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Database: UniProt
Entry: A0A830CTW3_9LAMI
LinkDB: A0A830CTW3_9LAMI
Original site: A0A830CTW3_9LAMI 
ID   A0A830CTW3_9LAMI        Unreviewed;       567 AA.
AC   A0A830CTW3;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   28-JAN-2026, entry version 11.
DE   RecName: Full=Growth-regulating factor {ECO:0000256|RuleBase:RU367127};
GN   ORFNames=PHJA_002473900 {ECO:0000313|EMBL:GFQ03301.1};
OS   Phtheirospermum japonicum.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Orobanchaceae; Orobanchaceae incertae sedis;
OC   Phtheirospermum.
OX   NCBI_TaxID=374723 {ECO:0000313|EMBL:GFQ03301.1, ECO:0000313|Proteomes:UP000653305};
RN   [1] {ECO:0000313|EMBL:GFQ03301.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Okayama {ECO:0000313|EMBL:GFQ03301.1};
RA   Yoshida S.;
RT   "Ethylene signaling mediates host invasion by parasitic plants.";
RL   Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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:GFQ03301.1}.
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DR   EMBL; BMAC01000816; GFQ03301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A830CTW3; -.
DR   OrthoDB; 1927209at2759; -.
DR   Proteomes; UP000653305; 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:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0099402; P:plant organ development; IEA:UniProtKB-ARBA.
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:SF42; GROWTH-REGULATING FACTOR 2; 1.
DR   PANTHER; PTHR31602; 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|RuleBase:RU367127};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU01002}; Reference proteome {ECO:0000313|Proteomes:UP000653305};
KW   Transcription {ECO:0000256|RuleBase:RU367127};
KW   Transcription regulation {ECO:0000256|RuleBase:RU367127}.
FT   DOMAIN          153..188
FT                   /note="QLQ"
FT                   /evidence="ECO:0000259|PROSITE:PS51666"
FT   DOMAIN          218..262
FT                   /note="WRC"
FT                   /evidence="ECO:0000259|PROSITE:PS51667"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           223..233
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01002"
FT   MOTIF           251..258
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01002"
FT   COMPBIAS        42..55
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..328
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..548
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   567 AA;  61341 MW;  EFB1552CCF2B350B CRC64;
     MDFGVVSHKH NASCLGSNEP GEGKGHGSAN LKHRRSGLAA DNNNNNNNNN NNSNSWRLSK
     MPRPGEVDFS SKKASEHFSS PFGRSNLWPS PDDDDGQKML SFSSDEPHCG GGGGGSSRSI
     AFSICEDEQY LSKTGGGGPS GGIRGPFARL KGPFTPSQWM ELEHQALIYK HIMANVPVPS
     NLLVPLKRSL YSYGSPGPYA SNLLGWGPFH LGYSGSNDPE PGRCRRTDGK KWRCSRDAVP
     DQKYCERHIN RGRHRSRKPV EGHNTVGHAN LNANVSSSSS KVPPIPTNNN APSSSSSGPV
     NNASSNNNSL GAMQRQFSSF QQQQQPSSTN NLDSRSQGFQ GLSLVPPTIG LKTKDSPPFS
     VQKQHATFQE SSSSSPHSEF GIVSSDSLLN PSERIIPYMN TNTSDSFLQF NSKETRNHQH
     PVHHFIDDWT KADDHQSEEL KSDWTQLSMS IPTMAAPDSP AQPKPISSLR LLSHELDPFH
     MSLGVSRDII NEPMQKQPAW LPVTWGNPVG GPLGEVLSAQ LGSSPTGVLQ KSTFVSFSNS
     SSVSSPTSGD NNRKSDLLVS SAPIPSL
//
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