ID D8SK03_SELML Unreviewed; 1296 AA.
AC D8SK03;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=SNF2 family DNA-dependent ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SELMODRAFT_155996 {ECO:0000313|EMBL:EFJ15143.1};
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:EFJ15143.1, 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; GL377624; EFJ15143.1; -; Genomic_DNA.
DR RefSeq; XP_002983647.1; XM_002983601.1.
DR STRING; 88036.D8SK03; -.
DR EnsemblPlants; EFJ15143; EFJ15143; SELMODRAFT_155996.
DR Gramene; EFJ15143; EFJ15143; SELMODRAFT_155996.
DR KEGG; smo:SELMODRAFT_155996; -.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_000315_31_0_1; -.
DR InParanoid; D8SK03; -.
DR OMA; PQMMMND; -.
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; cd18659; CD2_tandem; 1.
DR CDD; cd15532; PHD2_CHD_II; 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; 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 47..94
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 96..173
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 191..250
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 287..472
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 598..757
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1296 AA; 149990 MW; 6F3FCCC7443F310A CRC64;
MAEGLRVRAK RKASYFEDSS DEDDYEDSRE MELDGAGEDS DLEEAVEDFC TICKSGGKVL
CCDACTAVYH LQCLDPPMKS VPKGSWRCPK CEEPLADIEK ILDSQMRPLK ATEKEDEEGK
KEEEEELMKH YLVKWKSRSY LHCSWIPLNE MERASRMYPG LRMKMNHFHK TCEAMKELAD
EDQGPIRVEW ITVDRVIDER ETENTKEYLV KWKELGYDEA TWEVKEDIAQ FQSQIDYYEK
IAKRGPRKTK RTAARHQKTF TQFETTPDFL SDGVLHPYQL EGLNFLRFAW QQEKHVILAD
EMGLGKTIQT IAFLASLKQE EVTDPHLVVA PLSTLRNWER EFATWAPDIH IVVYAGNAKA
RSVIREFEFF YPKTDKTKKK YYSERKHSKQ DRIKFDVLLT SYEMITFDAA ILKSIKWECL
IVDEGHRLKS KESKLFQTLQ NYTTYHRVLL TGTPLQNNLD ELFTLMHFLD ASKFSSLEEF
QQEFRDINQE EQVSRLHKML ASHLLRRVKK DVLKQLPPKK ELMLRVELSS VQKELYKEIL
TRNYEALSKR GGPQVSLNNV VMELRKLCGH PYMVIEPDSK NEEEENRHRI ESSGKLSLLD
KMMVKLKASG HRVLLYSQFQ HMLDILEDYL THKNWSYERI DGNVTGAERQ IRIDRFNAPN
SNRFCFLLST RAGGLGINLA TADTVVIYDS DWNPHADLQA MARAHRLGQK NMVMIYRLVT
RGSIEERMMQ MTKKKMVLEH LVVGRMKTQV LNQEELDDIL RYGAKSVFGD ENDDSGKSWQ
IHYDDSAIDR LLDRSDVETG HEMSTDEDDN DLLKAFKVAN FEYVNHGKGR KEEAFRESEA
DYEAEHLSST ERLKYWESLL KERFEKKHVQ EQEMGKGKRS RKQVVHGEDD LAGMDYSSSE
NDENDELDTE YIQSVEEKTK KQKGESSVHP APLMEGDGKS LKVLGFRRKH RVRFVQILMR
FGLGDFTWSS FVPYFKQKQL HEIKEYGTLF LTHIAEDVTD SDTFADGVPK EGLRIQDVLV
RVAVLHLITN KVKQYTQNPK ARLFSYAVYA KFPALKGTTV WTEEHDKYLL DAIIKHGYGK
WLEIVEDARL QSAVREELKL PPIGSFSSPK AQDTVVNGHA PENDNHLTDA EAFFNRRIIE
FLKKRVALME KVLNAEYHLD DQDIPANRSN GGVEPGEGPK TSYQKPQPTF VPYPTPLTPE
EVLGTALDND PKRLKVPAYY NELCSMISEN RLDAFQTYAG NKSAGIRLRR CIRQIDVLCS
EMRRGLGVKG EEAMVDGAHD RDDVSDNEGI HVVIDD
//
