ID A0A401SDY0_CHIPU Unreviewed; 213 AA.
AC A0A401SDY0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
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};
GN ORFNames=chiPu_0006980 {ECO:0000313|EMBL:GCC28550.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC28550.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC28550.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC28550.1}.
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DR EMBL; BEZZ01000211; GCC28550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401SDY0; -.
DR STRING; 137246.A0A401SDY0; -.
DR OMA; FFYVWGI; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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; -; 1.
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; PTHR46222:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP7; 1.
DR PANTHER; PTHR46222; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP7/14; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..213
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019317509"
FT DOMAIN 47..136
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 136..171
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 180..213
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 213 AA; 24414 MW; 3775DE42B325E23E CRC64;
MYRYGTLLFY TLVCTIVFNH ISAKVAKEVK IEVMYRPENC PVKSKRGDAL NAHYDGYLED
GTQIYCSRTS NDGHPKWFVL GVGQVIKGLD IGMDDMCEGE KRKVTIPPSL AFGAIAREKI
PPNSTLIFEI ELYAVRRGPR SVESFQVIDL DGDKKLSRNE LKLYLQEEFK RDNRIKDSAH
KDRVLTDIFL KNDQDGDGYI SAREYNVLQH DEL
//