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Database: UniProt
Entry: M7T614_EUTLA
LinkDB: M7T614_EUTLA
Original site: M7T614_EUTLA 
ID   M7T614_EUTLA            Unreviewed;       603 AA.
AC   M7T614;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=UCREL1_892 {ECO:0000313|EMBL:EMR72067.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR72067.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC       subfamily. {ECO:0000256|ARBA:ARBA00038509}.
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DR   EMBL; KB705525; EMR72067.1; -; Genomic_DNA.
DR   RefSeq; XP_007788847.1; XM_007790656.1.
DR   AlphaFoldDB; M7T614; -.
DR   STRING; 1287681.M7T614; -.
DR   KEGG; ela:UCREL1_892; -.
DR   eggNOG; KOG0885; Eukaryota.
DR   HOGENOM; CLU_012062_14_5_1; -.
DR   OMA; CKNFLQH; -.
DR   OrthoDB; 1328057at2759; -.
DR   Proteomes; UP000012174; 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   Isomerase {ECO:0000313|EMBL:EMR72067.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012174}.
FT   DOMAIN          18..193
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          205..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..324
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  65993 MW;  038E10720C47DA72 CRC64;
     MSSIYNLEPQ PTASLILHTT LGDLSVELFA KQTPLASRNF LQLCLDGYYD DTIFHRLVPG
     FILQGGDPTG TGNGGESIYD GGAYGGDLDP WPMDQRRGKN AGPMGVNFKD EAHSRLKFNR
     RGLLGMANES KPDTNGSQFF FTLDKAPELD GKNTMFGRVV GDTIYNLARM GEAEVAEGSE
     RPVYPIKITG VEVLVNPFED MKKRERVAAR SQQQVVSSKP QKKKKPKAGG KKLLSFGDEE
     GGGDDDAPVI KKAKFDTRIV MVEEDEESSA AAPTVKPPKS SSVKKVQDKA VKKSIPAHEP
     TVSKTKPEAT RPPSPPPRHP PQQSREVPNP MYEESSPEPE PEPERPKKSA LERANEEIAA
     LKASMKRTVY EEGQPAKEVK KTALEQLIPE NSTRGRKRRR DGEGAMSNAD FSMFEAFRSK
     LVESASKAPS RSNPSSSKHT SGAAPVEADE GGENSRQQDQ QPDEAAPTTT TTAAAAAAGG
     AEDDDEAELC DLHFIANCQS CRSWAEEDTD EQKKKKKAED EEDEDWITHR LSFAADKLGK
     DLTYRKKAED ELIVIDPREK ARTLKEEQKA RRGGGDGATG REWDQARNAK LARASALAGR
     GAR
//
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