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Database: UniProt
Entry: A0A1Y2BGV3_9TREE
LinkDB: A0A1Y2BGV3_9TREE
Original site: A0A1Y2BGV3_9TREE 
ID   A0A1Y2BGV3_9TREE        Unreviewed;       897 AA.
AC   A0A1Y2BGV3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Putative heat shock protein {ECO:0000313|EMBL:ORY33956.1};
GN   ORFNames=BCR39DRAFT_517928 {ECO:0000313|EMBL:ORY33956.1};
OS   Naematelia encephala.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Naemateliaceae; Naematelia.
OX   NCBI_TaxID=71784 {ECO:0000313|EMBL:ORY33956.1, ECO:0000313|Proteomes:UP000193986};
RN   [1] {ECO:0000313|EMBL:ORY33956.1, ECO:0000313|Proteomes:UP000193986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-887.2 {ECO:0000313|EMBL:ORY33956.1,
RC   ECO:0000313|Proteomes:UP000193986};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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:ORY33956.1}.
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DR   EMBL; MCFC01000004; ORY33956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2BGV3; -.
DR   STRING; 71784.A0A1Y2BGV3; -.
DR   InParanoid; A0A1Y2BGV3; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000193986; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193986};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:ORY33956.1}.
FT   DOMAIN          1..154
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          871..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          422..509
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        877..897
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   897 AA;  99541 MW;  0C0078DCD430C11C CRC64;
     MDNFTDKSSE VLKAAFNRAE EMANSQVAPL HLISVLYEDP VSAPGGAEQP TLLKGALEAI
     GGNTTSFSRG MMSRLNKLPV IDPPPAPPLS LTNQMNAVIR NAQKLQKEQN DQFVAVDHLV
     LALVHESLDM KELLKQAGVD GKKLEDEVKR KRGGRKADSR GAEGQFEALA KYCQDLTALA
     EQGKIDPVIG RDNEIRRVIR VLSRRTKGNP VLIGEPGVGK TAIVEGLAQR IVDRDVPASL
     LSRLLALDMG ALMAGAKYKG EYEERVKAVL SEVEKSGDEG TQIILFIDEI HLIMAGKDSS
     GGMDAANLLK PMLARGKLKV IGATTLNEYR EYIEKDSAFE RRFAQVLVEE PSVPDTVAIM
     RGIREKYETH HGVRIMDSAL VLAAQLAKQY LTSRRLPDSA IDLLDEASSA VKVARETRPE
     AIDELERKKL GLEVEVHALE REKDEASKER LEAAKRAIAE VEDQLGPLKR EYENEKHLGD
     EIHDVRRRID ELRAKADEAE RRYDLATAAD IRYHSIPQRE AKLKELEQRE AERGGGQQVT
     PEMIAEVVGR WTGIPVSRLV ETEKAKLLRL EKLISKKVIG QPEAVRAVAN AIRLNRSGLS
     NQNRPIASFL LVGPSGTGKT LLAKTLAGVM FNSEEAMVRI DGSEYSEKHS VSRLIGAAPG
     YIGHESGGQL TEAVRRKPYS LILIDEIEKA AREFHQLFLQ VLDDGRLTDN KGRVVDFRNT
     IIMMTSNVGS AYLNENPSEG PVRPEVREKV QSAISATFPP EFINRIDDII LYRSLSRADI
     RKVVDVRLRE IQKRLDDNGR KIRLAVDETA TDWLASAGYS PTYGARPMAR LIQTEILNPL
     SKLLLQARIK DGETAHVTAD VRKNRLVVIP NHDQDVSMPD DEEESEDGMD IEVEEVD
//
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