ID   A0A3Q1FCF0_9TELE        Unreviewed;      1214 AA.
AC   A0A3Q1FCF0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000013954.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000013954.1}
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   AlphaFoldDB; A0A3Q1FCF0; -.
DR   STRING; 80966.ENSAPOP00000013954; -.
DR   Ensembl; ENSAPOT00000022261.1; ENSAPOP00000013954.1; ENSAPOG00000016783.1.
DR   GeneTree; ENSGT00530000064286; -.
DR   InParanoid; A0A3Q1FCF0; -.
DR   OrthoDB; 3152232at2759; -.
DR   Proteomes; UP000257200; Unplaced.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT   DOMAIN          190..282
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REGION          23..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          948..1214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          804..894
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        27..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..330
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..972
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        973..1004
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1094
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1214 AA;  133529 MW;  0113CB4D8E30926F CRC64;
     MFGGDDEDGD FLSPTGGAKL ASLFGLDRES SQGNESFQYT APKQPRKSTN PAPSNQKAAP
     QAGAPAVLFA TAVQAFRYIN DKYVKQGKLG AAVLGSHTTK EYKLLLYLSQ QKQVTTAKIH
     VGFVFTVQPN NYCTFYDDQR QNWSLMFESD KAAVDFCKEI CLAKANSSPS LDTVVVQDLS
     LGEGQGVENG DSLEVVYTGW LLQNHTIGQM FDSNHNKDKL LRLKIGAGKV IKGWEEGMLG
     MKKEGSRLIV IPPSLAYGSK GVPNRVPSDS TLIFEAELRR VKFSKDSGSD RASASSRDSA
     APSPAPSTAP SVQNPTPEPP VQPAASGPGR PGEPPLRAKS NSLSEQLANP DATKAKLISR
     MAKMGQPMLP FMTEVAGHPE SSDSELEDTS GSRAKDQAAA SSPVQITSAA PASAYVHPHP
     HNAQMSALLP VMTTVGPQPG LPGSSHAFQP YSYTQTSATP SQLQPVGQVY PAQTVPYMGS
     GDVTSFLMTE ARQHNTEIRL SVGKVADKVD QLASKIDDLQ RQGSLSMGVP NMSMETSMIM
     HNIQRIVQEN ECLKKEVFEK SARIEEQNHK IGELINQNQR YIEQSHQLLE QRNDSLKSSS
     DQNQARLLQA EQDKHALPVD LGSGQVRLTE DLALSASRVS QLQLDASAHQ QKSMELQNKL
     GSALQDSERH CQRIASLETQ LDELKEVAER AQTQYRSEKQ RRKEMELKVN TMEEELQDLK
     TDKESLERAL SERKKKWQAE RQRRDEEVEE LRKSSQQELD NLRAQLRKAR SSSDNAVSEQ
     LSQLQLELDE EWKRKCDHML TSAKEQHRGE LAELTEQRDE LQDKLSQLQE KFTALKQSRD
     SEEQSLLQHG NQSEELQALQ QKYASLEQQG AAVREKLESR VAELERQVEE QDGSGDTAAE
     VKRVMNGVYH SLRGEFDLSE SYSGQAVLGV IVSTIKNVTL QLLSGTNKSA LRPHEEEEEE
     EAEEEEEESE DVKQSEEKPL QNVNGKKEES KQEEKEEEES VADSGSLHVS EVQVDQDAAS
     ENETETVLES KTQSQAEASA ATDLHSVSTT APEPQETAAA ESEVQHEQRQ PSAPETCEGS
     ESVHPDDGPD KSLPPEDEQA VVSDSKAAVS TEVGPERAPV EELNDAPHKA FGPPANPPPP
     PNMLQTNSGE DTSLTGGVGE ENGEEPFFQN ITRAKPPAAP SEEEEEDEMS LKGRPPPAPL
     FGEDEDEDEL DWLN
//