ID C5E0V0_ZYGRC Unreviewed; 1651 AA.
AC C5E0V0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=ZYRO0G15796p {ECO:0000313|EMBL:CAR29734.1};
GN OrderedLocusNames=ZYRO0G15796g {ECO:0000313|EMBL:CAR29734.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR29734.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CU928179; CAR29734.1; -; Genomic_DNA.
DR RefSeq; XP_002498667.1; XM_002498622.1.
DR STRING; 559307.C5E0V0; -.
DR GeneID; 8206493; -.
DR KEGG; zro:ZYRO0G15796g; -.
DR HOGENOM; CLU_000315_15_2_1; -.
DR InParanoid; C5E0V0; -.
DR Proteomes; UP000008536; Chromosome G.
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 CDD; cd22541; SP5_N; 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; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 138..173
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 542..618
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 730..895
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1042..1205
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1493..1563
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 52..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1449
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1651 AA; 188440 MW; 860982A068FE4030 CRC64;
MNLEIPQRQF TKEEINRCYL RWQQLRNEHG ENAPNVPEFI YFTKVLHVAA KQQQEQQQQH
QHQHQQQQQQ QQQPPQQQQV PYAMPSMQAM NQQRQASGTP QPIPLQQPRS GSPGISSSQS
APQGAQQTNG HNSHHSTIFT AEQSELLKAQ ITSLKSLVNQ QPVSPECQNI IQQSVSSAPD
FKKMLMALSE FVKKRQLQQQ QNGPAQSPPP QQRQQQSPLP QQQQMQGPNP QQSPAPRQMT
PQMANARLQQ LQFQQQRQQQ QLQRQQWQQQ QQQQQLRNQQ LQQQKERILK AQMSAAATPS
GESNGTPNGI GGTPAGSLST PGGDVQSKEE REQSLSNVGD QQPSQSDPVE PPKQQQQPQP
QPQPQPQIPE EAKKPPKQQA PIPLSEFVEK TKEVGRVVDT DNPDLVVDSY DLPPTPNEMV
DYQSLFPNAI KPKLTITPGL LPVGLDVHTA EEIYQTLIAL NLDTSVDDCL AKVLDESVSD
ELKDQCIYDY YALQLLPLQK AVRGHVLQFL WYQSSLLTNT HPNFLSKIRN INVQDALLTG
ELYKKHESLQ YEKKRVEKIK KLEAVRTSCV DLYNKRLDNR TKRVKFGHKL IGIHANIEKE
EQKRAERKAK ERLMALKAND EEAYIKLLDQ TKDTRITHLL RQTNAFLDSL TRAVKDQQEY
TRDMIDSHLK EDSEDHDIVS TMNDDDDEES SNVDYYNVAH RIQEDIKEQP SILIGGQLKE
YQMKGLQWMV SLFNNHLNGI LADEMGLGKT IQTISLLTYL YEKKNIKGPF LVIVPLSTLT
NWSSEFEKWA PILRTIAYKG SPNERKAKQA IIKSGEFDVV ITTFEYVIKE KSVLSKPKWV
HMIIDEGHRM KNTQSKLSLT LNNFYHSDYR LILTGTPLQN NLPELWALLN FVLPKIFNSV
KSFDEWFNTP FSSAGGQDKI ELSEEEMLLV IRRLHKVLRP FLLRRLKKDV ERELPDKVER
VIKCKMSALQ SVMYQQMLKH RRLFIGDQTN KKMVGLRGFN NQIMQLKKIC NHPFVFEAVE
DQINPTRETN AAIWRVAGKL ELLERVLPKL KATGHRVLIF FQMTQIMDIM EDFLRYIDIK
YLRLDGHTKS DERSELLSLF NDEEAGYFCF ILSTRAGGLG LNLQTADTVI IFDTDWNPHQ
DLQAQDRAHR IGQKNEVKIL RLITQNSVEE VILEKAHKKL DIDGKVIQAG KFDNKSTSEE
QEALLRSLLD AEDERRRRRE MGLDEEEEID DNEINEILAR DDDELIKFAE IDAEKSRKAL
EMGITTRLME SNELPEIYHQ NLDIELERED SETVAYGGRG TRERKTMAYN DNMSEEQWLK
QFEVSDEEDA DGESSGFKRR KAGKSRFGTK KLKVEDGNGE AASGDQTPTS SIEPLAERET
SAVDEPPLPD GPTTLEEPVE DATMALSPTL PVTAGKTTSK STRGRGRGRG RKTTAGRVRS
TRGRGRGRPP KPKAGLEYVR DPSATTEPQD VRIKVSEEAR ELYNYALEYT SDDEARLSDI
FLEKPPKELF PDYYQLIKYP IAFETINSAI ESFSYDSLKQ VLEDFHLIFL NARIYNTEDS
LVYINSVELE QVVTDKYREM TGDDRLLDFS KFEESFATKP LNLAQVLPED SAAADVASDS
PTVDGTKMDT IEPSETPHSV EPNDGGGSSS T
//
