(data stored in SCRATCH zone)

SWISSPROT: E3J3G1_FRAIE

ID   E3J3G1_FRAIE            Unreviewed;       175 AA.
AC   E3J3G1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 50.
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   OrderedLocusNames=FraEuI1c_0075 {ECO:0000313|EMBL:ADP78163.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78163.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78163.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the 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; CP002299; ADP78163.1; -; Genomic_DNA.
DR   RefSeq; WP_013421286.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0075; -.
DR   EnsemblBacteria; ADP78163; ADP78163; FraEuI1c_0075.
DR   KEGG; fri:FraEuI1c_0075; -.
DR   eggNOG; ENOG4107XH4; Bacteria.
DR   eggNOG; COG0652; LUCA.
DR   HOGENOM; HOG000065981; -.
DR   KO; K03767; -.
DR   OMA; TSIYGQK; -.
DR   OrthoDB; 1861282at2; -.
DR   BioCyc; FSP298654:G1GOT-75-MONOMER; -.
DR   Proteomes; UP000002484; Chromosome.
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; -; 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   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; E3J3G1.
DR   SWISS-2DPAGE; E3J3G1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Isomerase {ECO:0000256|RuleBase:RU363019,
KW   ECO:0000313|EMBL:ADP78163.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN       14    170       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
SQ   SEQUENCE   175 AA;  18891 MW;  30C36828352F9609 CRC64;
     MAEELYATLR TTQGDIEVRL FPDHAPKTVR NFVGLATGDQ EWTDPSTGAK KTGTPLYSGT
     IFHRVIPGFM IQGGDPLGSG RGGPGYKFAD EFHPDLTFSK PYLLAMANAG PGTNGSQFFI
     TVGPTDWLNR KHTIFGEVTR GTEIVDAIAK APTGAQDRPK TDVVIQEIAI ETRPA
//

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