ID A0A2K6RS43_RHIRO Unreviewed; 299 AA.
AC A0A2K6RS43;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase E {ECO:0000256|ARBA:ARBA00021137, ECO:0000256|PIRNR:PIRNR001475};
DE Short=PPIase E {ECO:0000256|PIRNR:PIRNR001475};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PIRNR:PIRNR001475};
GN Name=PPIE {ECO:0000313|Ensembl:ENSRROP00000043853.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000043853.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000043853.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the cis-trans isomerization of proline imidic
CC peptide bonds in proteins. {ECO:0000256|PIRNR:PIRNR001475}.
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|PIRNR:PIRNR001475};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC subfamily. {ECO:0000256|ARBA:ARBA00009483,
CC ECO:0000256|PIRNR:PIRNR001475}.
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DR AlphaFoldDB; A0A2K6RS43; -.
DR Ensembl; ENSRROT00000068364.1; ENSRROP00000043853.1; ENSRROG00000044935.1.
DR GeneTree; ENSGT00940000158790; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0016018; F:cyclosporin A binding; IEA:UniProt.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR CDD; cd12347; RRM_PPIE; 1.
DR Gene3D; 3.30.70.330; -; 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 InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR016304; PPIE.
DR InterPro; IPR034168; PPIE_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_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 Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF001475; PPI_cyclophilin_E; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR001475};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PIRNR:PIRNR001475}.
FT DOMAIN 6..82
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 141..297
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 105..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 33382 MW; 3DD31EC3FD975B8C CRC64;
MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAELD
FQSFQNESEL FGRTIRVNLA KPMRIKEGSS RPVWSDDDWL KKFSGKTLEE NKEEEGSEPP
KAETQEGEPA AKKARSNPQV YMDIKIGNKP AGRIQMLLRS DVVPMTAENF RCLCTHEKGF
GFKGSSFHRI IPQFMCQGGD FTNHNGTGGK SIYGKKFDDE NFILKHTGPG LLSMANSGPN
TNGSQFFLTC DKTDWLDGKH VVFGEVTEGL DVLRQIEAQG SKDGKPKQKV IIADCGEYV
//
