ID W6UI63_ECHGR Unreviewed; 2572 AA.
AC W6UI63;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein {ECO:0000313|EMBL:EUB61175.1};
GN ORFNames=EGR_04023 {ECO:0000313|EMBL:EUB61175.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB61175.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB61175.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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:EUB61175.1}.
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DR EMBL; APAU02000023; EUB61175.1; -; Genomic_DNA.
DR STRING; 6210.W6UI63; -.
DR EnsemblMetazoa; XM_024493272.1; XP_024352371.1; GeneID_36339738.
DR OMA; WEHENED; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProt.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd17994; DEXHc_CHD3_4_5; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.220.160; -; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.170.270.10; SET domain; 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); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR046341; SET_dom_sf.
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; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000313|EMBL:EUB61175.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EUB61175.1};
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:UP000019149};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 33..73
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 891..938
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 988..1035
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1195..1244
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 1333..1517
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1649..1831
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 543..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1950..2002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2194..2215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2511..2541
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 554..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2572 AA; 287363 MW; 0A6926C34909F776 CRC64;
MLVQHKSYKP GDLIWSEEAL VCALHVDSSP QYCAYCLLSV SQQPLLRCSR CKHVFYCSRI
CQKSHWCSHK QECACIVSSG AFPGATIRLL FNIIVSKVYK NYPFFELLVS HVEELNANDE
TRLMMEQAYA MLMVFSNQNI SISKSCFFRL FGRVKINAFH LTSECGDEIG VALFERSSKL
DHSCLPNADF AFVGKRIKVI ATDEILDASQ IRISYVDLLM SMKRRQEELF NGYLFHCNCP
RCSDLEQDFD TRIPPCCGRR MRGLKADALE HQEPVSWPSE ANAFLPNLAK YSTVAPEEVY
VCGKCHRCYS AAVFDALECR CYEINTLKDA VGLYRACAAA ANTGNNEYLH LVYNHQGSLP
LLRLCRTMVM TYRVDEDNLN DRDCRAGVFT VDDLRDRVFT ICATIFSNGP DLNVNISISI
LYPPSHIDES GESGELDLML EVGLRLARCF DSVAAKYHSF HGHLFVCSLV CALLGLLGSV
VSAMEAHLSL SGGGGDDISG VTLERLEHFS AAFVRTAVAF APCIKRFAPH LPGVSEQLQR
LSSEAQRRRN KMRRRNIDIG DDSSGSATKR RTARVVKEKT LEQLCEELGV EDVELTYSTD
DFENWTVQKL FNQYVQPLIV EKNPHVPKEH IVQILDAKWK EFAIMNPYIP KGEEDLPDDE
EESSTLVAPS GSFGVEDEAE AEDTESTVVV TPVAPAVPRR ASSRHLRAAA AAAVVATATA
ASVGGGGGPA VVSPVAPTEL PGEGGEISQS SPASSAAATP ASSQAAPLRI KISKKKKRKA
PGGRSGGRRR EGGRLVGDNT SDEEFERQLE EAEAFQEEEQ KRRKQQRSLN ARRAAAAARV
SATAATGQMH VSASAPNLAA SASGVKRSII ARVPLMGGNR QAEDGYETDH QDYCDVCQQG
GNIMLCDTCP RAYHLVCLDP ELEEVPEGVW SCPHCEKQGI TVAHRSTADP AAAGDEDAST
ASEGPVHVSR KAATAGGAEE EGERDEHQEY CSECRDGGDL ICCENCPASY HLGCLDPPLS
QIPEGVWLCP RCGCKPLKAR VSKILFWRWR EPPKTAISVM EDVEKIEVDR EGMDGTVPPT
QATALDPQTG EVEQVSCVGA LAVTAPHPPA RRKPTREFFV KFHEMSYWAC EWVTELQLEV
FHSLMLRVFS KKYDMEEPPL PEDGSSYRGR AREKAPDPQN LEERFYKWGV RPEWLQPQRI
IDSRMTRQKE WFLVKWRDLP YDECTWEDVA TTEVPEFERF VEEFRLMRGL FKGETSFVTT
GKKKGSSSST ATATAAAIAS AKKTSISASL LKKIPPEKPI TDLRKQLTKQ PEYMDETGGE
LHPYQLEGLN WLRFSYGNKV DTILADEMGL GKTIQTIAFL YSLYKDGHSR GPFLVAAPLS
TIINWEREFE LWAPDFYVVT YVGDKDSRTV IREHEFTFEE GGVRGGSRVV KMRSGAQVRF
HVLLTSYELI SIDQALLSSI DWEVLVVDEA HRLKNNQSKF FRMLSTYKIA YKLLLTGTPL
QNNLEELFHL LHFMSPAKFY DMQGFLDEFA DISKEDQVKK LHEMLGKHLL RRLKADVLKN
MPSKGEFIVR VELSPMQKKF YKFILTKNFD ALSCRSGGAQ PSLINVMMDL KKCCNHPYLF
PSAAEDAPRL PNGAFEGLAL RKACGKLELL SAMLQKLKAG GHRVLIFSQM TKMLDLLEDF
LEAEGYKFER IDGNVTGQQR QDAIDRFNAI DSTSFVFLLS TRAGGLGINL ATADTVIIYD
SDWNPHNDIQ AFSRAHRIGQ ANKAIWIEVA EVMIYRFVTR ATVEERVTQV AKKKMMLTHL
VVRPGLGGKG ASQMSKKELD DILKFGTEDL FKHEDNDATD EHCIVYDDAA LDRLLDRSQQ
GMEEKQMEMN DYLSSFKVAH YEKREIQDGD SEEPGDEDSN VEVIKQESDT NDPAYWEKLL
RHHFEQAQED QAKLLGKGKR HRKPVNYWAN QQEDEEEWND NTSDHDSNFS TKDEDDDEYD
EKAGGNGEGM GSQIGRRVRR EREGKMPPLL SRVNGQIEVL GFNIRQRRAF VNSVLRYGLP
PPPSSFSMAG VPVASATAST AWHSRDLKGK PERVFRAYVA LFMRHLCEPE SMNQENNATY
SDGTPRDGIS HQPILSRIGI MALVRKKVQE FEQINGLYSI PDSTTTSDTA LAAMATTTTS
TAAAAGEGNS GDGPDGASTP LTQPLCVAVA TSHANGNGGA SCSDDASKAS DKTEPMDIST
VDEVTVPVTT VSSSKNGETD AATAMMTLAV EEGEAVEPEG RLKIDETNAG TSCDSMDADE
KPKAETLEAE TVDEGAVKLE TDVESRLHHR RSSFMFNIAD GGFTELHTIW LNEQRALEEN
TEGYEIWHRK HDYWLLAGVV QHGYGRWQDI HNDPRFALVN EPFRADQGKP NYLEMKNRFL
ARRFKLLEQA LIIEEQLRRA AHQNIVCDPK DTVQSLNRRF NELECLAVAQ QQVYAEALAG
NKSLVQLIHR ALTMMEDYLA EMKQDVSRLL TLVPRMPPVS DRLNLSHTGL LTKLTQHLTA
AKQAKLALQQ QQQQQQQQQQ QAVSNPATPI DTATVDESSR LLWKRSVAFF WF
//
