ID A0A2S6CB95_9PEZI Unreviewed; 638 AA.
AC A0A2S6CB95;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBER1_00590 {ECO:0000313|EMBL:PPJ56999.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ56999.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ56999.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PNEN01000503; PPJ56999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CB95; -.
DR STRING; 357750.A0A2S6CB95; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000237631; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000237631}.
FT DOMAIN 205..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 482..576
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 113..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 69901 MW; CEC860AF1CA73A37 CRC64;
MATVASHYTP RARLTYLGIA AITRRHFSAS HRTSSDSSSY IRSDFTNQPW TGVYEPGGPT
EGPLGGASEI GAPRITPAIL KQHLDQFVVG QERAKKTLAT AVYNHYQRIQ ELQRRDEEGE
EQLAAEERRR MHQEHPVEGR EGELKRGIAV PSLTKDFAED EFPGQQQTTI HVYPPDHSSQ
QRTIQQNGLG PPPSPLQDSS PLTVEKSNVL LLGPSGVGKT LMAKTLARVL EVPFSMSDCT
PFTQAGYIGE DADVCVQRLL AAANYDVTRA ERGIIVLDEI DKIATAKVSH GKDVSGEGVQ
QALLKIIEGT TLQIQAKQER SSTNEKYRGQ GSGYPTNSPL SGGNLNQPSQ PGGGKGDVYN
VRTDNILFLC AGAFNGLHKV ILDRVSRGSI GFGATVRAAP GSDTSNDNQH ETIIEGEDEL
FEKHLPYYTP TTQQNDDSNF NASKQKRKFN TLDLVEPQDL QKYGLIPELV GRIPISCALS
SLDVEALVKV LTEPRNSLMK QYQQLFALSS MEIRFTTAAL HAIATTASKM GTGARGLRTV
MERLLADAMF ETPGSGIKYI LINEDVARRK AGAVFFSRGQ QGAFRGMIAS EEDAWEERKR
IEEGTESEFE ARARNNSRGG AAKTFEEYRE KATAAGFV
//