ID M1BZW0_SOLTU Unreviewed; 1217 AA.
AC M1BZW0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA binding protein {ECO:0008006|Google:ProtNLM};
GN Name=102581044 {ECO:0000313|EnsemblPlants:PGSC0003DMT400056776};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400056776, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400056776}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400056776};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_006344601.1; XM_006344539.2.
DR RefSeq; XP_006344602.1; XM_006344540.2.
DR AlphaFoldDB; M1BZW0; -.
DR STRING; 4113.M1BZW0; -.
DR PaxDb; 4113-PGSC0003DMT400056776; -.
DR EnsemblPlants; PGSC0003DMT400056776; PGSC0003DMT400056776; PGSC0003DMG400022079.
DR GeneID; 102581044; -.
DR Gramene; PGSC0003DMT400056776; PGSC0003DMT400056776; PGSC0003DMG400022079.
DR KEGG; sot:102581044; -.
DR eggNOG; ENOG502QTVY; Eukaryota.
DR InParanoid; M1BZW0; -.
DR OMA; PAENIQN; -.
DR OrthoDB; 625276at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1BZW0; baseline.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd04301; NAT_SF; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd20405; Tudor_Agenet_AtDUF_rpt1_3; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR014002; Agenet_dom_plant.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032308; TDBD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46309:SF12; GB|AAC80581.1; 1.
DR PANTHER; PTHR46309; PHD FINGER PROTEIN 12; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF05641; Agenet; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF16135; TDBD; 1.
DR SMART; SM00743; Agenet; 2.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 788..833
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 931..1093
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 624..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1217 AA; 138564 MW; 11ED31A5192FC2C3 CRC64;
MSMASKLQLH QNVEVRSIES GFLGSWHLAT IIAFDNFVPQ VQYHHLLSDD DASINLIESV
KLSPIRPFPP PLQFHTSLLS YGQCVDLFYQ DAWWEGVIFD HQNGALNRRV FFPDMGDEIN
AQLHNLRITQ DWDEVSQQWK PRGSWMFLQI IQEIENLHPL FVSLKQIWYQ IREKNGYQYL
KEWTSTSADS WRNLIKEVVH ENAMLTVKHI FCESNTSPDF LEGGPLLEFS QPTIQVETYF
DNSAIVPFIE AICKSISGEM LCMDRDVSCL QPIEKQLVSE GFGPISEDVP LSGSALFSSV
LPIQEEQQTV SPNASPVLHP PKNEISGTLS ITTSERLNFE SSNKIHSRKR KRVEWMTIAH
VAELCPDAVS EYNDNYMSNH RSPESLQKLK KHLFHLGWKI EQPKDCSITR TRYIAPDGKI
FQSLRQVCKM LEKSETWAEG QKTSYDGSSD DLNLSTCLAK TKTCSEVSEL PYTSQEPIID
PEICREAVIE YCSLGSPDNP AYKKLNSGEK KFMIMKAKKH LVAIGWIFYY YRGRDKRELR
YHSPHGKTFN TLLAACRWCM QQWKAEEQMP ELFSRSTVLE YQGNSAPQKT SCEKLSAATF
SVLPHAKEPA QLNKVTVCEI SKTRKKTNHA GGMLRKGNES RSSRTVTDGT ESQSSVGLLR
SSKKARQGTL SSSLHHTPRT VLSWLIDNNV VLPRAKVQYR GKRDGRPMAE GRITRAGIKC
KCCQKVYGIS SFEVHAGSSY HRPSANIFLE DGRSLLDCQL QMKEKASLRH TRKRPPLLKK
RSHLGTNDYV CSVCHYGGEL LLCDECPSSF HTGCLGMKEI PDGEWFCPSC CCETCGQSRF
DKNKDHFTDS SLLICSQCDH KYHARCVRNK GLQKLDYYPV GSWFCNKRCE QICLGIRQLL
AKPVMVGIDN LTWTLLKYVK PDDFDLDAAN DEFILETYSK LSVALDVMHE CFEPVKEPYT
RRDLMEDVIF NRWSELHRLN FQGFYTVLLE RNDEVISVAT VRVYGEKVAE VPLVATRFQY
RRLGMCRILM NELEKKLMEL GVERLVLPAV PTVLNTWTTS FGFSMVKESQ RLNFLNYTFL
DFQGTILCQK LLQNIPPEVS SESTEAYQTQ FDHINSKENV ELDGNSALSE VFQAEQIEES
EIVDQGSTDA PGGCESNNID APAPFIIVVN QQAPLGCQDE TSLPYRAEVT DSKVLEKTGV
VQYICYKRRK KISACGS
//
