ID M7WHJ6_RHOT1 Unreviewed; 762 AA.
AC M7WHJ6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:EMS19952.1};
GN ORFNames=RHTO_03996 {ECO:0000313|EMBL:EMS19952.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS19952.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS19952.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS19952.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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DR EMBL; KB722665; EMS19952.1; -; Genomic_DNA.
DR RefSeq; XP_016271071.1; XM_016417664.1.
DR AlphaFoldDB; M7WHJ6; -.
DR GeneID; 27368009; -.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_1_2_1; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000016926; 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 Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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:EMS19952.1};
KW Hydrolase {ECO:0000313|EMBL:EMS19952.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EMS19952.1};
KW Protease {ECO:0000313|EMBL:EMS19952.1}.
FT DOMAIN 390..554
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 634..728
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 50..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 81417 MW; C7BA9C7C04F93E4A CRC64;
MLASTLKRPL PSLLLSRSPA AHLQPLLALA TSGPTTPARG LGRVARGVHR SGALSHTRTG
GGGGGGAGTG TATSQGEWSE RSREESERRR RSPRELVAHL DQYVVGQEKA KKVLAVATYN
HYARLAQLSS HSDSISGEPA PPTGAQVIPA LRPVTAAPLA SLMHGWVEIR PSAKQFKALK
ESLKRAGVAI DLGNFEGDGA KPKKGKKAAK KEEEAEAEEG DEPKDKAVAT KKDGEAEEGA
EEAKPAKSTR RRRTTAEEDD DTAPSNPSRR FYRTADDGLA IIESPPSTPL TDIFPILQRP
SIFVINEQDV PLSGPGLTEL SSRVIPWDPS EDKLPKEEDE KKAASSSKQD RPPVDDLPSP
SDLLTDFLGQ RPGQPLPPRP SASSQNPLFE KSNVLLLGPT GSGKSLLVRT LAKVLDVPFA
SAEATSMTSA GYVGEDVENC IARLLEAADG DVEKASRGIV FIDEIDKISS SRGLSKDVGG
EGVQQALLKM LEGTSINVSE YGYNPPNAGM FGMRRGPMRE AVIVDTTNIL FIVAGAFVGL
EKIIQSRLAK GSIGFTSRIA PTPSQSINSP DSATTFSPSN PSTFLSGTSG KGADGKQQDL
SHLLDQCEPD DLALFGLIPE FIGRIPITAA LKTLTEEDLL RVLQEPKNAL VKQYTELFAA
SGVQLLFTTP ALRAVAALAV KKQTGARGLR RIMEQALLDS MYEIPDSSIK YCLITADVVE
GKEPAKYYSR SQKHMFELDY TAEEEAGEEP QGGVAEKKRA AA
//
