ID K0TAM3_THAOC Unreviewed; 1585 AA.
AC K0TAM3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJK75763.1};
DE Flags: Fragment;
GN ORFNames=THAOC_02504 {ECO:0000313|EMBL:EJK75763.1};
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:EJK75763.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK75763.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK75763.1,
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:EJK75763.1}.
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DR EMBL; AGNL01002739; EJK75763.1; -; Genomic_DNA.
DR EnsemblProtists; EJK75763; EJK75763; THAOC_02504.
DR eggNOG; KOG0384; Eukaryota.
DR eggNOG; KOG1474; 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 CDD; cd04369; Bromodomain; 1.
DR CDD; cd00084; HMG-box_SF; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 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; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
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:SF11; KISMET, ISOFORM C; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000266841}.
FT DOMAIN 403..471
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 494..565
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 610..679
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 1269..1451
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DNA_BIND 403..471
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..957
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EJK75763.1"
SQ SEQUENCE 1585 AA; 179608 MW; C5EB566986D49D53 CRC64;
EVGSKANEEH VAHPNPTDNV AATQHEALES RTVGGRARVY GAGTVGGLID RQQTSSPTMS
QETLATGRSR RSRKAIDYSQ EQQFSDDDDV FDDVKVEKSK KSKSRRSNAN TGGYGLADAS
GVSTYKRDKP VYVERGYDLS SYAPIRERFT FEPEYDDDGT RLIETIVGRR PIEDTKDRVQ
ADGHGLNGAS DVDDSDEDGP TTRRNKKKPS KKSGEKEESK GINSDHDYEY LLKYKGRSYL
HLEWMGGADL ESMNTKSKGM YRRFLKKLDQ ESDEDLEDPT IDPSFTEPGR ILAEEDHEIM
VELTGKELAK WEKEQRQQME ELEESDSEEE ELEKPADDGA AKMETDGSPQ EEKKEDPEPI
EIPDPGKMDI ETLRRIVNRQ DPYYATYPGS NNAYRDGYIT EPPRKPRPSY LIFQGIYRGY
YDKQNPGLSL SKKMQILGDD WKSLSEEAQA PFIQIANEEL AQFEREKVLL EKAQRPKQVW
QPIRRCKAVL DRLKADPMAL IFLEPVDTTM FTDYLDIVDE PMDLNTLGEN LKKIKNYEGP
ETFARDARRI WNNCKIYNQH GSQIWYVADY MSKLFEKIYH AWVLDFRDKY IRWANLAARP
WDDPKLMAKL NKDKLLVSAR KKGEMGDIPK KMIKQKMFLV KWAGLGYDQC SWETRKDIND
DSIIAEFHRL EGVTPDEPDL TESQVQVVVE NSVSIMKGDI DSDLPMANMR AQLYAQSRAF
HFKKFGMSVP SLVGAECGPN EKALTNPAAA PTASTPEDIV ACVNELVWKI SQGERLSTGH
KSLPPCLLGE YDAAFPVTPH GLLLNVGEVK GMVAIMGYRN PPGGGRGPAE VSRLLRKTND
IIIAVNGQST LGKSFKEVVP MLKAKSGYCH MRLVHEGYQA NLGLTTSVGQ LGRFIEEDFS
RSMKEDRRRF LAKRSLALLN DQEEGSDSDE DAGSEAEASD SEDSEVSGME SDSEDEALTG
VETNNSMDEG ADVRHVAKKE ETRENMLAKL LSSPDAESIK VTKQQTTRHL AYSLLDMDIG
YSSDEGGDED VAYFMDGVDS TFTRSNEVTP PKEDTKDSSK DEKKEDTIVT LPVKKTDFGQ
IGKRAQLQVA VAITGREPDL EDFDNFPRPS TKQIAMAKAK AEEEARKAEE EARKLEELRK
KKAEEASKPK VKSKTKVEQI SPANNETVRV WINAADAAAT LNLSIEGIQN LLDGGYDAED
GDEFGGYRWR YADQDAEVTG KATSGRESKK GREAYLKFKD KLYDSKKPHL YKNGNKLRDY
QVDGVNWLSS CFYHQQGAIL ADEMGLGKTV QIVSYLEHLH RVEKISGPFL VVVPLSTIEH
WRREFDAWTD MQCCVYHDRM RQWRDVLREY EWYYEDRPHT PDYLKFNVLV TTYDTLISDF
DVIGDVPWRV TVVDEAHRLR NVKGKLLECM KETSAKGTMK YGYQSRVLMT GTPLQNNTQE
LWTLLNFIEP SLFRSLQDFE TNFGNMANRE QVDALQRKIS PFMLRRVKED VAKDIPAKEE
TVIDVELTSI QKQYYRAIFE QNHAFLSMGA SKAGAPSMMN IQMELRKCCN HPFLLDGIES
REMEKKARRP LCQGRVGRQV AGGAT
//
