ID A0A2P5D1S7_PARAD Unreviewed; 932 AA.
AC A0A2P5D1S7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE SubName: Full=ClpA/B family {ECO:0000313|EMBL:PON67248.1};
GN ORFNames=PanWU01x14_104230 {ECO:0000313|EMBL:PON67248.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON67248.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {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:PON67248.1}.
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DR EMBL; JXTB01000073; PON67248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5D1S7; -.
DR STRING; 3476.A0A2P5D1S7; -.
DR OrthoDB; 275944at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 90..232
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 519..554
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 508..535
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 932 AA; 103033 MW; B8D55E26528407A2 CRC64;
MALVQSTSAP GLVAGLKQGQ SKGSGRSKRS VKMLGCIRAP GLTMRSFSGL RSMNALDTVT
RPGQDFHSRV AITLSSRQRK ASRCVPKAMF ERFTEKAIKV IMLAQEEARR LGHNFVGTEQ
ILLGLIGEGT GIAAKVLKSM GINLKDARVE VEKIIGRGSG FVAVEIPFTP RAKRVLELSL
EEARQLGHNY IGSEHLLLGL LREGEGVAAR VLENLGADPS NIRTQVIRMV GESTEAVGAG
VGGGSSGNKM PTLEEYGTNL TKLAEEGKLD PVVGRQQQIE RVVQILGRRT KNNPCLIGEP
GVGKTAIAEG LAQRIASGDV PETIEGKKIL NELVIVCATK VITLDMGLLV AGTKYRGEFE
ERLKKLMEEI KQSDEIILFI DEVHTLIGAG AAEGAIDAAN ILKPALARGE LQCIGATTLD
EYRKHIEKDP ALERRFQPVK VPEPSVDETI QILKGLRERY EIHHKLRYTD EALVSAAQLS
YQYISDRFLP DKAIDLIDEA GSRVRLRHAQ LPEEARELEK ELRQITKEKN EAVRSQDFEK
AGELRDREMD LKAQISALVD KGKEMSKAES EAGDVGPVVT EVDIQHIVSA WTGIPVEKVS
TDESDRLLKM EETLHKRVIG QDEAVKAISR AIRRARVGLK NPNRPIASFI FSGPTGVGKS
ELAKALAAYY FGSEDAMIRL DMSEFMERHT VSKLIGSPPG YVGYTEGGQL TEAVRRRPYT
VVLFDEIEKA HPDVFNMMLQ ILEDGRLTDS KGRTVDFKNT LLIMTSNVGS SVIEKGGRRI
GFDLDYDEKD SSYNRIKSLV TEELKQYFRP EFLNRLDEMI VFRQLTKLEV KEIADIMLKE
VFERLKGKEI ELQVTERFRD RVVDEGYNPS YGARPLRRAI MRLLEDSMAE KMLAREIKEG
DSVIVDVDSD GNVTVLNGSS GSPGSLPEAI PV
//