ID A0A1I7T7X1_9PELO Unreviewed; 1678 AA.
AC A0A1I7T7X1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=DNA helicase {ECO:0000313|WBParaSite:Csp11.Scaffold536.g3282.t2};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold536.g3282.t2};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold536.g3282.t2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR STRING; 1561998.A0A1I7T7X1; -.
DR WBParaSite; Csp11.Scaffold536.g3282.t2; Csp11.Scaffold536.g3282.t2; Csp11.Scaffold536.g3282.
DR eggNOG; KOG0383; Eukaryota.
DR Proteomes; UP000095282; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
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; 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; 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 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 93..140
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 153..202
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 326..387
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 452..636
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 768..931
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1599..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1029
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1627
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1678 AA; 192987 MW; A39CE90B47F8D83B CRC64;
MTAQGKPIQK QPRGTKTPAA STPVVAFKPA PTKTRSARKK TRRDSEAPDS DQEERGCKSE
KSGGENRKKK EALDAARAAK KAKLEQGEEV ENNDFCEECK QGGELLLCDT CPRAYHTICI
DSSMEDPPEG DWSCPHCEEH GPEIVKEPVK QNDDFCKICK ETENLLLCDN CTCSFHAYCM
NPPLTELPPQ DDPWACPRCE LAKPEQKAEK ILCWRWIEIP YPDPVKEGTE PTEEEVFLKP
PRQMAPRRER EFFIKWKYLS YWQCDWVSEM MMEVHFRMLY IMYWRKNDSE IPPDFEESLT
SRHHSDNDPY KLREKFYQFG VKPEWMQIHR IINHQSYAKS QQDYLVKWKE LTYDQATWER
DDAKIANYEQ AIIKYWQHRE RMLNDDIPKN VQKMIAKQRE AKGLPPKEEE TRRPKKREKV
DIRKKYDVQP DYVSETGGNL HPYQLEGINW LRHCWSNGTD AILADEMGLG KTVQSLTFLY
TLMKEGHCKG PFLIAAPLST IINWEREAEQ WCPDFYVVTY VGDRDSRVVL REHEFSFVEG
AVRSGPKAGR MKTTENMKFH VLLTSYETIN MDKTILSSIE WGALVVDEAH RLKNNQSLFF
KNLNEYTIHY RVLLTGTPLQ NNLEELFHLL NFLSKERFNQ LEAFTAEFSE ISKEDQIEKL
HNLLGPHMLR RLKADVLTGM PSKSELIVRV ELSPMQKKWY KNILTRNFDA LNVKNGGTQM
SLMNVLMELK KCCNHPYLFV KASLEAPKEK NGMYEGTALI KNAGKFVLLQ KMLRKLKDGG
HRVLIFSQMT MMLDIMEDFC DVEGYKYERI DGSITGQMRQ DAIDRYNAPG AQQFVFLLST
RAGGLGINLA TADTVIIYDS DWNPHNDIQA FSRAHRLGQK HKVMIYRFVT KGSVEERITS
VAKKKMLLNH LVVRAGLGGK EGKSMSKSEL DDVLRWGTEE LFKEDECVEG AEGAEGAEKK
QEIVWDDAAV DFLLDRDKKE EAAAGPEEGE GKADWQNEYL SSFKVASYQT KEAEGQEEEE
EEEMEVIKEG DEKEPDPDYW EKLLKHHYEQ DKEIESQKLG KGKRVRKQIN YASENMGTDW
SKQNQAQDED DDNESYHGSD NMEGLNSDDD DYDERRKRRR DDNSEKMPPL MAKVNGQVEI
LGFNPRQRKA FYGAVMRWGM PPQDSHQSQW LVRDLRNKSE KVFRAYASLF MRHLCEPGAD
GHDTFNDGVP REGLNRQHVL GRIGLLSLVR RKVQEFEQHN GEWSMPEVQD EILARAANGS
AEGSSRNTPK PKEVKEETKD EIKDEPMKKE ADATEPTDTT EVREETVKET VEGTSNEATE
SNPTEEPMET EEPTEEIKVS QKPRAARPPF KFNICDGGFT ELHALWANEE KVARNGREYE
IWYRRHDYWL LAGVVVHGYG RFQANFNEII NDPRFAILSE PFKDGRVDTS SDIKAKFMQR
RFKLLEQALV IEEQLRRAAH AGRHLTPDNV GPLAQRFADL ENIAESQANM AKESAAGNRN
ANAVLHKCLV QLDEILTDMK SDVSRLPATF TQLSSVTERL NMTERQILSR LTTKDEDAKS
TRTPLPPPGP FVTPVLRQQM EGIQPKFAAL FSQFMSANGE RMEEDEPVES EETEEVKEEE
MEEETADAGD APPVLSAEDN SEERNEQIEN EPVESDVVGD APVVEEAPVV EPEEPMES
//
