ID A0A0N5C1M2_STREA Unreviewed; 178 AA.
AC A0A0N5C1M2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001189600.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001189600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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 ECO:0000256|RuleBase:RU363014};
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DR AlphaFoldDB; A0A0N5C1M2; -.
DR STRING; 174720.A0A0N5C1M2; -.
DR WBParaSite; SPAL_0001189600.1; SPAL_0001189600.1; SPAL_0001189600.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10657; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR10657:SF4; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000256|RuleBase:RU363014};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000256|RuleBase:RU363014}.
FT DOMAIN 19..53
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 64..178
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 94..121
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 36..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 178 AA; 20543 MW; 5D692EC0E33BD133 CRC64;
MSDEPNVKKQ KNNDGSAVPP LPKGWEKRMS TSRGREYYIN RATGQSQWTR PTPSDKSEET
SSSPSSVHCY HLLVKHRDSR RPSSWRSEKI TRTKDEAIDI LKKYRDEIEQ STDKLETFMK
LASEYSDCSS AKRKGDLGFF ERNRMERPFE NASYALRVGE MSDIVETNSG VHIIYRVA
//