ID M7BV10_CHEMY Unreviewed; 532 AA.
AC M7BV10;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like protein {ECO:0000313|EMBL:EMP41671.1};
GN ORFNames=UY3_01066 {ECO:0000313|EMBL:EMP41671.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP41671.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB486406; EMP41671.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BV10; -.
DR STRING; 8469.M7BV10; -.
DR Proteomes; UP000031443; 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; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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:EMP41671.1};
KW Hydrolase {ECO:0000313|EMBL:EMP41671.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EMP41671.1};
KW Protease {ECO:0000313|EMBL:EMP41671.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 184..335
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 408..502
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 498..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 59287 MW; 470395D6E46E426E CRC64;
MSKDGSGDGN KLSFILNTEN FRYLCHAYKY PAMMLLIQNN VTDIVNQEEL HEYNQDQNSV
NSMQSNIVNN IYNYLDKYVV GQCFAKKVLS VAVYNHYKRI YNNIPVNLRQ QAEVEKQTSL
TPRELEIRRR EDEYRFTKLL QIAGISPHGN ALGASMQQQV NQQMPQEKRG GEVLDSTHDD
IKLEKSNILL LGPTGSGKTL LAQTLAKCLD VPFAICDCTT LTQAGYVGED IESVIAKLLQ
DANYSVEKAQ QGIVFLDEVD KIGSVPGIHQ LRDVGGEGVQ QGLLKLLEGT IVNVPEKNSR
KLRGETVQVD TTNVLFVASG AFNGLDRIIS RRKNEKYLGF GTPSNLGKGR RAAAAADLAN
ISAESNTQQD SEEKDRLLRH VEARDLIEFG MIPEFVGRLP VVVPLHSLDE KTLVRILTEP
RNAVVPQYQA LFSMDKCELT VTEDALKAIA RLALDRKTGA RGLRSIMEKL LLEPMFEVPN
SDIVCVEVDK EVVDGKKEPG YIRAPTKDTS EEEYDSGVEE EGWPRQADAA NN
//