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Database: UniProt
Entry: K0T1P3_THAOC
LinkDB: K0T1P3_THAOC
Original site: K0T1P3_THAOC 
ID   K0T1P3_THAOC            Unreviewed;      1388 AA.
AC   K0T1P3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Chromatin-remodeling complex ATPase chain {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=THAOC_05886 {ECO:0000313|EMBL:EJK72568.1};
OS   Thalassiosira oceanica (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK72568.1, ECO:0000313|Proteomes:UP000266841};
RN   [1] {ECO:0000313|EMBL:EJK72568.1, ECO:0000313|Proteomes:UP000266841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK72568.1,
RC   ECO:0000313|Proteomes:UP000266841};
RX   PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA   Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA   Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA   Rosenstiel P., Hippler M., Laroche J.;
RT   "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT   limitation.";
RL   Genome Biol. 13:R66-R66(2012).
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:EJK72568.1}.
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DR   EMBL; AGNL01005642; EJK72568.1; -; Genomic_DNA.
DR   EnsemblProtists; EJK72568; EJK72568; THAOC_05886.
DR   eggNOG; KOG0385; Eukaryota.
DR   Proteomes; UP000266841; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00084; HMG-box_SF; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 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; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09011; HMG_box_2; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 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.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266841}.
FT   DOMAIN          27..99
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DOMAIN          367..536
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          683..834
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DNA_BIND        27..99
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1338..1388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1245..1272
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        70..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1019..1033
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1072
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1351..1378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1388
FT                   /evidence="ECO:0000313|EMBL:EJK72568.1"
SQ   SEQUENCE   1388 AA;  157739 MW;  ECEACC6F6E9D5015 CRC64;
     MSSKKEDRSG WVAVGSDAHA DTGPPPIRPA RSAYHYFQKE NAKRIQAELT SSGKSSDVGA
     LGREVSSRWQ TLTPDERRPY EVSAAADRDR FAAESHRRDV EVSAAREARR RERETLILDD
     QGEGKRAKKE EKKRARKAEA ARSKKKTKKR GRGDDDDDSD YDESAGGGPS SDEASYSPSS
     SEASSASSVS SSDEEEERPR KKRVVKLSES ALKRRAEARA QKAEKEAYIE QRQSDVREEK
     AAQAKRRLEF LLKQSDIFSH FGNVKAEKAR LGLKSSEAMN TSGLEQRGSR VGTSDGSGGE
     DRGAGTPGIV RKPSSVSGAE VQEEVEAERD EVDEHEATRM ASTGEFARES VVGFLWLSFE
     LTLASMPCAY SAPARSILAD EMGLGKTMQS ISILVYMMEY KQDTGPHLII VPKSTLSNWM
     NELARWGPTL NVVKFHGNKE ERADIAENVL RPGQRDEERS WNVCVTTYEI VNLDRNVVNK
     FAWSYLVIDE AHRLKNEAST FSRVVRTLET RFRLNNRKCF YHTLSRPLPR TQTLLLVHEL
     WALLNFLVPD VFASSEQFDE WFNLDIADDN EKSQLISQLH KILRPFMLRR LKADVEKSLP
     PKVETILFTG MSAMQKKLYK DILMRDLDTL TGKGGSGSRT AVLNIVMQLR KCAGHPYLFP
     GVEDRTLDPL GEHLVENCGK LVLLDKLLVR LRERGHRVLV FTQMTRILDI MEDYMHMRGF
     KYCRIDGNTS YEDREARIDS YNKPDSEQFC FLLSTRAGGL GINLQTADVV ILYDSDWNPQ
     ADLQAQDRAH RIGQKREVQV FRLVTEDTIE QKVVERAQQK LKLDAMVVQQ GRLKEKDKLS
     REELLDAIRF GADKIFKSKD SSITDDDIDL ILDAGKKKTQ ELNDKLQEAK KGDMLDFKLD
     GGISAQTFEG VDYSKEEAKS HLFQEEIFGI LDMGKRERRN VAYNENQLYM QQVKATQQQK
     KATKKKEVRL PRAYRLPKME DCQMFDREAL NALQDVAEKA FRALPEEVQL AAGGYKVPKP
     DKSKQDSDDS QLGSDYRPND SSGKTDADDK KDTTEQQDAS SDKKKLELPP LLTEEQEAEK
     ARLLAEGFID WSRHHYTAFL KGSGRYGRTN YAKIANEVGK PASAVETYAK AFWDEEYGKK
     RLGENEYERA VKHIEKGEKK IDDIKGLQRG TRILISLFEN PWVELQFTHV NTKDKKFSPE
     EDRYLLCWAH KFGYGQWEAI KFAIRRSSNF RFDYFLKSLP PDALGRRCEQ LMRAAEKEID
     MMEKAVREEA EKEGRTLPEG EIKLPMFKEL QAKKRLDAEK KFLEERTALE DNLRNIDAQI
     EEIQRKLLET DGVQKIDSFF KPNSSAKPKS KATSEHGKTA KMKQQAGKKR KAGEEGGQEK
     EGGAPGPG
//
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