ID D8S513_SELML Unreviewed; 1858 AA.
AC D8S513;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
GN ORFNames=SELMODRAFT_443867 {ECO:0000313|EMBL:EFJ20520.1};
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:EFJ20520.1, 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GL377602; EFJ20520.1; -; Genomic_DNA.
DR RefSeq; XP_002978534.1; XM_002978488.1.
DR STRING; 88036.D8S513; -.
DR EnsemblPlants; EFJ20520; EFJ20520; SELMODRAFT_443867.
DR Gramene; EFJ20520; EFJ20520; SELMODRAFT_443867.
DR KEGG; smo:SELMODRAFT_443867; -.
DR eggNOG; KOG1015; Eukaryota.
DR HOGENOM; CLU_002089_0_0_1; -.
DR InParanoid; D8S513; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd11726; ADDz_ATRX; 1.
DR CDD; cd18793; SF2_C_SNF; 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; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR007011; LEA_SMP_dom.
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; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; RAD54-LIKE; 1.
DR Pfam; PF17981; ADD_ATRX; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04927; SMP; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51533; ADD; 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 Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 742..874
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1002..1187
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1358..1531
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 127..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1819..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..253
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 487..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1819..1841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1858 AA; 205154 MW; 9826B507CECDF3EF CRC64;
MGDPELQVKF NAGLAAARRV AALIVGQPFC ASDCIKAENP LDDVKISLRS VREVPSIGER
SENGLLVEEQ GKVCEEDECQ EEKVSPQAQV KEEIRCEEQV DGNSCEIIRV DADEEKSCEL
VEKEDKACEV QREEGDGGVE KDSSEDECDG DGYMSESSSE GSKSDEEVTR MIDWLVEIES
ESADAQEHLE DESVKKVEEE VRLELSETLS GQELDMAVSC EMADYVSIWK KTLLELEEES
AKLQDRLEDA GVSLPDLFKA IEKQAAEGCM TDTWRNRAHW AGTQAPEDFA EVLHSAEKDL
DALRPVIRRR GKLVEEGASG FLERKVNDVD TVKGSTGWEA FDSAFQPKLS AVSLFESKKW
AAVYSASTPE QAARLGLKFP GVDKVDDIAD IDQHVGMEAA ALAEESEFGL TEHQKKTMKR
VREEDDVRQM QKKIGARRVN CGFGGAMASQ VKSSTSDVNI ITEPPAVLSR LQPDTIDLGT
AGDPQNTDEL RLEDEQRQSH ERQTGTDQAI ADNVTTRNQS FINGTPSRSE EKVKKGVAPA
REGKDHIRNA SSFGRPTTDG TEPMPVFMEQ TVRDNETQAE AVADGSQCHD EAVETEEFKV
LKRSNSFKAI GVRTSSAGDD AKKPTPSMVI VVSDDDDDDP PADCGSTAQP RTVDQGKVPS
KDVTALDETT SPLKPLKRVT EHGSSSRCKR KRCFMVNSSE DEEDATSAKK EQSGLKSDRD
EQEERNSDSC DLSQSKLSGD TRRRLTRGNR SFGCTVCGET MSAKDVLSHP VLKVIICTSC
KQQYDDGPFR KDEDGSEAEC RWCGEGGSLI CCDSCDKVFC ESCIGRNFGP AFLESIEDIS
WKCYLCDPSP LASLQQWLKV AEEEALKESL ANLDVRRNRK KQRKNIRRVL RDDELDEVTK
QKLALEKERR ERLAEWYAEA RKGKSLSGKA ANSEKAVEGT DGDDHICEGD CKTEGCVINI
ASRQTGEPLV RIPASISKHL KPHQLCGVRF MWDNCIESVE KVKSGDVGLG CILAHSMGLG
KTLQVIAFLY TVMRNVDLNF KTVLVVVPVN VLHNWKREFE KWRPAEVAPL EVSMLDTSRD
NATRASLLKS WKEKGGVMLI GYAAFRNLST GSHVKDKETR DTLCKCLQDP GADIVVCDEG
HTIKNDKADI TIALQRVKSG RRIAMTGSPL QNNLMEYYCM VDFVRPGFLG PQAIFRNKVQ
NPIANGQHAD STPDDVKKMK RTVHILHKRL SGFVQRRDMT VLKDELPPKC VWVISVRLSP
LQKQLYKKFL SLCETGRSKL FDHYHVLAKI WNHPDLLAIA KEQRLNEEFI VDSEKEDSAE
NGQGCPKRAS PEADSFEWCE EILKESKRDV LENSGKMVLI MTLLSLNSSR GEKTLVFSQS
LHTLDLIENF LDTIPLGGSQ DVWNKGREWL RLDGNTTASR RQQIADIFND PNNTAIKCLL
ISTKAGSLGT NMTGANRVII VDGSWNPTHD LQALFRAWRY GQTKPVFVYR LLAYGTMEEK
IYNRQLTKEG IAARVLDAHQ VGRHLNADDL ELMYTLDDDD DEEGTQLAGT EQQQQPGAKG
QKPKHKTFFV PSDAPPRDDH MAMLLLDFRP QWIAQYHEHE PLLEDLEEEK LTPEEMKTAW
DGYIIEHELQ NRQIPSQSPT NYPPQSQYPA SSTDVRPPFT ATPSKAACND VYHASLLESL
SIPVGGSVAC ATTNLSFRRL SHGGGDTYGD TRLYRKAEII AMGIDDGATA DANRPPPATI
AGALNSASQS LVGSKPLEAS DARAIQSAEA RATGIPAGVK GGVGAAAQHA VDKGEPVTVG
DVLRTPIPTG GDKIVTQADA SRVQSAEQRN NPDSVVSPGG VAASMQSAAD HNKAAGYA
//
