ID A0A0L0D455_THETB Unreviewed; 150 AA.
AC A0A0L0D455;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AMSG_00186 {ECO:0000313|EMBL:KNC46068.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC46068.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC46068.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC46068.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; GL349433; KNC46068.1; -; Genomic_DNA.
DR RefSeq; XP_013763048.1; XM_013907594.1.
DR AlphaFoldDB; A0A0L0D455; -.
DR STRING; 461836.A0A0L0D455; -.
DR EnsemblProtists; KNC46068; KNC46068; AMSG_00186.
DR GeneID; 25560005; -.
DR eggNOG; KOG0865; Eukaryota.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000054408; 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; IPR024936; Cyclophilin-type_PPIase.
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 D-RELATED; 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|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 1..149
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 150 AA; 15893 MW; F5B3D8D6D7ACDDF9 CRC64;
MALRSDVVPK TAENFRCLCT GEKGTGKSGK PLHFKGSKFH RVINNFMLQG GDFTRGNGTG
GESIYGSKFK DENFTLKHTG PGVLSMANAG PNTNGSQFFI CTVKTEWLDG KHVVFGSVVE
GMDVVKAIEA LGSSTGATSK NVIIADCGEL
//