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Database: UniProt
Entry: A0A498INT2_MALDO
LinkDB: A0A498INT2_MALDO
Original site: A0A498INT2_MALDO 
ID   A0A498INT2_MALDO        Unreviewed;       253 AA.
AC   A0A498INT2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
GN   ORFNames=DVH24_013109 {ECO:0000313|EMBL:RXH83864.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH83864.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH83864.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH83864.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) 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|RuleBase:RU363014};
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:RXH83864.1}.
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DR   EMBL; RDQH01000337; RXH83864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498INT2; -.
DR   STRING; 3750.A0A498INT2; -.
DR   Proteomes; UP000290289; Chromosome 11.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR43629; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR43629:SF2; RHODANESE-LIKE_PPIC DOMAIN-CONTAINING PROTEIN 12, CHLOROPLASTIC; 1.
DR   Pfam; PF13616; Rotamase_3; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014}.
FT   DOMAIN          90..172
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   DOMAIN          196..248
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   253 AA;  27891 MW;  34DE4FE6D6C4EDF7 CRC64;
     MFRASCNLRP IATVPPALNA LLSPNLHLSS PSNLPTISTF APLCHPTFLS HTSCKPASSR
     ERRLPLRLMG TPFPPKSTAS FSAESGSGTG REILVQHLLL KEDNLKLLVD IQQRVSAGED
     LSDLATEYSI CPSKEEGGML GWVRKGQMLC DAKMCQVPEF EEAAFSASLN KVVREESLLQ
     DIKPEELHVK MQDPSFLDEA QLIDVREPDE VAQASLLGFQ VLPLRQFGSW GPEITTKFDP
     QKDTYVMVGI FPV
//
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