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Database: UniProt
Entry: A0A1Y1WDQ3_9FUNG
LinkDB: A0A1Y1WDQ3_9FUNG
Original site: A0A1Y1WDQ3_9FUNG 
ID   A0A1Y1WDQ3_9FUNG        Unreviewed;      1364 AA.
AC   A0A1Y1WDQ3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=SNF2-family ATP dependent chromatin remodeling factor snf21 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DL89DRAFT_221932 {ECO:0000313|EMBL:ORX71304.1};
OS   Linderina pennispora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX   NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX71304.1, ECO:0000313|Proteomes:UP000193922};
RN   [1] {ECO:0000313|EMBL:ORX71304.1, ECO:0000313|Proteomes:UP000193922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX71304.1,
RC   ECO:0000313|Proteomes:UP000193922};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORX71304.1}.
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DR   EMBL; MCFD01000004; ORX71304.1; -; Genomic_DNA.
DR   STRING; 61395.A0A1Y1WDQ3; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000193922; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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: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; 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; 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; SM00573; HSA; 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: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:UP000193922}.
FT   DOMAIN          77..112
FT                   /note="QLQ"
FT                   /evidence="ECO:0000259|PROSITE:PS51666"
FT   DOMAIN          294..367
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          481..646
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          795..956
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1179..1249
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          15..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          961..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1032..1057
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1094..1150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1337..1364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1364 AA;  154747 MW;  E0DBECB54E24E141 CRC64;
     MAFIRQLAAQ QQQFQQQLQQ QQQPTPGSAT PVKTEPTLPT VTNGSTTNGS QSSETVTAVV
     SAEQSQQTKE PAVPPPQFSQ ADIATLRKQI HAFRLVSKNQ PLPPQLRQEL WASSIPEDEK
     RLLDTPPEGL DGVAGGPINF VSPHQLLKEK LHGGDQAARM QRLLVPSITP TGIDVRAMAQ
     ERERRRDARI EYRIKELSEM PANISDDRID IAQEGGLFMR PGLITNAESS ARLKSIIELK
     ALGLRHKQRE LRAEVVRGIT RASQLGVAGD RTALRRMKKQ SQREARLTEK MERQQRQERE
     RREVDQHRQQ LLAMTNHGAN LVAWHKGHQQ RMSKLGRSIL TFHSHAEREE QKRKERIARE
     RIQALKAGDE EAYLKLVDKE KDTRISHLLE QTDQFLSSLI DAVGQQKASV ATDSNPVSAN
     EPVPSWLQDN AEAVDDDPDD AQTRDYFAVA HRVKEPIVAQ PSILIGGQLK DYQLRGLEWM
     VSLYNNRLNG ILADEMGLGK TIQTISLVTY LIEKKQQDGP FLIIVPLSTI TNWILEFAKW
     APSVSVIGYK GNPTQRRTLQ NQIRRGAFQV LLTTYDYIIK DRPMLAKIKW IHMIIDEGHR
     LKNTQSKLAT ILTTYYNTRY RLILTGTPLQ NNLPELWALL NFVLPRVFSS VQSFDEWFNT
     PFAGAGGQDK IELNEEEQLL IIKRLHKVLR PFLLRRMKKD VEVDLPDKVE HVIKCSMSAV
     QSRLYHQMRK FGTLFPGVSI DRPGGRSSNA SLNNMIMQLR KICNHPFVYD EVEARINPTR
     TNNNLLYRTA GKFELLDRVL AKLLATNHKV LIFFQMTQIM TIMEDFLTWR GIRSLRLDGS
     TSDDARREQM HTFNSPDSPF KVFLLSTRAG GQGLNLQTAD TVVIFDSDWN PSADSQAMDR
     AHRIGQKNEV RILRLITTNS VEEKILARAE YKRDLDGKII QAGKFDQKST AEERENFLRS
     LLKADDNSED SEGEDGANTD EDLNELLARS DEERVIFARM DEERRAQEKV EWVDAGNTGR
     LPERLFTEAE LPEEYRHDYD PELERQRKEE EAVKDKARNS RRVYYDDGLS EEQWLDALED
     DNVDLDDYIA KKREKEERAR DATPSSGGRS RSGRKRAKLD DDATGSSTPA GAATPSGGSR
     KGRRKGGAVD PLAAEERAQL NGVFEASFKA VEACIDPEYQ RRRCDLFLEV PSKRDYPDYY
     VIIRHPIAMK NIRKKVRSAH YLTVEDFHKD WKLMFDNART YNEEGSMVYE DACEMQKALE
     DTLEKMTGQN YHTPIGTQSP LPAVFNLALQ QQQVQQAQMS PQPQLPQVPI AGVSPVQESP
     SMQNGVVAAH PASSLVNQAS PTMSGHGGFA TPEDPSHLHQ NGQL
//
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