ID A0A0E0A483_9ORYZ Unreviewed; 369 AA.
AC A0A0E0A483;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Growth-regulating factor {ECO:0000256|RuleBase:RU367127};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G01060.3};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G01060.3}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM06G01060.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Transcription activator. {ECO:0000256|RuleBase:RU367127}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU01002, ECO:0000256|RuleBase:RU367127}.
CC -!- DOMAIN: The QLQ domain and WRC domain may be involved in protein-
CC protein interaction and DNA-binding, respectively.
CC {ECO:0000256|RuleBase:RU367127}.
CC -!- SIMILARITY: Belongs to the GRF family. {ECO:0000256|ARBA:ARBA00008122,
CC ECO:0000256|RuleBase:RU367127}.
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DR AlphaFoldDB; A0A0E0A483; -.
DR STRING; 40148.A0A0E0A483; -.
DR EnsemblPlants; OGLUM06G01060.3; OGLUM06G01060.3; OGLUM06G01060.
DR Gramene; OGLUM06G01060.3; OGLUM06G01060.3; OGLUM06G01060.
DR eggNOG; ENOG502QSFK; Eukaryota.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032502; P:developmental process; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR031137; GRF.
DR InterPro; IPR014977; WRC_dom.
DR PANTHER; PTHR31602; GROWTH-REGULATING FACTOR 5; 1.
DR PANTHER; PTHR31602:SF107; GROWTH-REGULATING FACTOR 5; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF08879; WRC; 1.
DR SMART; SM00951; QLQ; 1.
DR PROSITE; PS51666; QLQ; 1.
DR PROSITE; PS51667; WRC; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU367127};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU01002}; Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transcription {ECO:0000256|RuleBase:RU367127};
KW Transcription regulation {ECO:0000256|RuleBase:RU367127}.
FT DOMAIN 24..59
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 97..141
FT /note="WRC"
FT /evidence="ECO:0000259|PROSITE:PS51667"
FT REGION 125..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 102..112
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01002"
FT MOTIF 130..137
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01002"
FT COMPBIAS 144..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 39956 MW; D8193DEB99508463 CRC64;
MLSSSPSAAA PGIGGYQPQR GAAVFTAAQW AELEQQALIY KYLVAGVPVP GDLLLPIRPH
SSAAATYSFA NPAAAPFYHH HHHPSLSYYA YYGKKLDPEP WRCRRTDGKK WRCSKEAHPD
SKYCERHMHR GRNRSRKPVE SKTAAPAPQS QPQLSNVTTA THDTDAPLPS LTVGAKAHGL
SLGGAGSSQF HVDAPSYGSK YSLGAKADVG ELSFFSGASG NTRGFTIDSP TDSSWHSLPS
SVPPYPMSKP RDSGLLPGAY SYSHLEPSQE LGQVTIASLS QEQERRSFGG GAGGMLGNVK
HENQPLRPFF DEWPGRRDSW SEMDEERPPS RQPSSRSPSR CPDVGPLSVI ENFAACGSGV
DLYPAFYRC
//