ID A0A183K7W6_9TREM Unreviewed; 1810 AA.
AC A0A183K7W6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS Schistosoma curassoni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001109501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SCUD_0001109501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 6186.A0A183K7W6; -.
DR WBParaSite; SCUD_0001109501-mRNA-1; SCUD_0001109501-mRNA-1; SCUD_0001109501.
DR Proteomes; UP000050789; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
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 InterPro; IPR040793; CDH1_2_SANT_HL1.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_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 PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 268..336
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 364..426
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 467..642
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 781..932
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 10..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1774..1810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1810 AA; 208434 MW; D86C3562AFCF9037 CRC64;
LLVCFCRSDG SISHTDQSES SPQEDTVLSN SPPQPVRSRK QNIRELREEF EDYPELYGIR
RSARSRKEPL RFKASEKDTP DALFREKRRN RFPSSSDSNN VTDSETDDWN DNISTRHRTV
RTRGNRVNYK SAFVDDSFDE SNDEPSERSS SSIFKSINQR TSYGTVPILN QQTCFQKPRG
PLVRKPYAPV LASRNSKSFI KSEDDNNLDQ IGVNEQYSEE DEDGVSGEVN REIEWGVDDE
EVDVIEEILT HAIRRKGATG NPTTLYNTQL EKDLNAGFNP KQEDGELQFL IKWRNWSHIH
STWETESSLR NPDRGAPVAG MKKFYAYQAI MREKSERLQY VEREELETVA YEEERDEQLL
QDKMNVERIV AHSRDPETNT FDYLIKWFRL DYRFCTWESG KVIHLLYESA VQAYETRCNS
TTLPNRKCEV LYTRPKFLPL MEQPSYLGRS KELRLRDYQL EGINWLIRAW TRRNSVILAD
EMGLGKTIQT IGFLSYLFNE HQVYGPFLIV VPLSTISSWQ KELQTWAPEM NTIIYTGDHV
SRQLIREHEW STGASNNRRH QSLKFNVCVT TYEILLKDKG WLSQVNWAFL GVDEAHRLKN
DSSQLYKTLK TFETNTRLLV TGTPLQNTMK ELWALLHFIM PDCFPDWEEF ERTYSVSPDD
PANKMNNEAF HNLHKTLKPF LLRRVKKDVE SSLPEKIEQI LRVDMTKEQA NIYRLILARN
YDGLLKVTRG HKASFINIVM ELKKCCNHAH LIAPPSEVDQ QYLTKEDRLR LFLKGSGKGT
LLDKLLQRLK SKGHRVLIFS QMVRMLDLIA DYLSLRGWGF QRLDGSIRGE VRKQALDHFN
CEGSTDFCFL LSTRAGGLGI NLATADTVII FDSDWNPQND LQAQARAHRI GQTKQVSVYR
FVTRESVEEK IIESATRKMV LDHLVIQRMD SAGIRSGRRG DTAKGHLLTE ILRYGAEGLF
KQADEDATEL EVDIDDILNR AETRDTEATV ESNPANALLS SFKVVNLDAL EEDTDIKNGN
DSLNSSINAG CEKTWDQIIP SEFRGQVKAE QDRKTLVELE LGPRRRRPVK TFQAGLNSNQ
SSSETSETEE NDKVLPTQLT EKEIRALVRA IRHFARPLER IDAIAADAEL PDHSESELRE
VVDAVLKGCR TAMEAASINS NEESQKQVTG GKGPVFQYGR VSVAARPLLQ SLEYLETLHL
CLPSTSKEAR MSYELPFSPK LVAWSCNWDN TDDVRLLAGV YEHGYDNWET IKLDADLGLG
SKLLPVSQTE RPQANHLRSR VDYLLKMLAK CHSSVSKNTE QQMVTKKRRK DDRESNKSNQ
KAKAITSKAN VKHTNKQIST PINSMPKSAE FVETDDSSSE SDCNKNNDDK QEENDIDNDN
TSNQLLKNTK QSRKSTNKSK IKSEKKDKYI SELKPPTLQP LSSNHQENLS NVPTMLFTKK
EEDEFRNMQG PIFVKCKKKF VPIKKHFKEL EDLERTDEQN PVKLANVVLQ IGDHIHSIVD
VYPDKEKRHA WKNYLWEFVH IFSKNSTEEL RHIYRHAVKR RLKEQRKKTN DADFNFSPKH
HKDSLRNTNS SIDYFEMTSN RHSSNRDYYS NNNDNNTGNA ALFRRYHTNR LSSHDRNDRH
EQHSGYSHGG QNKYYNNSDN DWPSSVTSSH KEFNRDRNNN SSRFDNAFNR PPGQSNIKHH
KDSGSFTSQM YSPRVPSSHY HQQQQHNSSS YSSVHHPWTN YSSSDDMINS SPKMETYKYT
SHYPPVLSSS TSSCMPESII STTITTKAPS YFSSMGQCLP PPPPLPPLLQ QQQHTTSQLS
RDPRLSSSRR
//
