ID A0A0V1PN99_9BILA Unreviewed; 2108 AA.
AC A0A0V1PN99;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein 3 {ECO:0000313|EMBL:KRZ97712.1};
GN Name=CHD3 {ECO:0000313|EMBL:KRZ97712.1};
GN ORFNames=T08_10108 {ECO:0000313|EMBL:KRZ97712.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ97712.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ97712.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ97712.1};
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:KRZ97712.1}.
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DR EMBL; JYDM01000002; KRZ97712.1; -; Genomic_DNA.
DR STRING; 92180.A0A0V1PN99; -.
DR Proteomes; UP000054924; 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:KRZ97712.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRZ97712.1};
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:UP000054924};
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 340..387
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 408..455
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 594..630
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 729..928
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1060..1225
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..1991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2011..2108
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 77..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2011..2064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2078..2102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2108 AA; 235103 MW; 31ECCEA921BBAAD6 CRC64;
MDEDEIENNV EEEDDAGVEF ESTESAGEVA TVASKRASAA AAKQQQIVVA DDSGQQRSRR
SKKRKTDGAA ELAAAPAQSP STVQPVSNSS PVTTTSVSPS SAQICQEYKL TDVVLNYLDD
DFQGITNYKA FNTKVRPMIL ESNPKIAKAR LVTLMATKWK EFQEVCSKSK AGLLQDDAQQ
QQTPVASSSA PPPSSAGSGK TTRADKEARE KTVAPIKIKL SSRASARKRR REGSSDKVTF
CVYAPFKTFF WFFLNSPQVE AAIEEDGRQD SDAEFEALLA EHEFEQDQVV STKKTSKSKS
GSRASARSKG GKAVAKRAPP KKKTKDGDDE EEENYDTDHQ DYCEVCQQGG EIILCDTCPR
AYHMVCLDPD MEEPPGGKWS CPHCENDLVN DNDAVTSKEA TPAKAGNMEF CRLCRDGGEL
LCCDSCPSSY HRYCLIPPLT TIPEGDWHCP RCTCVEPEHR PEKILSWRWM ELPPIPAEET
KSTEEAGEET TSSGIETAAV AKKNANRRMR EFYVKWKYLS YWHCSWVLEL VLDVWFPHVL
RMYFRKMDPE IPPEVDDGSQ EDLQTGNIEG KDREQDPHNL EERYYRYGIK PEWLQIQRVI
NHKVHRHGGV DYLIKWRELS YEQASWESDE FEIPNFYDAI QYYWDHRERM INEAPPKQVV
KRLKTMAVAA SNIAAAQAGT NPEKKKRRLT APPQPSTDLK KKIEKQPDYI TECGGNLHDY
QLAGLNFLRY SWATSVDAIL ADEMGLGKTI QTIVFLYSLY KEVREKGIEQ QLLNNPYGHC
KGPFLISAPL STIINWEREF EFWAPDFYVV TYIGDKDSRA VIREHEFSFV EGAVKGGPKP
GKLRTGEGIK FHALLTSYEL ISIDHTTLGS IDWAMLVVDE AHRLKNNQSK FFRTLRDFKL
NFKVLLTGTP LQNNLEELFH LLNFLSPERF CDMELFTQEF TDISKEEQIA KLHSLLGPHM
LRRLKSDVLK GMPAKSELIV RVELSTIQKK YYKYVLTKNF DALNTRCGGS QVSLLNIMMD
LKKCCNHPYL FPIAASEAPK LPNGAFEGSA LVKSCGKLIL LQKMLRMLKE GGHRVLIFSQ
MTKMLDLIED FLEYEGYKYE RIDGSVTGSL RQDAIDRFNA PNAPQFVFLL STRAGGLGIN
LATADTVIIY DSDWNPHNDI QAFSRAHRIG QNRKVMIYRF VTRNSVEERI TTVAKKKMML
THLVVRAGIG NRGPSMSKQE LDDVLRWGTE ELFKEGDDEK ENTDHQIIWD DKAVGALLDR
SQVGIEEKEN WANEYLDSFK VASYVVKQAE EEEDEEDEDT EVLKEEVQEA DPDYWEKLLR
HHYEQQQEDI ARHLGKGKRI RKQVNYAMGE QQEEWRDEYS DNYSASSNAS GDEADDDDFD
EKVEGVPRRR RREGKDEKLP PLLARVNGQI EFASENRTDA TKRSLFSLSK GESDGTRFQR
STTSRFLQCY YAMGNATGGF AFRLVRDLKG KSEKAFKAYV SLFFRHLCEP GNEANDAYSD
GVPREGVSRQ HVLTRIGIMS LLRKKVQEFE IINGPYSTPL AGQQNGNVLA DATVASVAEK
KSAGKEEDPP TSISKAEEDA AQQQTSSKGS SLVSSRSETP VVASTNLEST DDATSSSNKK
SKIDDGEDME VSGELVIDES AQCEQEAEEK KVKTEEKHKI DGDAAAAIAN ADNNNTTSPS
EAAGIGSAKV EEVNNEKPDG GTTEGQKSKV SADEEEVLAT TTDGDVAAAD GHQHADVKME
EVKTAKKESA AASTKPPFMF NIADGGFTEL HALWVNEERA ASMNRLHEIW HRRHDYWLLA
GIVVHGYGRY QDIQNDSRFA IINEPFSSEQ GKGNFVDIKN KFLQRRFKLL EQALIIEEQL
RRAAYLNLQQ DIINPVMALN MRFSEVECLA ESHQHLSRES LSGNRPANAV LFKVLNQLEE
LLNDMKSDVS RLPATLARLP SVTSRLAMSE RSILSRLTMK DSGEAVPPNP GLPPPGPFVT
PSFSGGGGVN QSVPVVPPNA VVGQVSLSQI PKGSSAALSP PSASTAHSSA AGRERGSNSN
NNANHSRSSK NKNNNNSSSS GSAAAVAAAA AAMTAARSTS PMGGNSNALL DDLSQKPSTS
SAIIPPLA
//
