ID A0A0B0NQU2_GOSAR Unreviewed; 463 AA.
AC A0A0B0NQU2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=Growth-regulating factor {ECO:0000256|RuleBase:RU367127};
GN ORFNames=F383_20386 {ECO:0000313|EMBL:KHG13446.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG13446.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) 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}.
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DR EMBL; KN399615; KHG13446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0NQU2; -.
DR Proteomes; UP000032142; 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:UniProt.
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:SF3; GROWTH-REGULATING FACTOR 8; 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:UP000032142};
KW Transcription {ECO:0000256|RuleBase:RU367127};
KW Transcription regulation {ECO:0000256|RuleBase:RU367127}.
FT DOMAIN 150..185
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 206..250
FT /note="WRC"
FT /evidence="ECO:0000259|PROSITE:PS51667"
FT REGION 231..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 211..221
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01002"
FT MOTIF 239..246
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01002"
FT COMPBIAS 250..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 50535 MW; C9CAA3080204ADBA CRC64;
MDTRNNAFVG TEKGLGRTDE ECDVGLGLMM MQQVEESCPN KSFMAMLPSH NHNHLSSSSS
SSSSSSCYVE GFDGGASGGG PLVCNTSNQE PCRGDIYDVV GAASASASVS SAAAAVVLKS
LHHHSFSADP PFPHHFSGEM AAAPANARVP FTAAQWQELE RQTMIYKYMM ASVPVPAELL
IPLTKNPSNV AIKGSLELGF ASNSSDPEPW RCRRTDGKKW RCSRDVAPDQ KYCERHSHKS
RPRSRKPVEL PNHSNININN NDHKSQTLHN MASDGTTNQP HQNPHFTNHH DPHFFTSSFD
QSRCLEWFMK GETTVPFASN PEWQRTNYGV NLQAQHHLNE QFTPSLASLE GSLNLNQTHS
QETRAFIDAW SIAEREVVEM EGIGSCKRPV SSNEKLPLSS LTLSMSGGGN ENNQEEDDEN
SHHEMRGTLS WMGSSPGGPL AEALCLGIAT SQTTSTSSCS KST
//
