ID L8LVR2_9CYAN Unreviewed; 251 AA.
AC L8LVR2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Parvulin-like peptidyl-prolyl isomerase {ECO:0000313|EMBL:ELS01784.1};
GN ORFNames=Xen7305DRAFT_00014900 {ECO:0000313|EMBL:ELS01784.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS01784.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS01784.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS01784.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELS01784.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ALVZ01000216; ELS01784.1; -; Genomic_DNA.
DR RefSeq; WP_006511117.1; NZ_ALVZ01000216.1.
DR AlphaFoldDB; L8LVR2; -.
DR STRING; 102125.Xen7305DRAFT_00014900; -.
DR PATRIC; fig|102125.3.peg.3964; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 507969at2; -.
DR Proteomes; UP000011203; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 1.
DR Pfam; PF00639; Rotamase; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:ELS01784.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011203};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278}.
FT DOMAIN 114..206
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 251 AA; 29341 MW; 5A88EA25DD4E119B CRC64;
MGVVLRIGNR VFNSDELSPL LAQYQMLPKL AQEILVDHEV ANIDYTEQEY EQAYQQFCQQ
FQLDTEEKIQ LWLDKQGMDR DNLKALVTRK VKIEKYKIEN WDNKVESFFL KRKAQLDRVV
YSLIRVEKAE LAQELYFRIQ ENEDSFRELA MEFSQGSESQ TGGLIGPVEI NAPHPKIAQI
LNTCQPGDLV PPTRVGEWIV IIRLENFIPA KLDEPMRQRM LDEMFRKWLN QQTAEEVSFF
PEPVISTPVT S
//
