GenomeNet

Database: UniProt
Entry: A0A5E4FXN8_PRUDU
LinkDB: A0A5E4FXN8_PRUDU
Original site: A0A5E4FXN8_PRUDU 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system