GenomeNet

Database: UniProt
Entry: R7Y3K5_9ACTN
LinkDB: R7Y3K5_9ACTN
Original site: R7Y3K5_9ACTN 
ID   R7Y3K5_9ACTN            Unreviewed;       168 AA.
AC   R7Y3K5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
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   ORFNames=CF8_0010 {ECO:0000313|EMBL:EON25825.1};
OS   Nocardioides sp. CF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=110319 {ECO:0000313|EMBL:EON25825.1, ECO:0000313|Proteomes:UP000015971};
RN   [1] {ECO:0000313|EMBL:EON25825.1, ECO:0000313|Proteomes:UP000015971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF8 {ECO:0000313|EMBL:EON25825.1,
RC   ECO:0000313|Proteomes:UP000015971};
RX   PubMed=23833136;
RA   Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT   "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT   of Its Metabolic Capabilities.";
RL   Genome Announc. 1:e00439-e00439(2013).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|ARBA:ARBA00002388,
CC       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|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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:EON25825.1}.
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; ASEP01000001; EON25825.1; -; Genomic_DNA.
DR   RefSeq; WP_010831105.1; NZ_CM001852.1.
DR   AlphaFoldDB; R7Y3K5; -.
DR   STRING; 110319.CF8_0010; -.
DR   PATRIC; fig|110319.3.peg.10; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_3_11; -.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000015971; 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   CDD; cd00317; cyclophilin; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 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   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:EON25825.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015971};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          13..166
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   BINDING         57..68
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         73..74
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         99..104
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         109..113
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         119
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT   BINDING         125
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
SQ   SEQUENCE   168 AA;  17901 MW;  8FEDA3B747AC3621 CRC64;
     MADPKATLKT NQGDIVINLF PNHAPETVDN FVGLAEGTKD YSAGDRSGPF YDGLGFHRVI
     EGFMIQGGCP QGTGTGGPGY TFKDEVHPEL VFDKPYLLAM ANAGPGTNGS QFFITLGATP
     WLNRKHTIFG EVADQSSRDV VDKIGATRTG AGDRPVDAVV IESVTIER
//
DBGET integrated database retrieval system