ID A0A5N6EGZ2_9EURO Unreviewed; 613 AA.
AC A0A5N6EGZ2;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 03-MAY-2023, entry version 11.
DE SubName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KAB8216074.1};
GN ORFNames=BDV33DRAFT_159535 {ECO:0000313|EMBL:KAB8216074.1};
OS Aspergillus novoparasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=986946 {ECO:0000313|EMBL:KAB8216074.1, ECO:0000313|Proteomes:UP000326799};
RN [1] {ECO:0000313|EMBL:KAB8216074.1, ECO:0000313|Proteomes:UP000326799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 126849 {ECO:0000313|EMBL:KAB8216074.1,
RC ECO:0000313|Proteomes:UP000326799};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Petersen T.I., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Pangilinan J., Riley R., Salamov A., Simmons B.A., Magnuson J.K.,
RA Henrissat B., Mortensen U.H., Larsen T.O., De vries R.P., Grigoriev I.V.,
RA Machida M., Baker S.E., Andersen M.R.;
RT "Fungal friends and foes A comparative genomics study of 23 Aspergillus
RT species from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; ML733487; KAB8216074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6EGZ2; -.
DR Proteomes; UP000326799; 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; 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 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:KAB8216074.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000326799}.
FT DOMAIN 182..372
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 460..554
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 138..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 67260 MW; E5C77C9C40DD23C4 CRC64;
MLWLPLRPSA PLRAHHHLIL RYRRAPSSIV RLTQRGFASS SATFPTLSQF NRSDFSNQPW
SGSYELGLPT AGPLGSTPAF GAPRITPKTL KQYLDQFVVG QDRAKKILSV AVYNHYQRVQ
ELQRRDEEAV ELLAKRARRE SVDRHPVEDE FPGQQRTSRP PLDSSSSLNQ TELTDSSTIQ
LEKSNILLLG PSGVGKTLMA KTLAKVLSVP FSISDCTPFT QAGYIGEDAE VCVQRLLAAA
NYDVEQAERG IIVLDEVDKI AAAKVSHGKD VGGEGVQQAL LKIIEGTTVQ VQAKQEKNAP
RAGGTPNTYP SNSPLGNSPY PPSNGGGMSQ KGEVYNVRTD NILFIFSGAF VGLHKVVMDR
ISRGSIGFGQ PVRTPSNSDE RPGQSTTANN QPVPIVPGSE EEALYKKHLP FFTSASPESP
DGEPTYFNAL DLINPTDLQN YGFIPELVGR VPVTAALSTL TQPLLVRILT EPRNSLLAQY
TTLFSLSGIE LRFTTPALHK LAANAFTMGT GARALRTEME TILSDAMYET PGSSVKFVLI
TESVAARKEK PIYLSRGQGG RFHAMIAAEE SQWEERQRRE KKQRAWKAKA QAASEEHPSI
SNFREYRTRA AGF
//