ID A0A094KWU1_ANTCR Unreviewed; 290 AA.
AC A0A094KWU1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=N321_06303 {ECO:0000313|EMBL:KFZ56372.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ56372.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ56372.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ56372.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|RuleBase:RU363019}.
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DR EMBL; KL346828; KFZ56372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094KWU1; -.
DR Proteomes; UP000053620; Unassembled WGS sequence.
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, ECO:0000313|EMBL:KFZ56372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053620};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 124..287
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFZ56372.1"
FT NON_TER 290
FT /evidence="ECO:0000313|EMBL:KFZ56372.1"
SQ SEQUENCE 290 AA; 32988 MW; 310F8319BD9555B6 CRC64;
VTVVGLLRDP AFHAAKCTAE ALKLKFPRKF ADPVIQPLVE FAWHEYLQEK KKELRGEVWA
YASSVMCFKD GQLLGDEKEL LKWSYHEWGY QDFKPKELYQ AIAEDFYAKY LKNSQASSTH
VFVYLEIAIV EQPVGRLLFE LFSDLCPRTC ENFRALCAGG AKSPRDGREL TYKNSLFHRL
VKNGWIQGGD IITGKGDEGE SIYGPTFEDE CFAVRHKGRG VLGMANKGRH TNSSQFYITF
QPAPYLDKKY VAFGQLIEGT EVLQRLEAVP TYNERPTVAC KIINCGTFEP
//
