ID D8S9B2_SELML Unreviewed; 1274 AA.
AC D8S9B2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=SNF2 family DNA-dependent ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SELMODRAFT_177985 {ECO:0000313|EMBL:EFJ18933.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ18933.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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DR EMBL; GL377608; EFJ18933.1; -; Genomic_DNA.
DR RefSeq; XP_002980063.1; XM_002980017.1.
DR AlphaFoldDB; D8S9B2; -.
DR STRING; 88036.D8S9B2; -.
DR EnsemblPlants; EFJ18933; EFJ18933; SELMODRAFT_177985.
DR GeneID; 9647056; -.
DR Gramene; EFJ18933; EFJ18933; SELMODRAFT_177985.
DR KEGG; smo:SELMODRAFT_177985; -.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_000315_31_0_1; -.
DR InParanoid; D8S9B2; -.
DR OMA; MEANPRN; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd15523; PHD_PHF21A; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF17; CHD3-TYPE CHROMATIN-REMODELING FACTOR CHR7-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 48..95
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 97..175
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 185..232
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 281..463
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 591..747
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 145662 MW; 29DACD540841FCE1 CRC64;
MAGRLRTRSR KKPSYREQEA ADSDEIDDDD AAGNAANAAD AGGAKQSDDH CSVCSLGGKL
LCCDTCTAVY HLECLDPPMK SVPKGDWSCL KCREPLADLE KILDCQIRPP EPSEDAGVAE
ESTKHYLVKW KSKSYMHCSW VTQAALDKAI KSYPGIRLRL MNFNRQSELK LEDEEEKVPV
KPEWTTVDRI IDYRKRSGKD EFLVKWKELG YEECTWETED DIVAFQAEIK RYKAASTNEE
YQDVDHDKRR QKAFTPYDKT PEFVVGGVLH PYQLEGLNFL RYAWQQGKPV ILADEMGLGK
TIQTISFLTS LLHEGVSLPH LIVAPLSTLR NWEREFSIWA PQMSIVTYIG SAQAREIIRQ
KEFFLPKERK PEKGKKNASR QRRVKFNVLL TSYEMVNTDS AVLKPIKWEC LIVDEGHRLK
NKDSKLFQTL HNYSTYSRVL LTGTPLQNNL DELFTLMYFL DSSKFSSLEE FQLEFKDINH
EEQVQRLHTM LSSHLLRRVK KDVLKELPPK KELIVRVELS AIQKDYYRAV LTRNYEVLSR
HSGVQVSLNN LVMELRKICA HPFLLDGVEE ETEDEDAVQK TLVEASGKLL LLDKMTTKLK
AEGHRVLIYS QFQRVLDILE DWLAYKNWNY ERIDGKVSGA DRQSRIDRFN APGSKIFCFL
LSTRAGGLGI NLATADTVVI YDSDWNPHAD MQAMARAHRM GQTSKVMIYR LITRGTIEER
MMQLSKKKMV LEHLVVGRMK TQILNQEELD DILRYGAKEL FADETAEEAK LRQIHYDDSA
IDRLLDRSLL EETEELDEDN SFFKAFKVAN FEYVNQGDAQ AAEAIEQEKE AEADLESQTM
DPSARTTYWE NLLKNKYEAR AREELGKGKR SRKQVNHFPA EDDLAGMSDT SSEEEDDNKP
EAEVSKDAAK RTPGSRKKPR VEATGPPPLM EGEGKSILIL GFNRKQRAMF VQVLMRFGFG
DFSWSEFASC FKHKTVDEIK EYAALFLMHV TEEQTDIPTF SDGIPKEGLR IQDVFVRLAI
LHLIWEKVKN LNENPSTSLF PSVAYNKYAA LKETKVWKEE QDRKLLKGIV KHGYGRWQAI
CEDEEYGLQP VLFQELFSSI PNSNSSAPAT TDLNQDAGAE AIPLHPENKN LTGDKQEDAA
KPSDPHSDEH RDAMDAQLQR KTMEFFRKRI LVLEKVLNAE YHDELLDQEQ GAAEGDQEGL
EDETKLYISQ VYSEMTLLVA DSEIDAVQAY AGNKSAGSRL RRSIRQLEGL CMELETALYQ
RCATGSDEND PSPS
//
