ID A0A1Y2GKG8_9FUNG Unreviewed; 580 AA.
AC A0A1Y2GKG8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:ORZ13847.1};
GN ORFNames=BCR41DRAFT_89852 {ECO:0000313|EMBL:ORZ13847.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ13847.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ13847.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ13847.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORZ13847.1}.
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DR EMBL; MCFF01000022; ORZ13847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2GKG8; -.
DR STRING; 64571.A0A1Y2GKG8; -.
DR InParanoid; A0A1Y2GKG8; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000193648; Unassembled WGS sequence.
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; 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 Hydrolase {ECO:0000313|EMBL:ORZ13847.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193648}.
FT DOMAIN 198..452
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 436..530
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 64..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 62004 MW; 991633A35C36DEA0 CRC64;
MIVKHLDEYV IGQEKAKKIL AVAVYNHYSR VNENLRQHHI QETAAAMANN PPLSTNMYYG
SSVLMSDGPS TPDPIIEPYN PPSPPTSPSS SSSSPSSSGS DSSSSSKETN SGSSSGTNSN
SNNSEAHVPG RQAIHYPHRQ PWINTATNGH GHGQNPPSMF SQPYDTYQKP PSPPHTQQSP
LARKGVETQT KTPPTIFDKS NVLLLGPTGS GKTLLARTLA KVLNVPFSMS DATPFTQAGY
VGEDVEMVIH RLLQNCDYNI KKAECGIVFI DEIDKIAKRP DTMSISKDVS GEGVQQALLR
MLEGTVVNVT EKNGSSWNGS SMGRKNGLPG IGGPNSGGGG PGAKGEIYSV DTSNILFILS
GAFIGLEKIV MDRVSKGSIG FDANVRAPSS ELSSSKGAAT HVSKLLDQVD PADLIKFGLI
PEFIGRLPVV ASVNHLDEAA LVRILTEPRN SLVKQYQGLF GLADVKIHFS QSALHSIAAQ
AIEKQTGARG LRRIMESMLL DMMYEAPDSS IKHIVINKEV VLGKKPALCF GRGAESTVTE
ALDRDDEEFG FRHPQIQETP AAVAGQSQDD EPAAAEAVSV
//