ID D7FX84_ECTSI Unreviewed; 1332 AA.
AC D7FX84;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBJ49262.1};
GN ORFNames=Esi_0320_0007 {ECO:0000313|EMBL:CBJ49262.1};
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:CBJ49262.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ49262.1, 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; FN648510; CBJ49262.1; -; Genomic_DNA.
DR STRING; 2880.D7FX84; -.
DR EnsemblProtists; CBJ49262; CBJ49262; Esi_0320_0007.
DR eggNOG; KOG0387; Eukaryota.
DR InParanoid; D7FX84; -.
DR OrthoDB; 5399336at2759; -.
DR Proteomes; UP000002630; Chromosome LG27.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18005; DEXHc_ERCC6L2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT DOMAIN 475..657
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 879..1036
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1332 AA; 140138 MW; B5BCB04C21E16495 CRC64;
MSSGGGRGPR PPTFGRRTEP GEPSEDQEDN PFVRQLELML QKSASNRAAA VSPPPPRARA
AAYAASTSAW RPRTSLSSDG GGAASGRMVA TGGASQYGGQ SLVANCKPEE KAVTSNGGGG
LPRASSRSLF SLPESSSDED EEAFQRRYFG LPPLRKPSAA AAAASVPPPA AALAEAKVAR
PGSDGGWPET KRCSPPNLKA SLISNGRGAA CRKTEGGSGD SRGDDSANGS KGNGKGKGQS
ARDGDAASSG RAGLGITGDR WYGGAGITRP QPTAQRRTGD GIGSAGAAAA GSDNEWMSDA
EDPRGATPNA IDSPTRRAGG LNDEEESSKP GAGGRRKGSR GGEGGGRKEL QLLSNPATAA
GSTAVGRGRK RGHEDFLNEK IEAMRVGSDE EGPHAGGGGG RGGGRGRSRG GAVTMGPDEE
EEEEEVDYED LKPHIEDPPW LGKLVPFDLG EGGFINPSIN RYLRDYQREG VRWLYAKFQA
GQGGILGDDM GLGKTVQSIA LLASVLRKSG TGRDSEELRR RRKEGLPASS TGLPWLIVAP
AAVVPEWIKQ IKVWGHFAAY QLESGRDADD LMVALKAGRY EVVATSYDLL RACVDRLKKQ
RFDAVIFDEY HTIKSATTMV SQAACELRTK RVFGLTGTLI QNDMKELWFL LHLIDPLAVG
EQSRFTEHFS EPIKRARAMN ATASDRRLGE KRLKELDGIR DKNMIRRTKD EELGDVLKGK
SDTVVFCDLS EVQRELYQRV LSLPEFQLLA RAKEPCNCGR SGRPTRARCC HKTPDSRGGG
GDGVDPRAVL FRRLHPTLME CDKCPFCCQL PAVSKLQKIA NHPCLLQENI RDPEHKRQQQ
RQFAEVAFTD RAREIMGGLE RSQKFLDVSK VGVCGKMKSL ETLLAKFHET RDKVLVFSWS
TAMLDVLESF VGAKGYVYRR LDGTTSSKER QARINEFNSD RAGVFVFLIS TRAGGQGLNL
HTASRVVLYD VNWNPALGLQ AQDRAYRIGQ KRKVAVFRLI SKGTIEEMCY MRQIYKLQIT
SAAMGDQARG GRRQFNAVQG SKEQQGELFG IQNLLKFSDD SLLKTLRMKH EAGLAAATAT
GGGAAAAAAA AAGGAGSKGV GGIAGVDAAD EEDLVVAMKN ALGLSKEGGA KGEGEGPPED
NELAGLLGDL GVDAYTHDQL VAKDEGEEEL AEESCGVAEL TLSPLPSGGA RNAMEEKIAM
PRSGGGGGGG GGGGGGGGGG GVLVPSAGRE RMSAASATGG VVGRGQGLGP KGPSVSGGSG
KAPATAAAVV EIEDGTGGPP GGGQPQQQEP AKKRRNLASL GWGKGRAGGG GGSGARVELF
MPQYGSGGGG RK
//
