ID A0A2U9C7L2_SCOMX Unreviewed; 370 AA.
AC A0A2U9C7L2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN Name=ppid {ECO:0000313|Ensembl:ENSSMAP00000015319.2};
GN ORFNames=SMAX5B_019124 {ECO:0000313|EMBL:AWP11716.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP11716.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP11716.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSMAP00000015319.2}
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP026255; AWP11716.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000015285; -.
DR Ensembl; ENSSMAT00000015514.2; ENSSMAP00000015319.2; ENSSMAG00000009341.2.
DR GeneTree; ENSGT00940000154672; -.
DR OMA; EMEQNCN; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000246464; Chromosome 13.
DR Proteomes; UP000694558; Chromosome 13.
DR Bgee; ENSSMAG00000009341; Expressed in head kidney and 6 other cell types or tissues.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AWP11716.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 19..183
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REPEAT 307..340
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 41073 MW; 21763CF584F0BAFB CRC64;
MSHPTPSVKP SNPENPRVFF DVDVDGERAG RIVFELFADI TPKTAENFRA LCTGEKGTGQ
STGKPLHFKG CPFHRIIKKF MIQGGDFSNH NGTGGESIYG EKFEDENFHY KHDKVGLLSM
ANAGPNTNGS QFFITTVPTP HLDDKHVVFG QVLKGLGLVK MLEMVDTKDD APVKPCLIGD
CGEHKDGDGW GAAPSDGSGD AHPDFPEDSD VDFKDVDKVL SVAEDLKNIG NNLFKSQNWK
AAIEKYSKAL RYLEVSGDVL EDEVQQKLKP TVLSCFLNTA ACKLKMQLWQ EALDSCNEAI
ELDQANTKAL FRRAQAWQGL KEFSQAMADL KKAQEIAPED KAISNEMKRV QLKVQEEKEK
EKKIYAKMFA
//
