ID V8NH23_OPHHA Unreviewed; 543 AA.
AC V8NH23;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 03-MAY-2023, entry version 31.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial {ECO:0000313|EMBL:ETE60862.1};
DE Flags: Fragment;
GN Name=CLPX {ECO:0000313|EMBL:ETE60862.1};
GN ORFNames=L345_13393 {ECO:0000313|EMBL:ETE60862.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE60862.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE60862.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE60862.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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:ETE60862.1}.
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DR EMBL; AZIM01004333; ETE60862.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NH23; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:ETE60862.1};
KW Hydrolase {ECO:0000313|EMBL:ETE60862.1};
KW Nucleotide-binding {ECO:0000313|EMBL:ETE60862.1};
KW Protease {ECO:0000313|EMBL:ETE60862.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT DOMAIN 419..513
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 508..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE60862.1"
SQ SEQUENCE 543 AA; 60363 MW; A2A10CDAAFBC6ECE CRC64;
QIYAYLPRRI SCGRSCFPAL GIIGTCETQP LRIIPFRTFS ETPAYFASKD GASKDGSGDG
TSTRFVKCEK CHHFFVVLSE ADSKKSILKE PETAAEAVKL AFQQKPPPPP KKIYNYLDKY
VVGQCFAKKV LSVAVYNHYK RIYNNIPANL RQQAEVEKQA SLTPRELEIR RREDEYRFTK
LLQIAGISPH GNALGASMQQ QVNQQMPPEK RGGETLAKCL DVPFAICDCT TLTQAGYVGE
DIESVIAKLL QDANYNVEKA QQGIVFLDEV DKIGSVPGIH QLRDVGGEGV QQGLLKLLEG
TIVNVPEKNS RKLRGETVQV DTTNILFVAS GAFNGLDRII SRRKNEKYLG FGASSNLGKG
RRAAAAADLA NLSNESNSEQ EMEEKDRLLR HVEARDLIEF GMIPEFVGRL PVVVPLHSLD
EKTLVRILTE PRNAVIPQYQ ALFSMDKCEL NVTEDALKAI ARLALDRKTG ARGLRSIMEK
LLLEPMFEVP NSDIVCVEVD KEVVEGKKEP GYVRTPTKDS SEEEYDSGVE EESWARQADA
ANH
//
