ID A0A2J5HGJ3_9EURO Unreviewed; 1227 AA.
AC A0A2J5HGJ3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=SWI/SNF family DNA-dependent ATPase Ris1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BDW42DRAFT_26920 {ECO:0000313|EMBL:PLN76070.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN76070.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KZ559628; PLN76070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5HGJ3; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000235023; 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; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16449; RING-HC; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 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 SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 533..725
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 884..935
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1055..1216
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 72..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..985
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 137553 MW; C616508B55483084 CRC64;
MAAGPEAISS TRLQWVNEQM ASPTSPSVGD ILDDIELNHV ILQSLDEERP DAVEDRQDIV
NTIRNLEARL AELRGVPQPS ESRPSSPPRH QPSASEDLEV LRAQLDGSAD NGHRMVVSPP
HGRSAMSPPP RPGPPGSGQG TTTVLHSLGS SSAPKRPHTP ETDASDDTDD LERPPPKRTL
LSRPSPRPNS RDMPDRSFDR EGSAESQTDD SLMELLNLGG SDLRALEEAQ KELERDIQRR
KEQERQDEEL ARKFEQGYWE PPSSSQSTPS HHSNSPLSSR SQQPPGTMDR HPYPYRTYQN
PTLPNPPHRH VEPSALHSMG PSNPKRPAPI YLADSDDSDI AEITAGDFRR NAPPQMPRMT
DRPTLPPLPA QPSHSPYNNT WMSSFRKFSS LPSLPNPYAS LGGPSRPGPG DMTGRPAPMF
GPHVLHSTMS RLNQGKQMLQ DAGRSAMADL NFLFPTSRVA PYDLSSDYEV PSYFWEKFED
GVDPKKVNEE IKQLLETIRP DSDIDLKNRE GTPEALKLNL LEHQKLGLSW MKTMEENEQK
GGILADDMGL GKTIQAISLM VSRPSTDPDR KPTLIVAPVA LLQQWKREIE RTLRPGKHQL
TTYVLHGERR TMAFRDLKHY DVILTTFGTL SSELRRREKY DELHASGTAG EAQARDMLKS
MPCLGPSSKW HRIIIDEAQC IKNRHTKAAL ACCRLNSTHR WCMTGTPMMN NVEELHSLLK
FLRIRPYNSL DRFTKDFTRP LKSGSNDARD KAMRQLQVLL KAVLLRRTKE SKIDGKPILQ
LPPRVSEKVH AVFSEDELEL YRSLETKTQL QFNKYLAAGT VGRNYSNILV LLLRLRQACC
HPHLISDFSV QVNANTDEVD LIANAKAFGS DVVVRLKDND DLECPCCMDA VDNPLIFFPC
GHSTCAECFS RLCDPARAVS QGHDGSVEAR CPNCRRNIDP KKNTDHVSFR KVHYNEGPDD
AEQPEPAQAA DDEPSDDDSD DSDDDDGSLS RFIVDDSDAK TGSSSSQSNS KRKGKAPTKT
TKKTIAELKK EASKNQKSKR KYLRRLEKTW IPSAKIEKTL EILESIHAGE AGEKTIIFSQ
FTSLLDFLEV PIMRRGWGYR RYDGSMKPAD RNAAVLEFTD NPNCRVMLVS LKAGNAGLNL
VAASQVIIFD PFWNPYIEEQ AIDRAHRIGQ QRKVQIHRIL VESTVEDRIL ELQDKKRELI
EGALDENASK NVSRLGTREL AYLFGVH
//
