ID A0A2P4XGI2_9STRA Unreviewed; 207 AA.
AC A0A2P4XGI2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN ORFNames=PHPALM_19796 {ECO:0000313|EMBL:POM64651.1};
OS Phytophthora palmivora var. palmivora.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=611791 {ECO:0000313|EMBL:POM64651.1, ECO:0000313|Proteomes:UP000237271};
RN [1] {ECO:0000313|EMBL:POM64651.1, ECO:0000313|Proteomes:UP000237271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sbr112.9 {ECO:0000313|Proteomes:UP000237271};
RC TISSUE=Mycelia {ECO:0000313|EMBL:POM64651.1};
RX PubMed=28186564;
RA Ali S.S., Shao J., Lary D.J., Kronmiller B., Shen D., Strem M.D.,
RA Amoako-Attah I., Akrofi A.Y., Begoude B.A., Ten Hoopen G.M., Coulibaly K.,
RA Kebe B.I., Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W.,
RA Bailey B.A.;
RT "Phytophthora megakarya and P. palmivora, closely related causal agents of
RT cacao black pod rot, underwent increases in genome sizes and gene numbers
RT by different mechanisms.";
RL Genome Biol. Evol. 9:536-557(2017).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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:POM64651.1}.
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DR EMBL; NCKW01011066; POM64651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4XGI2; -.
DR OrthoDB; 45411at2759; -.
DR Proteomes; UP000237271; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF578; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 3-RELATED; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 2.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:POM64651.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237271};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 14..203
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 98..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 23047 MW; FCB4FE7C6A99852B CRC64;
MHPQRERSDN PIVFFDVSIG EKLAGRILIE LRADVVPRTA ENFRRLCTGE TMDHRTRRRR
HYARCPFHRV VKDKFCQSGD YANHDGSGGE CTFGHSPRQI SPTDDDHNGT ASEIPTTPST
FDDENFILRH TGAGVLSMAN AGPDSNTCQF YLHFCPQPSF DGKHVVFGCL TDSESYAVLE
QINAVATARG DPKQPVKIAR AGQLFPV
//
