ID W2LWP3_PHYPR Unreviewed; 1297 AA.
AC W2LWP3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Chromatin structure-remodeling complex subunit snf21 {ECO:0008006|Google:ProtNLM};
GN ORFNames=L917_01624 {ECO:0000313|EMBL:ETM01832.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM01832.1};
RN [1] {ECO:0000313|EMBL:ETM01832.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETM01832.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI677592; ETM01832.1; -; Genomic_DNA.
DR EnsemblProtists; ETM01832; ETM01832; L917_01624.
DR VEuPathDB; FungiDB:PPTG_06878; -.
DR Proteomes; UP000054423; 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:0042393; F:histone binding; 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; 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; 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; 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.
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}.
FT DOMAIN 306..378
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 485..651
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 799..966
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1176..1246
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 55..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1297
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 149502 MW; AF0364AD9CBAE526 CRC64;
MESTAGASAA PRVTLTPADV KKLMDAALRM QRAGQKSHPK YQQIVTLLRQ YQQQHRARQQ
QMQTQMQPPA QSQAPPQSLD VAANPFMQQK TTLFSDRQLE YLHNQIRAYK ALCHSMDTAI
AQAKQLSAAG LSMQPMDPTN AMMGATQQPP PSAVDPPVLE LMTPKWTRAA RNLLYVGPNY
LDGDLIGIEN KGNLAFGPFN ICTPWLGTND VGLKMRYMHT LQQFLASSLE KLESHTGDLD
ENEQRTLRDL RCVLLQQKLR RHVAKAHTTR LALLGEPSAV DRKSFRRRRP VSRVELQSDE
REKRKKSVAM EKKRRADHQM YLKAVLNHSR EFFAYHKNVK AQVSKSAKAV KALIDQRASK
AEREEDRQEK LRLKALKAND MEAYGKLVAE AKNERLTYLL SQTNSYLDSI RKLVRQHKQK
HHLVDEYTAH YDAHHGGSKD TNADDVDDDL NYLEIASKGE LPRQPLMLVG GDLKEYQLRG
LQWMVSLYDN HLNGILADEM GLGKTIQSIS LLTYVTEVKH NHGPFLVVVP LSTLSNWVNE
FKKWAPDLVL VVYKGPPQVR KELHKQEMAS CQFNVLLTTY EYIMKDKHVL RKYDWQYIIV
DEGHRMKNAQ SKFAMTLGSM YTSRNRLLLT GTPLQNSLPE LWALLNFLLP TIFESVDTFE
QWFSKPFAQF SGNGDSNELS DEERMLIINR LHQVLRPFLL RRVKASVLDQ LPDKVEKVLK
CELSGWQKIM YRRIQEGGAL LMETTDGSGK KKGKAKYTSK GLSNVLMQLR KVCNHPYLFQ
TNGYQIDFDI VRSSGKFELL DRMLPKLKAA GHRVLMFSQM TQLMHVLEDY FNYRGFRYLR
LDGSTSADER EQRMFMFNAP DSPFFIFLLS TRAGGLGLNL ATADTVIIFD SDWNPAMDAQ
AQDRAHRIGQ KNEVRVFRLV TNSPVEEKIL SRATDKMNMN NLVVEAGKFN NKSKEAERRA
MLESLIKMEQ EEAAHAAHGD DESSNVLLDD EINEMMALTD EELALYHRLD AERIARETKE
WEDYCKQYNV PYSPRSRLMA EKDAPAWLRE ANDVMEHDIA TGKHDKDAWN FDMETVAGKP
RKRKEMSYRD QFTDAEFVKM CEDGIDENEM KAAVKSPKES KPSKRKRDED EEFVDPNAID
VDDNPNDDDA GRRERKMLCY YYKKVYDAVI KLKDPTGRLR SELYMEKPSA VDYPDYYTIV
KEPMDLATIK ARLDMYYYAS HDQFEADFNL MVGNAQLYNH PESLVVFDAL EIDKCVKTKM
KPLHLKTMEQ IAAAYEKAKK DHKRRSKNRK DKKRRHH
//
