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Database: UniProt
Entry: A0A1R0H6N7_9FUNG
LinkDB: A0A1R0H6N7_9FUNG
Original site: A0A1R0H6N7_9FUNG 
ID   A0A1R0H6N7_9FUNG        Unreviewed;       140 AA.
AC   A0A1R0H6N7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
GN   ORFNames=AYI68_g1081 {ECO:0000313|EMBL:OLY84748.1};
OS   Smittium mucronatum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY84748.1, ECO:0000313|Proteomes:UP000187455};
RN   [1] {ECO:0000313|EMBL:OLY84748.1, ECO:0000313|Proteomes:UP000187455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY84748.1,
RC   ECO:0000313|Proteomes:UP000187455};
RX   PubMed=27343289; DOI=10.1093/molbev/msw126;
RA   Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT   "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT   Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL   Mol. Biol. Evol. 33:2544-2554(2016).
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:RU363014};
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:OLY84748.1}.
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DR   EMBL; LSSL01000376; OLY84748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R0H6N7; -.
DR   STRING; 133383.A0A1R0H6N7; -.
DR   Proteomes; UP000187455; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR001202; WW_dom.
DR   PANTHER; PTHR10657; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR10657:SF4; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187455};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014}.
FT   DOMAIN          1..19
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          29..140
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          8..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   140 AA;  15578 MW;  E36FE9ABD38C2A4D CRC64;
     MPYYFNTVTR ESRWDPPSGK DVTTHDSSSE KVRVSHLLIK HNESRRPSSW KQDNILRSKQ
     EAIEIAKTLQ KQIQSGIATL PELASSESDC PSAKRQGDMG YFGRGQMLPA FESTAFNLSV
     GQLSDPVSTD SGIHLILRTA
//
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