ID A0A0C7N4U0_9SACH Unreviewed; 1621 AA.
AC A0A0C7N4U0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=LALA0S01e11650g1_1 {ECO:0000313|EMBL:CEP60472.1};
GN ORFNames=LALA0_S01e11650g {ECO:0000313|EMBL:CEP60472.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP60472.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP60472.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP60472.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LN736360; CEP60472.1; -; Genomic_DNA.
DR STRING; 1245769.A0A0C7N4U0; -.
DR HOGENOM; CLU_000315_15_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000054304; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR014978; Gln-Leu-Gln_QLQ.
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:SF973; ATP-DEPENDENT HELICASE BRM; 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; SM00951; QLQ; 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.
DR PROSITE; PS51666; QLQ; 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:UP000054304};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 208..243
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 586..662
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 779..944
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1092..1255
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1504..1574
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 49..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1244..1271
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 49..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1621 AA; 185862 MW; 1799BE2645CF0346 CRC64;
MEIPQRQLTR EEINRCYLRW QQLRNEHGEN ASTVPEFIYF TKVLRVAAKQ QQQQQQQQQQ
QQQQQQQQQP QQQQPQQQQP PQHQSEPQTI EQSIQSPNVP PNPNHPGQGV SEAQRNTPTQ
ASPSHWPSGA QQPESAQQVP QQHHHQQQLQ QQQQLPPQQQ QNIPPRYSNG SLNSGMQNGN
AQSPVAQPSS GPAPSNSSSN LGPQGQTLFT TEQSELLKAQ ITSLRYLLSR QPVPHEAQEV
IQQSLNNPPN FKQMLLELSE TVKQRQTTQQ HVASPSRPNS MLNSNSATQQ SFSNVNQPQV
QQQSPVQVPQ QFPAQAPVQA PVQAPVQAPV QAPVQAPVQA PVQASIRASP QVYQEQMRPY
GSETHESDGR VPVTAAKSLS YNGDLNAPPP KAEEEITSIT SRKSIPQNDE NNVKTQPEKE
DTIKVPIPLE EYRTLNPEIE KIVNINASDI VDCYTLPPPI DEPIHYHQLF PTKAHPLPLL
RPGTLPPGID VHCAMEVYQT LIALDIDTAV DSCLTDLLND ETSLASKESA RNDYYSLQLL
PLQKAVRGHV LQFEWYQKAL LTNTHPNFLS KIRRVNLQDA LLTDELYKRH EVLQSQRRKH
EHITKLKSIA DSSIACYTNR LSRRTQRVKY GHRLVSLHTN IEKEEQKRVE RNAKQRLQAL
KANDEEAYIK LLDQTKDTRI THLLKQTNAF LDSLTKAVKD QQQYTKEKID SHLKVEEDIA
VDDPDAISSL PDVQDEDERR NIDYYNVAHR IKEEVKVQPS ILVGGTLKEY QLKGLQWMVS
LYNNHLNGIL ADEMGLGKTI QTISLLTYLY EVKNVRGPSL VIVPLSTLTN WDSEFEKWAP
VIRMVAYKGT PNERKSKQGI IRSGQFDVVL TTFEYIIKER SLLSKIKWVH MIIDEGHRMK
NAQSKLSLTL NNYYHTDYRL ILTGTPLQNN LPELWALLNF VLPKIFNSVK SFDEWFNTPF
ANTGGQDKIA LSEEETLLVI RRLHKVLRPF LLRRLKKDVE KELPDKIEKV LKCKMSGLQQ
KLYELMLKHR RLFSGDITGN NKTVTLRGFN NQIMQLKKIC NHPFVFEEVE DQINPTRETN
SNIWRVAGKF ELLERILPKF KATNHRILIF FQMTQIMDIM EDFLRLLGLK YLRLDGHTKS
DDRSMLLRLF NEPNSEYFCF LLSTRAGGLG LNLQTADTVI IFDTDWNPHQ DLQAQDRAHR
IGQKNEVRIL RLITENSVEE VILDRAHKKL DIDGKVIQAG KFDNKSTAEE QEALLRSLLE
AEENLKKKRE LGLEEDEQID DNELNEILAR NEEELKIFAD IDEERSRKHL ENGITTTLME
TAELPNIYHQ DIEAELKKED EDEVLAGGRG SRERKTALYD DEVSEEQWLK QFEVSDHEDD
DQAENDMAAD RKRSASEVST QNKKAKLETE EPENLDEKSP AEAMERGDTP TALPTTGQKF
TASNFDVKPK PRGRGRPPRS MDKKTGNPYI RDGSLLTLSE DERTRVAQEA RSLFDYAIKY
EDEDERRLAD IFLVKPSKKL YPDYYKLIRY PVAFENIMTH IESKAYGTLK NALEDFHLIF
ANARIYNTEE SLIYLDSLEL EKAIIEKYKE MTGTTDEVDF TEFDEKFATG PLKTQLPSGL
S
//
