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Database: UniProt
Entry: A0A2A9M8Y6_9APIC
LinkDB: A0A2A9M8Y6_9APIC
Original site: A0A2A9M8Y6_9APIC 
ID   A0A2A9M8Y6_9APIC        Unreviewed;      1039 AA.
AC   A0A2A9M8Y6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   SubName: Full=Putative ATP-dependent hsl protease ATP-binding subunit hslU {ECO:0000313|EMBL:PFH32087.1};
GN   ORFNames=BESB_020280 {ECO:0000313|EMBL:PFH32087.1};
OS   Besnoitia besnoiti.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX   NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH32087.1, ECO:0000313|Proteomes:UP000224006};
RN   [1] {ECO:0000313|EMBL:PFH32087.1, ECO:0000313|Proteomes:UP000224006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH32087.1,
RC   ECO:0000313|Proteomes:UP000224006};
RA   Schares G., Venepally P., Lorenzi H.A.;
RT   "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771}.
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:PFH32087.1}.
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DR   EMBL; NWUJ01000012; PFH32087.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9M8Y6; -.
DR   STRING; 94643.A0A2A9M8Y6; -.
DR   VEuPathDB; ToxoDB:BESB_020280; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000224006; Chromosome xi.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00390; hslU; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1.
DR   Pfam; PF00004; AAA; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:PFH32087.1};
KW   Hydrolase {ECO:0000313|EMBL:PFH32087.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:PFH32087.1};
KW   Protease {ECO:0000313|EMBL:PFH32087.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224006}.
FT   DOMAIN          637..931
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          930..1025
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..431
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..522
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..570
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1039 AA;  109289 MW;  7EA60EDCF568250F CRC64;
     MWRVAAYAAG HSPPGSSGGL RRQSARQAYS SSAGNPTSFS FSKRCSSPSC TTGESRNRGE
     QTGGRRCFRP GAGSPAPHHS DSFAARSASS SLPSSAPSSP RASLESLRAS FPPPLPGSCC
     SADAGTRRVC LSALSSPRLS PLSQPVALSF APRRSAGGSS SAFSLFSKRS VSFGAHAQNQ
     PASHARVSFL LSRLSGSPVP CPSAKRFLSH SASDGDGRSE DPRQAIDGDP ARNSPPRPPC
     GAPSIEAVGG VRTPEPGSDG EARAHSGCGS FSLRGPKTGA SCRQAERGGM MSYGTLEGGR
     SGEKVRDSGS RQGESCSQQG RAAAEPDASS SPLLRAPRVP PGSGRPAPSA LSARRPQAAE
     GSQRTSASSS SASSFPPLGE RARANAVASA ERSRVPSPLF DSSGGSAKAL GGGAPCAQPE
     PWPPAPPAPV SAFPDAGTDS PFFSPPCAAA SLRLPAAPAS PAVLALPQVS LAPRNGPFRG
     ASAPPAPSAE PDCPLSSPPP SSALPPSSAL PPSSPWPPQF SPFSPSRVAS FSAAPPPASS
     LSSPGSASPA PPPPSSGPAS LSPPPPRCPA AEQGAGGSSL AVEAATKSQA LCPSEMVAYL
     DKYIVGQADA KKAVAVALRQ RWRRRQIEDE KLRDDITPKN ILLIGPTGVG KTEVARRLAR
     CIDAPFIKVE ATKFTEVGFH GRDVDQIIKD LVEVAMKNQR TRLQEAMRPT AERRAETKIL
     EALLGQMPAE EHQQWLEHLR GGALDSRRVH VDIPPARQHG APPGVAGFDE SGRDSIVADL
     ESIIRDIDRP RHAFFTARRG ARGLEARNLT VKEARKKLMQ AELDAMITKD LVVQKALEAV
     EQEGIVFIDE IDKICTKGGR SGYNPDASDE GVQRDLLPLI EGTTVTTRYG DVRTDYILFI
     ASGAFHCVRP SDLLAELQGR LPIRVTLKPL AEADLRDILT KTKNNLIEQN RALLQTEKVD
     LHFTEEAVNE IARVACEVNA NVENIGARRL HTIIEKIMED VNFAAPSMAP GMRVEIDLER
     VRSSVSSLLT KMDYTRFVL
//
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