ID A0A212C647_CEREH Unreviewed; 194 AA.
AC A0A212C647;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
DE Flags: Fragment;
GN ORFNames=Celaphus_00018876 {ECO:0000313|EMBL:OWK01458.1};
OS Cervus elaphus hippelaphus (European red deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Cervus.
OX NCBI_TaxID=46360 {ECO:0000313|EMBL:OWK01458.1, ECO:0000313|Proteomes:UP000242450};
RN [1] {ECO:0000313|Proteomes:UP000242450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29294181;
RA Bana N.A., Nyiri A., Nagy J., Frank K., Nagy T., Steger V., Schiller M.,
RA Lakatos P., Sugar L., Horn P., Barta E., Orosz L.;
RT "The red deer Cervus elaphus genome CerEla1.0: sequencing, annotating,
RT genes, and chromosomes.";
RL Mol. Genet. Genomics 293:665-684(2018).
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|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:OWK01458.1}.
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DR EMBL; MKHE01000028; OWK01458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212C647; -.
DR Proteomes; UP000242450; Chromosome 28.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
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; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000242450};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 129..194
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT NON_TER 194
FT /evidence="ECO:0000313|EMBL:OWK01458.1"
SQ SEQUENCE 194 AA; 22154 MW; 97D6515B63D650E3 CRC64;
MGSQQPSVPC ISRSPPEQPL QVKVVGLFKS SSFQIAKSAA ESLKSNYPSK FEDPIIIPVQ
EFAWHQYLQE KKRELKNEVW EYSSYVMCFI NDELLGDALD LQKWAHKVWD IVDFKPPALY
EALTHNFVFL DISIDLYPIG RLIFELYSDT CPKTCKNFQI LCTGKAGFSQ SGIKLHYTGS
IFHRVVQNGW IQGG
//
