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Database: UniProt
Entry: D8RI44_SELML
LinkDB: D8RI44_SELML
Original site: D8RI44_SELML 
ID   D8RI44_SELML            Unreviewed;      1538 AA.
AC   D8RI44;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=SNF2 family DNA-dependent ATPase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SELMODRAFT_411494 {ECO:0000313|EMBL:EFJ28029.1};
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:EFJ28029.1, 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; GL377580; EFJ28029.1; -; Genomic_DNA.
DR   RefSeq; XP_002970703.1; XM_002970657.1.
DR   STRING; 88036.D8RI44; -.
DR   EnsemblPlants; EFJ28029; EFJ28029; SELMODRAFT_411494.
DR   Gramene; EFJ28029; EFJ28029; SELMODRAFT_411494.
DR   KEGG; smo:SELMODRAFT_411494; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   HOGENOM; CLU_000315_28_0_1; -.
DR   InParanoid; D8RI44; -.
DR   OMA; REICQQH; -.
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:InterPro.
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:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd18660; CD1_tandem; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 1.
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   InterPro; IPR025260; CHD1-like_C.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
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   PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF13907; CHD1-like_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01176; DUF4208; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          277..365
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          467..636
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          768..919
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1042..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1267..1363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1460..1538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..113
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..138
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..277
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1065
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1267..1302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1303..1319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1477..1519
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1538 AA;  175832 MW;  92EAB0338ADF5ED8 CRC64;
     MMSEYEEADE SNENEDSFVG QQEHFSSRPR KSRYEPSDGD DASQSDHGDP EYKEDSGDEN
     YEDGGYENGA ASYRYSTVES RDFQLEPEES EEYVMEEEEE DDNGGDDPQD ADFDPVSPEN
     NFSQQEEDDD DDYNASAEEQ EEAASTGGFD VSSDEELVRP ANPRKRPAIK IAQPRFGSNN
     QKRHRIVQKK DYPSDEEDSS DGEDQRNHRK VVVASSIRPV VIAPSQRAPA DFSSRETRSR
     RSIPRKSYVE EESEEDEEDQ KAKKKVSPDE IEEEDSDKIE RVVWHQPKGI AEAEMLEGRK
     AEPFILDTDP HADLDWEEQE FYIKWKGQSY LHCQWQGLAD LHQLSGYKKV VNYMKKVEED
     RQKRRNLSGE EAEVHDLSKE MELDLLKQYT QVFVTTIPVE KDIDLAFAQD FIDEYKERES
     ASNFQGKSVD FQRKRGKLIL RKLEEQPEWL KGGKLRDYQL EGLNFLVNGW RMNTNVILAD
     EMGLGKTVQS LSMLGYLQYN LEILGPFLVV VPLSTIANWA KEFRKWLPNM NVLVYVGNVA
     SREMCQKYEF FTASGRAKFN TLITTYELVL KDKDVLSQFK WDFLMVDEAH RLKNNEAALY
     TELMKFSAKN KVLVTGTPLQ NNVEELWALL HFLDPIKFRN KDDYKNLVSF NEAELARLHA
     ELRPHLLRRV IKDVEKSLPP KIERILRVEM SPLQKQYYKW ILERNFSDLN KGVRGNQVSL
     LNIVVELKKC CNHPFLFESA DHGYGANATM TDNSRVQRVV LSSGKLVLLD KLLVRLKETG
     HRVLIFSQMV KMLDILADYL RLRGFQFQRL DGSTKHHLRQ QAMEHFNAPG SEDFCFLLST
     RAGGLGINLA TADTVIIFDS DWNPQNDLQA MSRAHRIGQE FVVNIYRFVT CRSVEEDILE
     RAKKKMVLDH LVIQKLNAQG RLEMKETKKA TTMFDKNELA AILKFGAEEL FKEEKKSEEE
     AKSKLENMDI DEILERAEKV SGDTEQPGGE LLGAFKVANF SQGEDDAAFW SRLIPAETAK
     EAPDLGPRAA RKIRTYAEDL PADRYSKRRK NAEEVGRKRS TRLSRAPEPP PRVDGASAHV
     YEWEGTTISK RDANAFVKGV KKFGDKSRID MIVVNTGSAI ENASEDSQLD LMDALLDGCT
     EAVDNSHNPK AAILDFFGVT VKAQEVLTRV KELTLLGKRI RRYQDPVSQF RLRSHSKNPS
     SMWSRWSQVD DARLLLGVYY HGYGNWEKIR TDERLLLGKK MAPGGATAGE TSLPRATHLD
     ARVNTLLRKE TELDKGSNGE TSKSRSKRNQ ESSSKLRQGK DRASNSSRPS GTRKSARNIN
     RENAAIAAAA REEAEDKEEG EISDDDESTQ RRPKGVTDEK ERDQRWHNWC EGVMKGEVRT
     LKRLQNLKSA HSESNEKVVV RVKKYLQKLG QKIDSILDDN KGEKCNPQKM AMRLWNYVAR
     FSDLSGPDLS DLYHKLKRQP EAAAPSAASV ENNNENNGTS REKHEPLTYK RRHGRKDNAE
     SSKRRRKGGD EEETGARNSS ADKAHYFYGK GDFSQGPS
//
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