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Database: UniProt
Entry: A0A094GK85_9PEZI
LinkDB: A0A094GK85_9PEZI
Original site: A0A094GK85_9PEZI 
ID   A0A094GK85_9PEZI        Unreviewed;      1613 AA.
AC   A0A094GK85;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   03-MAY-2023, entry version 32.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
DE   Flags: Fragment;
GN   ORFNames=V501_09994 {ECO:0000313|EMBL:KFZ01439.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ01439.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ01439.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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:KFZ01439.1}.
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DR   EMBL; JPKD01003277; KFZ01439.1; -; Genomic_DNA.
DR   STRING; 1420914.A0A094GK85; -.
DR   HOGENOM; CLU_000536_3_2_1; -.
DR   Proteomes; UP000029315; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd05491; Bromo_TBP7_like; 1.
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; IPR041569; AAA_lid_3.
DR   InterPro; IPR045199; ATAD2-like.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23069:SF0; TAT-BINDING HOMOLOG 7; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029315}.
FT   DOMAIN          652..793
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1325..1562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1295..1322
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..84
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..258
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1349..1385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1398..1486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1499..1538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1613
FT                   /evidence="ECO:0000313|EMBL:KFZ01439.1"
SQ   SEQUENCE   1613 AA;  176212 MW;  AE28A71D04B3DCDA CRC64;
     MPVKRKLEHF DPNKSDSNDD DYESGPERRT SRKSVGRSKS KGGASAKKKK RAKYRGSDVD
     DDDDDLTDDS LLDQSFDEEE EEPERTETGR PLRGVVKKSV KYEESESDVE DVGTNNDDDE
     EEEDIAPKKN RSPKKMMITL KVKTPVPSSK RTTRAGSVRA SAEPTTAANR PRRNTRAHTE
     EVDEGLVALS NSGRHAVVQG ESPTPETSKA LRPMRGGKGL KMPVGETILE ASHESTVPEE
     GEEDAEGEAM EVDEETKGDI EIGDSHATKD DTQAFSEKDE GGGDLMAELT AAAAVGDGAN
     DEEDDDEDDD LPVSRTRVNR TSVSQTVTNV EQTVEETVEG EPSTPPGGRR LRKRTQPQKA
     GLEQTSDFEP NEESEEDISA SDASPRKRKG SDNDTDSTPR RGRGAHGKSK SSRSRRRDDS
     DGDSEALDAD ELLEEAAELK ANGRRRPRAR RDPEILYESM GRRERKRVDY TIKPMDQIYA
     ADEDLEDAAP APSGRSKRNT GSQAKWERTL HTTYGPFGGG GGPTPVTGPG PWGTGAAGGA
     DSDSSDDENL ARPTGVAGNV GMTPTTGMPA GLLPGLGQTN PSEPMAAVGG TPNNLGKIKS
     QKALADADPL GVDQNVDFSK VGGLAGHIDQ LKEMVQMPLL YPELFLKFHV TPPRGVLFHG
     PPGTGKTLLA RALAASVGSG GRKITFYMRK GADALSKWVG EAERQLRLLF EEARKTQPSI
     IFFDEIDGLA PVRSSKQEQI HASIVSTLLA LMDGMDGRGQ VIVIGATNRP DNIDPALRRP
     GRFDREFYFP LPDIEGRRSI IDIHTRDWGV DDKFKDSLSH VTKGYGGADL RALCTEAALN
     AIQRTYPQIY SSNDKLIVDP DKIKITAKDF MLSIKKMVPS SERATSSGAA PLPKAVEPLL
     RDQLKSIEAL LDGLIPIKKK TTALQEALYE QYEDADAGFG RETLAQDFEK ARVFRPRLLI
     GGDPGMGQGY LGSALLNHFE GLHVQSFDLP TIYSDSARSA ETAIVQLFAE VKRHKPSVIF
     LPGVDTWYHT LSDSAITTFL GLLRGIPPTD PVLVLGICDA EPDQASQEMI RDLFGFTKKN
     RFLITKPTRH NREDFFKNII DYIKKQPTDF PDPVNRKLRK LDTLAIAPPP PPRVPTKEET
     KALKHRDRQT LNTLKVMIQP IMDQIQKKYR KFRNPAVPQS VIQYLYDEQD PNYVRPDVVQ
     FRPYELDVDK DGVSGLRDSA TGKFFYNLET TTIEERLSNG FYARPKDFVA DIRRLAKDMK
     NTGDQERALR GKELLANVEV DLALIEANPV VADCENVYQR QLQRVKEKAE KHRKRAEEEA
     ILIGSDIPAE GSREEPIVLG MPTPKSRAPG LFSTPTSLSN GTATHSSLSS EQRLSNGSSL
     PSTRHSDGDD VAMGGTDEAS QLDSQNMPPP PATTGGSLFR SRTSMPSALN TQGSQFSQRS
     AFQSLPHDVS PTALFNDAST TTSGRKTESS GDKSTQLTNG HGGSQQYSPH LHGHGEGDSQ
     LPDTQSQDWV HSQVHGRPPT ALSASVSHST SAPSQPGGAS APTPAYPSMH AGSDQDLAST
     AGEPSQVVSV AASSQKEVII DEVYLAQLLE MFVSRTDGWG VEDLEMAYRE MME
//
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