ID A0A2K1KEP6_PHYPA Unreviewed; 936 AA.
AC A0A2K1KEP6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYPA_008629 {ECO:0000313|EMBL:PNR52255.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR52255.1};
RN [1] {ECO:0000313|EMBL:PNR52255.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c6_7360V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR52255.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c6_7360V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c6_7360V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; ABEU02000006; PNR52255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1KEP6; -.
DR STRING; 3218.A0A2K1KEP6; -.
DR PaxDb; 3218-PP1S252_87V6-1; -.
DR EnsemblPlants; Pp3c6_7360V3.1; Pp3c6_7360V3.1; Pp3c6_7360.
DR EnsemblPlants; Pp3c6_7360V3.2; Pp3c6_7360V3.2; Pp3c6_7360.
DR Gramene; Pp3c6_7360V3.1; Pp3c6_7360V3.1; Pp3c6_7360.
DR Gramene; Pp3c6_7360V3.2; Pp3c6_7360V3.2; Pp3c6_7360.
DR InParanoid; A0A2K1KEP6; -.
DR OMA; CCTLRAP; -.
DR OrthoDB; 275944at2759; -.
DR Proteomes; UP000006727; Chromosome 6.
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; -; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 102..244
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 519..554
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 936 AA; 102598 MW; E92C734DA45B0326 CRC64;
MASMAHSLTL PSVGSSLVGQ LNDSAKSKRR TIAQAASTGR KNLKKSASLS VSGFQSFSGM
RKASAVDALT VKQGKDLKSV VAKSMAVAGH SRPSRGVTFA MFERFTEKAI KVIMLAQEEA
RRLGHNFVGT EQILLGLIGE GTGIAAKVLK SMGVNLKEAR VEVEKIIGRG SGFVAVEIPF
TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLLREGEGVA ARVLENLGAD PSNIRTQVIR
MVGENNEAVG VGGGSGSGSN KMPTLEEYGT NLTKLAEEGK LDPVVGRVAQ IERVTQILGR
RTKNNPCLIG EPGVGKTAVA EGLAQRIASG DVPETIEGKK VITLDMGLLV AGTKYRGEFE
ERLKKLMEEI KQADDIILVI DEVHTLIGAG AAEGAIDAAN ILKPALARGE LQCIGATTLD
EYRKHIEKDP ALERRFQPVL VPEPTVEETI EILKGLRERY EIHHKLRYTD EALIAAAQLS
YQYISDRFLP DKAIDLIDEA GSKVRLKHAQ LPEEARELDK QLRAVTKEKN EAVRGQDFEK
AGELRDKEME LKAQISVFIE KGKEQMKAES ETGDVGPTVE ESDIQQIVAA WTGIPMEKVS
SDESDRLLKM EDTLHNRVIG QDEAVKAISR AIRRARVGLK NPNRPIASFI FSGPTGVGKS
ELAKALASYY FGSEEAMVRL DMSEFMERHT VSKLIGSPPG YVGYSEGGQL TEAVRRRPYT
VVLFDEIEKA HPDVFNMMLQ ILEDGRLTDS KGRTVDFKNT LLIMTSNVGS SVIEKGGGGI
GFQLDYGEKD SSYNRIKSLV NEELKQYFRP EFLNRLDEII VFRQLTKLEV KEIADIMLKE
VFERLKKKEI DLQVTERFRD RVVDEGYSPS YGARPLRRAI MRLLEDSMAE RMLSGEIKEG
DSAIIDVDSD GGVTVLNGTT GTSTNTAIDQ APAGIA
//