GenomeNet

Database: UniProt
Entry: A0A388KLN4_CHABU
LinkDB: A0A388KLN4_CHABU
Original site: A0A388KLN4_CHABU 
ID   A0A388KLN4_CHABU        Unreviewed;      3957 AA.
AC   A0A388KLN4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=CBR_g8252 {ECO:0000313|EMBL:GBG70952.1};
OS   Chara braunii (Braun's stonewort).
OC   Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC   Chara.
OX   NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG70952.1, ECO:0000313|Proteomes:UP000265515};
RN   [1] {ECO:0000313|EMBL:GBG70952.1, ECO:0000313|Proteomes:UP000265515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S276 {ECO:0000313|EMBL:GBG70952.1,
RC   ECO:0000313|Proteomes:UP000265515};
RX   PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA   Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA   Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA   Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA   Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA   Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA   Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA   Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA   Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA   Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA   Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA   Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA   Rensing S.A.;
RT   "The Chara Genome: Secondary Complexity and Implications for Plant
RT   Terrestrialization.";
RL   Cell 174:448-464(2018).
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|RuleBase:RU363044};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU363044};
CC   -!- SIMILARITY: Belongs to the helicase family.
CC       {ECO:0000256|RuleBase:RU363044}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBG70952.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BFEA01000138; GBG70952.1; -; Genomic_DNA.
DR   STRING; 69332.A0A388KLN4; -.
DR   EnsemblPlants; GBG70952; GBG70952; CBR_g8252.
DR   Gramene; GBG70952; GBG70952; CBR_g8252.
DR   Proteomes; UP000265515; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 2.
DR   Gene3D; 1.20.1500.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR025476; Helitron_helicase-like.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049163; Pif1-like_2B_dom.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   InterPro; IPR040801; Ski2_N.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF24; DEXH-BOX ATP-DEPENDENT RNA HELICASE DEXH11; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF14214; Helitron_like_N; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   Pfam; PF21530; Pif1_2B_dom; 1.
DR   Pfam; PF17911; Ski2_N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363044};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|RuleBase:RU363044};
KW   DNA recombination {ECO:0000256|RuleBase:RU363044};
KW   DNA repair {ECO:0000256|RuleBase:RU363044};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363044};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363044};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265515}.
FT   DOMAIN          2967..3122
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          3228..3430
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1681..1709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1737..1756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1785..1837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1878..1909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1941..1972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2434..2497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2698..2780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2802..2837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2867..2891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3170..3201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3576..3596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2395..2422
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..47
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..137
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..307
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..617
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1878..1895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1956..1972
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2438..2490
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2760..2780
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2810..2825
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3957 AA;  436565 MW;  A609EC4FD2DCE248 CRC64;
     MMGRRRREWS RDWRDNEVEE KRARRRRRRT TMKKKRARRR TKKRWRRRRE VVAMEKNEED
     DGEGGGRGGG GDLDDGGGGG GGRRGGGGGG GGGGEGGRRK GGGGGGRAKR ARRRRGRRRR
     MTKKKRARRW TKKRWRRRRE VAAMEKNEED DGEGGGGGGG GLDDGRGGGE RRGGKGGRRG
     GGGRRGGGGE RRGGGGGGEG GRRRGGGGGG GHEEEEEEEE EEEEEEEEEE EEADNEEGEE
     EEEEEEVEEK EDDEEEEEEE EEEATVNEED EEEEEEEDEE EEEEEEEEEE EEEEEEEEEE
     EEEEGPTMEE LAHLAWAGNG SWEGRNLLPR NERCAPFAVV TIAEKNTLSS DSAVRHSSIR
     LGENECGVPT GATTHWRGGK VLDTGHSLPR GHASFVEERG REWALNEDLG RTQGQRAALS
     EASSRSYDFG ACHGWLDGGS LGGVVPVPCS VSWPGTDNVA FESGEAGGVA PDVDSTVFGD
     GRVFQLPLEM EQEPSCVPQC VRAACCAAGS LDGLDPQGKS VPVEGGVGGG SCEPVRKDRA
     SDGPVSGDNS GRSVGQGLAS SMATARAARR LRVSSRRKRR ASTPGEGAQH RSDLERHAPA
     IEEGGEGAEE RHVDTGSRSG VDVAMLRFGS VSLASDAVAD YPTLPKATPT TSPNNFMRSI
     CMRGVVSVPP CFVRSDCFKS TAAWHTPRLR LKEKMRCERY KELRRAVQEN EHRDGVGTKV
     FLPSTFTGGP HYMAEKYYDA MAVVQKLGRP DLFITMTCNS NWPEILDAVM PGQVPSDRQE
     LLPRVFRGHL KQLIHEIKDK RVFRAVSAVF YTVEFQKRGL PHAHILVILD RGQKLSNPDA
     MDEAISSEIP SDGELREKVS KFMIHQLCGA AKPSAACTTN KRCTKHFPKP FVRKTTFQTG
     KGYPLYRRSS PDAGGCTLCE GGVVYDNGRV VPYNGYLLLR FNSHINVESC ANILACKYLY
     KYILKGNDKV MVAELERQHS VNEIRMSHEV DGVDELNKEL QRCGCNRLPL YADITETHMW
     HKTEKRWKLR LSAGRSGAFP KIGRLQRAYP AQGDLFYLRI LLGHEHSRGA TSFXALRTVE
     HGELATFREV CQRLHLLDDD FEYDKDMETA ALHYMPHQIR QVFAMLLAYG PVSDPMALFF
     KHWQPMCEDY VRKLRSMSVA PGVLQALALL DIHVQLLDMK TTMGGVGLAF PDPEAQRVAE
     ELRARILLEG LPELIQEELM YDRADMERQW GANYPLLRPS RKELVDGVMS AVLNRSPLCV
     FVDAPPGTGK TFCINTILAG VRRHENCIAL AVASSGIASL LLPGGRTFHS RFQAPLRPDA
     KKAFPIRRQG ELVRLIRMCS LIVWDEASIT HRAQLEALNI TLQDICQTDE PFSGKVLLLA
     GDFRQVLPVV RRGSRPKQIR ASIKSSPLWA HFKTHRLHEN MRVLRRGDDE VERKFAAFLL
     RVGDGEHDVV DPADPETIEL PPEICMALDL GALIDWTFPD LGRHLHDPDY LTGRFVLCPK
     NDAAYVINNL ILDGLPQRDI LYRSLHSAPT DSYGLNVPVE YLNSLSCSGL PPHVLRIKEG
     VPIMLLRNIS VQMGMCNGTC LIVNKSVSGR LIEATILPSH KIAVIPRMTL DSDDSDGFLW
     KRRQFPLHLA FAITINKSQG QSVSRAGLYL EKPVFGHGQL YVGLSRAGHP DDICVALPAD
     STRTKNGRAP PASNAAHGSA LETGSTPACG SRNQSLLASA FSPDDEDFLD YDYDEVPATL
     DAPSEPERCG RTPTESVRAR SPLAIHTPMG SLLLDIYQAG VDIGDLSGDE STDSWEWDRS
     SPAELRGGSD GAPARYVGQS SPYGVSAGRS PLPPTTPVAA AQMNADCARA HGVSKQACEI
     DAGTDNLQTP FTASTKRVRT SQPDGTSTFV PYIRPSQSSA PAVHDGAPPL RPFGSTPACG
     NCGPVSVFAK LPREVVVGPS LTSDAAHRPD ASSSLARRGA TDSGQSENVV MGPMITPSYG
     RNGFRPGTTL VYHDINSYDP PIWVDAKRTV ILDGKKQRIV ESWTDVLDRV GRRRIVNWML
     FGLFLDGDRV EPTEHIWLDF LLARGRIERG FVPHRDKFLC DNGSLDDAHE LIEAILRHEH
     ATRPGFDVPS LCEKVAKFED DYVPFEIYRY ARLDEIASRL PDVPRVSRPY AKACHGDCLI
     ATYAPPVQWV SQAYIRTRTR RIAEASAARD YAHGRSPLTF SKPAANSPMT PAFTAPAARR
     VQRSLFLPAT PPPFPLPAAD REAGSSACKH CSAQLSAGPS ALRQIGAVMA AKNEAVEDCS
     AVEAVMFVDY CRQGYNKVAS FEQYKTAAAS YIAKDDPSIS LLSFGLHHHV CFFCHLLLYP
     HAKMSPKNRG AAKDPHPLLA KSIEEEESVR WRIAELNEKL VKLRSRGYDD TDVRWLRVEE
     KIDEAEEKRQ RAASRAERMR NIIDAGDIYS DADYRSGDEW IEEQEEASDS TDPEEMVTDY
     DVSDLEAAVD TDYADADDDT DDDNSSSDDS TEEGDGSTNL STLCFSVLFS ALSYSRLSYP
     LNGITSHDDL GTFRFRVGLS GSAGHMAIRG PLITSSCPSP QLPPTAFTLP HVLHVETASQ
     IKERLEREYL TPRLDHKEGD SVVQCGLTWD VDWLSDWTRA EPTPCRDVVE PVWRPHLKTP
     KLVNEADCNH HEDDRPCRCD RPDSFEQQPT PEIPEFREVE IATFNETASN SSSLLRRMGR
     PEDFVRGSKS SQPFQPGGFD GGGGDEGRPR APPDAENGGW LHEVLHQTGP WQTVPPGFKH
     GIRFDDEPQP EDSKKEEADK AIRMGDQHQQ VSTLSFGSIF QKAWETSYGG EEGEEEEEEE
     DEEEEGENVK MRRDASGAEA SVARTAFSGR AQGEAVVELP ARPAETGVVG VGGGGGGAGV
     GGGGGGGEEE AVPRIKDQDE LLDKLLSRTP GQLDMLSQKG ISDKERKEEV WAIMDGMHGI
     DKRFKELVPE MAMEFPFELD TFQKEAIYRL ENYESVFVAA HTSAGKTVVA EYAFALVTKH
     CTRAIYTSPI KTISNQKFRD FSGKFDVGLL TGDISIRPEA PCLIMTTEIL RSMLYRGADL
     IRDVEWVVFD EVHYVNDAER GVVWEEVIIM LPDHINMIML SATVPNTKEF ADWIGRTKQK
     KIFVTGTTRR PVPLEHNLFY SGKLYRICDR ETFLPEGHRE AMVAHKAKNE KKAPAGGMGQ
     GRGGAGAGGR SRTGASGQTK AAAAQAARAI GSAMTGGGGG GWRSETSQWY NFLDMLKKQS
     LLPVVVFCFS KNRCDQIADS LTASDLTTSQ EKSEIRVFCD RAFSRLKGTD RQLPQVLRIM
     ELLKRGIGVH HAGLLPIVKE VVEMLFCRGV IKILLSTETF AMGVNAPART VAFHGLRKHD
     GKTFRQILSG EYTQMAGRAG RRGLDKVGTV IILCWDDIME EGDLRRLLTG KATKLESQFR
     LTYNMILNLL RVEDLKVEDM LKRSFAEFHG QKTMPLHMQE LIKREGVLNG MNTEINCILG
     SPTIEEYYEM AVEADRVGEQ LMETGLQSRV AQQALVPGRV VLVRTAAESP SLGVIVRGSS
     GEGQSRPYIV LALHRGPVPA SAQAMLAPAG QDVVGGGGSG GNNFPTTLPG DSPLDGMAMM
     RVHRKGQKDV DYSVFSGGSK KGPEVVTIAL PRYGEVGGSG YVVMNVDKRG ILSICKARVK
     VDTSAILEQP RPVAYASAVQ QLEQLERENP GQDPAALDPV KDLKLNDVET IERYRRRQAL
     QAAMARNQCH RCPKLQEHYA EVRKRALLRE HVRDLKFIVS DANLQQMPEF RQRLAGGGDD
     GDAAPWKDLP TMARLHRVMV QLVGGGDERA AGCRRRRQSG CTDWRLFETA CRIGAVQGSC
     GLQVSPAEYA HGALKFGLME VVYEWAKGTP FADICDLTNV PEGTVVRAIV RLDELCREFR
     DAARVIGDAT LFQKLEVASA SIKRDIVFAG SLYITAGQFP MLIRSGDMLA VAIRVQI
//
DBGET integrated database retrieval system