ID A0A087YLW0_POEFO Unreviewed; 448 AA.
AC A0A087YLW0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000019013.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000019013.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AYCK01001940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007545769.1; XM_007545707.2.
DR AlphaFoldDB; A0A087YLW0; -.
DR STRING; 48698.ENSPFOP00000019013; -.
DR Ensembl; ENSPFOT00000019035.2; ENSPFOP00000019013.2; ENSPFOG00000018881.2.
DR GeneID; 103133796; -.
DR KEGG; pfor:103133796; -.
DR CTD; 2288; -.
DR eggNOG; KOG0543; Eukaryota.
DR GeneTree; ENSGT00940000157200; -.
DR OMA; FGAEGNE; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000028760; 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 PANTHER; PTHR46512:SF9; TETRATRICOPEPTIDE REPEAT DOMAIN 9; 1.
DR Pfam; PF00254; FKBP_C; 2.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
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 46..134
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 163..249
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 349..382
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 50404 MW; 1F84BCC076997354 CRC64;
MTAEEQNSEG QNTMPMEGED ITPKKDGGVL KLVKREGTGT DFPMTGDKVF VHYVGTLLDG
THFDSSRDRG EKFSFELGKG QVIKAWDIGV ATMRVGELCQ LICKPEYAYG SAGSPPKIPP
KATLVFEVEL FEFRGEDITE EEDGGIIRRI ITKGEGYSKP NEGAVVEVFV QGTCDGRVFD
ERELKFEIGD GESFGLPSGV EKAIMAMEQG EEALFIMKPK YGFGGDGSER YCIPCGATLQ
YKIKLTAFEK AKESWEMNTM EKLEQSGIVK EKGTQCFKDG KYKQASVQYK KIVAWLEHES
GLSDEDEKKA KALRLAAHLN LAMCFLKMHE PNKAFENCDK ALEMDSTSEK ALFRRGEALF
GMNEFEKARD DFQRVVQLYP SNKAAKSQVV LCQKRIKEQH EKDKRIYANM FQKFAERDSK
KEAEKVKPES KENGEEAMEV ENGEKETQ
//
