ID A0A074XN07_AURPU Unreviewed; 1259 AA.
AC A0A074XN07;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=SWI/SNF family DNA-dependent ATPase Ris1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=M438DRAFT_343328 {ECO:0000313|EMBL:KEQ86905.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ86905.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ86905.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ86905.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584977; KEQ86905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XN07; -.
DR STRING; 1043002.A0A074XN07; -.
DR HOGENOM; CLU_000315_2_0_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000030706; 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; 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 Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 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 Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 503..692
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 853..903
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1067..1227
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 57..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..982
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1010
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 141989 MW; D51D516BE3C97A62 CRC64;
MSFLSSNADM EDLEDELIFQ QTILETLDPS DGNSGERRQE VELAILDLER RMAQFNNAAS
QPVAATDTST SYNAPGAYPQ DKDDEDDDDM NDLPQFDGST PAPNRNAQLK RTRDQMSPLA
GFDSNKRPAS SPMGPPGPVN QDRRAAYLER QRELEHAARQ RRESVAADAA FASSLSQQSA
SSPVAGPSRN QMSPSQMAPV FKRTPQSSAP APYPAPYAVP HPTSSYPRVK AEAHSSPSHA
YVPRPVKPES PQHPAPLSSR FGTPMVIDLT GDDEPESQQA RMQRMTNPED ALRRRHLWEQ
NNASTPQHKI EIMMRQRREM DFRHQQESQR QAEIALRNSA GQQDRAAHDH ANFIRLQQWR
QQVQAIQAHN LQYPHQPRPF PNHVPYQQQP SPSIIRSSQQ PVPRAAHDDF SQLRGLINGR
GRQPSFDSGE DELQFLRSTA IERPPWDIYD VDNMDTEEEL RKLMENIQPD DVSKIASEED
VPVEGLTIKL KPYQFAGLEW LQKMENGSNK GGILADDMGL GKTVQAIALM VTNRSEDPVN
KTTLILAPVA LLRQWEQEIM TKVKPGRHRL HTFVHHAGTK KKQHKDLREF DVVLTTFGTI
AAELKKMEKY ELRKKSDPMA QPRDDEKCVF IGPDCRWYRI IIDEAQCIKN KTTKTARAAF
YLQARSRFCM TGTPMMNSVE ELYSLIHFLR IRPYNSWQNF RTDFNQPLKG SSERARQLAM
QKLQALLKAI LLRRNKKTEI NGRPILNLPE RRVEEINPDF SEDERNLYVA LETSSAVKFN
KYLKAGTVSN SYMQILVLLL RLRQACCHPN LIKDLGIVAA TAEITQDTMD DICRNLDPNV
VARIKEANGT FECPVCYDAV ENPAIFTPCG HDTCPDCFSR IADPSNALAE GDEGRVAKCP
ECRGPINTKK VIDYECFKRI HMPEEIVSVK AEGAGDDADG EDMAAVDTDD DDSDDEEDEE
DDDDTDSLDG FIVEDGAEEE NDEEAAERRQ KAALKKSIKK KGKSKMSKKA KGKLKESSTS
DKKKKAATMT IPELKKMAIR KPSWRKIYLR MLKKDFQPSS KIERTMEILD GIMTAPENEK
IIIFSQWTSL LDLLEVPVSE KSWGYRRYDG SMNAKLRADA VDDFKNKPTV RMMLVSLKAG
NAGLNLNCAS QVVIMDPFWN PYIEEQAIDR AHRLGQTRPV MVHRVLIKET VEDRIIALQE
KKRALISEAL DEKASQSLGR LSVQELAFLF GISRNVNDAL PNAGPRARVR QGGAGGMGA
//
