(data stored in ACNUC7421 zone)

SWISSPROT: A8LCF2_FRASN

ID   A8LCF2_FRASN            Unreviewed;       175 AA.
AC   A8LCF2;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
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=Franean1_0124 {ECO:0000313|EMBL:ABW09591.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09591.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000820; ABW09591.1; -; Genomic_DNA.
DR   RefSeq; WP_012157568.1; NC_009921.1.
DR   STRING; 298653.Franean1_0124; -.
DR   EnsemblBacteria; ABW09591; ABW09591; Franean1_0124.
DR   KEGG; fre:Franean1_0124; -.
DR   eggNOG; ENOG4107XH4; Bacteria.
DR   eggNOG; COG0652; LUCA.
DR   HOGENOM; HOG000065981; -.
DR   KO; K03767; -.
DR   OMA; TSIYGQK; -.
DR   OrthoDB; 1861282at2; -.
DR   BioCyc; FSP298653:G1G9X-121-MONOMER; -.
DR   Proteomes; UP000001313; 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; A8LCF2.
DR   SWISS-2DPAGE; A8LCF2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   Isomerase {ECO:0000256|RuleBase:RU363019,
KW   ECO:0000313|EMBL:ABW09591.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN       14    170       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
SQ   SEQUENCE   175 AA;  19190 MW;  6CBDC7D03F55581A CRC64;
     MAEELYATVR TTQGDIEIRL FPDHAPKTVK NFVGLATGSR EWTDPATGEK KTGVPLYSGT
     IFHRVIPNFM IQGGDPLGSG RGGPGYQFVD EFHPDLRFDR PYLLAMANAG PGTNGSQFFI
     TTAATDWLNR KHTIFGEVTR GTDVVDKIGK TPTGAQDRPK TDVVVQEIVV ERRPA
//

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