ID A0A453BVY5_AEGTS Unreviewed; 918 AA.
AC A0A453BVY5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:AET2Gv20652200.10};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20652200.10, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv20652200.10}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR AlphaFoldDB; A0A453BVY5; -.
DR STRING; 200361.A0A453BVY5; -.
DR EnsemblPlants; AET2Gv20652200.10; AET2Gv20652200.10; AET2Gv20652200.
DR Gramene; AET2Gv20652200.10; AET2Gv20652200.10; AET2Gv20652200.
DR Proteomes; UP000015105; Chromosome 2D.
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:UP000015105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 87..229
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 505..540
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 101650 MW; A9236ECB9672CE18 CRC64;
MEGTLVQSAI APTAYRSSST RSRVRTRATM LRSTPTRTLT LGGFQGLRQT NFLDTRSVIK
RDFGSIVASQ ISRPRGSGSR MVVRAMFERF TEKAIKVIML AQEEARRLGH NFVGTEQILL
GLIGEGTGIA AKVLKSMGIS LKDARVEVEK IIGRGSGFVA VEIPFTPRAK RVLELSLEEA
RQLGHNYIGS EHLLLGLLRE GEGVAARVLE SLGADPNNIR TQVIRMVGES TEAVGAGVGG
GSSGQKMPTL EEYGTNLTKL AEEGKLDPVV GRQDQIERVT QILGRRTKNN PCLIGEPGVG
KTAIAEGLAQ RICNGDVPET IEGKKVITLD MGLLVAGTKY RGEFEERLKK LMEEIKQNDD
IILFIDEVHT LIGAGAAEGA IDAANILKPA LARGELQCIG ATTLDEYRKH IEKDPALERR
FQPVKVPEPT VEESIQILRG LRERYELHHK LRYTDDALVA AAQLSYQYIS DRFLPDKAID
LIDEAGSRVR LRHAQQLPDE AKELDKKLRQ ITKDKNEAVR GQDFEKAGEL RDEEMELKAQ
ITAIIDKSKE MVKAETESGE VGPLVTEADI QHIVSSWTGI PVEKVSSDES DRLLKMEETL
HTRIIGQDEA VKAISRAIRR ARVGLKNPNR PIASFIFSGP TGVGKSELAK ALASYYFGSE
EAMIRLDMSE FMERHTVSKL IGSPPGYVGY TEGGQLTEAV RRRPYTVVLF DEIEKAHPDV
FNMMLQILED GRLTDSKGRT VDFKNTLLIM TSNVGSSVIE KGGRKIGFDL DSDEKDTSYN
RIKSLVTEEL KQYFRPEFLN RLDEMIVFRQ LTKLEVKEIA DIMLKEVFDR LKAKEIDLQV
TEKFRDRVVD EGYNPSYGAR PLRRAIMRLL EDSLAEKMLA GEVKEGDSAI VDVDSDGKVV
VLNSGGGIAE PLEPALSA
//