ID K1VX28_TRIAC Unreviewed; 474 AA.
AC K1VX28;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=A1Q2_01701 {ECO:0000313|EMBL:EKD04027.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD04027.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD04027.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD04027.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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 -!- 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:EKD04027.1}.
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DR EMBL; AMBO01000237; EKD04027.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VX28; -.
DR STRING; 1220162.K1VX28; -.
DR eggNOG; KOG0546; Eukaryota.
DR HOGENOM; CLU_604366_0_0_1; -.
DR InParanoid; K1VX28; -.
DR OMA; MSEGSDM; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
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 H; 1.
DR Pfam; PF00160; Pro_isomerase; 2.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:EKD04027.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT DOMAIN 46..160
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 164..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 55315 MW; B5F72C6A249D1C0D CRC64;
MNATGVLHTI HHAEPAHLLR PYGQRQAPGA RCGKLNDPLC SADDSSNSLP MSNSSFRALC
VGHQGPDGLQ GYKGSPIHRV IDGFMIQGGD YTKRNGTGGA SIYGGMFKDE RLEGPGTEVD
KEGVFGRVVS GMEYIATIGK LDTDERDRPL SPVIVSHCGE LELRRRARTP SPTPSEDSEE
EYRRRKRERR ERKEKEREER RRERKERRRD RSRSPSRRDT EDREDRDRSD RRDRKDRKDK
KERRSGRRRS DSRDSRDSRS RSPFETLSEL DARLLREETE RLEAERKARE EEKRARIAAE
RERAKESGGI VYKGRGTMRY RDPDARWDTW GRPENYNARG QDTRSRFRRR DGGGDRWERG
MDVRADRFER ERGDRGGRDS RERFDRWDHG RRGRDERDDK RDDRREEEER KKLDQDLDKS
LAERISLNYE EKPAEPAEGK EQRASAWNAA RRASPSPDRG ARSPSSDMVM DDDD
//
