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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//