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Database: UniProt
Entry: Q85G08_CYAM1
LinkDB: Q85G08_CYAM1
Original site: Q85G08_CYAM1 
ID   Q85G08_CYAM1            Unreviewed;       821 AA.
AC   Q85G08;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   SubName: Full=ATP-dependent clp protease ATP-binding subunit {ECO:0000313|EMBL:BAC76183.1};
GN   Name=clpC {ECO:0000313|EMBL:BAC76183.1};
OS   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:BAC76183.1}.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699 {ECO:0000313|EMBL:BAC76183.1, ECO:0000313|Proteomes:UP000007014};
RN   [1] {ECO:0000313|EMBL:BAC76183.1, ECO:0000313|Proteomes:UP000007014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10D {ECO:0000313|EMBL:BAC76183.1,
RC   ECO:0000313|Proteomes:UP000007014};
RX   PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA   Ohta N., Matsuzaki M., Misumi O., Miyagishima S., Nozaki H., Tanaka K.,
RA   Shin-i T., Kohara Y., Kuroiwa T.;
RT   "Complete sequence and analysis of the plastid genome of the unicellular
RT   red alga Cyanidioschyzon merolae.";
RL   DNA Res. 10:67-77(2003).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; AB002583; BAC76183.1; -; Genomic_DNA.
DR   RefSeq; NP_849021.1; NC_004799.1.
DR   AlphaFoldDB; Q85G08; -.
DR   STRING; 280699.Q85G08; -.
DR   EnsemblPlants; CMV107CT; CMV107CT; CMV107C.
DR   GeneID; 844877; -.
DR   Gramene; CMV107CT; CMV107CT; CMV107C.
DR   KEGG; cme:CymeCp089; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_1_1; -.
DR   OMA; NIRRIHI; -.
DR   Proteomes; UP000007014; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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   InterPro; IPR001943; UVR_dom.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 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.
DR   PROSITE; PS50151; UVR; 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   Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:BAC76183.1};
KW   Hydrolase {ECO:0000313|EMBL:BAC76183.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:BAC76183.1};
KW   Protease {ECO:0000313|EMBL:BAC76183.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007014};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          416..451
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
SQ   SEQUENCE   821 AA;  92113 MW;  B7FF8D5897349C96 CRC64;
     MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGLAARALK TLGVDLKEAR
     VEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLDEARILSH NYIGTEHLLL GLIREGEGVA
     ARVLESLGVD LATLRSLVLR MLDETSEVVI GGGYSRSRTP TLEEFGVNLT ELAMEGELDP
     VVGREKEIER VIQILGRRTK NNPVLIGEPG VGKTAIAEGL AQRIADRDIP DILEDMKVIT
     LDIGLLVAGT KYRGEFEERL KKVMDEIREV GNVILVIDEV HTLIGAGAAE GAIDAANILK
     PALARGELQC IGATTLEEYR KHIEKDAALE RRFQPVMVGE PTVDETIEIL KGLRDRYEEH
     HRVRISDAAL EAAAKLSSQY IADRYLPDKA IDLIDEAGSR VRLMYYKLPK VTLELDKELR
     EVMRLKDEMI REDHFEIAAE LRDREKEIRS QIMAMTKSHR EETQEQILQA RPVVSEEDIA
     QIVASWTGIP VKKLTRSESE KLLHMEETLH QRIVGQNEAV SAVSKAIRRA RVGLKNPNRP
     IASFIFSGPT GVGKTELTKA LASYFFGSNE AMVRLDMSEY MERHTVSKLI GSPPGYVGYN
     EGGQLTEAVR KRPYTVILFD EIEKAHPDVF NILLQILEDG RLTDSKGRTV DFKNTLLIMT
     SNIGSKIIEK GGGGLGFELG DSWQDTQYSR LKNLVNEELK QYFRPEFLNR IDEIIVFRQL
     TKEEVGQIAE MMLKEVYDRL AQQQQIQLQV TDRFKRKIIE EGYSATYGAR PLRRAIMKWL
     EDPLAEHVLA NTLSPGMTAV VDLDGEDVKV LPSKQMETQI A
//
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