ID D8LYM1_BLAHO Unreviewed; 1198 AA.
AC D8LYM1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=GSBLH_T00000965001 {ECO:0000313|EMBL:CBK20676.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK20676.2};
RN [1] {ECO:0000313|EMBL:CBK20676.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK20676.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; FN668639; CBK20676.2; -; Genomic_DNA.
DR RefSeq; XP_012894724.1; XM_013039270.1.
DR AlphaFoldDB; D8LYM1; -.
DR EnsemblProtists; CBK20676; CBK20676; GSBLH_T00000965001.
DR GeneID; 24918250; -.
DR InParanoid; D8LYM1; -.
DR OMA; KYAYHCA; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000008312; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008312}.
FT DOMAIN 241..422
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 451..695
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..831
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 136261 MW; BFCDDFADF5608284 CRC64;
MKEEKLAKKA EQKGKRAKKR EELEKKKQMK ILHDKMLEEI QKKQLNSAEL SVFTPTGALG
KKATKKERVK QAFYKEKLGM KLNEEEDAIL HVRIEKPEDN PDTKEEHEEE EEEEEEEESC
EEGVETQEAP TEGTFIDPLE ESDNNNEEKE EEEEEEEEDT GPKGPTYFEE INKVMESAPK
GINLRINDDS VEDLRRIKED LEAAIPSDLK KKAYFINVNR KPEITAIRSQ LPVCAMEQEI
MEAVNYHDVV IICGETGSGK TTQVPQFLYE AGYGADESGH PGMIGITQPR RVAAVSMARR
VADELNSTCD GKGLVGYQIR YDHHTVGPNT KVKFMTDGIL LKEIQSDFIL RSYSAILLDE
AHERNLNTDL LLGLLSRIIP LRSQLYSEGK VKSKLKLIIM SATLKVEDFK NPVLFPTTPP
IIHVQARMYP VGVHFAKKTE MDDYVGAAYK KVVQIHKRLP DGGILVFLTG QQEIETLCRK
LNSKWEFSPT AVAKRKKELK ERNEGEDEPE SMIIQPTKLP NGEEDVTVDH LAVYEEDSDI
EEEGEVPFEK GPDAFYDDIS QSTAPMHVLP LYSLLDEKKQ LRIWDPIPEG ERLVVVATNV
AETSITIPNI KYVVDCGRAK EKVWEKETGI CEYKVQWISQ ASAEQRQGRA GRVAPGHCYR
LYSAAVFQQQ FPVWDTPEVC RTPLEDTVLL MKDMGIKNVE SFPFPTQPDA ASLHAAVEIL
RALGAVDGSK DEITVLGKEM MKYPVGVRYA KMIVLARERE NVLPLVVGII AALTGRTPII
RPEELLMREN GNENNENNGN NGNENENENK EDENENKEDE MEIENETTDP TEENEELKKC
RESLLLWRDA SSDALSSLRL LGAFLHTNTP SLFCKEHFLR EKSMREMVDL RKQINRLLIS
QQPSLSAVLS KPLVPPTSKQ ATILRQIVAA GFIDHVARRM TPSEARDIDI PRGKVPYLTT
TLNELTPAFI HRESFVLPIK TSDYVRVGIV FFMNRTNIRT ILCSKIWFKR KEGRNCSVTT
INKSWLPSLS GEGPLCVYSS PLETPQPFYD PKKEEMMCYV IPRFGSHLWE LSAYCRKFPQ
SDPSIYKWFG KQLLEGKVIP EFAILVSFYS SSPAMLTKPQ LPIKGMALLN ALQREKVVTR
TSLLKIWERN RIFLKAELTA WVLPRYLDIL TTIWPYIIVG KSVPDSILDA IKVKYDVK
//
