(data stored in SCRATCH zone)

SWISSPROT: C7QFR1_CATAD

ID   C7QFR1_CATAD            Unreviewed;       193 AA.
AC   C7QFR1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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=Caci_0045 {ECO:0000313|EMBL:ACU69000.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69000.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69000.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000256|RuleBase:RU363019}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; CP001700; ACU69000.1; -; Genomic_DNA.
DR   STRING; 479433.Caci_0045; -.
DR   EnsemblBacteria; ACU69000; ACU69000; Caci_0045.
DR   KEGG; cai:Caci_0045; -.
DR   eggNOG; ENOG4107XH4; Bacteria.
DR   eggNOG; COG0652; LUCA.
DR   HOGENOM; HOG000065981; -.
DR   KO; K03767; -.
DR   OMA; TSIYGQK; -.
DR   OrthoDB; POG091H01WZ; -.
DR   Proteomes; UP000000851; 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.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PTHR11071; 1.
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; C7QFR1.
DR   SWISS-2DPAGE; C7QFR1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00156,
KW   ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:ACU69000.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00156,
KW   ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN       20    188       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
SQ   SEQUENCE   193 AA;  21319 MW;  A87BED4A24B59A38 CRC64;
     MTETERQQTV AENLYATIKT NHGDIVVRLL PDYAPKTVAN FVGLAEGTRE WTHPETNVTS
     TTPLYDGTIF HRIIPQFMIQ GGDPLGQGFG GPGYVFDDEP HPDQTFNDRD YLLAMANAGI
     RNGKGTNGSQ FFITVPTPRR PTHLNGKHTI FGEVVDADSR KVVDEIAGVR TGAQDRPVND
     VVIEKISIER REG
//

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