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}.
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; 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
//