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Database: UniProt
Entry: Q2UQ09_ASPOR
LinkDB: Q2UQ09_ASPOR
Original site: Q2UQ09_ASPOR 
ID   Q2UQ09_ASPOR            Unreviewed;      1026 AA.
AC   Q2UQ09;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=SNF2-related protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AO090005001434 {ECO:0000313|EMBL:BAE56356.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE56356.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE56356.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AP007151; BAE56356.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UQ09; -.
DR   STRING; 510516.Q2UQ09; -.
DR   EnsemblFungi; BAE56356; BAE56356; AO090005001434.
DR   HOGENOM; CLU_000315_16_2_1; -.
DR   OMA; ELQAYND; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:EnsemblFungi.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0031934; C:mating-type region heterochromatin; IEA:EnsemblFungi.
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:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000729; P:DNA double-strand break processing; IEA:EnsemblFungi.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0033120; P:positive regulation of RNA splicing; IEA:EnsemblFungi.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:EnsemblFungi.
DR   CDD; cd17998; DEXHc_SMARCAD1; 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; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT   DOMAIN          494..661
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          848..1004
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  114169 MW;  16EC4C96448407A9 CRC64;
     MAPSGTQFRP PAVGPAKRAP VIDLEDDGPT YRGGSSDDDD IQMISSTDIK PSLFAKSSRN
     PEKVLDSPGS ATNSSFDRFK EITASAVYNP SSAKRPAAQM DPVPKGTAVK KPRQDGPSRA
     QPVELDISSL HDIEDYQLRA KVEKMQRVIP QKSVKACMQA LLTKRGNYDD ALDYLASMVE
     DEADGRADLS DDELAFNKRA SPVAPAKQQI KARGTIQNKW AAMRLDNRNT PKAPAQPSDE
     ESKPRRRLIR GPKTRVSSPS PDRSESPPKK KTGRLVQGRK HPSPEPSEPE ASMSDDSDSG
     VEAITEGESA LETKVLRFFN TCNVLDLADI AAITEDVAKV IISNRPFASL DEVRVVTAPT
     TEQTAKPKGS RGRKTPKPIG DKIVDKCMDM WVGYEAVDSL VAKCEALGKP IASEMKKWGV
     DIFGKRDGEL ELTSIDPGAS HDSGIGTPAS QRSEDDSDGP ATGSRKSRFI SQPGIMREDL
     KMKDYQIVGI NWLSLLFEKE LSCILADDMG LGKTCQVIAF LAHLYEKGIK GPHLIVVPSS
     TIENWLREFQ KFCPTLSVMP YYAGQAERAV IRETIEDNRD SINVIVTTYT IAKAKVDAHF
     LRNMDFSVCV YDEGHMLKSS TSVLYEKLIR IRARFRLLLT GTPLQNNLQE LASLLGFILP
     KVFQERKEEL QNIFANKAKT VDESHSALLS AQRIERAKSM LKPFVLRRKK HQVIDLPPKV
     SKVEYCELNE SQREIYEHEQ EEVRKLLADR AAGKKTGNKS ANILMKLRQA AIHPLLYRRH
     YKDTTLSRMA KACLKEEQWS LSNPDIIFEE LQAYNDFECH TMCVNYPKSL GKFALKNNEW
     MDSGKIDKLC ELLKRFKENG DRTLIFSQFT MVMDILEHVL ENQHLGFVRL DGRTNVEDRQ
     SILDAFHERT DIPVFLLSTK AGGAGINLAC ANKVVIFDSS FNPQEDVQAE NRAHRVGQTR
     EVEVIRLVTK DTIEEQIYAL GQTKLALDQA VAGEDAGESK KSEEAGMKAV EDMLIAGSGG
     EKHSSS
//
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