ID A1DP49_NEOFI Unreviewed; 1276 AA.
AC A1DP49;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=SWI/SNF family DNA-dependent ATPase Ris1, putative {ECO:0000313|EMBL:EAW16570.1};
GN ORFNames=NFIA_059210 {ECO:0000313|EMBL:EAW16570.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16570.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW16570.1; -; Genomic_DNA.
DR RefSeq; XP_001258467.1; XM_001258466.1.
DR AlphaFoldDB; A1DP49; -.
DR STRING; 331117.A1DP49; -.
DR EnsemblFungi; EAW16570; EAW16570; NFIA_059210.
DR GeneID; 4584983; -.
DR KEGG; nfi:NFIA_059210; -.
DR VEuPathDB; FungiDB:NFIA_059210; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_0_1; -.
DR OMA; ENENLEC; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000006702; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000006702};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 565..757
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 916..967
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1093..1254
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 56..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 252..279
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 62..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1035
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 143273 MW; 673C65EAA4A8C894 CRC64;
MTNIAEDASI DDLEDDLQLH QVILQSLNEQ RPSAVEERQE ILDIIRDLET RLARLRRGGQ
ATKTRSPVSR SGTPGSPLSQ AQLDGAALPR SNGALSPPQW GSSALSPPIR PYQPALDISP
YRPGLPISVG RPSGRISSAS ADNANSNKRS SSYGYDDDDL DRPLRGGSTH TRVSSSSAMS
ASREPAGLPL EAESSRKRRR QSSSGDLNFL RPQKRATDDR RPSNSSTASS HTHQSQLNDE
SEELKRLLGL DNDDTLRALQ EEQRKAEQWL EERKEQERRD EEYARMLMNG LYEPPRPASA
RSTASTNYLR SSIQFPSEAP LVYRGEAGPS SIPEHRSINT PLVDRLVDRS RSSYSIPSTP
ESGHSEVQHL PLITLRDSDD SDIAEISPRD FHSGQARPQS HHRLYPSYNT RPGHSSNRRS
VATELARYVP VTQPSIPPGY SAPQGSVYGP NVLQNTMARL QASRQMLQQA GRSVFEGFSS
YFSPSGSSGL PTGLSADDYY ASLKGYSDFS EPGVDPKQVQ EEIKQLLETI RPDTEIAKEK
REGTPEALRY TLLEHQKLGL TWMKTMEESE KKGGILADDM GLGKTIQAIA LMVSRPSTDP
ERKPTLIVAP VSLMQQWKRE IQKAVKPGRH QLSVYVLHGD KRAVSYRDLK DYDVVLTTFG
TLSSELKRRE KYDELQSAGA NEEALSRTLL KNLPCLGPSS LWHRIIIDEA QCIKNRNTRS
AQACCRLNST YRWCMSGTPM MNTVEELQSL LKFLRIRPYS SIDRFNKDFT RPLKGPPGEP
RDKAMQQLQV LVKAVLLRRT KTSKIDGQPI LRLPPRVLEK VHAVFSEDEQ AIYDALESKT
QVQFNKYLRA NAIGRNYSNI LVLLLRLRQA CCHPHLMTDF SVEVNAATDE LDLVANAKAF
GDEVVVRLKE NENLECPICI DAVDNPIIFF PCGHSACAEC FSRMTDPSLA VQRGEDGAAE
IKCPNCRGRV DPKKVTDHLT FKKVHSPDAD DPDQVGSLKP LRDEEDDDDS DDDDDDDDDD
DDDDDDDDDS LSRFIVDDED DPASVRKPKT KKGKKAKKTK KSLAELKKEA SKNIKSKQKY
LRRLEKTWVT SAKIEKTLEI LQEIQDREDS EKTIIFSQFT SLLDLLEVPI VRRGWGYRRY
DGSMRPGDRN AAVLEFTDNP DCKIMLVSLK AGNAGLNLVA ASQVIIFDPF WNPYIEDQAI
DRAHRIGQMR QVHIHRILVQ KTVEDRILEL QEKKREVIDG ALDEKAQKKV SRLGTQELAY
LFVCESIPQS FVQETN
//
