ID A0A316ZDK5_9BASI Unreviewed; 653 AA.
AC A0A316ZDK5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase cyp15 {ECO:0000313|EMBL:PWN99611.1};
GN ORFNames=FA09DRAFT_328415 {ECO:0000313|EMBL:PWN99611.1};
OS Tilletiopsis washingtonensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC Tilletiopsis.
OX NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN99611.1, ECO:0000313|Proteomes:UP000245946};
RN [1] {ECO:0000313|EMBL:PWN99611.1, ECO:0000313|Proteomes:UP000245946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN99611.1,
RC ECO:0000313|Proteomes:UP000245946};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819287; PWN99611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316ZDK5; -.
DR STRING; 58919.A0A316ZDK5; -.
DR OrthoDB; 275452at2759; -.
DR Proteomes; UP000245946; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01927; cyclophilin_WD40; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:PWN99611.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245946};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT REPEAT 73..105
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 117..158
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 498..652
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 71470 MW; 10B3CF48EBD1D517 CRC64;
MGKRAASASA SPSSRSPSRS ASPERAPGVV VAVDADDAAP AAGAASARKR RRTLPYEALY
LAGLPDASRY YKSLMHRDTL SFVTLTPHSH FLVTASADGH VKFWKKQEVG IEFVKHYKAH
TAPITAVACS ADGALYASVG KDGSAKVFDV ANFDLINMLT LGYTPRACAW VHKGGRAGSV
LAIAEEGSNV IRFYDGRGDG TPTAVVDSVH RAPVHLLAYN QVYDTIVSAD ISGMVEYWSP
REPYELPKGN GLWEYKSQTD LFDFKKSKSV PATLTFSPDY QRFNTTSPSD RQIRVFNFAT
GKLLRKYDES LKSIQEMQSN GAAATKLDDM EFGRRLALER DIDASADGAV GDAVRSAGGA
MTANAVFDES GNFLLYGSML GIKVLNIVTN KVAMLLGKDE TIRFLNVSIF QGAAKRTVKS
IALAASENPL AQEKDTLDPT LFCTAYKRAR FYLFTKQEPE SDPRSRNGAE RDVFNEKPTR
EEQTIASAAP GAKLRSKVAS TAVLHTTMGD IHLRLFADQV SKTVENFVGL ARKGYYDNVL
FHRVIPKFML QTGDPLGDGT GGESLWGREF EDEFKKELRH DRPYTLSMAN AGPNTNGSQF
FITTVPTPWL DNKHTVFGRC VAGLDVVHAI ENVRCDKSDR PREDIKILNV TIA
//
