ID A0A0V0UC29_9BILA Unreviewed; 2106 AA.
AC A0A0V0UC29;
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:KRX48996.1};
GN Name=CHD3 {ECO:0000313|EMBL:KRX48996.1};
GN ORFNames=T05_11762 {ECO:0000313|EMBL:KRX48996.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX48996.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX48996.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX48996.1};
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:KRX48996.1}.
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DR EMBL; JYDJ01000021; KRX48996.1; -; Genomic_DNA.
DR Proteomes; UP000055048; 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:KRX48996.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRX48996.1};
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:UP000055048};
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 357..404
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 425..472
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 611..647
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 748..947
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1079..1244
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..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..1989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2009..2106
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 37..54
FT /note="Polar 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 1400..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2009..2062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2106 AA; 235079 MW; 723792475BE568C1 CRC64;
MDEDEIENNV EEEDDAGVEF ESTESAGEVA TVASKRASAT AAKQQQIVVA DDSGQQRSRR
SKKRKTDGAA ELAAAPAQSP STVQPVSNSS PVTTTSVSPS SAQICQEYKL TDVVLNYLDD
DFQGITNYKA FNTKVRPMIL ESNPKIAKAR LVTLMATKWK EFQEVCSKSK AGLLQDDAQQ
QQTPVASSSA PPPSSAGSGK TTRADKEARE KTVAPIKIKL SSRASARKRR REGSSDKVTF
CVYAPFKVIS LTFSMLLSER VEVTTFLWFF LNSPQVEAAI EEDGRQDSDA EFEALLAEHE
FEQDQVVSTK KTSKSKSGSR ASARSKGGKA VAKRAPPKKK TKDGDDEEEE NYDTDHQDYC
EVCQQGGEII LCDTCPRAYH MVCLDPDMEE PPGGKWSCPH CENDLVNDND AVTSKEATPA
KAGNMEFCRL CRDGGELLCC DSCPSSYHRY CLIPPLTTIP EGDWHCPRCT CVEPEHRPEK
ILSWRWMELP PIPAEETKST EEAGEETTSS GIETAAVAKK NANRRMREFY VKWKYLSYWH
CSWVLELVLD VWFPHVLRMY FRKMDPEIPP EVDDGSQEDL QTGNIEGKDR EQDPHNLEER
YYRYGIKPEW LQIQRVINHK VHRHGGVDYL IKWRELSYEQ ASWESDEFEI PNFYDAIQYY
WDHRERMINE APPKQVVKRL KTMAVAASNI AAAQAGTSGA PEKKKRRLTA PPQPSTDLKK
KIEKQPDYIT ECGGNLHDYQ LAGLNFLRYS WATSVDAILA DEMGLGKTIQ TIVFLYSLYK
EVREKGIEQQ LLKNPYGHCK GPFLISAPLS TIINWEREFE FWAPDFYVVT YIGDKDSRAV
IREHEFSFVE GAVKGGPKPG KLRTGEGIKF HALLTSYELI SIDHTTLGSI DWAMLVVDEA
HRLKNNQSKF FRTLRDFKLN FKVLLTGTPL QNNLEELFHL LNFLSPERFC DMELFTQEFT
DISKEEQIAK LHSLLGPHML RRLKSDVLKG MPAKSELIVR VELSTIQKKY YKYVLTKNFD
ALNTRCGGSQ VSLLNIMMDL KKCCNHPYLF PIAASEAPKL PNGAFEGSAL VKSCGKLILL
QKMLRMLKEG GHRVLIFSQM TKMLDLIEDF LEYEGYKYER IDGSVTGSLR QDAIDRFNAP
NAPQFVFLLS TRAGGLGINL ATADTVIIYD SDWNPHNDIQ AFSRAHRIGQ NRKVMIYRFV
TRNSVEERIT TVAKKKMMLT HLVVRAGIGN RGPSMSKQEL DDVLRWGTEE LFKEGDDEKE
NTDHQIIWDD KAVGALLDRS QVGIEEKENW ANEYLDSFKV ASYVVKQAEE EEDEEDEDTE
VLKEEVQEAD PDYWEKLLRH HYEQQQEDIA RHLGKGKRIR KQVNYAMGEQ QEEWRDEYSD
NYSASSNASG DEADDDDFDE KVEGVPRRRR REGKDEKLPP LLARVNGQIE VLGFNVRQRR
AFYNAIMRWG MPPADCYNSQ WLVRDLKGKS EKAFKAYVSL FFRHLCEPGN EANDAYSDGV
PREGVSRQHV LTRIGIMSLL RKKVQEFEII NGPYSTPLAG QQNGNVLADA TVASVAEKKS
AGKEEDPSTS ISKAEEDAAQ QQTSSKGSSL VSSRSETPVV ASTNLESTDD ATSSSNKKSK
IDDGEDMEVS GELVIDESAQ CEQEAEEKKV KTEEKHKIDG DAAAAIANAD NNNTTSLSEA
AGIGSVKVEE VNNEKPDGGT TEGQKSKVSA DEEEVLATTT DGDVAAADGH QHADVKMEEV
KTAKKESAAA STKPPFMFNI ADGGFTELHA LWVNEERAAS MNRLHEIWHR RHDYWLLAGI
VVHGYGRYQD IQNDSRFAII NEPFSSEQGK GNFVDIKNKF LQRRFKLLEQ ALIIEEQLRR
AAYLNLQQDI INPVMALNMR FSEVECLAES HQHLSRESLS GNRPANAVLF KVLNQLEELL
NDMKSDVSRL PATLARLPSV TSRLAMSERS ILSRLTMKDS GEAVPPNPGL PPPGPFVTPS
FSGGGGVNQS VPVVPPNAVV GQVSLSQIPK GSSAALSPPS ASTAHSSAAG RERGSNSNNN
ANHSRSSKNK NNNNSSSSGS AAAVAAAAAA MTAARSTSPM GGNSNALLDD LSQKPSTSSA
IIPPLA
//
