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Database: UniProt
Entry: A0A316UAD4_9BASI
LinkDB: A0A316UAD4_9BASI
Original site: A0A316UAD4_9BASI 
ID   A0A316UAD4_9BASI        Unreviewed;       918 AA.
AC   A0A316UAD4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Putative heat shock protein HSP104 {ECO:0000313|EMBL:PWN21431.1};
GN   ORFNames=BCV69DRAFT_282156 {ECO:0000313|EMBL:PWN21431.1};
OS   Pseudomicrostroma glucosiphilum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Pseudomicrostroma.
OX   NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN21431.1, ECO:0000313|Proteomes:UP000245942};
RN   [1] {ECO:0000313|EMBL:PWN21431.1, ECO:0000313|Proteomes:UP000245942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN21431.1,
RC   ECO:0000313|Proteomes:UP000245942};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; KZ819325; PWN21431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316UAD4; -.
DR   STRING; 1684307.A0A316UAD4; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000245942; 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; 3.
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:UP000245942};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:PWN21431.1}.
FT   DOMAIN          3..165
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          432..521
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   918 AA;  100016 MW;  13BE50CB3D1F5DC1 CRC64;
     MTTPDFTDKA ASSINTAVQL AKDYSHPHVV PAHIALALLT ESSGPAASSS RPATPSGASA
     NDSLFKSVLS KAGVTPSKVE DALRATLRKT PQQNPPPTDL SFNGAAAKVI KKASEIKATQ
     HDNFVAQDHL LLALIQDPTI EALLKTHGLA NTQLLVTAIN QARGNRRVDT KTEGEFDALN
     KYCVDLTALA ADGKIDPVIG RDEEIRRIAR ILSRRTKNNC ALIGEPGVGK TAVAEGLAMR
     IVDRDVPPSL IARLLSLDTG ALMAGAKYKG EYEERVKAVL DEIEKSQDAG TGIILFVDEA
     HLLMSGRGGD SGMDAANLIK PALARGKLRM IAATTTKEYR EYIEKDPAFE RRFSLVQVAE
     PTVDQCISIL RGIKEKLENH HGATIKDSAL VAAARLAKRY LSQRRLPDAA IDLVDEASAD
     VSVTSETVPA QIDALQRRKV ELEVAIHALA REAKKDPASK EALEAARKDL SELQETLAPA
     LAQWESKRAK GDELNNAKRR LDELKAKAEA AERRYDLQTA ADIRYGAIPD LEHRIAVLED
     EERKRHESGE DEGQNVVGAE QIATIVARWT GIPVTKITEG ELQKLLKLEK LLRKEVIGQP
     EAVKAVADAV RLSRSGLSDP GKPISFLFAG PSGTGKTLTA KALAKLLFDD ESAMLRIDAS
     EYSEKHSVSR LIGAAPGYVG YESGGQLTEK VRRRPFSVIL VDELEKASRE FVQIWLQVLD
     DGRLTDGQGR LVSFKDTVII FTSNLGAQYI NDSSADALTP ETISLVNASL AAALPPEFRN
     RLSASVIFGK LTRNDIKAIV GARIREVQQR LRANGRRITV DVDEEAMAYL AERGYDPAMG
     ARPLARVIQN ELLSPLSILL LKGGILDNEV ARVTYDSAKM KILVLPNHEV TEMDADMDDE
     DEYEMDMEDQ DMKVEPLD
//
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