ID A0A319DVI1_ASPSB Unreviewed; 882 AA.
AC A0A319DVI1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative dsDNA-dependent ATPase {ECO:0000313|EMBL:PYI01777.1};
GN ORFNames=BO78DRAFT_401060 {ECO:0000313|EMBL:PYI01777.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI01777.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI01777.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI01777.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ826407; PYI01777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DVI1; -.
DR STRING; 1448318.A0A319DVI1; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18004; DEXHc_RAD54; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248423}.
FT DOMAIN 220..390
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 543..697
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 97951 MW; 654A88C04A906D00 CRC64;
MQFSKHKGVE ANESQRRKVT TKKNKTWDGD GILTIRNGYA YLQDVSGKDM GRGMHGSRLE
PGVMLSIGGK EVEIDSEMSR KEYLSGRQFL KANNEPLPTA LPTKAFVPVR SSTSASTTSA
KSQPAKPNTA TLANPASKRG TISSAFKKPL LESTVLPQTP SEKPIPRHDP NQPGALVMKR
PESVPKGKQI VDVVVDPFLA KHLRPHQREG VQFLYECVMG MRSFNGEGAI LADDMGLGKT
LQTIALLWTL LKQNPVYESP PVIKKALIVC PVTLINNWRK EFRKWLGNER IGVFVFDDKR
KRITDFTRGK AYSIMIVGYE KLRTVQEGLA RGDSVDIIVA DEGHRLKTLQ NKSGQAIQSL
NATKRIILSG TPIQNDLKEF FAAVDLVNPG VLGTFKSFIR EFEGPIVKSR QPEATKKDIE
KGDARNEELR ELTSKFMLRR TADILAKYLP PKTEYVLFCN PTRTQASIYQ NVLASPVFQT
ALGSSENALQ LITILKKLCN SPSLLSPRNV NETPSETITA LMSSLPPNLL RHFSPSSSAK
IRVLDQLLDN IRTNTSEKIV LVSNYTSTLN LLATLLTSLS LPFLRLDGST PAQKRQSLVE
DFNRLPPNLC FAFLLSAKAG GTGLNLIGAS RLVLFDVDWN PATDIQAMAR IHRDGQKHHC
RIYRILLKGS LEEKIWQRQV TKIGLADSVM EHRDSVAQFS RDELKDLFRL DEKSKCQTHE
LLGCDCGGNG ILPSENESKE DKDDDKHSTS SDSELEDFPD LPTLLKASEV DMEKQERQIR
DSRAALRSGS NRSSKPGKDD GNGTTKQKHR MQQSLSQYCH IDPSHLVSTE TNTPEGIESA
LDDDILLSLL KDEDNRVGFI FKKSSTAEAK GDTPSSPVVI LD
//
