ID A0A2J6SNE0_9HELO Unreviewed; 618 AA.
AC A0A2J6SNE0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 1 {ECO:0000256|ARBA:ARBA00040798};
GN ORFNames=K444DRAFT_575354 {ECO:0000313|EMBL:PMD52285.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD52285.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD52285.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD52285.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ613912; PMD52285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6SNE0; -.
DR STRING; 1095630.A0A2J6SNE0; -.
DR InParanoid; A0A2J6SNE0; -.
DR OrthoDB; 275452at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-EC.
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; 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; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT REPEAT 63..95
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 107..148
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 472..617
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 69469 MW; D49C9B068139793E CRC64;
MTGDDSETQS KKRSRSDDDN SSSDDDMGPQ LPSTDAPKKK RRKLPYEKLY ISALPTSARY
SKSLMHKEQL AFVTMTPLTD FLITSSVDGV VKFWKKGAEG IEFVKEFRAH NGEIKSVSVS
ADGRSFATAG ADKSIKIFDV MTFDLLSMLT VEFTPKCVCW IHKRGASLPL LAVSDEVNHT
IRIYDGRGEN QEPIHTISGL HRSVVSLMAF NDAYDCVISA DENGMIEYWR PGSYEKPNNV
FEYKSSTDLF EFKKAKSTPA SLTISPSGSQ FATFSFPDRK IRVFNFPTGK LYRTYDESLQ
TIEEMQQAGT ALQKLEDLEF GRRLGVEREL DNPAFRNKVN VIFDETGHFI IYGSMLGTKV
LNTYTNRVVK VYGKDENFRP LSIAMYQGQP QKKGITTVAM AASNNPLLQE SEARDPILFT
TGVGKVRFYM FTNDENISKS ERDVQNEKPT NPHAKKAVEA KAAETGTAAI IHTTYGDIHI
RLFPDAAPKA VENFVVHSKQ GYYNNTIFHR VIRKFMIQCG DPLGDGTGGE SIWGKEFEDE
FSTLKHDKPY TVSMANAGPN TNGSQFFITT DKTAWLDNKH TIFGRAIQGL DIIHKIENAK
VYKEKLEEDI KILNIEIM
//
