ID A0A090LCJ2_STRRB Unreviewed; 292 AA.
AC A0A090LCJ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=SRAE_2000051300 {ECO:0000313|EMBL:CEF65838.1,
GN ECO:0000313|WBParaSite:SRAE_2000051300.1,
GN ECO:0000313|WormBase:SRAE_2000051300};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF65838.1};
RN [1] {ECO:0000313|EMBL:CEF65838.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000051300.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF65838.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000051300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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 EMBL; LN609529; CEF65838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LCJ2; -.
DR STRING; 34506.A0A090LCJ2; -.
DR EnsemblMetazoa; SRAE_2000051300.1; SRAE_2000051300.1; WBGene00260708.
DR WBParaSite; SRAE_2000051300.1; SRAE_2000051300.1; WBGene00260708.
DR WormBase; SRAE_2000051300; SRP08528; WBGene00260708; -.
DR OMA; MHETALI; -.
DR OrthoDB; 977989at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR46512:SF1; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:CEF65838.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT DOMAIN 56..128
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 292 AA; 33979 MW; 11E02153A3C0CFC1 CRC64;
MNNLTLNNNI NDTDLNEPYE DVIGTGVLLK KVINEGNNIK PVDGDIIKII LIYHGLNNSH
SEEITFTLGY LLNTEGIELA CKYMDVGETA IFKIKSHLAY GEIGLLENSC IIPPNHDLIV
QIHLISIEGH QKLLLDDTPI DEILENFKIF RKKGKFYFQR GELDRAMFIY NKLLHILDEI
TINRFDKLLL IEMSILQNNL AVCYYKLKDH TNALKMSTAA VSTNPENVNI IYKHLIILKD
LRLYEKAITL IEKSMINLPS EKMELEKRFN QFIKYKKKVD DDQREFYRKM MR
//
