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Database: UniProt
Entry: A0A1G4IN04_9SACH
LinkDB: A0A1G4IN04_9SACH
Original site: A0A1G4IN04_9SACH 
ID   A0A1G4IN04_9SACH        Unreviewed;       505 AA.
AC   A0A1G4IN04;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=LADA_0A03576g1_1 {ECO:0000313|EMBL:SCU78057.1};
GN   ORFNames=LADA_0A03576G {ECO:0000313|EMBL:SCU78057.1};
OS   Lachancea dasiensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU78057.1, ECO:0000313|Proteomes:UP000190274};
RN   [1] {ECO:0000313|EMBL:SCU78057.1, ECO:0000313|Proteomes:UP000190274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10888 {ECO:0000313|EMBL:SCU78057.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT598460; SCU78057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4IN04; -.
DR   STRING; 1266660.A0A1G4IN04; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000190274; Chromosome A.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000190274}.
FT   DOMAIN          126..288
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          359..444
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          82..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  56278 MW;  FAD881AB92300B5A CRC64;
     MSRVALRAFT TTQPLRFAAA KTGGFKYQKI PSPKELRQFL DNYVVGQTVG KKVLSVAVYN
     HYLRVNDKQK RLEAKLQSEL LEQQRQEDDE NEPIYSESTE AKSGYRQLRK QLSQDMGLGD
     ADLELSKSNV LVVGPSGSGK TLLASTLARV LDVPIAITDC TQLTQAGYIG EDVEVCIERL
     LVNADYDVAK AERGIIVLDE IDKLAKPAAS IGTKDVSGEG VQQSLLKILE GHSVEVTVKK
     PVKQKKDDKQ NQINAKKDET FVVDTSNILF MLMGAFVGLD KHVVKRINSL RAQSAGEMQE
     DKNDDIKRLR FSNTIEKVQL PNGQKTSALN LATPSDLVSY GLIPELIGRV PIITALEPLE
     RSDLYHILRE PKNALLNQYE YIFKQFGVKL CVTQKALIKV AHFAQNEGTG ARGLRGIMER
     LLLNVNYECP GSGIAYVLVD EKTVNALKQS NHSLSSHVVA RYYSRGERDR FIEDVYKEDT
     EQGKLLDNLY GRVGSRIIEG KAIHE
//
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