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Database: UniProt
Entry: F0Y6J0_AURAN
LinkDB: F0Y6J0_AURAN
Original site: F0Y6J0_AURAN 
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
//
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