ID A0A183E895_9BILA Unreviewed; 1010 AA.
AC A0A183E895;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=DNA helicase {ECO:0000313|WBParaSite:GPUH_0001720801-mRNA-1};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001720801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0001720801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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DR AlphaFoldDB; A0A183E895; -.
DR WBParaSite; GPUH_0001720801-mRNA-1; GPUH_0001720801-mRNA-1; GPUH_0001720801.
DR Proteomes; UP000050760; 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: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; -; 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; 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; 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; IPR001841; Znf_RING.
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; PF00385; Chromo; 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; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00184; RING; 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; 2.
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 45..92
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 108..155
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 281..314
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 411..584
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 716..883
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 117612 MW; 74063FA43599B68B CRC64;
LLKEHEKQLD EEEREKEERR AARARAAKKK GKKKKGEDGY ETDHQDYCEV CQQGGEIILC
DTCPKAYHLV CLDPDMEEPP EGRWSCPTCE AAGIVKEEEE EKKVTTNMEF CRICKEGGWL
LCCDTCPSSF HAYCINPPLT EVPEGDWSCP RCLCPEPKNR PEKCLSWRWT EVAYPPPMTE
EELKEFEAQE GDRKIALKPL KELPNRRERE LFIKWKYMSY WHCEWFLRMF WRKMDPETPP
EVDDGSQEDL QTGKIENKEK EKDPHNLEER FFRYGIKPEW MQVHRIINHV QYGKTQFDYL
VKWRELVYEQ ATWERDDFDI MGYEEAIMKY WTHRQRMNGD VIPKHIAKKI ALKRVEEGKD
KEDEDEEDSR KKKKREPKSD LRKKYETQPD FITETSGKLH DYQLEGVNWL RHCWSQGTDA
ILADEMGLGK TIQSMVFLYS LVAAPLSTLI NWEREAEFWC PDFYVVTYVG DKDSRTVIRE
HEFSFIEGAV RGGVKPSRMK TDQGIKFHVL LTSYELINID KTILSSIEWA GLVVDEAHRL
KNNQSLFFRT LRDFRINYRL LLTGTPLQNN LEELFHLLNF LSPERFYDMD SFTHEFAEIS
KEDQIQKLHS LLGPHMLRRL KTDVLSGMPS KSELIVRVEL SSMQKKYYKN ILTRNFEALS
PKGGGSQISL LNIIMDLKKC CNHPYLFPKA SIEAPKLKNG MYEGAALVKA SGKFVLLQKM
LKKLKDQGHR VLIFSQMTKM LDIMEDFCEN EGYKYERIDG SITGQARQDA IDRFNAPNAQ
QFVFLLSTRA GGLGINLATA DTVIIYDSDW NPHNDIQAIL FPFAFSRAHR IGQQRKVLIY
RFVTRNSVEE RITSVAKKKM LLTHLVVRAG IGQKGPSMSK SELDEVLRWG TEELFKEDET
TTEGEQGEKK TSEQEIIWDD EAVEALLDRS ADDPKEKAGE KKEHWSNEYL SSFKVAQYTT
READEEEAEE EVSIFLSGVN LSNCCHAFRM FLIVKFCLLH MASGILRSLA
//
