ID A0A1U8A2S7_NELNU Unreviewed; 2402 AA.
AC A0A1U8A2S7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Protein CHROMATIN REMODELING 4 isoform X1 {ECO:0000313|RefSeq:XP_010260564.1};
GN Name=LOC104599649 {ECO:0000313|RefSeq:XP_010260564.1};
GN ORFNames=HUJ06_002172 {ECO:0000313|EMBL:DAD43942.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010260564.1};
RN [1] {ECO:0000313|EMBL:DAD43942.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD43942.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010260564.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; DUZY01000006; DAD43942.1; -; Genomic_DNA.
DR RefSeq; XP_010260564.1; XM_010262262.2.
DR STRING; 4432.A0A1U8A2S7; -.
DR GeneID; 104599649; -.
DR KEGG; nnu:104599649; -.
DR eggNOG; KOG0383; Eukaryota.
DR OrthoDB; 450745at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd11660; SANT_TRF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF28; PROTEIN CHROMATIN REMODELING 4; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 91..138
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 627..687
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 701..753
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 807..984
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1114..1273
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1853..1909
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2167..2189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2324..2402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2353..2368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2377..2402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2402 AA; 266700 MW; 05B685793FDF8FA4 CRC64;
MLPDTVSHES RTRDPKMREN SSVNTKMIDR NWVLKRKRKR LSCGPDLSNG KEGSSVPSES
PRNNPPAKRR LKCGIGLARS PRKKKGNDGY YFECVICDLG GNLLCCDSCP RTYHLQCLTP
PLKRTPPGKW QCPNCSEKTV SLKSINHPES ISRRARTKVI AEKSKTGTKL SDCPKLSRVL
ESSIPGKSRS SKGKPSSSHS VPSLEKKPEP SQTDVHCSTK SSQSSHGGSA EGISSCANTD
AEKKPNFSCT DAGRKSSSPA NEVQSSGRML DKEPIEESSG RKSDSQHNNG APLNEPIPLL
DRAAKKARKK KQKNNKEESH KKFGIDKGKC AVKNPSKRGA KSASACPEGS KSRQKNNSAD
HRVSVSLSKE GLGTKSPVTK QEDEKLAEEM PRSSHALEEQ SGQAVKSVVC EENVPSEVQQ
VDRILGCRVQ SSATDSSSLD VPMKVSNSPR TPIHAASGKN SVVVGNEMLS QDLPISENNN
RLSDGSPMPD KVIDVGDAED IAEGFQNTVM QVDKGKNIDN DSRTDKIHVY RRNVNKECTE
GINVGSKRRS FKDWGLTARN NEGKDRSTVD TNTAEVAEKM TMEENTVIEQ LNLNDPGNNP
LSKDCATPIS DGSGDAKDTD KEVKLNSSAE NKIHEANLDE SMPSDRDFVL YEFLVKWVGR
SHIHNSWVSE SQLKVIAKRK LENYKAKYGT TVINICQEKW SKPQRVIALR TCNNGMTEAF
VKWSGLPYDE CTWERLDEPV IQKSSNLIDE FKQFECQTVA KDAMKDDSLC CKGDQQQSEI
ATLAEQPKEL KGGSLFPHQL EALNWLRRCW HKSKNVILAD EMGLGKTVSA CAFISSLYFE
FKVRLPCLVL VPLSTMPNWL AEFSLWAPNL NVVEYHGCAK ARAIIRQYEW HASNPDSSNK
RTASYNFNVL LTTYEMVLAD YSHLRGVPWE VLVVDEGHRL KNSGSKLFSL LNTFSFQHRV
LLTGTPLQNN IGEMYNLLNF LQPASFPSLS SFEEKFNDLT TAEKVEELKK LVAPHMLRRL
KKDAMQNIPP KTERMVPVEL SSIQAEYYRA MLTKNYQVLR NIGKGVAHQS MLNIVMQLRK
VCNHPYLIPG TEPESGSVEF LQEMRIKASA KLTLLHSMLK VLNKEGHRVL IFSQMTKLLD
ILEDYLTVEF GPKSFERVDG SVSVADRQAA IARFNQDRSR FVFLLSTRSC GLGINLATAD
TVIIYDSDFN PHADIQAMNR AHRIGQSNRL LVYRLVVRAS VEERILQLAK KKLMLDQLFV
NKSESQKEVE DILRWGTEEL FSDSASVTGK DASENSSNKD ETTTDTDHKH RRKTGGLGDV
YKDRCTDGST KVVWDENSIF KLLDRSDLQS GSSEIAEGDL DNDMLGSVKS LEWSDEPNEE
QTGAEVPPAT GDVCAQNSEK KEENSVNVPE ENEWDRLLRV RWEKYQNEET AALGRGKRLR
KAVSYREAFA PHPSETPSES GNEEEEPEPV PEPEYTPAGR ALKEKFARLR ARQKERLAQR
NIIDGSRPVE EQVGPESLPP PTATDDKETE QPVEPVREKA LVIDLEDYKF NQPSDVPKSK
SDTNMRQGRF SKHGYKNMLG SLDLSVRPPG SLPPDIFLPS HQYHSTSYSS SVPTSNLLPV
LGLCAPNANP PESSHRNSRS CNVPRSDSGQ NSLGLGFQDF PFRLAPGAGN SVNIGLQGRE
TAADTCTIPD ASDIPQCRLK NVISDGCFPF NQYPPSTSQG RGLDPLDNSD AAFSAFQEKM
AAPKLAHDDN QLSKFSHSAK TVSKPLPDFL PSLSLSTRAE PANDSVQDFS TMPLLPNFRL
APQDMPKHTL VRDMPPTLGL GQMQTTYPSL PENHKKVLDN IMMRTGSGSN MFRKRLKVDA
WCEDELDALW IGVRRHGRGN WDAMLRDPKL KFSKHRTSED LSLRWEEEQL KIFDGATYTT
TKSTKSTSFP GISDGMMARA LHGSRFSGLG TDHCPPPKFR THLTDMQLGY GDLTPTLPHV
EPSDHFGFPN EHYTPFPSRN SDRFWPNFSG DLNAGPSDRQ GTSSNLHLEQ PFLHSSLVSS
SLGSLGVNYP SSCDLQKKEE QFASKYAKLP SLLNKSLNFL RDCHNNLRGG ESTSSGLQPD
PNKRLHYGHS PAKDDVAGSS STTSKLPHWL REAVNAPAKP PEPELPPTVS AIAHSVRLLY
GEEKPTFPPF TVPGPPPFQP KDPRKSLKKK KRRLRKLRRV TPDIIAESSK NFQNNMFGEN
VASSSISLAP PLPLLPQSTS SASGFPWIEP NLNMSSLNLN LTCSPSSSVY INHRKKLAAG
LSPSPEVLHL VASCVAPGPH MSSAPGSESS SIPRNELPFT NIRESVVQDD SPSLKGAFNK
RKAGQSPLSH IWSQDPKERR ERTESGDSSK TQSDPCNIDR PEVEEISSEE TVSDDHGSEH
EP
//
