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Database: UniProt
Entry: K0R9M3_THAOC
LinkDB: K0R9M3_THAOC
Original site: K0R9M3_THAOC 
ID   K0R9M3_THAOC            Unreviewed;      1829 AA.
AC   K0R9M3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=HMG box domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=THAOC_35763 {ECO:0000313|EMBL:EJK45616.1};
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:EJK45616.1, ECO:0000313|Proteomes:UP000266841};
RN   [1] {ECO:0000313|EMBL:EJK45616.1, ECO:0000313|Proteomes:UP000266841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK45616.1,
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   -!- SIMILARITY: Belongs to the SBNO family.
CC       {ECO:0000256|ARBA:ARBA00006992}.
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:EJK45616.1}.
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DR   EMBL; AGNL01048385; EJK45616.1; -; Genomic_DNA.
DR   EnsemblProtists; EJK45616; EJK45616; THAOC_35763.
DR   eggNOG; KOG0381; Eukaryota.
DR   eggNOG; KOG1513; Eukaryota.
DR   Proteomes; UP000266841; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
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   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR026937; SBNO_Helicase_C_dom.
DR   InterPro; IPR026741; SNO.
DR   InterPro; IPR039187; SNO_AAA.
DR   PANTHER; PTHR12706:SF30; PROTEIN STRAWBERRY NOTCH; 1.
DR   PANTHER; PTHR12706; STRAWBERRY NOTCH-RELATED; 1.
DR   Pfam; PF13872; AAA_34; 1.
DR   Pfam; PF13871; Helicase_C_4; 2.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266841}.
FT   DOMAIN          80..148
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DOMAIN          967..1137
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DNA_BIND        80..148
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1577..1616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1794..1829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..226
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..829
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..887
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1577..1604
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1814..1829
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1829 AA;  203588 MW;  9B3619658E1A8455 CRC64;
     MADLADLREG ENAPRSDFVV IDSFGEDENR DNRQNNPAAQ LQPLKAEAAG EKCRLEKTRN
     DRDVGPENLE PLSHAHPSAP KQYMSAFFLY SEAKRDSIKQ ANPSASPQEI AKLLSRDFKA
     MASEERAYWD KKAAEDKERY KREMENYDPT LTTATSSSDT GITSGASARK VSMSPPTYSQ
     HKRPKKKKRN KKENKVKTEE AQTEAASDAE KEAEGEGEDV EEADEITYEP YQPAKLKYGR
     PHPDPVVENA TLAAVAPPDV TYNLALPADI ISQGKLSGLQ LEAIVYGCQR HEMDLPVKKK
     EVWQVEQGVV DEVPLRAGFL LGDGAGMGKG RTLAGFVMEN ISRGRQKHVW ISVSADLYED
     AKRDLRDLGL DDYAADHCHN LGKLPYGKLS KKYRKGVMFL TYHQLIAKKS RGKETRLDQL
     LEWCGGEDFG GLIMAKTIEL DANGNPKTTG KGPKKKELSS KTAIAVLDLQ KRLPRARVVY
     CSATSVSHPK NLGLGLWGPG TQHPSGFKQF LGGLKSLGTG ASEFAFQTLR VSLCAVDDCQ
     PNLPFDCSGD SRNAFEVHRT LSYESCEFDL VDGIGSEDVT KVYNKASQLW GELHSQLGEQ
     TRQMEANARV EENMKKCLDK GIPVTQDMRY HMDLIRDSDS EPDEDSADEE ERKFRRKCRR
     RAPKQLQSLF WSAHQRFFRS LCIATKVPKA IELAKESLEN DKCVVIGLQS TGEARAKGAT
     KAAGFSNDQG ELDDFVSAPN EDLKRVIMMM FPLPPKPRGV NPPSFLNPNN RKTNDDDLSL
     TEDDEGTEAE PEEVQNRSRS RRGRARKTVD YSEMGIDDDG YEVNGKAAGR KRKQSKKTSK
     TSKKKEKRGS DDESDYADDE SSIDLSDPPS DDEAATKKGE PKGDAASDDD TFATAQDDED
     SSDAEDYQPK NGKSWESKRL NWDEIELNVK KSDLTVETER RIAYRRAAAT VHKYLQSVDG
     LDLPPNPLDE LLNKLGGPSM VAELTGRKIR QVQCINKETG QSFVRIEKRK GVKSFDKVNI
     EEKEAFQSGE KNVAILSEAA STGISLQADH RVQNQRRRVH ITLELPWSAD KAIQQLGRTH
     RANQSSGPEY KFLISDVGGE KRFAAAVAKR LALMGALTQG DRRSTGQSSS LGLGNFDMDN
     KFGNKALRDM LGEVWKMNAR SLSEIENRHA SGALEIIDKH LSVVLDDTPA GADWRTSLAP
     YDDDGETIHS YYSMMQSFLT SSRLIRFTEK RVEAIKNGKG LHQLMQSLED GDCSQEECLT
     QLNEQVEESK SLGLNFNAVA RLFLYDVGVT QESSCASKSR PPINVAKFLN RCLGLPLSRQ
     AMLTNHFLKW LEKEIKDAKR TGRYDIGIKT LSGNEVSIEK PRAFCFRGLD AKDDRVLLYS
     VNIDRGMTSD TALDLWDEVK NNGNDSGSRI KTGFYYDDRT IFKQCDRMFL IINQGRTSTS
     AIVARPNAGR GTFAVSADAC LIQTQGTSLA SLFAAVRLTP NFSSPVKNDY VLTHLLGGFA
     ALKRCNDLTI VKQKWDQEFE LADLPSDEMY QRSCYGRQFS TVAFGGEVVP VLSKLLAAAN
     PGGINNQDED RRTLPSIVRI EPEQHEKKKI TAAQSPRRSD DEDHDEADGE SPPAVGQNVA
     CKLLGSNILR GEVVECKDDT TYTAVFTNGS SVELNLEEVS KARQLFSNEL EKLMNVNVSK
     ADASNIGTKA SIAEKESAPR PLMADGDDIP DDCERAYEVE FQGDTPKLLV GLQFPKVKRI
     WYNSTTQLHE EVDMWEVAPD STSVKKEIWV VTPAHAKPPS PLLYLTKGQY LRKPRKNTNK
     TIHGAPRARQ IAPQPRDSIK RRLATLKED
//
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