ID A0A6A3CB60_HIBSY Unreviewed; 182 AA.
AC A0A6A3CB60;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=F3Y22_tig00009009pilonHSYRG00001
GN {ECO:0000313|EMBL:KAE8725081.1};
OS Hibiscus syriacus (Rose of Sharon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8725081.1, ECO:0000313|Proteomes:UP000436088};
RN [1] {ECO:0000313|EMBL:KAE8725081.1, ECO:0000313|Proteomes:UP000436088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekdansim {ECO:0000313|Proteomes:UP000436088};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAE8725081.1};
RA Kim Y.-M.;
RT "Draft genome information of white flower Hibiscus syriacus.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KAE8725081.1}.
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DR EMBL; VEPZ02000430; KAE8725081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A3CB60; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000436088; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
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:SF573; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR Pfam; PF00160; Pro_isomerase; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000436088};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..175
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 182 AA; 20238 MW; 07A651053A47C55A CRC64;
MRREILILLQ PRCIPLLTAV SIFFIFAFSG AKREEEKVVE EEHEITHRVY LDVDIDGQHV
GRIVIGLYSE VVPKTVVEKG KGAKGKALNY KGTPFHRIIS GFVIQGGDII HGDGRGSEPI
YGGTFRDESF KIKHSHAGVV FMANTGPDSN GSQFFITTVK ASWLDGSTLF SVRLFRAWTL
CL
//
