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Database: UniProt
Entry: A0A183LGE7_9TREM
LinkDB: A0A183LGE7_9TREM
Original site: A0A183LGE7_9TREM 
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
//
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