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Database: UniProt
Entry: A0A150G3B5_GONPE
LinkDB: A0A150G3B5_GONPE
Original site: A0A150G3B5_GONPE 
ID   A0A150G3B5_GONPE        Unreviewed;       996 AA.
AC   A0A150G3B5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN   ORFNames=GPECTOR_69g431 {ECO:0000313|EMBL:KXZ44338.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ44338.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, 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:KXZ44338.1}.
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DR   EMBL; LSYV01000070; KXZ44338.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150G3B5; -.
DR   STRING; 33097.A0A150G3B5; -.
DR   OrthoDB; 1083884at2759; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; 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; IPR017730; Chaperonin_ClpB.
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   NCBIfam; TIGR03346; chaperone_ClpB; 1.
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:UP000075714};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          99..241
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          68..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          569..623
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   996 AA;  108724 MW;  BF24B0B944D58FD9 CRC64;
     MLHTGTSTLN RQSAPSAAQV PRALSGLYAG PRHAPAYGGS RHLEASLLPF SALPLARSPA
     VTGHALAPAR QRLGRPGRRS FAAAASQAGS GGGGKRITAN QFTEKAWQAI VAAPEVCKEY
     SQQIVETEHL LKAMLEQPNG LARRVLAKAG SNPTRLLERT DEYIRRQPKV SGDSAQVLGR
     FLEALVARAM DLQSKWGDQF VSIEHLVVAL ADDTRFGEQL FRSEGLSKDK LEQAVKDIRG
     SNKVVDQDPE GKYEALSKYA RDLTAAAREG KLDPVIGRDD EVRRTIQILS RRTKNNPVLI
     GEPGVGKTAV VEGLAQRIVA GDVPQALQGR TLMALDMGSL IAGAKYRGEF EDRLKAVIKE
     VTDSAGRIVL FIDEIHTIVG AGATGGAMDA SNLLKPMLSR GELRCIGATT LDEYRKYIEK
     DPALERRFQQ VYVDQPSVAQ TVSILRGLRE RYEVHHGVRI SDSALVEAAV LSDRYIADRF
     LPDKAIDLVD EAAAKLKMEI TSKPLALDEI DRKVLQLEME RLSLQKAAGS DRGAAARLAT
     LDGELARLKD DQRVLSDQWS REKADMSRVQ DLKEEIERVN IEIAQAERDY DLNRAAELKY
     GTLHSLQNQL KAAEDALASK AASSGNGSGS KLLKEEVTEA DIAEIIAKWT GIPVSKLVES
     ERDKLLHLTD ELHRRVIGQD DAVEAVADAI QRSRAGLSDP NRPIASFMFL GPTGVGKTEL
     AKALAQFLFN SEDAMVRLDM SEYMEKHSVS RLIGAPPGYV GYDEGGQLTE AVRRRPYAVI
     LFDEVEKAHA DVFNVLLQIL DDGRVTDSQG RVVSFKNSII ILTSNLGSTN ILEMASALES
     NDSATRSAIK NLVMAQVRTH FRPEFVNRID EFIVFDPLRS EQIAQIVRLQ AKRVAERLAE
     KKIGLQLSDS AVRYLASTGY DPVYGARPVK RAVQRELETA IAKALLRGEF VEDDTIVVEA
     DELHGGVALR HGPKLSESAG GKGPAAAPYA AARSGR
//
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