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
//