ID A0A3Q3BD98_KRYMA Unreviewed; 561 AA.
AC A0A3Q3BD98;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN Name=FKBP10 {ECO:0000313|Ensembl:ENSKMAP00000027490.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000027490.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000027490.1}
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 RefSeq; XP_017284993.1; XM_017429504.1.
DR AlphaFoldDB; A0A3Q3BD98; -.
DR Ensembl; ENSKMAT00000027835.1; ENSKMAP00000027490.1; ENSKMAG00000020381.1.
DR GeneID; 108243814; -.
DR KEGG; kmr:108243814; -.
DR GeneTree; ENSGT00940000156331; -.
DR OMA; GMGYVIH; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR46046; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR46046:SF7; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 4.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF54534; FKBP-like; 4.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..561
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018736004"
FT DOMAIN 44..133
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 157..245
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 269..357
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 381..468
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 524..559
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 561 AA; 62227 MW; 056DDAF3C144BA34 CRC64;
MDLRKCLKLL FFVHAARCGS GPLVDVVVDR YDIPKVCPRE VQTEDFVRYH FNGTFYEDGK
QFDSSYDRGK AFISQVGLGR LITGMDRGLQ GMCVNERRRI TVPPHLAYGS IGTGGVIPPD
ATLVYDVLLL DMWNAEDKIQ IRTISKPASC SRTSAASDFI RYHYNGTLLS GETFNSTYSR
NSTYDTYVGQ GDLIKGLDEG LLGMCVGERR IIIIPPFLAY GESGYGSKVP PQATLVLEVL
LVDVFNPNDN VTSEVKEVPK GCTRRTVTGD YIRYHYNGTF HDGTAFDSSY QRNSTYNTYI
GMGYVIRGMD KALQGLCTGE KRRIVIPPHM AYGEEGVKNL IPGSAVLIFD IHVIDFHNPN
DPVEIRVTRK PPGCNATSEA DDWIQYRYNC SLMDGTLLYS SDQYHSPSVT TLGAGKVILG
LEEGLKGMCV GERREVVVPP HWAHGENGAA GVPSSAVLLF ELELVELQKG VPEGFMFVWT
GDAPDSLFGA LDLNGDKEVP LAEFSEFIRL QVKEGKGRLR PGVDADDVIK NMFDNQDQNK
DGKITEDEVM LQEDQAVRDE L
//
