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Database: UniProt
Entry: A0A3Q0KKB1_SCHMA
LinkDB: A0A3Q0KKB1_SCHMA
Original site: A0A3Q0KKB1_SCHMA 
ID   A0A3Q0KKB1_SCHMA        Unreviewed;      1038 AA.
AC   A0A3Q0KKB1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Helicase, putative {ECO:0000313|WBParaSite:Smp_120360.1};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_120360.1};
RN   [1] {ECO:0000313|Proteomes:UP000008854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [2] {ECO:0000313|WBParaSite:Smp_120360.1}
RP   IDENTIFICATION.
RC   STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_120360.1};
RG   WormBaseParasite;
RL   Submitted (DEC-2018) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q0KKB1; -.
DR   STRING; 6183.A0A3Q0KKB1; -.
DR   EnsemblMetazoa; Smp_120360.1; Smp_120360.1; Smp_120360.
DR   WBParaSite; Smp_120360.1; Smp_120360.1; Smp_120360.
DR   InParanoid; A0A3Q0KKB1; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   CDD; cd18024; DEXHc_Mtr4-like; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 2.
DR   Gene3D; 2.40.30.300; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR048392; MTR4-like_stalk.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21408; MTR4-like_stalk; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008854}.
FT   DOMAIN          130..286
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          354..555
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          814..841
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        17..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1038 AA;  117376 MW;  D11334AA1C677F50 CRC64;
     MSAFGLDLDE LTSAFDPKKP SSETSADTGS TQPGDFEEKK RKAEASLKPL LKEVGEDSTD
     DSPKRSKLSV TDTLEFNAPR IQIHKISSPE TCTHEVAVPP DIEYKPITKD CGFPAKTFPF
     TLDAFQQQAI ICIDNNQSVL LSAHTSAGKT VVAEYAIATA LREKQRVIYT TPIKALSNQK
     YREFFEAFPE VGLLTGDATI NPSASVLIMT TEILQSMLYK GASMVREVGW VIFDEIHYMR
     DPERGVVWEE TIVLLPDSVR YVFLSATIPN ARQFAEWIAH LHHQPCHVVS SDCRPVPLRH
     YLYPVGSEGL FLVLDEGKYL EQNFERAMRS FLSDESSNKR QKSQVDYNKR SENNVIQIVR
     LVKHRSLEPI IVFSFSKKEC EIYALQLAKF DFTTDAEKKV VDEVFRNAID GLSPEDRALP
     QVESVLPLLK RGIGIHHGGL LPLLKETIEI LFSENLIKCL FATETFAMGL NMPARTVLFT
     SARKYDGQSY RWITSGEYIQ MSGRAGRRGK DDSGTVILMV DESMTSELAH QIMMGPPPPL
     NSAFHITYNM LLNLLRVEEI NPEYMMERSF CQFQNFSSLP NMYKELNELR ATYASTVVDD
     EESVESYHQI QLCFDELVGQ QWQYIRRPQY IVPFLQPGRL VKIVVQSISY GWGAVINLKK
     RQRKDRSSTP ESFYILDCLL CNNPSRSDSD ESGSDVPSGN PVDNLGITNS VTPTGSDTLP
     MAEIIPVRLD CVVGISAVRL VVPNDLRSKE ARQGVLNAIE KVKVRMGGSL PVLDPIADMH
     ISDPRFLEIN EKVTAFQERL QHHWLHDDPR LSELSKVYRK KEQLRKRIDA LTANLNSKVS
     LIQLEELSAR KRVLRRLNFV SEYDVIELKG CVACEITSAD ELLLTELLFD GVFNRLSSEH
     IAALLSCFVF EERASEMPKL TKELSDALRT LQDTARRIAR ISNECRLPVD EDNYVDSFKP
     HLMDLVDAWT RGASFASVCS MTDLFEGTII RTLRLLEELL RQMANAARTI GSNVLEKKFV
     EAIEKIKRDI VFAASLYL
//
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