ID A2QTI7_ASPNC Unreviewed; 1166 AA.
AC A2QTI7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Contig An09c0050, genomic contig {ECO:0000313|EMBL:CAK40162.1};
GN ORFNames=An09g02250 {ECO:0000313|EMBL:CAK40162.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK40162.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK40162.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270194; CAK40162.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QTI7; -.
DR EnsemblFungi; CAK40162; CAK40162; An09g02250.
DR VEuPathDB; FungiDB:An09g02250; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR014905; HIRAN.
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:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 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|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 520..718
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 888..933
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 992..1148
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 131282 MW; F051E709A1B74F42 CRC64;
MNIHDADERP LKKRRFFVDD EDLATPQPST DSVTASLHTP DSSSLAGQES QPQPTRSQNG
LEDTKELLMD DSTRVEDHAV PHVEQEIVQA EHHNADSRTE GALLQVDYDG FDISTFTSII
GENLSADSIQ RIRSAAGDDL ERAVNIYFDG SWKKSPTPRA QNQTTLTARQ RPLPTQPHKI
ATPLSATCKP HTQILPPDKI TSRPATQPPL RYIGAFGVGA WATRSGAGFL RHGDLVNIER
TRSQPLSKRN RAGKLVSNQK SDVLTRFTTK SGQEIGRLPR ETAEWVSTLL DQRVCTFEGV
CVYVPDRVRV NDTIYLQLRC YLRIEAFQPR IFSQSMDDNR SVAIFEEKES ADEKALRLRQ
VALVKLFDEI HLQPTSVNDM TRNHKKEGLL RAAEMAEQHE RVKKENQTND DSSEEDSPEL
EEDQLDTLYK KAQSFDFSMP EAEPASSFTL HLRKYQRQAL YWMLAKEKDN KSARETSLHP
LWEEYSWPSR DVDDKELPAV AGIDHFYVNP YSGELSLDFP VQEQHCLGGI LADEMGLGKT
IEMLSLVHSH RIMPQKPTDL VRLPQSASGV VPAPYTTLVI APTSLLSQWE SEALKASQPG
TMNVLMYYGA DKNINLKNLC ASGNAAAPNL IITSYGVVLS EYRQHMSALL SSMSSGGLFS
VDFFRVIVDE AHVIKNRLSK TAKACYELKA THRWVLTGTP IVNRLEDLFS LVRFLKVEPW
NNFSFWKTFI TVPFESKDYV RALNVVQSVL EPLVLRRTKT MKTPEGEPLV PLPRRTITIE
EVELPDQERE IYDLIFTRAK QTFNHNVEAG TLLKSYSTIF AQILRLRQTC CHPILTRNKA
IDDMDLQDLI DRFKASTEAA ESNEPQDPSA KFTAHALKQI QNEASGECPI CSEEPMIDPA
VTACWHSACK KCLEDYIRHQ TDKGMDPRCF SCRAPTTSRD IFEVVRHESP NTTPEDDIYS
STPTPSQAPP RISLRRIHPL SPSAHTSAKV HALLAHLARV PANTKSVVFS QFTSFLDLIS
PQLTRAGIHH VRLDGTMPHK ARAETLAQFN RHRHSTAPPP PTVLLISLRA GGVGLNLTAA
SNVFMMDPWW SFAIEAQAID RVHRMGQTRD VQVTRFVVKD SIEGRMLRVQ ERKMNIAGSL
GLRVGGDGSE DDKKKERIEE LRLLFE
//
