ID A0A4U5PI39_STECR Unreviewed; 255 AA.
AC A0A4U5PI39;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN ORFNames=L596_010287 {ECO:0000313|EMBL:TKR96238.1};
OS Steinernema carpocapsae (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=34508 {ECO:0000313|EMBL:TKR96238.1, ECO:0000313|Proteomes:UP000298663};
RN [1] {ECO:0000313|EMBL:TKR96238.1, ECO:0000313|Proteomes:UP000298663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALL {ECO:0000313|EMBL:TKR96238.1,
RC ECO:0000313|Proteomes:UP000298663};
RX PubMed=26392177; DOI=10.1186/s13059-015-0746-6;
RA Dillman A.R., Macchietto M., Porter C.F., Rogers A., Williams B.,
RA Antoshechkin I., Lee M.M., Goodwin Z., Lu X., Lewis E.E.,
RA Goodrich-Blair H., Stock S.P., Adams B.J., Sternberg P.W., Mortazavi A.;
RT "Comparative genomics of Steinernema reveals deeply conserved gene
RT regulatory networks.";
RL Genome Biol. 16:200-200(2015).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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:TKR96238.1}.
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DR EMBL; AZBU02000002; TKR96238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5PI39; -.
DR STRING; 34508.A0A4U5PI39; -.
DR Proteomes; UP000298663; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
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 InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
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 SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000298663};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 83..240
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 255 AA; 27567 MW; 8B6DA79539330FC6 CRC64;
MLRSDSATAH PKSVVDHHSA VLRSIAGHVH RSKICSGFSL QRSNSEAAHP KTGVELYSAA
LRSGSSTAVD SQERMLRSTD KVYFDMTIGD EPIGRIVIGL FGKTVPKTAK NFIELAKNPK
GEGYPGSSFH RVIKDFMIQG GDFTNGDGTG GRSIYGEKFA DENFKLKHYG AGWLSMANAG
QDTNGSQFFI TVKKTSWLDG RHVVFGKILE GMDVVRKIEN TPTAAGDRPE KPIVIAASGH
IAVETPFSVE RADAV
//
