ID A0A067L7D7_JATCU Unreviewed; 1065 AA.
AC A0A067L7D7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 28-JUN-2023, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDP40014.1};
GN ORFNames=JCGZ_02012 {ECO:0000313|EMBL:KDP40014.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP40014.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP40014.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP40014.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KK914334; KDP40014.1; -; Genomic_DNA.
DR RefSeq; XP_012069393.1; XM_012214003.1.
DR RefSeq; XP_012069394.1; XM_012214004.1.
DR AlphaFoldDB; A0A067L7D7; -.
DR STRING; 180498.A0A067L7D7; -.
DR GeneID; 105631817; -.
DR KEGG; jcu:105631817; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138}.
FT DOMAIN 202..367
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 495..646
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 840..892
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 123781 MW; 86D2D561907F6232 CRC64;
MAKTSKQPAS SDEALSNSSS SSSEQQINEQ IEEEDEEELE AVARSADSDD EEAADATGDD
VNADGEDVEE DENNNEISKR EKERLKEMQK MKKQKIQEIL DAQNAAIDAD MNNKGKGRLK
YLLQQTELFA HFAKPDQSTS QKKAKGRGRH ASKLTEEEED EEYLKEEEDG LSGAGNTRLV
AQPSCIQGKM RDYQLAGLNW LIRLYENGIN GILADEMGLG KTLQTISLMG YLHEFRGITG
PHMVVAPKST LGNWMNEIRR FCPVLRAVKF LGNPDERKHI REELLVAGKF DICVTSFEMA
IKEKSSLRRF SWRYIIIDEA HRIKNENSLL SKTMRLYNTN YRLLITGTPL QNNLHELWSL
LNFLLPEIFS SAETFDEWFQ ISGENDQQEV VQQLHKVLRP FLLRRLKSDV EKGLPPKKET
ILKVGMSQMQ KQYYRALLQK DLEVVNAGGE RKRLLNIAMQ LRKCCNHPYL FQGAEPGPPY
TTGDHLITNA GKMVLLDKLL PKLKERDSRV LIFSQMTRLL DILEDYLMFR GYQYCRIDGN
TGGEDRDASI DAFNKPGSEK FVFLLSTRAG GLGINLATAD VVILYDSDWN PQVDLQAQDR
AHRIGQKKEV QVFRFCTEYT IEEKVIERAY KKLALDALVI QQGRLAEQKT VNKDELLQMV
RFGAEMVFSS KDSTITDEDI DRIIAKGEEA TAELDAKMKK FTEDAIKFKM DDTAELYDFD
DDKDENKFDF KKIVSENWIE PPKRERKRNY SESEYFKQTM RQGGPAKPKE PRIPRMPQLH
DFQFFNTQRL SELYEKEVRY LMQTHQKNQL KDTIDVDEPE EVGEPLTAEE LEEKERLLEE
GFSSWSRRDF NTFIRACEKY GRNDIKSIAS EMEGKTEEEV ERYAKVFKER YKELNDYDRI
IKNIERGEAR ISRKDEIMKA IGKKLDRYKN PWLELKIQYG QNKGKLYNEE CDRFMICMVH
KLGYGNWDEL KAAFRTSPLF RFDWFVKSRT TQELARRCDT LIRLVEKENQ EYDERERQAR
KEKKLAKNMT PSKRAMGRQT ESPTSLKKRK QLSMDDYVTS GKRRK
//