ID   PPIL_MIMIV              Reviewed;         234 AA.
AC   Q5UP71;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Structural PPIase-like protein L605;
DE   AltName: Full=Mimicyp;
GN   OrderedLocusNames=MIMI_L605;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF 188-LYS--LYS-194,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=18342330; DOI=10.1016/j.jmb.2007.08.051;
RA   Thai V., Renesto P., Fowler C.A., Brown D.J., Davis T., Gu W.,
RA   Pollock D.D., Kern D., Raoult D., Eisenmesser E.Z.;
RT   "Structural, biochemical, and in vivo characterization of the first virally
RT   encoded cyclophilin from the Mimivirus.";
RL   J. Mol. Biol. 378:71-86(2008).
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18342330}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:18342330}. Host
CC       cytoplasm {ECO:0000269|PubMed:18342330}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Arg in position 83 necessary for PPIase
CC       activity, and does not display any PPIase activity in vitro
CC       (PubMed:18342330). This protein was presumably a host PPIase stolen and
CC       converted by the virus to play a different function.
CC       {ECO:0000305|PubMed:18342330}.
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; AY653733; AAV50868.1; -; Genomic_DNA.
DR   RefSeq; YP_003987122.1; NC_014649.1.
DR   PDB; 2OSE; X-ray; 2.04 A; A=1-234.
DR   PDBsum; 2OSE; -.
DR   SMR; Q5UP71; -.
DR   GeneID; 9925243; -.
DR   KEGG; vg:9925243; -.
DR   BRENDA; 5.2.1.8; 9231.
DR   EvolutionaryTrace; Q5UP71; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host cytoplasm; Reference proteome; Virion.
FT   CHAIN           1..234
FT                   /note="Structural PPIase-like protein L605"
FT                   /id="PRO_0000064219"
FT   DOMAIN          18..205
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MUTAGEN         188..194
FT                   /note="KPYAGRK->SGSSG: Complete loss of homotrimerization."
FT                   /evidence="ECO:0000269|PubMed:18342330"
FT   STRAND          5..7
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          16..23
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          26..35
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   HELIX           41..52
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   TURN            106..109
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          167..175
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   HELIX           177..186
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   STRAND          198..205
FT                   /evidence="ECO:0007829|PDB:2OSE"
FT   HELIX           209..212
FT                   /evidence="ECO:0007829|PDB:2OSE"
SQ   SEQUENCE   234 AA;  26539 MW;  68B07B450A4B39CD CRC64;
     MNYSLEDLPN SGKNPRVYMD IVLNNEIIGR LQIKLFRDAF PAGVENFVQL TNGKTYRVNS
     NGTGKYKYNR HINRTYEGCK FHNVLHNNYI VSGDIYNSNG SSAGTVYCDE PIPPVFGDYF
     YPHESKGLLS LVPYTDESGN RYYDSTFMIT LDDIRPSNVL DELDRDQVVI GQVYGGLDVL
     DKINSMIKPY AGRKYPTFSI GKCGAYLDSS QAQRKRPVNV NGTKRFLNKP TRVN