ID A0A1I7S5J6_BURXY Unreviewed; 1720 AA.
AC A0A1I7S5J6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein 4 {ECO:0000313|WBParaSite:BXY_0828100.1};
OS Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS xylophilus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0828100.1};
RN [1] {ECO:0000313|WBParaSite:BXY_0828100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR WBParaSite; BXY_0828100.1; BXY_0828100.1; BXY_0828100.
DR eggNOG; KOG0383; Eukaryota.
DR Proteomes; UP000095284; Unplaced.
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:InterPro.
DR GO; GO:0004386; F:helicase 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; 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; 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; 2.
DR Pfam; PF06461; CHDII_SANT-like; 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; 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 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 94..141
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 159..208
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 249..313
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 479..659
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 791..951
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1720 AA; 198794 MW; F666955DE7340F81 CRC64;
MSSRPKRSTR QAANTSTVSN GDAERELRDR KPKKASKKRK RDESDDDFGN PDSEEEFEKL
MQRAEEEEDE RIAKKKKRKE ERQRKENHVQ EEHQDFCEVC QQGGEVILCD GCPKAYHKIC
LDPELDEVPE GSWFCPSCAE NGVPEEGKKK EKDQPPGNMD TCLICKEGGF ILCCDSCPNS
YHAYCTTPPM EELPDANDPW HCPYCTVEEP PHKPHKIISW RWVSVPYPDP VDPADLPKDG
ERQEDMDEER VQRLMLRPPR KMEPRKEREL FVKWKNLSYY HATWVPELPL QVHHRTFMTV
YWRMNGDMEP PENDDGSTDA ETGNVADQEK ESDEHDLEKR FYRYGVKPEW MQIARIINHY
QAGSRAFDYL IKWSDLAYDQ ATWEADDMDI ANYMEKINKY WTHRELMTNE KIPKSVLKKI
EAWRDENGMP SWEEEKQKKK EERKKKNDIS KKYEEQPQFV VDTGGKLHEY QMEGINWLRH
CWSQDINAIL ADEMGLGKTV QALTFLYSLY KEGHSDGPFL VAAPLSTIIN WEREAEFWAP
DFYVVTYCGL KEARAVIREH EITFDEVKNS SKACKVKGNL KFHVLLTSYE CINVDKATLA
SIKWEALVVD EAHRLKNNQS LFFRNLKEYD IAYKLLLTGT PLQNNLEELF HLLNFLSPDE
FTNVEEFTSE FADIAKEDQV AKLHSMLGPH MLRRLKADVL TGMPSKSELI VCVDMVPLQK
RYYRNILTRN YDALNIKGGG RMVSLSNILM ELKKCCNHPY LFPKAEEEAP KTKTGAFEGE
AMIKGCAKLE LLAKMLKKLK AGGHRVLIFS QMTRLLDILE EFCEHLGYRY ERIDGSITGQ
MRQESIDRFN APNSEHFVFL LSTRAGGLGI NLATADTVII YDSDWNPHND IQAFSRAHRL
GQRNHVMIYR FVTRNSVEER ITTVAKKKML LTHLAIRNNN KQTTMSKSEL DDVLRWGTEE
LFKEEEDQIQ IVWDDEAVDA LLQRAEEADK ETGEKKDWAN DYLSSFKVAQ YVTKEKDEKD
ITEEEVKELI EEKPQAEDPD YWERLLRHHH ENEVEQQAAQ LGKGKRVRRQ VNYAADHMDY
RGKKDQENDD DYNASSDEEG TGESGHATGE EDEGGERGER RRKKEREEKL PPLLTRNQGQ
IEVLGFNPRQ RKAFFNAVMR YGMPPPDAYH SQWLVKDLKC KSEKAFKAYA SLFMRHLCEP
GSDHIDHFND GVPREGLNRQ HVLTRIGIMS LIRKKVQEFQ EVNGVWSVSE ESDKQLADCL
VTLGLRESEE KEEPEKDGSQ EPQETEKEEK EKEENDEKEE KEASEKPEDK PEEEMDTENN
ENKPEEIKDD ENKAEIIENG ARKRGVATFK FNICDGGFTE LHTIWKNEED ALKKEEKDYE
IWNRRHDYWL LAGFATHGYG RYNDVINDVR FSLLNEAFKN EKDRPGFNDM RLRFMQRRFK
LLEQSLIVEE QLRRAANISY GQKPPKEEKK EEKEEVQENG EKSEAEKTAE ALEKKYIQIT
SLVDANQALA KEAFAGNKNA AAVLHKVLSQ LEDILNDMKA DVSRLPASVA QLPSVAERLE
LSERTILNRL TTRDSQAFAG KSPIPPPGPF ATPVQNTRFH GIQPKFAALV SAKPARTPTY
GQPTVISVDD KSNKKDEASP APSNGVPPKS ENSENGTPAP EKKEEREENE ESSQEPSQER
SLESSQERSV EPAEKNGEEE KEAKPEKEEN SAEEEVVMEE
//
