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Database: UniProt
Entry: A0A437MIZ9_9PROT
LinkDB: A0A437MIZ9_9PROT
Original site: A0A437MIZ9_9PROT 
ID   A0A437MIZ9_9PROT        Unreviewed;       335 AA.
AC   A0A437MIZ9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE   AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN   ORFNames=EOD42_07235 {ECO:0000313|EMBL:RVT97609.1};
OS   Rhodovarius crocodyli.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Rhodovarius.
OX   NCBI_TaxID=1979269 {ECO:0000313|EMBL:RVT97609.1, ECO:0000313|Proteomes:UP000282957};
RN   [1] {ECO:0000313|EMBL:RVT97609.1, ECO:0000313|Proteomes:UP000282957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP-6 {ECO:0000313|EMBL:RVT97609.1,
RC   ECO:0000313|Proteomes:UP000282957};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000256|ARBA:ARBA00007656}.
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:RVT97609.1}.
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DR   EMBL; SACL01000002; RVT97609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437MIZ9; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000282957; 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:SF1; FOLDASE PROTEIN PRSA; 1.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 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   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000313|EMBL:RVT97609.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282957};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..335
FT                   /note="Parvulin-like PPIase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018970084"
FT   DOMAIN          180..270
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          22..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  35680 MW;  D41979C309C2E02F CRC64;
     MRRIALLAAT FLAGAPAFAQ APPPVAAPPG ARPAAPSAAP SAAPSAAAPA APAAAGTPAA
     AEDPVLARVE GEAIKLSDVL AAAGDVLPPE LRNVPPEALA SMLPPEAMRQ LVERTITDRA
     LGIAARRAGL QNDPELRARL ARLEQQELTQ ALLRREVLPR VTDEAVRARF DRDFANRPAE
     EEVRARHILV PTEAEARAAL ADIQRGQDFD EVGRRFAQGT GTRESGELGW FKRGDMVPEF
     SAAAFGMQPG QVSAQPVRTQ FGWHVIKVDE RRSSQGPSFD DSKEEIRQRL LQEEVQAAVE
     RIRGTVNIER VTPPAAPGGL MQGAQPPAAP APARR
//
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