ID A0A5E4FXN8_PRUDU Unreviewed; 204 AA.
AC A0A5E4FXN8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=ALMOND_2B017052 {ECO:0000313|EMBL:VVA32098.1};
OS Prunus dulcis (Almond) (Amygdalus dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3755 {ECO:0000313|EMBL:VVA32098.1, ECO:0000313|Proteomes:UP000327085};
RN [1] {ECO:0000313|Proteomes:UP000327085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Texas {ECO:0000313|Proteomes:UP000327085};
RX PubMed=31529539; DOI=10.1111/tpj.14538;
RA Alioto T., Alexiou K.G., Bardil A., Barteri F., Castanera R., Cruz F.,
RA Dhingra A., Duval H., Fernandez I Marti A., Frias L., Galan B.,
RA Garcia J.L., Howad W., Gomez-Garrido J., Gut M., Julca I., Morata J.,
RA Puigdomenech P., Ribeca P., Rubio Cabetas M.J., Vlasova A., Wirthensohn M.,
RA Garcia-Mas J., Gabaldon T., Casacuberta J.M., Arus P.;
RT "Transposons played a major role in the diversification between the closely
RT related almond and peach genomes: results from the almond genome
RT sequence.";
RL Plant J. 101:455-472(2020).
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|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR EMBL; CABIKO010000236; VVA32098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5E4FXN8; -.
DR EnsemblPlants; VVA32098; VVA32098; Prudul26B017052.
DR Gramene; VVA32098; VVA32098; Prudul26B017052.
DR InParanoid; A0A5E4FXN8; -.
DR OMA; CSIINSG; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000327085; Chromosome 6.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF562; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP19-4; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000327085};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 24..204
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5023154630"
FT DOMAIN 38..201
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 204 AA; 21913 MW; 1A4FD0868E09581D CRC64;
MARTTSFLLC TLVVFGTLAL IQAKKSKEDL KEVTHKVFFD VEIAGKPAGR VVIGLFGKTV
PKTAENFRAL CTGEKGIGKS GKPLHFKGSK FHRIIPSFMI QGGDFTLGDG RGGESIYGEK
FADENFKLKH TGPGLLSMAN AGSDTNGSQF FITTVTTNWL DGRHVVFGKV LSGMDVVYKI
EAEGNQNGTP KSKVVIADSG ELPL
//