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Database: UniProt
Entry: A0A3B3XRG5_9TELE
LinkDB: A0A3B3XRG5_9TELE
Original site: A0A3B3XRG5_9TELE 
ID   A0A3B3XRG5_9TELE        Unreviewed;       197 AA.
AC   A0A3B3XRG5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000017611.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000017611.1}
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC         ProRule:PRU00277};
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DR   RefSeq; XP_014827031.1; XM_014971545.1.
DR   AlphaFoldDB; A0A3B3XRG5; -.
DR   STRING; 48701.ENSPMEP00000017611; -.
DR   Ensembl; ENSPMET00000026496.1; ENSPMEP00000017611.1; ENSPMEG00000020465.1.
DR   GeneID; 106906311; -.
DR   KEGG; pmei:106906311; -.
DR   CTD; 51303; -.
DR   OrthoDB; 4243887at2759; -.
DR   Proteomes; UP000261480; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR044609; FKBP2/11.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR45779:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP11; 1.
DR   PANTHER; PTHR45779; PEPTIDYLPROLYL ISOMERASE; 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|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}; Membrane {ECO:0000256|SAM:Phobius};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..197
FT                   /note="peptidylprolyl isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017376471"
FT   TRANSMEM        155..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          56..143
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   197 AA;  21589 MW;  A9A343DEF5454A46 CRC64;
     MAAALLHKFT MKTRVFLLVL AVFSCALAQV DESETDELQV ETLVKPETCS VLSTIGDTLK
     VHYTGKLMDG QIIDSSLSRD PLVIVLGKRT VIPGLEQSLI GVCEGQKIKA TIPSHLAYGK
     KGYPPTIPGD ATLEFEVEVL SLSPQTQWQK IINDIFPLVC FALVPMLLGL VGLYLYKKAN
     AQKASKKKSK DKKSKKK
//
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