ID K7LTB1_SOYBN Unreviewed; 806 AA.
AC K7LTB1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN Name=100807188 {ECO:0000313|EnsemblPlants:KRH24768};
GN ORFNames=GLYMA_12G061400 {ECO:0000313|EMBL:KRH24768.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH24768};
RN [1] {ECO:0000313|EMBL:KRH24768.1, ECO:0000313|EnsemblPlants:KRH24768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH24768};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH24768.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH24768}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH24768};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH24768.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH24768.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR EMBL; CM000845; KRH24768.1; -; Genomic_DNA.
DR RefSeq; XP_003539663.1; XM_003539615.3.
DR AlphaFoldDB; K7LTB1; -.
DR SMR; K7LTB1; -.
DR STRING; 3847.K7LTB1; -.
DR MEROPS; M41.022; -.
DR PaxDb; 3847-GLYMA12G06580-2; -.
DR EnsemblPlants; KRH24768; KRH24768; GLYMA_12G061400.
DR GeneID; 100807188; -.
DR Gramene; KRH24768; KRH24768; GLYMA_12G061400.
DR KEGG; gmx:100807188; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_2_1; -.
DR InParanoid; K7LTB1; -.
DR OMA; GFHNDER; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000008827; Chromosome 12.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.1690.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF2; SD01613P; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 352..491
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 94..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 88529 MW; 2DF0800B02A7FDFA CRC64;
MIFSRIARSV SSSSRARNLL HGDGRLGTHV GSPRTNACSE GAEGVLGSVR GYVSSARARS
NGFVSNLPDF KSVAANPTIR RLFCSKAPKK ENYGNFYPKE KKEVPKGNDK KYESKDNSNA
NTEDSGNFQE AFMKQVKYLV TPLLLMGLFL TSFSFGPPEQ NQISFQEFKN KLLEPGLVDH
IVVSNKSVAK VYVRNTPLNQ TDNEVAQGTQ PAIGSGGQYK YYFNIGSVES FEEKLEEAQE
ALGIYSHDFV PVTYSFELGY REWITLASIL LLLGFLVCAV GFIKGAIDAA RGKGAPGIFN
IGKAPVTKVD RNAKNKIYFK DVAGCDEAKQ EIMEFVHFLK SPKKYEELGA KIPKGALLVG
PPGTGKTLLA KATAGESGVP FLSISGSDFL EMFVGVGPSR VRNLFQEARQ CSPSIVFIDE
IDAIGRARRG SFSGANAERE STLNQLLVEM DGFGTTSGVV VLAGTNRPEI LDKALLRPGR
FDRQITIDKP DIKGRDQIFQ IYLKKIKLDH EPSYYSQRLA ALTPGFAGAD IANVCNEAAL
IAARGEGTQV TMEHFEAAID RIIGGLEKRN KVISKLERRT AAYHEAGHAV SGWFLEHGEP
LLKVTIVPRG TAGLGFAQYV PNENLFMTKE QLFDITCMTL GGRAAEQVLI GRISTGAQND
LEKVTKMTYA QVAVYGFSDK VGLLSFPPTE GSYEFSKPYS SKTAAIIDKE VREWVNKAYK
HTIQLIEEHK EQVTEIAELL LEKEVLHQDD LLRVLGERPF KATEPTNYDR FKQGFIEEEE
KGAESTIDTP EEGGGSSPLE PQVVPT
//
