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Database: UniProt
Entry: A0A267EPK4_9PLAT
LinkDB: A0A267EPK4_9PLAT
Original site: A0A267EPK4_9PLAT 
ID   A0A267EPK4_9PLAT        Unreviewed;      1673 AA.
AC   A0A267EPK4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=RNA helicase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BOX15_Mlig016460g1 {ECO:0000313|EMBL:PAA62682.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA62682.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA62682.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA62682.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA62682.1};
RA   Berezikov E.;
RT   "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT   model organism for stem cell research.";
RL   Submitted (JUN-2017) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAA62682.1}.
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DR   EMBL; NIVC01001911; PAA62682.1; -; Genomic_DNA.
DR   STRING; 282301.A0A267EPK4; -.
DR   Proteomes; UP000215902; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 4.10.1000.40; -; 3.
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   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF234; ATP-DEPENDENT RNA HELICASE DHX40-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00356; ZnF_C3H1; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT   DOMAIN          250..277
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          305..332
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          621..782
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          808..978
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   ZN_FING         250..277
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         305..332
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1673 AA;  187636 MW;  DC308BA7C8E4A043 CRC64;
     MQRPRGAASG VRRQATSSPQ ELFSVQITGL PPGVSSQSLV DRFQQSAGQF VIPPEPKQRD
     KTAWCAYLNG LTENQAETFQ ERWNNKIFPG GQHSIRCKTS SSKLKGSENI QGKATQPQPM
     IYNVELSGLP PNASNKFLAA TFKQSAEKFE VLPEPKQRDK TAWCAYLNDV PESEAHRFIQ
     KYDNFKIGNN KFVVRCKLIF KADRRTTEDR SRVRSRVHGD SLRQQTEKLG AEASSSQSSV
     STTHSETTNQ DKGILCKYNI LGTCKFDNDC KHIHMSCPME EDCDDDECCL GHPANVKTQI
     GRSVGRRLVL CNLFRFGACR YESECRFKHL DCPLAELCED SCCFFGHPQG WGSDFSDPNE
     CSVDCDQYDC TKSHPVGRTK RCQFGDKCTK FECSFLHSEK RQACESAGDC QDFDCSKLHP
     ESREEPCVKG AKCLEFHCQK LHPASRELCD KGKLCTEYAC DKLHEAGRRK KCKWRDRCKL
     PFCPWLHPIN RSKQFCDRGD SCDDFDCALV HPPGRCSPCK YGERCWNHIC ECLHPEAWNP
     CPNGLGCRDV TCDCSHSPRR PKPCTQGSDC RNRDCAGLHP GMSSVSNAPL QRSSALKSDH
     QRRIDREANR LPVLNYREQF LERLQTEKVL IVRAETGSGK TTQLPQYAAE CFGGLVICTQ
     PRVMAAVSIA HRVAQEFDGC DVGESVGYKV GGENSAPGSG IMFMTESCLI RYCQSNESLD
     NVSVLIVDEA HERSLNVDIV LGLAKLIRIK RPDNFYVVIA SATIDPQLFR DFFNCGVLDI
     PGRMYDVSLQ YIPPAFDSNP DVFIKSHLVP SLIKALRDHS DGYALVFLPG EREIQQAIKA
     FQQQQTEDNC VALPLYGSLP REEQVKVLDF KPSQDSDRLV VFCTNVAETS LTINGVRLVV
     DSGLAKESRF DAKRRITVLE LRQISQSAAN QRKGRAGRTA PGHCVRLYSE DVLKSAEFVP
     EILRSSLDLV VLLLIKLKLK PLEFSFLDKP NEEMLIHSYQ TLMDLGCLSG VESLSNAGEL
     FAELGLDPRL SAFIVRAHEH FGQLELAVTV ACILTAPGSI FFLGRDKEKK EGLQKRALEA
     FSHESDILYE VSVFDSWSNA GKLINGKCKN CGKVARNFQN SCRSCRVGHS NSNRLNNKVM
     EHIEKTRTSF LKTIKKSKWF LELQKVESSC EDTIQVVGSC LEQVIPEQVT CLLVKRLPSE
     GIKIVDSNIR ARISNTSVFA QRPQDCEYFV AVRVRQMVSG MYIVDGLHPL KDPTTVSDRR
     SHPLEKIFTE ANASSNLLKA VNSKIKDESS QISEEQRRWI VLSHNADEAS IDVYARASES
     SELRSKLKSL IDKSKLTYLQ EQHMLETKGF RATFQGGLQV KEVHICTLNR TDSEVSSSNN
     EGATDSAESD NGLAQLLVSA PCGFEEETIR AHSDSTAKIH HTNQRRRRQE KFKVFISNMP
     ANWKESDVQD LIRKSECLNA VVPIRIFPPA QPGIGTSRAL LTLNSETERD SLIKSLSTVL
     CNIGPFPISL ISKKNGGTFV KQVSPEIKPC EDKTPSIPEL FFVKFNESKH AVEFYNKIRA
     GSIVGCSAEW TESVFISHPD LFPDLNSLIE QSGDPTVKST SVPKPDKTLE IRLSGPQQDK
     IKLVANKLRS LFSPITIRHV SNKEKTLFYE IKKTGLFDAW AKELNLVCEF RDD
//
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