ID W5M3Q9_LEPOC Unreviewed; 276 AA.
AC W5M3Q9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003017.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000003017.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHAT01021563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01021564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M3Q9; -.
DR STRING; 7918.ENSLOCP00000003017; -.
DR Ensembl; ENSLOCT00000003023.1; ENSLOCP00000003017.1; ENSLOCG00000002569.1.
DR eggNOG; KOG0552; Eukaryota.
DR GeneTree; ENSGT00530000064286; -.
DR HOGENOM; CLU_087960_0_0_1; -.
DR InParanoid; W5M3Q9; -.
DR OMA; EVESHPQ; -.
DR Proteomes; UP000018468; Linkage group LG21.
DR Bgee; ENSLOCG00000002569; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR44927; FK506-BINDING PROTEIN 15; 1.
DR PANTHER; PTHR44927:SF1; FK506-BINDING PROTEIN 15; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT DOMAIN 71..163
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 169..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 29311 MW; 5A0B6270B5659437 CRC64;
MLSSLSQVHP GNYGSFYDDQ RQNWSVMFES EKAAMDFCKE VCVAKGNSAP SLDAVVIQDL
VLGEGQAVET GDSLEVAYTG WLLQNHAIGQ VFDSNVNKDK LLRLKLGAGK VIKGWEEGMV
GMKKGGRRLL CVPPSLAYGA QGIPSRIPAD STLVFETEIR RVKFAKDSGT DRLGAGSRDS
AAPSPAPSVD SLGPETHLQP LASTPPKPGD LPLRAKSNSL SEQLTNPDAT KAKLISRMAK
MGQPMLPFLT GAVSSQPDSS DSEMEVKAFF LGGGGS
//