ID A0A0V1N720_9BILA Unreviewed; 2051 AA.
AC A0A0V1N720;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein 3 {ECO:0000313|EMBL:KRZ79816.1};
GN Name=CHD3 {ECO:0000313|EMBL:KRZ79816.1};
GN ORFNames=T10_8991 {ECO:0000313|EMBL:KRZ79816.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ79816.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ79816.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ79816.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ79816.1}.
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DR EMBL; JYDO01000005; KRZ79816.1; -; Genomic_DNA.
DR Proteomes; UP000054843; 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:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 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); 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
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 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: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 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 PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000313|EMBL:KRZ79816.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRZ79816.1};
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:UP000054843};
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 317..364
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 385..432
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 574..610
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 711..895
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1027..1192
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1901..1924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..2051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2051 AA; 228614 MW; CE7F6B8336B35891 CRC64;
MDEDEIENNV EEEDDAAVEV ESTESAGEVS TVASKRSTTA AAAAAASKQQ TNVADDSGQQ
RSRRSKKRKT ESAAEVTATP APATESPSSV QPVSNSSPVT TSVSPSSAQI CQEYKLTDVV
LNYLDDDFQG ITNYKAFNTK VRPMILESNP KIAKARLVTL MATKWKEFQE VCSKSKAGLL
QDDGQQQQTP VAAPPSASAT SGKTTRADKE AREKTVAPIK IKLSSRASAR KRRREGSSEE
DGRQDSDAEF EALLAEHEFE QDQVVSTKKT PKSKSGSRTS ARSKGGKTVA KRAPPRKKAK
DGDDEEEENY DVSTDHQDYC EVCQQGGEII LCDTCPRAYH MVCLDPDMEE PPGGKWSCPH
CENDLVNDND AVTSKEATTA KAGNMEFCRL CRDGGELLCC DSCPSSYHRY CLIPPLTTIP
EGDWHCPRCT CVEPEHRPEK ILSWRWLELP PIPAEETKSA QSEEAGAGEE ATSAGSETAV
AKKNVNRRMR EFYVKWKYLS YWHCSWVLEL VLDVWFPHVL RMYFRKMDPE IPPEVDDGSQ
EDLQTGNIEG KEREQDPQNL EERYYRYGIK PEWLQIQRVI NHKVHRHGGV DYLIKWRELS
YEQASWESDE FEIPNFYDAI QYYWDHRERM INEAPPKQVV KRLKTMAVAA SNIAAAQAGT
SGAPEKKKRR LTAPPQPSTD LKKKIEKQPD YITECGGNLH DYQLAGLNFL RYSWATGVDA
ILADEMGLGK TIQTIVFLYS LYKEGHCKGP FLISAPLSTI INWEREFEFW APDFYVVTYI
GDKDSRAVIR EHEFSFVEGA VKGGPKPGKL RTGEGIKFHA LLTSYELISI DHTTLGSIDW
AMLVVDEAHR LKNNQSKFFR TLRDFKLNFK VLLTGTPLQN NLEELFHLLN FLSPERFCDM
ELFTQEFTDI SKEEQIAKLH SLLGPHMLRR LKSDVLKGMP AKSELIVRVE LSTIQKKYYK
YVLTKNFDAL NTRCGGSQVS LLNIMMDLKK CCNHPYLFPI AASEAPKLPN GAFEGSALVK
SCGKLILLQK MLRMLKEGGH RVLIFSQMTK MLDLIEDFLE FEGYKYERID GSVTGSLRQD
AIDRFNAPNA PQFVFLLSTR AGGLGINLAT ADTVIIYDSD WNPHNDIQAF SRAHRIGQNR
KVMIYRFVTR NSVEERITTV AKKKMMLTHL VVRAGIGNRG PSMSKQELDD VLRWGTEELF
KEGDDEKENT DHQIIWDDKA VGALLDRSQV GIEEKENWAN EYLDSFKVAS YVVKQAEEEE
EEEDEDTEVL KEEVQEADPD YWEKLLRHHY EQQQEDIARH LGKGKRIRKQ VNYAMGEQQE
EWRDEYSDNY SASSNASGDE ADDDDFDEKV EGVPRRRRRE GKDEKLPPLL ARVNGQIEVL
GFNVRQRRAF YNAIMRWGMP PADAYNSQWL VRDLKGKSEK AFKAYVSLFF RHLCEPGNEA
NDAYSDGVPR EGVSRQHVLT RIGIMSLLRK KVQEFEIING PYSTPLAGQQ NGSVLADAAV
ASVVEKKSAG KEEDPSPSVI KAEEDTTQQQ NSSKGSSLVS SRSETPLVAA STNVESTDDA
TSSPNKKSKI DDSEDMEVSG ELVIDESAHC EQEAEDKNVK TEEKHKIDGD AANADNTTST
SEAAEIGSAK VDEVKEESDG GTTEGQKSKV KAEEEVVLTT TDGGDVAVDG PQQAGVKLEE
VKVEKKEPAA AAAPTKPPFM FNIADGGFTE LHALWVNEER AASMNRLHEI WHRRHDYWLL
AGIVVHGYGR YQDIQNDSRF AIINEPFSSE QGKGNFVDIK NKFLQRRFKL LEQALIIEEQ
LRRAAYLNLQ QDIINPVMAL NMRFSEVECL AESHQHLSRE SLSGNRPANA VLFKVLNQLE
ELLNDMKSDV SRLPATLARL PSVTSRLGMS ERSILSRLTM KDSGETVPPN PGLPPPGSFV
TPSFSSAGSG GVVNQTVPVV PPNAVVGHVS LSQIPKGSAA VSTPSMSAAH SAAAVGRERG
SNSNNGSHNR NSKNKNNNNN SSSSSAAAVA AATAAMTAAR STSPMGGNSN ALLDDLSQKP
STSSAIIPPL A
//
