ID A0A183LGE7_9TREM Unreviewed; 1025 AA.
AC A0A183LGE7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0000287101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0000287101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
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DR AlphaFoldDB; A0A183LGE7; -.
DR STRING; 48269.A0A183LGE7; -.
DR WBParaSite; SMRZ_0000287101-mRNA-1; SMRZ_0000287101-mRNA-1; SMRZ_0000287101.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24031:SF2; ATP-DEPENDENT RNA HELICASE DDX55; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01178; DUF4217; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365068};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 1..85
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 711..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 117808 MW; 20B4235762A6416B CRC64;
LCTDVMARGI DVPHIDWVIQ CDPPTNANEF VHRCGRTARC GLEGNALLFV NSQEAAYINF
LHINQQVNLL HMERDELNQH IAPLTTVDSM DSITERIRNL CKKDNYCVEQ AALLKGRLML
VAIFLNLPSN ISAQEDMNNV NSANFLQNCY FVYIDIFFLF QRLLHEKAIR AFVSYVQFYR
KHECNILLNY KKLDYGRLAN GFGLLKLPSM PELRTGNVSS FNPSNMDPPY PPTRLKHRTF
AFCPLNFVNN NPVVSEGGED KSVAKQRELM QLSDETHKEN KPKWLIKKEK NKAWIAKKKR
ARKIKALKKQ HLVNESSHPE ICEKKNKEII ETKQENSVKD INELLVDYRL LKKSYKGKVI
PQLKSVHFDL NEGDNRVSSV SNIHQNAVSQ LQELLDMHDN CSYLLELHQA INSFESSVNQ
LLHQCSRRSV DDKKKKLEDT VVKSPKDSEI DSELDDKCVE VDEETYRLCV DSVVTSLEES
EHLLAKHKKF NKDVVLIFQS CQQTFTRCKN RLTQHVDDLW RRWIILEVPS KHQNVSSKFN
VNNIYPSIRG QLQSNDFFSF LFDDCIPSPT DMCKFLRQPS YTSDSVFYEV SDHDVPTTQS
YGESTILASL KILAKPELIS QLLRILEALK ESKSRILQLG NQIWTYIFKP WLKKVPCVSG
PNVGWGKLKC QIIEQSVNIE SDHELFIKEI GLETTDNDCV HMTQYLRLTL IAPNTPPPNT
ITNPNENNHN HDEDDEDDDD DNDDLISSSC NQLIKVFQEL YTYLFGLQAI QSDNKRFIDI
IVNNNIDGNT GMFNNELVKD LINGRFTVGL PSVEKLHKSE IIAILTQVVL QLISIGRNTG
FLTDDINHLH DDDDHDDHNK IDLFNVSSIG GATKLNLWID SLSILKHKRS ANAILEELRE
LLSNRQLFYS MCSTNSLIKI CEKNTTTTTT NFTTKHNNNT DEGIYEEDDL ILDDFIQNDT
IELEYSNKIN KNDQILSKLL KSKGNLDNIS HHLDLGQFDF PDCMVSNNSM YCPLIIEMVL
YLSIY
//