ID B8C4D6_THAPS Unreviewed; 1008 AA.
AC B8C4D6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=Chromatin-remodeling complex ATPase chain {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=THAPSDRAFT_35129 {ECO:0000313|EMBL:EED91309.1};
OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128 {ECO:0000313|EMBL:EED91309.1, ECO:0000313|Proteomes:UP000001449};
RN [1] {ECO:0000313|EMBL:EED91309.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED91309.1};
RX PubMed=15459382; DOI=10.1126/science.1101156;
RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA Wilkerson F.P., Rokhsar D.S.;
RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT metabolism.";
RL Science 306:79-86(2004).
RN [2] {ECO:0000313|EMBL:EED91309.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED91309.1};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
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DR EMBL; CM000643; EED91309.1; -; Genomic_DNA.
DR RefSeq; XP_002291202.1; XM_002291166.1.
DR AlphaFoldDB; B8C4D6; -.
DR STRING; 35128.B8C4D6; -.
DR PaxDb; 35128-Thaps35129; -.
DR EnsemblProtists; EED91309; EED91309; THAPSDRAFT_35129.
DR GeneID; 7442773; -.
DR KEGG; tps:THAPSDRAFT_35129; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_0_1; -.
DR InParanoid; B8C4D6; -.
DR OMA; EFQFRES; -.
DR Proteomes; UP000001449; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001449}.
FT DOMAIN 153..324
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 457..608
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 978..1005
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 80..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EED91309.1"
FT NON_TER 1008
FT /evidence="ECO:0000313|EMBL:EED91309.1"
SQ SEQUENCE 1008 AA; 116044 MW; DCBCA98F3D243D2F CRC64;
KRREQAKQEK LQKEQYIEQR QSDVRSERAE QAKRRLEFLL KQSDIFSHFG NVKQEKARLG
LSSSVAAATS VVGKDGGPDD TTSGSVSESG QTNHEGGIVR KPSNVGESDE EEVQDEEREE
ADEHEATYLT MQPSTLGGGK MRQYQLEGLN WMIRLQENGV NGILADEMGL GKTMQSISIL
VYMLEYKQDT GPHLIIVPKS TLSNWMNELA RWGPKLNAVK FHGTKDERLD IAENILQPGQ
KDEKRKWNVC VTTYEVCNLE RNVFNKFAWS YLIIDEAHRL KNEASTFSKI VRTLETRFRL
LLTGTPLQNN LHELWALLNF LVPDVFASAD QFDEWFNLDI DDADEKNKLI SQLHKILRPF
MLRRLKADVE KSLPPKTEMI LFTGMSAMQK KLYKDILMRD VDTLTGKGGS GSRTAVLNIV
MQLRKCAGHP YLFPGIEDRS LPPLGEHLVE NSGKMVLLDK LLIRLKERGH RVLLFTQMTR
ILDILEDYMH MRGFQYCRID GNTTYEDREE RIDEYNKPDS EKFLFLLSTR AGGLGINLQT
ADVVILFDSD WNPQADLQAQ DRAHRIGQKR TVQVFRIVTE DTIEQKVVER AQQKLKLDAM
VVQQGRLKDK DKLSREELLD AVRFGADKIF KSKDSSITDD DIDIILGYGA KKTQELNDKL
QAAQKGDMLD FKLDGGLSAQ TFEGIDYSEE AKNAQFQAEI LGIMDVGKRE RRTVAYNENQ
LYMQQMAQQG ANPPKKKVKK EIKLPKMFRL PRMEEWQMFD RDSLNALQEV EEQAFRALPE
DIQETKEGEA EEKVEPESKE MPPLLSDEQK VEKARLLAEG FADWSRHHYS SFVKASAKYG
RTNYAKIAID VGKPVSAVKT YAEAFWNEEF GKKRFSEHEH DRVVKLIEKG EKRIEDVKGL
QRGTKILISL FENPWVELQF THVNCKDKKF TADEDRFLLC WAHKYGYGQW EAIKFAIRRS
SNFRFDYFLK SLPPDAIGRR CEQLMRAAEK EVDIMEKQVI DEAEKEGK
//