ID F0Y6J0_AURAN Unreviewed; 164 AA.
AC F0Y6J0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
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};
DE Flags: Fragment;
GN ORFNames=AURANDRAFT_7665 {ECO:0000313|EMBL:EGB09024.1};
OS Aureococcus anophagefferens (Harmful bloom alga).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureococcus.
OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN [1] {ECO:0000313|EMBL:EGB09024.1, ECO:0000313|Proteomes:UP000002729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT "Niche of harmful alga Aureococcus anophagefferens revealed through
RT ecogenomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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; GL833126; EGB09024.1; -; Genomic_DNA.
DR RefSeq; XP_009035999.1; XM_009037751.1.
DR AlphaFoldDB; F0Y6J0; -.
DR EnsemblProtists; EGB09024; EGB09024; AURANDRAFT_7665.
DR GeneID; 20228995; -.
DR KEGG; aaf:AURANDRAFT_7665; -.
DR eggNOG; KOG0546; Eukaryota.
DR InParanoid; F0Y6J0; -.
DR OMA; FAFEDEG; -.
DR Proteomes; UP000002729; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
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; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000002729};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 3..163
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGB09024.1"
FT NON_TER 164
FT /evidence="ECO:0000313|EMBL:EGB09024.1"
SQ SEQUENCE 164 AA; 16985 MW; 4A9E78071F96E0A8 CRC64;
RCFFDVAVDG EAAGRIELEL LDELLPETCE NFRLLCGDGA PSGFGYAGAN LARRVVKGVG
LLGGVVDAPG GSHSAFAGRR VFADEGFFVP HAEPGLLSMA NAGVDTNGSQ FYLTTAAAPH
MDGRCVAFGR VAAGLDVVQT LADTLYTQRG VPVEHVEIAA CGTL
//