ID D8S131_SELML Unreviewed; 901 AA.
AC D8S131;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SELMODRAFT_176012 {ECO:0000313|EMBL:EFJ21770.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ21770.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; GL377598; EFJ21770.1; -; Genomic_DNA.
DR RefSeq; XP_002977161.1; XM_002977115.1.
DR AlphaFoldDB; D8S131; -.
DR STRING; 88036.D8S131; -.
DR EnsemblPlants; EFJ21770; EFJ21770; SELMODRAFT_176012.
DR GeneID; 9638801; -.
DR Gramene; EFJ21770; EFJ21770; SELMODRAFT_176012.
DR KEGG; smo:SELMODRAFT_176012; -.
DR HOGENOM; CLU_005070_4_2_1; -.
DR InParanoid; D8S131; -.
DR OMA; NIRRIHI; -.
DR OrthoDB; 275944at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
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:UP000001514};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 68..210
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 485..520
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 901 AA; 99283 MW; 1F3A2610A6A46475 CRC64;
MIRGSNHGQV RAAFITRTRT LQTYVGMRKP SPLDSLATRT CKDWNSVVSS VSTSGGRGAS
RGVVVAMFER FTEKAIKVIM LAQEEARRLG HNFVGTEQIL LGLIGEGTGI AAKVLKSMGV
NLKEARVEVE KIIGRGSGFV AVEIPFTPRA KRVLELSLEE ARQLGHNYIG SEHLLLGLLR
EGEGVAARVL ENLGADPGNI RTQVIRMVGE STEAVGASVG GGSSSNKMPT LEEYGTNLTK
LAEEGKLDPV VGRQQQIERV TQILGRRTKN NPCLIGEPGV GKTAIAEGLA QRIATGDVPE
TIEGKKVVTL DMGLLVAGTK YRGEFEERLK KLMEEIKQSD DIILVIDEVH TLIGAGAAEG
AIDAANILKP ALARGELQCI GATTIDEYRK HIEKDPALER RFQPVNVPEP TVDETIQILK
GLRERYEIHH KLRYTDEALV AAAQLSYQYI SDRFLPDKAI DLIDEAGSRV RLRHAQLPEE
ARDLDKELRQ ITKEKNEAVR GQDFEKAGEL RDREMELKAQ ISAITEKGKE KSKAETEAGE
TGPLVTEADI QQIVSAWTGI PVEKVSTDES DRLMKMEETL HQRVIGQDEA VKAISRAIRR
ARVGLKNPNR PIASFIFSGP TGVGKSELAK ALAAYYFGSE EAMVRLDMSE FMERHTVSKL
IGSPPGYVGY TEGGQLTEAV RRRPYTVVLF DEIEKAHPDV FNMMLQILED GRLTDSKGRT
VDFKNTLLIM TSNVGSSVIE KGGGGIGFQL DYGEKDSSYN RIKTLVNEEL KQYFRPEFLN
RLDEIIVFRQ LTKTEVKEIA DIMLKEVFER LKKKEIDLQV TERFRDRVVD EGYSPSYGAR
PLRRAIMRLL EDSMAERMLS GEVKEGDSAI IDVDSEGNVT VLNGTAGTAS SSSIEAPAGV
A
//