLLDMGI
AQGLLNGLDE VVQASRQKVY EWLNSDLVAE QKRLQGKRER RRRQEEERQR QLAKDQELYA
KHQAELAAIE RARHAQIEGL MIEVEFEGDG RNFPLAGQFA RVHYVASFER TGEIFESTRV
RCGSALEFCV GAGHTIQGFD LALQRMSVGE TAKVTIAPAL TYGVKGRPPR IPPNSALVFR
IELISIKEKL QSNEMAPMTP LERVRNR
//