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Database: UniProt
Entry: R4X9X3_TAPDE
LinkDB: R4X9X3_TAPDE
Original site: R4X9X3_TAPDE 
ID   R4X9X3_TAPDE            Unreviewed;       932 AA.
AC   R4X9X3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   22-FEB-2023, entry version 32.
DE   SubName: Full=Related to stress protein ORP150 {ECO:0000313|EMBL:CCG81029.1};
GN   ORFNames=TAPDE_000708 {ECO:0000313|EMBL:CCG81029.1};
OS   Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS   / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Taphrinaceae; Taphrina.
OX   NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG81029.1, ECO:0000313|Proteomes:UP000013776};
RN   [1] {ECO:0000313|EMBL:CCG81029.1, ECO:0000313|Proteomes:UP000013776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC   NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX   PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA   Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA   Overmyer K., Hauser P.M., Pagni M.;
RT   "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT   agent of peach leaf curl.";
RL   MBio 4:e00055-e00013(2013).
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:CCG81029.1}.
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DR   EMBL; CAHR02000023; CCG81029.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4X9X3; -.
DR   STRING; 1097556.R4X9X3; -.
DR   VEuPathDB; FungiDB:TAPDE_000708; -.
DR   eggNOG; KOG0104; Eukaryota.
DR   Proteomes; UP000013776; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10230; HYOU1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013776};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..932
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004381956"
FT   REGION          547..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          843..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..571
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..748
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  101964 MW;  0CB180AB34C32DC1 CRC64;
     MRLPSVHLLL WHAASAAVLS IDYGTEWTKA ALVKPGIPLE IVLTKDTKRK EQSVIAFKGE
     ERLYGGDAAN MGARIPQYTY PALKSLLGKS YDSKAVKEYN LLYPAVKLSQ TAQNGIAVGQ
     GAETFTVEEL VAMEFINMRK NAELMASGEI RDAVLTVPPF FDHRQRAALL TAAELANLRP
     LELLNDGLAV AMDYAKSRTF DQPQIHAIFD VGAGSTSATI VRFSSASVKD VGRLNKTVTT
     IEVLGTEATD RVSGNVMSER IFHHLVEEFD TSKAEKASSS VKTNPRALAR LLKEATRVKQ
     VLSANNEAAV SVESLHDDLD FRYKITRTTF ERLTSDLGTV TTEVVAKALT IAKTAVSEID
     SLILHGGAAR VPFVQKALLD VVAESQIARN VNADEAAVMG AVFRGAGLSG SFRVKELQIR
     DVSAIRYSYE QGRTRETLFE QNTSFGTTKN ITLPNVDADF EIIITSDMPQ TVQAAQEVAN
     FAFQDVSNSV NSFVKKSGCQ AADLVITFIL NYSGIATIHD ASVVCEVDDR PGVADKLKGW
     FGSKESATAK DTGEKGKTVT ENAEDEPPKK LQKSKRLSYV SSNTAHSLQH NEKELSLGKI
     AKYEKFDNQR IALQTARNGL EAYIYKVRDL LENDGFQQVS SDREREDLKA LAAAANEWIY
     DEGESATLDE LVSKKKAMTD ISDKVLFRKQ ESGLRQQKID ALQKQLSSAR KFIKTQSAKI
     AEYASKVAEN SEKAKRDAAT KKSNSDEDDN GNEEQEITDT GDSNSSNTTK DDEIELPEPV
     YSETELTNLG DKLDRNEKWL SIKIAEQAAL GSAEDPALLT ADLEKRTSRI TEDFMYLLRK
     ATYAEQSKTK SKPKQKSSTV RPKTKTSASA QSASSQKDAA SKATRINSQD APEPSPAVTP
     SAGEQVADPS TERNDPVPEA APVANDEKHD EL
//
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