ID D7FKF5_ECTSI Unreviewed; 917 AA.
AC D7FKF5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=Esi_0144_0010 {ECO:0000313|EMBL:CBJ29357.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ29357.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ29357.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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DR EMBL; FN648026; CBJ29357.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FKF5; -.
DR STRING; 2880.D7FKF5; -.
DR EnsemblProtists; CBJ29357; CBJ29357; Esi_0144_0010.
DR eggNOG; KOG0922; Eukaryota.
DR InParanoid; D7FKF5; -.
DR OrthoDB; 51171at2759; -.
DR Proteomes; UP000002630; Chromosome LG26.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd17917; DEXHc_RHA-like; 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; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT DOMAIN 136..335
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 362..554
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..96
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 100609 MW; 3FE7D945C761169F CRC64;
MGNDDRHRRS SDRERARGEH VDSRSGHPSG SSRHGDRDDR RGASDRRSGR KASKRSRSRS
RSSSSDHQRR RRERGHSRSR SRERSHERSR RKSRWGNHER RQQDAPESED KGDKIAEEEE
DAAEPLPVTL FKDELMKAVR GSQVLVCTGE TGSGKTTQIP QYLLELVRER DADTTASGGK
DKDKDEGVAL DTPAPGDGKR PSHNNKKLLV AVTQPRRVAA TSVAKRVADE RGCRLGEEVG
YSIRFEDRTG PRTRIKYMTD GVLVRECLED PYLSRYGVVM LDEAHERSID TDILFGLLKR
ALARRPDLRA VITSATLDVE RFAAFFDGCP FINVPGRTHA VDVYHSKTRQ VMTATGPASP
RYVEDAVDII RKVHRTQGPG HVLAFFTGQD EIERASRLLS EAVAQEKIDR RAMGIEEEAD
NGVSEMIVVP LFGALSAEAQ ADAFKSARAG VRKVVMATNI AETSVTVPGV RFVVDPGYVK
QKTYDPARRM ESLVVVPISQ VAAQQRAGRA GRTAPGQCYR LYTRNCYGGM LGETVPEILR
TNLANTVLYL KVLGVDDILA FDFLDPPAED QSLEALQHLY CLGALDQDGR ATDTGRRMSR
FPLEPSLSRT LLEAGELGCL EEVLTIVALL SVESIWFTRS KGGGGGGGGA GSGARGKRGE
RDEEAEASHA LFRHPLGDHF TYLAVYRAWE ASGFSDAWAK EEFLRVRALR TARSVRSQLL
GEVRKASGGG RRRGRQEGGL EVTSCGRDLD KVRKAVCAGY FTKAGQRCSK EWVYRSLAVG
ALQQEGDDGA GRSGLTLMYL HPTSSLVHAQ EPPEHVVYTE LVFTARPFMR HAMAVKGRWL
RSRLEAVRPC SSDRLCGRAL AAAPGAGGGK EEEEAAAAAA AAAGAAGRTA EASSLAKKND
AIEAARARFL ARKRTKG
//
