ID A0A5N5F8M8_9ROSA Unreviewed; 228 AA.
AC A0A5N5F8M8;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-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=D8674_001301 {ECO:0000313|EMBL:KAB2598381.1};
OS Pyrus ussuriensis x Pyrus communis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=2448454 {ECO:0000313|EMBL:KAB2598381.1, ECO:0000313|Proteomes:UP000327157};
RN [1] {ECO:0000313|EMBL:KAB2598381.1, ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 {ECO:0000313|EMBL:KAB2598381.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAB2598381.1};
RA Ou C.;
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang F., Wang J., Li S., Zhang Y., Fang M., Ma L., Zhao Y., Jiang S.;
RT "A de novo genome assembly of a pear dwarfing rootstock.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAB2598381.1, ECO:0000313|Proteomes:UP000327157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 {ECO:0000313|EMBL:KAB2598381.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAB2598381.1};
RA Wang F., Wang J., Li S., Zhang Y., Fang M., Ma L., Zhao Y., Jiang S.;
RT "A de novo genome assembly of a pear dwarfing rootstock.";
RL Submitted (NOV-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|ARBA:ARBA00000971,
CC 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:KAB2598381.1}.
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DR EMBL; SMOL01000768; KAB2598381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5F8M8; -.
DR Proteomes; UP000327157; Chromosome 1.
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; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 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 Reference proteome {ECO:0000313|Proteomes:UP000327157};
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..228
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5024516746"
FT DOMAIN 59..222
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 228 AA; 24826 MW; 058653EBD43876D3 CRC64;
MTTGRRLFSA ALLWVLLLFG TLAFILTRFG GDGALNKPNV VKSELREESD LEQVTHKVYF
DIQINGKPIG RIVMGLFGKT VPKTIENFRA LCTGEKGTGT SRKPLHYKGS TFHRIIPSFM
IQGGDFTLGD GRGGESIYGD KFADENFKLQ HTGPGILSMA NAGPDTNGSQ FFITTVKTGW
LDGRHVVFGK VISGMDVVYK VEEVGDANGV PRSKVVITDS GELPMSLH
//
