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Database: UniProt
Entry: A0A316UVZ5_9BASI
LinkDB: A0A316UVZ5_9BASI
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ID   A0A316UVZ5_9BASI        Unreviewed;       912 AA.
AC   A0A316UVZ5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:PWN28491.1};
GN   ORFNames=BDZ90DRAFT_231477 {ECO:0000313|EMBL:PWN28491.1};
OS   Jaminaea rosea.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Jaminaea.
OX   NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN28491.1, ECO:0000313|Proteomes:UP000245884};
RN   [1] {ECO:0000313|EMBL:PWN28491.1, ECO:0000313|Proteomes:UP000245884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN28491.1,
RC   ECO:0000313|Proteomes:UP000245884};
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; KZ819665; PWN28491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316UVZ5; -.
DR   STRING; 1569628.A0A316UVZ5; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000245884; 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   Hydrolase {ECO:0000313|EMBL:PWN28491.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245884};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          4..165
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          44..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          431..520
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        48..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..912
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   912 AA;  99427 MW;  B34E01D789728E16 CRC64;
     MSSMPDFTDK AAASLNAAIQ LAKDHAHPQV QPAHLALALL TDDAAASSKR PGTPSTSASP
     TDSLFRSVLT KAGVDVNKFE QSLRAALRKT PQQNPPPDDV SLSGAAAKIL RSAESHKSQQ
     HDSFVAQDHL LLALLDDSTI ETQLKSAGLA NKQLLKTAIS SSRGARRIDT RNAEQGFDAL
     NKYCVDLTAL ATEGKIDPVI GRDETLRRVV RVLSRRTKNN VALIGEPGVG KTAVVEALAQ
     RIVDNDVPPS LTGRLLSLDM GSLMAGAKFK GEFEERVKSV LEEIEKAQET TPVILFIDEM
     HLIMAGREGG SMDAGNLVKP ALARGKLRCI GATTLNEYRT SIEKDSALER RFQTVIVQEP
     TVEQTVSILR GIKDKYQHHH GVRITDPALV SAARLAKRHL TARKLPDAAI DLVDEACADT
     RVTRETVPAH IDDMQRRKIE LEVAVHALER EAKKDAASKE SLDAARKDLA SLEENLQPAL
     AEWEAKRAKG DELANAKRRL DELRSKAEAA ERRRDVATAA DLKYGAIPDL ENRIVALEAE
     EKARAEKEDN AEGTVGPEQI ATIVARWTGI PLTKLQEGEK EKLLRLEKLL SREVVGQPEA
     VKAVADSIRL SRSGLADPNR PVSFLFAGPS GTGKTLTAKS LAKLLFDDET AMVRIDASEY
     SEKHAVARLL GAPPGYVGYE QGGTLSEAVR RKPFSVILVD ELEKAAREFV QLWLQILDDG
     RATDGQGRTV SFKDTLIVFT SNLGAQFVND DASETLTPNT INLVQGALAA HLPPEFRNRL
     SATVVFQKLT RANIQSIVDQ RVREITARLR ANGRRIAIEL SAEARTYLGE RGYDPSMGAR
     PLQRVITNEV LSPLSILLLR GGVRDGETAR IGYDAASKRI VVAPNHELEA IGEDAMDTDD
     MEDDQIDEEP LD
//
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