(data stored in SCRATCH zone)

SWISSPROT: A8FQH4_SHESH

ID   A8FQH4_SHESH            Unreviewed;       262 AA.
AC   A8FQH4;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   OrderedLocusNames=Ssed_0484 {ECO:0000313|EMBL:ABV35097.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35097.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35097.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35097.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000256|RuleBase:RU003915}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC       {ECO:0000256|RuleBase:RU003915}.
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DR   EMBL; CP000821; ABV35097.1; -; Genomic_DNA.
DR   RefSeq; WP_012140834.1; NC_009831.1.
DR   ProteinModelPortal; A8FQH4; -.
DR   STRING; 425104.Ssed_0484; -.
DR   EnsemblBacteria; ABV35097; ABV35097; Ssed_0484.
DR   KEGG; sse:Ssed_0484; -.
DR   eggNOG; ENOG4108V1T; Bacteria.
DR   eggNOG; COG0545; LUCA.
DR   HOGENOM; HOG000154888; -.
DR   KO; K03772; -.
DR   OMA; MGANPHK; -.
DR   OrthoDB; POG091H05SW; -.
DR   BioCyc; SSED425104:GH7Q-506-MONOMER; -.
DR   Proteomes; UP000002015; 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; 1.10.287.460; -; 1.
DR   InterPro; IPR023566; PPIase_FKBP.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   PANTHER; PTHR43811; PTHR43811; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQH4.
DR   SWISS-2DPAGE; A8FQH4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915, ECO:0000313|EMBL:ABV35097.1};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    262       Peptidyl-prolyl cis-trans isomerase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002719938.
FT   DOMAIN      151    236       PPIase FKBP-type. {ECO:0000259|PROSITE:
FT                                PS50059}.
SQ   SEQUENCE   262 AA;  28485 MW;  A6F0E3CA81DC6B6A CRC64;
     MKTFKKSIIA ISCLPLFLSV QCMAETELLA DSNKESYSIG ASFGSYISSQ LYSQSQLGAE
     VDVDIVVEGL LDALKGQSKL SNEDIVSYLN IRAEQLNTAK EEKDKDLALK NLVAGEKFLA
     ENKKSADVRT TESGLQYEVI SQGSGAKPQA NDVVTVHYKG YLIDGTEFDN SYTRDEANRF
     SLVTVIEGWQ EGLQLMKEGA KYKFNIPSEL AYGERQVGMI SPNSALVFEV ELVKVEAPGE
     NAHGMGLSGM GMGGMMGANP HK
//

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