ID F2UA26_SALR5 Unreviewed; 2192 AA.
AC F2UA26;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=SNF2 family DNA-dependent ATPase {ECO:0000313|EMBL:EGD73601.1};
GN ORFNames=PTSG_05311 {ECO:0000313|EMBL:EGD73601.1};
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.
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DR EMBL; GL832966; EGD73601.1; -; Genomic_DNA.
DR RefSeq; XP_004993883.1; XM_004993826.1.
DR STRING; 946362.F2UA26; -.
DR EnsemblProtists; EGD73601; EGD73601; PTSG_05311.
DR GeneID; 16074462; -.
DR KEGG; sre:PTSG_05311; -.
DR eggNOG; KOG0385; Eukaryota.
DR eggNOG; KOG0941; Eukaryota.
DR InParanoid; F2UA26; -.
DR OMA; RTEWIAN; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF879; CHROMATIN-REMODELING COMPLEX ATPASE CHAIN ISWI; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00415; RCC1; 1.
DR Pfam; PF13540; RCC1_2; 3.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 4.
PE 4: Predicted;
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 101..268
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 399..550
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REPEAT 1063..1115
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1116..1168
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1169..1220
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1221..1266
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 38..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1439..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..2192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..782
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1899
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1926..1947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2114..2135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2136..2159
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2171..2192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2192 AA; 241267 MW; DE2996C3E8AC1B0E CRC64;
MSSVDEDVDV SQCTEAERMI AMFVDKLKDA GGSNANAFSM LADKGHSDDS GSARSRRKAQ
SDESWKSIDA AHTTLPFAQP KIIEHGTLRP YQLESLQFFA NLYRHGVSGG ILADEMGLGK
TLQTISLLAY LHEHNLSRGV HLVTCPLSVL GSWSNEFKRW CPSLTVQVYH GPERAAVAKK
LRKIAKPQDS VQVLLTTYEM VSKDKRMFRI FNYDCVVVDE AHRLKNENSQ LSLSLRALKS
SFRLLLTGTP IQNNMHELWS LLNFLFPQLF GESTTFDTLF DVKTGHADKD VLAKLHYILK
PFTLRRLKQD VEKALPDKIE TNLYVTLTDL QKKYYKAILE KDVHGLLAEM RGRSKTRLLN
TIMQLRKACN HPYLFDGVEP GPPFTNGPHL WQSSGKMIIL HKLLQKLKAQ GSRVLIFSQM
NRMLDLIHDY CFSQGYKVCQ IDGSMNALDR QEAIERFQED DSDVFAFLLS TRAGGLGLNL
TKADAVILYD SDWNPFADIQ AIDRAHRIGQ TKAVKVYRLI TDNTVDEHIQ QRAEAKLYLN
ALILQGEQVA DSATKVSNAE LLQMVSFGAD RVFKSDAPIT DEDIDVIIGR GEYRTQENMK
RLQEKCQHSL QTFSLKSESD IKDNYQAFLR SVTAMGGEEA SVSAMRLAEF VAPEPSARHR
STRTAAPLFE GFFSDSDDDD DDGAGKKDAR ARRPSSDDDY VLPEEATISK PRAPRKKRGK
NSTASNGAGT AAAAAGGGGG DTDGGDEHDA TGDDFEEGED DDDDEDDDED EDEDEEGDST
AKDDVPDEVA VPLVTDAHVA AGMTEERVGT FVEAFNQHWR LCHCCRWFGQ DSIEEMVFKF
RRALDAETPP NPRSFPLPSL GDVPSATWKH CKVLLAKLGF EIVDRRQAYV TAAVEKEWET
MVRALVVLAL RMRRHKRSDT FGCSILTHKA TDEVPDIQGV QFKPNTGLRV AVWGHVDWKA
ARTAIRSPTG CVATPAIMKH VQPFAVAGVV SGPGARHVAV FQTATDTPEL APSAGFFGSG
RGGVLGRQAT FAAAPVLLNN RSDAHPCSVA CGAQHTLVAQ SNGQMLSFGN NTCGALGRVC
ADDATAENPP MKMRLRRQFI YVSCGPRSSF AVTTNGTVYS WGDNTHRTLG IASRASSMAR
PRIVVALNCV HIVQISSNEF HTLFLDKHGR VFVCGHGQHG QLGFRGRKKA PTPRPIPAFE
NVVIKQVSAG RFHSLALATN GAVYVWGRPV SSAPVMQTPQ LVTRLRGRNV VKVVAGDSVS
YALTSTGQVW AWGSPDIPEL LCTDKADMPT PKQLPLPEHL HAEDICCGFG FCAASLSQRE
KTQDSRICEA CLNKIDSPSQ ERDAASASSK SICYSCRLLK AQVPMPPAWK QQYGAAWPLV
LTAPFVRPHP FVFPTALLSK PPKHQVRAEA QLGLRASLER AWTSLRQGAF QQYNAQQMHT
LPSPPQQQQQ QQQQQQQQQQ QQQQQQQQQQ PDKADSRDDD GDRSALGEEK EEEEEEEEEV
DVAHAGTAEA EAGDEEQKPD TQEAEPEQDV TTEGETKAKR AKRTQEGEEK TAEENHHLQQ
WSQYAMNHSQ SYAQHFLDVV KEYHECKATI RDLMCQLVNA KHRMSAVKLQ LRDLMSLGVM
GVPNQSEVLE MFAPGITTVD DVAAMHTAIH DVFTHSVRRE LDMLKDGLNR HRREIAAMPA
KDLLQQHFAS SERFMGYSQR NASRAGTDPV AIARAQQLVG PGDVATVDAT FTLMSRVLGD
GAFDLHKQRL QQQQQQQQQQ QQQQQQQQQQ QQQQHNQQQF QQLLQRQQQQ QQQQQEEQRR
RQQQMQQRQR QYNKRLRHQQ LGGDAQAPAH GGKRRADGAD AAGHQLQHPL SASSSVHASK
RSKRVGHEAT AATASDAVVL IADDDDDDDD DDNEADNDGD AAAEGGRVRG HEAGEGAVAA
SVENDHEGRQ AAETHTKHRK AAGARMDTTG ERDAITTGVA HGTHAAGGGN DGDDEATETG
SVETESDPST VATDNNDNHD HHNNAGIPGR LHQRKGSDET VTDEGSDHGY GHGQGAQASL
HAPPSHFHQQ QPPLRAMPTM ATAAASANPR GGGGGGGGGG GGGGGGVVPL QVHLLQEHPM
LSDALAAPPS QGGAAAVSPQ SSSRTSTASP FSTGSSSKKK KKKKKHKKHK KKHKKHRKQD
KPMERSEDKD ETSDDGVDDD EDDDNDEQTS LK
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