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Database: UniProt
Entry: A0A1Z5TF18_HORWE
LinkDB: A0A1Z5TF18_HORWE
Original site: A0A1Z5TF18_HORWE 
ID   A0A1Z5TF18_HORWE        Unreviewed;      1422 AA.
AC   A0A1Z5TF18;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Chromatin structure-remodeling complex subunit snf21 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BTJ68_04252 {ECO:0000313|EMBL:OTA34599.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA34599.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA34599.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA34599.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OTA34599.1}.
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DR   EMBL; MUNK01000056; OTA34599.1; -; Genomic_DNA.
DR   STRING; 1157616.A0A1Z5TF18; -.
DR   VEuPathDB; FungiDB:BTJ68_04252; -.
DR   InParanoid; A0A1Z5TF18; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000194280; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd04369; Bromodomain; 1.
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; 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; 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; PF08880; QLQ; 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; 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:ARBA00022806};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT   DOMAIN          150..185
FT                   /note="QLQ"
FT                   /evidence="ECO:0000259|PROSITE:PS51666"
FT   DOMAIN          375..447
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          553..718
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          864..1015
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1276..1346
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1154..1249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1363..1422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1154..1171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1203..1244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1377..1394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1422 AA;  163038 MW;  ACC3702AD14C06F1 CRC64;
     MAAVQPAQQG MPQQQGVNPA MGGQGQSVLP QGMTKEQVQQ MYQKYQAMKR QGVPDTDPEM
     MKARTILQQI QQRQELMKRQ QAYRQMQMKQ QQQQQQQAAA MHNGDMSANG AAASQAEPPA
     SNGTPQTTTQ TAQPAQTTAG PTQTDGSQDG FSKDQMMTLR AQMQAFGHLQ KNMPIPQAIQ
     ERIFTQKQNP KPAVADAVTA AGKVLDRTAT PAKPADGESD GNPRHRFETF TDPHSLLLKQ
     ISYTDHTQRA YRPFIPSIMP LGVDPERVRD ERENMVYNRV LARKNELSKL PANIGAWDTS
     KSDAPQDNAN LKLKALIEYK MLSLLPKQRE IRQKLSKEMM LSDNLSMTAN RAMYRRVKKQ
     SLREARVTEK LEKQQRDAAE NKEKKRHNDF VNSIVRHSED MRNSAAVHRS RNQKLGRLMQ
     QTHMNIEKEE QKRIERTAKQ RLQALKANDE ETYLKLLGQA KDSRISHLLK QTDGFLNQLA
     SSVKEQQRNM SQKYAPEPDE PEPEEPDSED ETKTKVDYYE VAHRIKEDVR EQSTNLVGGI
     LKEYQLKGLQ WMLSLYNNNL NGILADEMGL GKTIQTISLV TYLIEKKKQP GPFLVIVPLS
     TLTNWNNEFE KWAPSVQRIV YKGPPQQRKN YQQQIRYGQF QVLLTTYEFI IKDRPVLSKI
     KWLHMIVDEG HRMKNAGSKL SSTITQYYHT RYRLILTGTP LQNNLPELWA LLNFVLPHIF
     KSVKSFDEWF NTPFANTGGQ DTMALTEEEQ LLVIRRLHKV LRPFLLRRLK KDVEKDLPDK
     QERVIKCNFS ALQSKLYKQL VTHNRIMVND DKGRKTGLRG LSNMLMQLRK LCNHPFVFEE
     VEDQMNSSRM TNDLIWRTAG KFELLDRILP KFRATGHRVL IFFQMTQIMN IMEDFLRWRG
     LKYLRLDGST KADDRSELLK EFNAPDSDYF CFLLSTRAGG LGLNLQTADT VIIYDSDWNP
     HQDLQAQDRA HRIGQKNEVR ILRLISSNSV EEKILERAQF KLDMDGKVIQ AGKFDNKSTN
     EERDEMLRVM LESAEAAENL DENEMDDDDL NMMMMRNESE LAVFQELDRD RSRKSGYGPD
     KKLPRLLGES ELPEIYMNED NPVVEEIEYN YGRGARERTK VKYDDGLTEE QWLDAVDADD
     DTIEEAIARK QARMQKRATK KEGKLRDDFD LGTSPPPEPS RQASESPAPA TAKKRGRKSA
     GRQSTKRTAE EASLDGGSEP PSKRERGTGR SEAKTPRGKV AETLSPEDRA TLQKILDNVH
     DSLQDLEEPS TDPSIPNRGI IDPFLALPPK VHYPDYYQLI KEPIAMKQIE NKINKKQYQS
     LRQFWQDIKL LCKNCRQYNE DGSVLYNDAD MIERACAQKL REETEDHPDW QNWDEESEGT
     STRPISSTGT PQPPKSGIKL KLGSKANGTS RPVSAAQSDD DE
//
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