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Database: UniProt
Entry: W5M3Q9_LEPOC
LinkDB: W5M3Q9_LEPOC
Original site: W5M3Q9_LEPOC 
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};
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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
//
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