ID F2TWH7_SALR5 Unreviewed; 1106 AA.
AC F2TWH7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Transcription activator {ECO:0000313|EMBL:EGD72423.1};
GN ORFNames=PTSG_00442 {ECO:0000313|EMBL:EGD72423.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; GL832955; EGD72423.1; -; Genomic_DNA.
DR RefSeq; XP_004998992.1; XM_004998935.1.
DR AlphaFoldDB; F2TWH7; -.
DR STRING; 946362.F2TWH7; -.
DR EnsemblProtists; EGD72423; EGD72423; PTSG_00442.
DR GeneID; 16067728; -.
DR KEGG; sre:PTSG_00442; -.
DR eggNOG; KOG0385; Eukaryota.
DR InParanoid; F2TWH7; -.
DR OMA; VHDYQFF; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000007799; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799}.
FT DOMAIN 247..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 541..692
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 901..953
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 128052 MW; FA9A94BF1091BCD4 CRC64;
MSDTEQKLAV DGEEAARKQQ TDAMDVAADD GEATTDATAA NGATKEEDEE ASENDESNGN
GDVEDEERSP SSNASEESSK AGDNEEEGQE DEEDDGDDED EDDEEDDDEG ADEDEKVKEE
QDDLHKGYVW PDRETRNVEI RRKIAQDQPK RIHYLVEETE LFDHLVDLES VRRVDPRGKK
RRPGAGAASS GGGASRRHRK TEKEEDEELL KEEAEVEDDH VHFTESPNYI AGGKMRDYQL
RGLNWLIGLH ANSVGGILAD EMGLGKTLQT ISLLGYLKNF RRMDGPFLLL VPKSTLKNWM
RELAKWCPTL KAVCLTGSKE ERPKIIEEQI MPGQWDCVVT SYEICVIEKS ALKKFVWEYI
VIDEAHRIKN EKSKLSLIAR EIESRNRLLI TGTPLQNNLH ELWALLNFLL PDIFQSSEEF
DKYFHAENLQ QESMVHKLHS VLKPFLLRRL KKEVEKSLPP KKEIKVYVGM SKMQRDWYKN
ILMKDIDTIN GAGRVEKMRL LNILMQLRKC CNHPYLFDGA EPGPPFTTDQ HLVDNSGKLV
VLDKLLTKLK AQGSRVLIFS QMTRMLDILE DYSWWRGHKY CRLDGSTAHE IRGEMIDDFN
RPNSDKFMFL LSTRAGGLGI NLYTADVVII YDSDFNPQMD LQAQDRAHRI GQTKEVRVFR
FITEKTVEER IVERAEMKLR LDAVVIQQGR LSDKQKQLSS GDMLNMIQFG ADHIFRTTEA
TVTDEDIDAI LSRGETKTEE FNKKLEAMGE SNLLKEFTFD TQSSSILEFE GEDYRKKRER
KKPMRWIEPP KRERRQAINV NKYFSELLGT SNTTKAPKAP KPPKQPKIEE FQFYPARLTE
LLQREVYAYR KAVGYKVPKK PVEGVWTDEQ EEERQKEQAL VDTAEPLTEA ELEEKEKLLQ
QGFKSWQKRD FQQFVKANER WGRDNIEKIA QEIDSKTFEE VQEYAKVFWK KYKTLSNADQ
IMAQIERGES KIQRRLEVQE YLDRKVAQYK LPLQQLHLHY GGSRGKNFTE EEDRFLVCGL
QRIGFDADNV YEELRRQIRA APQFRFDWFI KSRTATELQR RCNTLISLIE KELKDADAKA
KKDRKKKQGK RKSEASSSSK KSKKSK
//