ID A0A0L1J1F9_ASPNO Unreviewed; 1142 AA.
AC A0A0L1J1F9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative SNF2 family helicase/ATPase {ECO:0000313|EMBL:KNG85485.1};
GN ORFNames=ANOM_005143 {ECO:0000313|EMBL:KNG85485.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG85485.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG85485.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG85485.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KNG85485.1}.
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DR EMBL; JNOM01000155; KNG85485.1; -; Genomic_DNA.
DR RefSeq; XP_015406408.1; XM_015550400.1.
DR AlphaFoldDB; A0A0L1J1F9; -.
DR STRING; 1509407.A0A0L1J1F9; -.
DR GeneID; 26806947; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000037505; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; PTHR45626:SF14; ATP-DEPENDENT DNA HELICASE (EUROFUNG); 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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:0000313|EMBL:KNG85485.1};
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:UP000037505}.
FT DOMAIN 356..560
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 904..1065
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..327
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..863
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 127271 MW; AC18E059BFF17654 CRC64;
MAKESENPLN PITPGKPKDQ SHRHVSNQPE FGKPSPLGGG RPQNHQSNHP FNIPKQNRPR
PEHHRPQQQQ RPGAPFHSHR PPTTPGVAVS TPRRAEPFDP FKPVRPSAYN NSRFSRPVND
DVVVIKRPEN FTFNTPRAPK TFFASNASAV KVSNASKNLR NFVDLTGEGG FTPSSRSRNV
GFGSMDVNGY VDTAKANENI KALLEGAFED EDEKQDSKSK NKKKNKNKKN KDKNKKAEAQ
INKNKESSEI DDLAAQLQGV TVNESCTDET EADRSSEDTT DREAVEEQTK IQDKHVVTGD
IGSKNEDGEE EEDEDEEEEE DEDEDDGTVE GLKVKLLPHQ REGVNWMRDK EIGNSKTKGV
LPKGGILADD MGLGKTVQAI TLMLTNRKPK DGRRRIIDCE EDDNSGNDSE NDGGKDNSKL
PPGLSKSTLV VAPLALIKQW EAEIADKVET SHRLRVCVYH GNTRTKATDN LEDYDVVITT
YGTLTSEHGA IDKKNKKSGI FSVYWYRIIL DEAHTIKNRN AKATQSACAL DAEYRWCLTG
TPMQNNLDEL QSLIKFLRIK PYNDLAAWKE QITKPLANGR GALAIERLQV VLKAFMKRRT
KDVLKLNNNL KPNEAASDGG QKKSSGFHIV KREVIKVSAE FTPGELNFYK RLEQRTDNSL
EKMMGGSKLD YAGALVLLLR LRQSCNHPDL VKSDLAKDKD ILLQNGTSGS QPAAGKQDDL
DSMADLFGAL SVVSKKCDIC QAELSQKETK AGASRCGECE KDLNVSFAGN HSDKKKRYSE
REVVDLTESP SNRRSGAQLA RSRRNRKVVV DSDDEEDDGE WLVPEDQRTV PDLGKAGGSD
DEDAEGGGDW LGSEDSETDS DDEGGPESPT RNRMAGRKQA NESDEDDIYL NPGDDDNQVL
PSTKIRHLMK ILRRESADYK FIVFSVFTSM LDKIEPFLQR AGIGFARYDG GMRNDFREAS
LNKLRNNSGT RVLLCSLRAG ALGLNLTAAS RVVILEPFWN PFVEEQAIDR VHRLNQTVDV
KIYKLIVKDT VEERIINLQE RKRELANVTI EGKTAAAKLT MNDMMALFGR DAESRFTGER
GNIDLTQSTR LLSTADENNS SNSQSSDRPR TQASHSSSRD RSRQPEKRGG PRGEDSVFGR
RW
//
