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Database: UniProt
Entry: S2JNP0_MUCC1
LinkDB: S2JNP0_MUCC1
Original site: S2JNP0_MUCC1 
ID   S2JNP0_MUCC1            Unreviewed;       597 AA.
AC   S2JNP0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   13-SEP-2023, entry version 40.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:EPB90157.1};
GN   ORFNames=HMPREF1544_02991 {ECO:0000313|EMBL:EPB90157.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB90157.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KE123924; EPB90157.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2JNP0; -.
DR   STRING; 1220926.S2JNP0; -.
DR   VEuPathDB; FungiDB:HMPREF1544_02991; -.
DR   eggNOG; KOG0745; Eukaryota.
DR   InParanoid; S2JNP0; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000014254; 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00382; clpX; 1.
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:EPB90157.1};
KW   Hydrolase {ECO:0000313|EMBL:EPB90157.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:EPB90157.1};
KW   Protease {ECO:0000313|EMBL:EPB90157.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014254}.
FT   DOMAIN          250..415
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          469..563
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          47..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  65765 MW;  443638619255AA30 CRC64;
     MRILSIYTPI LKTSCYTKSA VVFSISTKSS RFYHSADYSG GGLMGRGDFS NMSTPPSSSH
     ASSSSSRGPE DPFAHLDLGQ IADPRSIVQH LNEYVIGQER AKKVLAVAIF NHYNRVRANM
     KRTYLQQQKL QQQQQQQQQQ QQQLLQQQQQ AATIDGVIAV DERLHAEHHH QPTTPHHDGY
     YSSQIPIQPH STEFPSTERS MSFGAQRRAW LNPPTEATND KSAFPHNDTK AASTDFADDT
     AEEEESTVHD KSNVLLIGPT GSGKTLLART LAQVLQVPFS MSDATPFTQA GYVGEDVELV
     IQRLLQSCDF DVKKAETGIV FIDEIDKISR RSDSHTASRD VSGEGVQQSL LRMLEGTVVN
     VTDKSGAGNH KRGPNGGGSM SPNKGETYSV DTSNILFILS GAFIGLDRII GDRMSKGSIG
     FAAQLKSEAD IEKESKDALH QVEPTDLVKF GLIPEFVGRV PVVASVNNLR VDDLVRVLKE
     PKNSLLKQYE GLFKLNNVDL RFSQNALRAV AAQALEKKTG ARGLRRIMEN LLLEPMYDAP
     ASCIKQVIID SKVVNNEKTP VYITSEKSQL AEKIIAEDDG LDLASTEDDV PQQMTQI
//
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