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
//