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Database: UniProt
Entry: K3Z3I7_SETIT
LinkDB: K3Z3I7_SETIT
Original site: K3Z3I7_SETIT 
ID   K3Z3I7_SETIT            Unreviewed;       965 AA.
AC   K3Z3I7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0008006|Google:ProtNLM};
GN   Name=101767419 {ECO:0000313|EnsemblPlants:KQL14789};
GN   ORFNames=SETIT_3G183600v2 {ECO:0000313|EMBL:RCV17000.1};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL14789, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EMBL:RCV17000.1, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL14789,
RC   ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC   {ECO:0000313|EMBL:RCV17000.1};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EMBL:RCV17000.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV17000.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQL14789}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL14789};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AGNK02001606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM003530; RCV17000.1; -; Genomic_DNA.
DR   RefSeq; XP_004961548.1; XM_004961491.1.
DR   AlphaFoldDB; K3Z3I7; -.
DR   STRING; 4555.K3Z3I7; -.
DR   EnsemblPlants; KQL14789; KQL14789; SETIT_021105mg.
DR   GeneID; 101767419; -.
DR   Gramene; KQL14789; KQL14789; SETIT_021105mg.
DR   KEGG; sita:101767419; -.
DR   eggNOG; KOG4362; Eukaryota.
DR   HOGENOM; CLU_004218_0_0_1; -.
DR   InParanoid; K3Z3I7; -.
DR   OMA; PVCKVPY; -.
DR   OrthoDB; 318045at2759; -.
DR   Proteomes; UP000004995; Chromosome III.
DR   GO; GO:0070531; C:BRCA1-A complex; IBA:GO_Central.
DR   GO; GO:0031436; C:BRCA1-BARD1 complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0071480; P:cellular response to gamma radiation; IEA:EnsemblPlants.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd17734; BRCT_Bard1_rpt1; 1.
DR   CDD; cd15571; ePHD; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR031099; BRCA1-associated.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13763:SF0; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN; 1.
DR   PANTHER; PTHR13763; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN BRCA1; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF52113; BRCT domain; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          16..54
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          578..698
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          756..831
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          852..965
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          91..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   965 AA;  105919 MW;  AC526DD243A69355 CRC64;
     MADAGSLEKM GRELKCPICL SLLSSAVSIT CNHIFCNGCL MESMKSASSC PVCKVPFRRR
     EIRPAPHMDN LVSVFKSMEV AAGTSIVATP LAPSPKVADG SQCGGNSGSK PKSSRKKKVA
     SKKKNNTSKA AAASASCPTT KPSISMNKRI HVTLFPECET PTRPKKIMKP EEQKTKLNGD
     AEEDKNKTLN SDRPESPSLS PFFWLRGEEQ EEGGTAGSLS EPLSLDTPLR HNAPTFSDIM
     DSDDEIPNNV TPNSKAEVSE IFDSEIFEWS QRPCSPELRS TPLKKQGKLK KILDQITETD
     DVEDMNLGGS FDKLDHESNA AQLVNGAEIK KRKSARARTK KNSKLPDCGK LCTKGCDAVH
     QVTDIPVSIT TMPGQKNSGK KESNTSSGRS KVSCNSSRFL CSSDKSMETF PPQENSLEIE
     ASENQLSERS HKNDKDSRRK LERTGNSALK TAENKSEQTS KRIRRISHGA VADEIRVISV
     AENKTESPQH HTLIKGCTRH KHLDGRSKQS MESNIGPNTP SPLPGRCQFN EAIRTVPSVK
     NFLVKNGSVK SIEQSDYSET IRSARNAVLQ KCEEKAPMAS CAFCQSDDIT EESGKMVHYH
     NGKEVPAEFN GGTGVIHSHK NCLEWAPDVY FKDDSVFNLT TELARSRRIK CACCGIKGAA
     LGCFDMSCRK SFHFTCAKLI PECRWDDENF VMLCPLHQSS KLPIETSESK KKSQRRLTPK
     GSAQVRPCQV YGNKWTWPSG SPQKWVLCCS ALSPAEKGIV SEFAKIAGVP ISTSWNPSVT
     HVIASTDLSG ACKRTLKFLM AILNGKWVVS IDWVKTCMEH MEPVDEVRFE VTTDVHGTRE
     GPKLGRQRVI NKQPKLFASI HLYLHGDYTQ SYRGYLQDLV VAAGGTVLQR KPVSRDQQKL
     LDDSSLILIV YSVENQDKGN PKSKDGVDTG RSQADAQALA CASGGKVVSS AWIIDSISAC
     NLQPL
//
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