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Conserved domains on  [gi|356537057|ref|XP_003537047|]
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growth-regulating factor 3 isoform X1 [Glycine max]

Protein Classification

growth-regulating factor family protein( domain architecture ID 10556208)

growth-regulating factor (GRF) family protein such as Arabidopsis thaliana GRF6, which is a transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledon tissues

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WRC pfam08879
WRC; The WRC domain, named after the conserved Trp-Arg-Cys motif, contains two distinctive ...
 137-178 1.34e-23

WRC; The WRC domain, named after the conserved Trp-Arg-Cys motif, contains two distinctive features: a putative nuclear localization signal and a zinc-finger motif (C3H). It is suggested that the WRC domain functions in DNA binding.


:

Pssm-ID: 462621  Cd Length: 42  Bit Score: 91.17  E-value: 1.34e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 356537057  137 PEPGRCRRTDGKKWRCSKDTVAGQKYCDRHMHRGRNRSRKPV 178
Cdd:pfam08879   1 PEPGRCRRTDGKKWRCSRRVLPGQKLCERHMHRGRKRSNKSK 42
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 78-111 8.06e-13

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


:

Pssm-ID: 462622  Cd Length: 35  Bit Score: 61.58  E-value: 8.06e-13
                          10        20        30
                  ....*....|....*....|....*....|....
gi 356537057   78 FSFAQWQELELQALIFRYMLAGAPVPPELLLPIK 111
Cdd:pfam08880   2 FTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
 
Name Accession Description Interval E-value
WRC pfam08879
WRC; The WRC domain, named after the conserved Trp-Arg-Cys motif, contains two distinctive ...
 137-178 1.34e-23

WRC; The WRC domain, named after the conserved Trp-Arg-Cys motif, contains two distinctive features: a putative nuclear localization signal and a zinc-finger motif (C3H). It is suggested that the WRC domain functions in DNA binding.


Pssm-ID: 462621  Cd Length: 42  Bit Score: 91.17  E-value: 1.34e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 356537057  137 PEPGRCRRTDGKKWRCSKDTVAGQKYCDRHMHRGRNRSRKPV 178
Cdd:pfam08879   1 PEPGRCRRTDGKKWRCSRRVLPGQKLCERHMHRGRKRSNKSK 42
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 78-111 8.06e-13

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


Pssm-ID: 462622  Cd Length: 35  Bit Score: 61.58  E-value: 8.06e-13
                          10        20        30
                  ....*....|....*....|....*....|....
gi 356537057   78 FSFAQWQELELQALIFRYMLAGAPVPPELLLPIK 111
Cdd:pfam08880   2 FTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
 78-110 3.11e-08

QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.


Pssm-ID: 214931  Cd Length: 36  Bit Score: 49.07  E-value: 3.11e-08
                           10        20        30
                   ....*....|....*....|....*....|....
gi 356537057    78 FSFAQWQELELQALIFRYMLAG-APVPPELLLPI 110
Cdd:smart00951   3 FTPAQLELLRAQILAYKYLLARnQPVPPELLQAI 36
 
Name Accession Description Interval E-value
WRC pfam08879
WRC; The WRC domain, named after the conserved Trp-Arg-Cys motif, contains two distinctive ...
 137-178 1.34e-23

WRC; The WRC domain, named after the conserved Trp-Arg-Cys motif, contains two distinctive features: a putative nuclear localization signal and a zinc-finger motif (C3H). It is suggested that the WRC domain functions in DNA binding.


Pssm-ID: 462621  Cd Length: 42  Bit Score: 91.17  E-value: 1.34e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 356537057  137 PEPGRCRRTDGKKWRCSKDTVAGQKYCDRHMHRGRNRSRKPV 178
Cdd:pfam08879   1 PEPGRCRRTDGKKWRCSRRVLPGQKLCERHMHRGRKRSNKSK 42
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 78-111 8.06e-13

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


Pssm-ID: 462622  Cd Length: 35  Bit Score: 61.58  E-value: 8.06e-13
                          10        20        30
                  ....*....|....*....|....*....|....
gi 356537057   78 FSFAQWQELELQALIFRYMLAGAPVPPELLLPIK 111
Cdd:pfam08880   2 FTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
 78-110 3.11e-08

QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.


Pssm-ID: 214931  Cd Length: 36  Bit Score: 49.07  E-value: 3.11e-08
                           10        20        30
                   ....*....|....*....|....*....|....
gi 356537057    78 FSFAQWQELELQALIFRYMLAG-APVPPELLLPI 110
Cdd:smart00951   3 FTPAQLELLRAQILAYKYLLARnQPVPPELLQAI 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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