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Database: UniProt
Entry: A0A066XCS8_COLSU
LinkDB: A0A066XCS8_COLSU
Original site: A0A066XCS8_COLSU 
ID   A0A066XCS8_COLSU        Unreviewed;       719 AA.
AC   A0A066XCS8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Putative ATPase {ECO:0000313|EMBL:KDN66702.1};
GN   ORFNames=CSUB01_01787 {ECO:0000313|EMBL:KDN66702.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66702.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN66702.1}.
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DR   EMBL; JMSE01000907; KDN66702.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XCS8; -.
DR   STRING; 1173701.A0A066XCS8; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_0_1; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000027238; 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; 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; 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:SF176; 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; 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:UP000027238}.
FT   DOMAIN          47..191
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          443..594
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          621..712
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          260..340
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   719 AA;  79771 MW;  B51C380675BA64BC CRC64;
     MGGEPEKPAL EQFGIDLTAK AKEGRLDPVI GRDAEIQRTI QILSRRTKNN PVVIGKAGTG
     KTAILEGLAL RIVRGDVPES IKNKRVIALD LGSLIAGAKF RGDFEERLKK VLTEVQQAEG
     EVILFIDELH TLLGLGKAEG SIDASNLLKP ALARGELQCC GATTMDEYRL IEKDVALARR
     FQPIIVNEPT VQDTISILRG IKDKYEVHHG VRITDGALVA AATYSNRYIT DRFLPDKAID
     LMDEAASHLK LEHESKPEDI MALDQKIMTI QIELESLRKE KDVASQERRE KLQADLKKYE
     DEISELTKRW EAERAEIESV KKTQEDLDKA RIELEQAQRE GNFGRASELR YSVIPTLEQK
     IPKDGEKTGG TLVHDAVTAD DIAAVVSRVT GIPVSKLTSG HIEKLVHMED TLREAVRGQD
     EAIKAVSNAV RLQRAGLSGE NRPLASFFFL GPTGVGKTEL CKKLANFLFS TESAVVRFDM
     SEFQEKHTIS RLIGAPSGYV GYEDAGQLTE AVRRKPYAVI LFDEFEKAHR DISALLLQVL
     DEGYLTDAQG HKVDFRNTII VLTSNLGADI LVGANMMHPY KETADGDIDP SVRKAVMDVV
     AANYPPEFLN RIDSFIIFKR LALTALRDIV DIRLRELQQR LDDKRIVLSV SGEVRDWLAE
     RGYDPKFGAR PLNRLITNEI GNGLADKIIR GELRSGDTAV VSIKEDNSGL DVTAQSRTS
//
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