ID B9S7N2_RICCO Unreviewed; 1447 AA.
AC B9S7N2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
GN ORFNames=RCOM_0610050 {ECO:0000313|EMBL:EEF40405.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; EQ973886; EEF40405.1; -; Genomic_DNA.
DR STRING; 3988.B9S7N2; -.
DR eggNOG; KOG1015; Eukaryota.
DR InParanoid; B9S7N2; -.
DR Proteomes; UP000008311; 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 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 InterPro; IPR025766; ADD.
DR InterPro; IPR044574; ARIP4-like.
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; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; RAD54-LIKE; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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 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:UP000008311};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 424..554
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 688..871
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1070..1241
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 1356..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 62..89
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 120..147
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1367..1389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1447 AA; 164225 MW; 527E9F468ECFCD77 CRC64;
MEEKHKQVDD VEIVSSDSFI VDSDDDDDEP STSGQDNGMH LEASHQNSFS CNFREPLTEQ
EVEELVAELL EVESKAAEAQ EALEKESLSK VESEVREELG QSLHGDDLEA AVEDEMTAFK
EEWETVLDEL ETESAHLLEQ LDGAGIELPS LYKWIERQAP NGCQTEAWKS RAHWVGSQVT
SEITEAVADA EKYLQSHRPV RRRHGKLLEE GASGFLDKKL SIDGTKDNVA ENGDIDWDSL
NKLFSSGSCK DVASFGSKHW ASVYLANTPQ EAAEMGLKFP GVDEVEEIED IDGCSNDPFI
AVAIANEKEL ILSEEQRKNY IKVKEEDDAI IDRKLQLHLK QRRRRKRSKQ VMIMTTSNFL
FCESRKSKRP NESGEPTNDA KKIRTVIIDS DDEADGINES VSSANRVVVE STLQENIGES
GADGHLSQCV NEEFHCTVCH KICFEVHSHP LLKVIICKDC KCSIEKKMHV KDPECSECYC
AWCGRSNDLV SCKSCKTLFC TTCVKRNIGE ECLSEAQSSG WQCCCCSPNQ LQRLTLELEK
AMGSEDLMDT SSDSESENSD ADIHVAIRKK NKKKKKIRRI LDDAELGEET QRKIAIEKER
QERLKSLKVQ FTDKSKMMNT ASCNGNLPEG ASFEVLGDAA TGYIVNVVRE KGEEAVRIPP
SISAKLKAHQ VAGIRFMWEN IVQSIGKVKS GDRGLGCILA HTMGLGKTFQ VIAFLYTAMR
SIDLGLRTAL IVTPVNVLHN WRQEFMKWRP SETKPLRVFM LEDVSRDRRA ELLAKWRAKG
GVFLIGYTAF RNLSLGKNVK DRNMAREICY ALQDGPDILV CDEAHIIKNT RADTTQALKQ
VKCQRRIALT GSPLQNNLME YYCMVDFVRE GFLGSSHEFR NRFQNPIENG QHTNSTANDV
KIMNQRSHIL YEQLKGFVQR MDMSVVKKDL PPKTVFVIAV KLSPLQRKLY KKFLDVHGFT
KDIVSSEKIR KSFFAGYQAL AQIWNHPGIL QLRKDRDYVT REETVDNFIA DESSSDENLD
CNTIIGEKPR NANDFVQRKS DNGFFQKGWW NDLLQENNYK ELDYSGKMVL LLDILTASSH
VGDKALVFSQ SIPTLDLIEL YLSRLSRHGK KGKLWRKGKD WYRLDGRTES SERQRLVEKF
NDPENKRVKC TLISTRAGSL GINLHAANRV VIVDGSWNPT YDLQAIFRAW RYGQTKPVFA
YRLMAHGTME EKIYKRQVTK EGLAARVVDR QQVHRTISRE EMLHLFDFGD EENSDPLAEV
GEEDKQVDDQ NMSYKVGSSL KHKAPLSHVS CSSDKLMESL LGKHHPRWIA NYHEHETLLQ
ENEEEKLTKE EQDMAWEVYR RSLEWEEVQR VSLDESTFER KPPISNAVPS APNTNSKGPP
VRETSSSNVA PSKGILRCRM VQRKCTNLSH LLTLRSQGTK VGCTTVCGEC AQEISWEDLN
KDSRTAR
//
