ID   A0A066WDQ1_TILAU        Unreviewed;       767 AA.
AC   A0A066WDQ1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KDN52082.1};
GN   ORFNames=K437DRAFT_221320 {ECO:0000313|EMBL:KDN52082.1};
OS   Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX   NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN52082.1, ECO:0000313|Proteomes:UP000027361};
RN   [1] {ECO:0000313|EMBL:KDN52082.1, ECO:0000313|Proteomes:UP000027361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBC 951 {ECO:0000313|EMBL:KDN52082.1,
RC   ECO:0000313|Proteomes:UP000027361};
RG   DOE Joint Genome Institute;
RA   Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA   Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT   "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT   951.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675}.
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:KDN52082.1}.
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DR   EMBL; JMSN01000014; KDN52082.1; -; Genomic_DNA.
DR   RefSeq; XP_013244932.1; XM_013389478.1.
DR   AlphaFoldDB; A0A066WDQ1; -.
DR   STRING; 1037660.A0A066WDQ1; -.
DR   GeneID; 25262318; -.
DR   HOGENOM; CLU_005070_4_0_1; -.
DR   InParanoid; A0A066WDQ1; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000027361; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 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; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002078; Sigma_54_int.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:KDN52082.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027361}.
FT   DOMAIN          432..626
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   REGION          364..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          263..343
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   767 AA;  84641 MW;  CC88599C267F068C CRC64;
     MGGNDQSSQS PLEKYTTDLT QLAADGKLDP VIGRDAEVRR TLQVLARRTK SNPVLLGPAG
     VGKTAIMEGL AQRIANREVP ESLLDKSVKS LDLAGLLAGA GVRGMFEERI KALLQEIEKQ
     EGKIILFIDE IHMLFGLGKA EGALDAANMM KPLLARGVLR LCGATTFEEY RNTIEKDAAL
     ARRFQPVMVK EPSLSATISI LRGLRGRYEA FHGIGISDSA LVTAAQYAER YLSERKNPDA
     AIDLLDEAAS ALRLQQESKP EAIESLERNV ITMQIELESL RHETDIASKS RRDTLEIELR
     DKKEEMERLT AVWNEEKRKL DDVRDIKEKL EDAQVELERM TREGNLQRVA ELQYAVIPEL
     KKRLPQEDED GSSQEGQQGQ DDKDQGSFLH DRVTSEDIAA VVARTTGIPV SNLLRGDRER
     LLHIEDSLRQ RIVGQDEALT TMAEAIRLSR AGLQSQTKPL ASFLMLGQTG TGKTETCKAV
     ADFLFDSKDA LIMLDCSELS EQHSISKLVG APPGYIGYDQ AGGLTERVRR KPYSIILFDE
     IEKAARSVQM VLLQILDEGK LTDAQGRQVD FRQTIVVCTS NLGAEVLSES GATTPDGKLT
     CRAKESVSSA VQHALPPELL NRFDEILHYN RLSRDSLRGI VDIRLKEIQA RLTDRRIELA
     VDDGAKQWLA TNGYSDIYGA RPLNRLIQKA LLTPLAKVLI EGSVRDGDTV FMGLKKDAKP
     DEEAIVISGI RHEQTTAAAN ADTTCASAVA EDIGPDVIEG EILPLRK
//