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Database: UniProt
Entry: A0A1E3PSV0_9ASCO
LinkDB: A0A1E3PSV0_9ASCO
Original site: A0A1E3PSV0_9ASCO 
ID   A0A1E3PSV0_9ASCO        Unreviewed;      1579 AA.
AC   A0A1E3PSV0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ODQ68501.1};
GN   ORFNames=NADFUDRAFT_81447 {ECO:0000313|EMBL:ODQ68501.1};
OS   Nadsonia fulvescens var. elongata DSM 6958.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX   NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ68501.1, ECO:0000313|Proteomes:UP000095009};
RN   [1] {ECO:0000313|EMBL:ODQ68501.1, ECO:0000313|Proteomes:UP000095009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ68501.1,
RC   ECO:0000313|Proteomes:UP000095009};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KV454406; ODQ68501.1; -; Genomic_DNA.
DR   STRING; 857566.A0A1E3PSV0; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000095009; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF1012; NUCLEAR PROTEIN STH1_NPS1; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000095009};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          530..602
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          709..874
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1022..1209
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1488..1558
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1317..1402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1417..1447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1175..1211
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1375..1391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1417..1432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1579 AA;  180610 MW;  A740EA0231975A37 CRC64;
     MSYNDENNNP NGINNNINND NNNSHSNNSP TQGFAPQFNQ SPAPAPHTPS TLNTPTPAPA
     EINHMSVPVL NENNNHSHLD SNSSNYNGEN HYGHTQDQFQ PLVSSQGQGQ GQSFVSHPAQ
     SFNTESVKSY NRESQQFSNG TQQPLVPNYN DYSSQNIQNN QNTQASVPYT DQQNQQNEQQ
     FQSSQQFQNQ QFQPNQQYQS QQQSQQPQSQ QFQRSYSHPT QQMTENQQFA ELQQFVPMPT
     PMPESIKKPV VIANVPHPET TGHVQLLLMR WKALKSQNIK EEDHAELAGI TYNLQRLVKE
     QKTYQDRLVK LRTMREKANQ RNLQQQADRL NTLRTQISAF NLLSHNLDLP TQTIDALIKT
     SSYNVPSKTT TQANPVFEDK HNEENIIVPN DLSFEERTAR MAVPPSGGFV TDRATGGLHE
     RIISNRITQR IIELESLPSN LGTLNVQDVA LESYDTIAKD ADSLKVKAVV ELKSLRLLTK
     QKSLRQHLVY NSAANSNNVY DSVTNRIIHR RVRIHSANDI RITEELERQQ RLDKEMKERQ
     KQFAYVSSIC HFSQSVLGES RCKHSRKLAL GRAVISMHAN IEREESKRVE RTAKQRLMAL
     KANDEEAYIK LLDQTKDTRI THLLKQTNSF LDSLAEAVQV QQREAKNMAA PYSNQVTAVP
     DGEVAGQDPE KIDYYEVAHK IKETVTEQPS ILVGGKLKEY QIKGLQWMVS LYNNNLNGIL
     ADEMGLGKTI QSISLVTYLI ESKRQPGPFL IIVPLSTLTN WTLEFERWAP TVKKIVYKGP
     PNSRKAYHAQ IRSGNFQVLL TTYEYIIKDR PILSKIKWIH MIIDEGHRMK NANSKLSRTL
     TTYYHTRHRL ILTGTPLQNN LPELWALLNF VLPKIFNSVK TFDEWFNTPF DNTGGQDKIE
     LTEEETLLVI RRLHKVLRPF LLRRLKKDVE KDLPDKVETV IKCKMSAIQS KMYGQMLRHN
     AIFTGEGSMG ATKTGVKGLN NKVMQLRKIC NHPFVFEEVE NMLNPTKLNN DILWRTAGKF
     ELLDRILPKF KDTGHRILMF FQMTQVMDIM EDYLRLKGLQ YLRLDGSTKA DDRTELLKLF
     NAPNSPYFAF LLSTRAGGLG LNLQTADTVI IYDTDWNPHQ DLQAQDRAHR IGQTKEVRIL
     RLITEDSVEE VILQRAHAKL EIDGKVIQAG KFDNKSTAEE QEAFLRNLLE AEENKRLAKD
     VDDELDDEEL NDLLARSEEE RIRFTQIDLE RQRTDNYSKD HSRLFTEAEL PDTYSADIAE
     RLEPVREENL GRGARERKVA FYDDGLTEEQ WLDAIDDDDD SVEAAIERKK RRIAKREINK
     AQHDSLGSGH SENEDDEDDE DNDELARSHK DVDDDVDGDD FIDNYDGDMM DVDNLTVSRG
     KRDRKSRSFD MNNDEIMSTS PAIIDELESN GADVKVESEI KDHEDIVNPP PRKKSRGRPA
     KSAVNGALSE ERKQLIDSCE KILNAVLAAR ETVSEVGDET ESGEAGVPGR YLNEIFLKLP
     SKRLYPDYYV LIKQPIAIDA IKKRIKSDAY ATLSDCKYDF DLMFENAMKY NEEGSFVYED
     AVTLKQIVQD QFNAMNNGD
//
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