ID A0A401RN65_CHIPU Unreviewed; 568 AA.
AC A0A401RN65;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=chiPu_0000086 {ECO:0000313|EMBL:GCC19582.1};
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:GCC19582.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC19582.1, 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; Evidence={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:GCC19582.1}.
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DR EMBL; BEZZ01000001; GCC19582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RN65; -.
DR STRING; 137246.A0A401RN65; -.
DR OMA; YYKPENC; -.
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; -; 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:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP9; 1.
DR PANTHER; PTHR46046; 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; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
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:UP000287033};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..568
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019066435"
FT DOMAIN 49..137
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 161..249
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 273..361
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 385..473
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 485..520
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 530..565
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 540..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 63320 MW; 122516CE845D3DFB CRC64;
MILGFQWLLV PAVLLVRAGG SPPPSVPLDD VVVESKFRPK ECVRAAEPGD FVRYHYLGTL
PGGNQFDSSY NRGSTYNVFV GKGRLIAGMD KALIGMCVNE RRFIKVPPHL AYGDEGMPDK
IPPDATLFFD VLMLDIWNPE DKVKIEVHYK PENCSRVVQV SDFVRYHYNG TLLDGTFFDS
SHTRQRTYDT YIGIGWLIPG MDEGLLGMCM GEKRTITMPP FLAYGDRGDG NDIPSQATLV
FHVTLVDFHN PKDSVAIEQE FVPDPCLRKT KKGDFVRYHY NGTLMDGTLF DSSYSLNQTY
NTYIGEGYVI AGMEEGLLGV CIGEKRTIII PPHLGYGEEG ISGSIPGSAV LAFHIHMIDF
HNPADKIKIK TYHKPTNCTV LSKKGDYIKY HYNATLMDGT KLDSTHNYGK TYNVVLGSGQ
VVIGMDMGLT NMCVEEKRTI IIPPHLGYGE SGIAGEVPGS AVLIFDVELV ELVAGLPEGY
MFVWTTSQVS PDLFQEIDKD KNKEICLEEF SEYILMQVES GQGKLAPGFP PDKIIENIFS
NQDRNEDGNI SADEFKLKEE ETNHHDEL
//
