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Database: UniProt
Entry: A0A067L7D7_JATCU
LinkDB: A0A067L7D7_JATCU
Original site: A0A067L7D7_JATCU 
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
//
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