ID A0A507DWZ8_9FUNG Unreviewed; 892 AA.
AC A0A507DWZ8;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN ORFNames=PhCBS80983_g05342 {ECO:0000313|EMBL:TPX55400.1};
OS Powellomyces hirtus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Powellomycetaceae; Powellomyces.
OX NCBI_TaxID=109895 {ECO:0000313|EMBL:TPX55400.1, ECO:0000313|Proteomes:UP000318582};
RN [1] {ECO:0000313|EMBL:TPX55400.1, ECO:0000313|Proteomes:UP000318582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 809.83 {ECO:0000313|EMBL:TPX55400.1,
RC ECO:0000313|Proteomes:UP000318582};
RX PubMed=31209237; DOI=.1038/s41598-019-45128-9;
RA van de Vossenberg B.T.L.H., Warris S., Nguyen H.D.T.,
RA van Gent-Pelzer M.P.E., Joly D.L., van de Geest H.C., Bonants P.J.M.,
RA Smith D.S., Levesque C.A., van der Lee T.A.J.;
RT "Comparative genomics of chytrid fungi reveal insights into the obligate
RT biotrophic and pathogenic lifestyle of Synchytrium endobioticum.";
RL Sci. Rep. 9:8672-8672(2019).
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:TPX55400.1}.
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DR EMBL; QEAQ01000111; TPX55400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A507DWZ8; -.
DR STRING; 109895.A0A507DWZ8; -.
DR Proteomes; UP000318582; 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; 2.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000318582};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..531
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 892 AA; 99031 MW; 0284E14EFC1006EC CRC64;
MNPEIFTDKT NTVLGRAQEL AREFGHIQLA PVHLASAMFD DEDGLIRSIV TKAGGDPAVA
ERRLKSLLVK QPTQDPAPDQ ISFHPNTAKT MRAADEIRKK QKDSHLSIDH LILALADQKD
IMTAFQDAGV TSKALEEAIS QIRGTRRVDS KTADSTYEAL SKYAIDLVGM AEQGKLDPCI
GRDDEIRRVI RVLARRTKNN PVLVGEPGVG KTAIVEGLAQ RIVRKDVPKS LQCRIFSLDM
GSLIAGAKYR GEFEERLKAV LKEVKDAQGN IIMFIDELHT VLGAGKTEGS MDAANLLKPM
LARGELRLIG ATTLAEYQKY IEKDAAFERR FQMVQVGEPS VEATISILRG IREKWETFHG
VRILDAALVN AAMLADRYIT NRFLPDKAID LVDEACANIR VQLDSQPEII DMLERKHLQL
EVEATALEKE NDTASQQRLV KVRDEMARLR EQLKPLKLRY EQEKGRIDEI RNLKAKLDEL
KHKIADAERR YDLALAADLK YYAVPEVEKK IAQLEQDLKD ERERMAASAA DSADASQQLV
SEIVTPDQIM EVVARWTGIP VTKLNKSQID RLLNLRDVLH KRVVGQDEAV KAVAEAVLRS
RAGLGGGGTI GSFLFLGPTG VGKTELAKTL AGELFDDDKK GLIRIDMSEY MEQHTVARLI
GAPPGYVGYD EGGQLTEQVR RHPYAVILFD EIEKAHPQVL NVLLQVLDDG RLTDGKGRTV
DFSNTVIIMT SNVGSQLLQQ STSVSSEIKD AVMAQVRRTF KPELLNRITD IVVFHSLAPP
QLREIVKIQL AEIAKRLESK QILLRMSDAA ADVVLEKSYD PLYGARPLKR YLERALVTKL
SKMLISGELT EHCLAYVDAA PKGANSGDDD DDGLVLKVQK VPGADPHSMD MD
//