ID A0A093PQE1_9PASS Unreviewed; 422 AA.
AC A0A093PQE1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
DE Flags: Fragment;
GN ORFNames=N305_14268 {ECO:0000313|EMBL:KFW78621.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW78621.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW78621.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW78621.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|PROSITE-
CC ProRule:PRU00277};
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DR EMBL; KL670305; KFW78621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093PQE1; -.
DR STRING; 328815.ENSMVIP00005020058; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 2.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS50005; TPR; 2.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:KFW78621.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT DOMAIN 16..104
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 133..219
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 285..318
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 319..352
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 392..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW78621.1"
FT NON_TER 422
FT /evidence="ECO:0000313|EMBL:KFW78621.1"
SQ SEQUENCE 422 AA; 48077 MW; 5F1C7FBFE9641A1E CRC64;
QVVKREGSGT ESPMIGDKVT VHYTGWLLDG TKFDSSLDRR DKFSFDLGKG EVIKAWDIAV
ATMKIGEICR ITCKPEYAYG SAGSPPKIPP NATLIFEVKL FEFKGEDLTD EEDGGIIRRI
RKKGEGYSKP NEDALVEIQF EGRYGDRVFD KRELRFEIGE GENFDLPHGL EKAIQKMEKS
EESVFYLKPS YGFGSTGNEK FQIPPDAELQ YEVKLKSFEK AKESWEMNTD EKLEQSSIVK
ERGTQYFKEG KYKRAALQYK KIVSWLEHEA GLSDEEESKA KSLRLAAHLN LAMCHLKLKE
YSQALENCNK ALELDSNNEK GLFRRGEAHL AVNDFELARG DFQKVIQLYP SNKAAKVQLV
TCQQKIREQH EKEKKMYANM FQRLADKDLK SAATLQTSHT EDAEMKDEQN GVEDKSEAEA
EA
//
