ID A0A4U8UZP6_STECR Unreviewed; 160 AA.
AC A0A4U8UZP6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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_005575 {ECO:0000313|EMBL:TMS38962.1};
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:TMS38962.1, ECO:0000313|Proteomes:UP000298663};
RN [1] {ECO:0000313|EMBL:TMS38962.1, ECO:0000313|Proteomes:UP000298663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALL {ECO:0000313|EMBL:TMS38962.1,
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).
RN [2] {ECO:0000313|EMBL:TMS38962.1, ECO:0000313|Proteomes:UP000298663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALL {ECO:0000313|EMBL:TMS38962.1,
RC ECO:0000313|Proteomes:UP000298663};
RX PubMed=31113823;
RA Serra L., Macchietto M., Macias-Munoz A., McGill C.J., Rodriguez I.M.,
RA Rodriguez B., Murad R., Mortazavi A.;
RT "Hybrid Assembly of the Genome of the Entomopathogenic Nematode Steinernema
RT carpocapsae Identifies the X-Chromosome.";
RL G3 (Bethesda) 0-0:2687-2697(2019).
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|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:TMS38962.1}.
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DR EMBL; AZBU02000001; TMS38962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U8UZP6; -.
DR Proteomes; UP000298663; Chromosome x.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 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|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000298663};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 1..154
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 160 AA; 17553 MW; F2ADC80E959D6AEA CRC64;
MPYVTLETSM GKISVELYWE HADRTCRNFT ELSKRGYYNG TIFHRVIGDF MIQGGDPTGT
GRGGESIYGS AFKDEIHPEL KHSGAGIISM ANAGPNTNGS QFFITLAPTS HLDGKHTIFG
RVAAGMKVVQ NIGHVDTDNN DRPKSTVKIV KAYPSTEFRI
//