ID A0A151M8Z4_ALLMI Unreviewed; 895 AA.
AC A0A151M8Z4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial {ECO:0000313|EMBL:KYO20986.1};
GN Name=CLPX {ECO:0000313|EMBL:KYO20986.1};
GN ORFNames=Y1Q_0001309 {ECO:0000313|EMBL:KYO20986.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO20986.1};
RN [1] {ECO:0000313|EMBL:KYO20986.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO20986.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:KYO20986.1}.
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DR EMBL; AKHW03006295; KYO20986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151M8Z4; -.
DR STRING; 8496.A0A151M8Z4; -.
DR eggNOG; KOG0745; Eukaryota.
DR Proteomes; UP000050525; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 InterPro; IPR031974; PDCD7.
DR InterPro; IPR010603; Znf_CppX_C4.
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 Pfam; PF16021; PDCD7; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KYO20986.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KYO20986.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KYO20986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 145..198
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 120..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 809..841
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 133..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 100642 MW; FBABBB043D791291 CRC64;
MLVGPLVRRF PWFEGPLSAC LYHPEPLVGE KMSLTACSEG QTSRCLCDQE ERSECILPPW
ASHLMCCVDY MPPLLSSAGI TCGRSRLPVL RRLGAFETRS LRRVPFRCFS ETPAYFASKD
GASKDGSGDG NKKSVSEGGS KKSGSGNSGK GGNQLRCPKC GDLCTHVETF VSSTRFVKCE
KCHHFFVVLS EADSKKSIIK EPDSAAEAVK LAFQQKPPPP PKKIYNYLDK YVVGQSFAKK
VLSVAVYNHY KRIYNNIPAN LRQQVEVEKQ ASLTPRELEI RRREDEYRFT KLLQIAGISP
HGNALGASMQ QQVNQQMPQE KRGGEVLDSP YDDIKLEKSN ILLLGPTGSG KTLLAQTLAK
CLDVPFAICD CTTLTQAGYV GEDIESVIAK LLQDANYNVE KAQQGIVFLD EVDKIGSVPG
IHQLRDVGGE GVQQGLLKLL EGTIVNVPEK NSRKLRGETV QVDTTNVLFV ASGAFNGLDR
IISRRKNEKY LGFGTPSNLG KGRRAAAAAD LANISGETDT QQDIEEKDRL LRHVEARDLI
EFGMIPEFVG RLPVVVPLHS LDEKTLVRIL TEPRNAVVPQ YQALFSMDKC ELNVTEDALK
AIARLALDRK TGARGLRSIM EKLLLEPMFE KAKKSQDTLG LRLKIHPRKS MTPELKRKAG
LVKQTLQTIN YRFNRASGIL REPVKPAGFV EDGEDARAAE REALIDRWRA RRGHEAAERA
REQELKAAAD SVLSEVRRKQ ADTKRMVEIL RGLEKLRKLR KEAAGRKGVC PPPSADEAFE
HNIQKMRTLI KKRTELYEAE ERALRVMLEG EQEEERKREM EKKQKKEREK LLQQKREIES
VLFGNPDEFP LGHLLRPFQQ YYLQAEHSVP VLIQIRHEWD RLKFWSVTLK QLMAL
//
