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Database: UniProt
Entry: A0A0F9WR60_9MICR
LinkDB: A0A0F9WR60_9MICR
Original site: A0A0F9WR60_9MICR 
ID   A0A0F9WR60_9MICR        Unreviewed;       169 AA.
AC   A0A0F9WR60;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 30.
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=AAJ76_2200010923 {ECO:0000313|EMBL:KKO75393.1};
OS   Vairimorpha ceranae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC   Vairimorpha.
OX   NCBI_TaxID=40302 {ECO:0000313|EMBL:KKO75393.1, ECO:0000313|Proteomes:UP000034350};
RN   [1] {ECO:0000313|EMBL:KKO75393.1, ECO:0000313|Proteomes:UP000034350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA08 1199 {ECO:0000313|EMBL:KKO75393.1,
RC   ECO:0000313|Proteomes:UP000034350};
RX   PubMed=25914091;
RA   Pelin A., Selman M., Aris-Brosou S., Farinelli L., Corradi N.;
RT   "Genome analyses suggest the presence of polyploidy and recent human-driven
RT   expansions in eight global populations of the honeybee pathogen Nosema
RT   ceranae.";
RL   Environ. Microbiol. 0:0-0(2015).
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|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|ARBA:ARBA00000971,
CC         ECO:0000256|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {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:KKO75393.1}.
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DR   EMBL; JPQZ01000022; KKO75393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9WR60; -.
DR   VEuPathDB; MicrosporidiaDB:AAJ76_2200010923; -.
DR   VEuPathDB; MicrosporidiaDB:G9O61_00g014070; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_101263; -.
DR   OrthoDB; 339082at2759; -.
DR   Proteomes; UP000034350; Unassembled WGS sequence.
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; 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   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D-RELATED; 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|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034350};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          6..166
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   169 AA;  19134 MW;  A4D6AED0BC899FB2 CRC64;
     MSSKCFFDIQ IGNSNPKRIK FLLYDDVVPK TTRNFRELCT QEAPHGYKKS VFHRIIPDFM
     AQGGDFTHGT GVGGKSIYGS KFEDENFIKK HDKKYLLSMA NAGPNTNGSQ FFITFNKCDW
     LNNKHVVFGE VIYDDKKELE ILKEMEAVGS QGGKPKEIVK IVDSGIVEK
//
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