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Database: UniProt
Entry: A0A1Z5TF44_HORWE
LinkDB: A0A1Z5TF44_HORWE
Original site: A0A1Z5TF44_HORWE 
ID   A0A1Z5TF44_HORWE        Unreviewed;       566 AA.
AC   A0A1Z5TF44;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=BTJ68_04221 {ECO:0000313|EMBL:OTA34647.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA34647.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA34647.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA34647.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC       subfamily. {ECO:0000256|ARBA:ARBA00038509}.
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:OTA34647.1}.
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DR   EMBL; MUNK01000056; OTA34647.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TF44; -.
DR   STRING; 1157616.A0A1Z5TF44; -.
DR   VEuPathDB; FungiDB:BTJ68_04221; -.
DR   InParanoid; A0A1Z5TF44; -.
DR   OrthoDB; 1328057at2759; -.
DR   Proteomes; UP000194280; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd01925; cyclophilin_CeCYP16-like; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 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   PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   PANTHER; PTHR45625:SF6; SPLICEOSOME-ASSOCIATED PROTEIN CWC27 HOMOLOG; 1.
DR   Pfam; PF00160; Pro_isomerase; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT   DOMAIN          18..171
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          178..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  62228 MW;  73CAD46D5725D9C3 CRC64;
     MSALYNLEPQ PTAKCILHTT AGDLLLELFA KQTPLASRNF LQHCLDGYYT NTVFHRLVKD
     FIIQGGDPTG TGAGGESALN HGQPFQDEIH TRLKFNRRGL LGMANEGKDS NGSQFFLTLA
     ATPELQGRHT MFGRIEGDTI FNLMKMAEAE MEEGADAERP LYPTRVTGAE ILVNPFEDMV
     PRVKEAPRTR DDEGRREGAG SVKKRKKPAG MNVLSFAGDD EDGKGEGEVK PVKKKSKANP
     KLVSVGEEQP EELNNTKVPD APPVKERKKQ LPRAPEPEEE VVPDVMEDSR AQPIPARKPT
     EDTPDEDKDD DDEYSEDDDD RQRHRQRQQK TALDTTNAEI AALKASMKRT VDTGPKEQHE
     KPKSALESMI PSTSTRGRKR GKVGDEKGAM DLFKQFKSKL EVLPAEKTSG ENAAAGSRPE
     DKSNETGSPD QAGQGEDGGR SVSSTANGKP SDPTDEEEVL CDLHFIANCQ SCKAWIDDND
     PTAPNGEGGD GNNLDDDNDP SSSWMAHSLT FAKDTLGKDL EWKRKMEEIE IIDPREKARE
     LGVEKGGKKG ERGRDGLGKG KGKRRE
//
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