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Database: UniProt
Entry: A0A5N6ZGZ6_9EURO
LinkDB: A0A5N6ZGZ6_9EURO
Original site: A0A5N6ZGZ6_9EURO 
ID   A0A5N6ZGZ6_9EURO        Unreviewed;       609 AA.
AC   A0A5N6ZGZ6;
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:KAE8356638.1};
GN   ORFNames=BDV28DRAFT_154492 {ECO:0000313|EMBL:KAE8356638.1};
OS   Aspergillus coremiiformis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=138285 {ECO:0000313|EMBL:KAE8356638.1, ECO:0000313|Proteomes:UP000327118};
RN   [1] {ECO:0000313|Proteomes:UP000327118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 553.77 {ECO:0000313|Proteomes:UP000327118};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., 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   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; ML739036; KAE8356638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N6ZGZ6; -.
DR   Proteomes; UP000327118; 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:KAE8356638.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000327118}.
FT   DOMAIN          179..369
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          457..551
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          35..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  66913 MW;  13DCD95B18EED117 CRC64;
     MLWLRLSAPL QAHSRSIPRC RRAPSLLVRL PRHGFSSSST SFPTRSQFNR SDFTNQPWSG
     SYEPGLPTTG PLGSTPAFGA PRVTPKALKQ YLDQFVVGQD RAKKILSVAV YNHYQRVQEL
     QRREEEAIEL LAKRARRESV ERHPVEGQQR TTRSQFDPNL SASALNQIEL TDSSSTQLEK
     SNILLLGPSG VGKTLMAKTL ARVLSVPFSI SDCTPFTQAG YIGEDAEVCV HRLLAAANYD
     VELAERGIIV LDEVDKIAAV KVSHAKDVGG EGVQQALLKI IEGTTVQVQA KQEKNAPRVG
     GTPNTYPSNS PLGNSPYPPS SGGNMPQKGE VYNVRTDNIL FILSGAFVGL HKVIMDRISR
     GSIGFGQPVR TPSSSDVRSE QSAAANNQPI PILPGSEEEA LYKKHLPFFS SASPESSDGE
     PTYFNALDLI NPTDLQNYGF IPELVGRIPV TAALSALTQP LLVRILTEPR NSLLAQYTTL
     FSLSGIELRF TTPALHKIAS NAFTMGTGAR ALRTELETIL SDAMFETPGS SVKFVLITEP
     VASRQEKPIY LSRGQGGRFH AMIAAEESQW EEKQRREKRR DMKGKAQTAS EENHNISNFR
     EYRNRATGF
//
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