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Conserved domains on  [gi|1002239183|ref|XP_015623826|]
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uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

FCS-Like zinc finger protein( domain architecture ID 10518910)

FCS-Like zinc finger protein (FLZ) may act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-FLZ pfam04570
zinc-finger of the FCS-type, C2-C2; zf-FLZ is a FCS-like zinc-finger domain found in higher ...
64-110 1.99e-19

zinc-finger of the FCS-type, C2-C2; zf-FLZ is a FCS-like zinc-finger domain found in higher plants. It is bryophitic in origin. It carries a zf-FCS-like C2-C2 zinc finger, consisting of a consensus cysteine-signature sequence with conserved phenyl alanine and serine residue associated with a third cysteine. It acts as a protein-protein interaction module.


:

Pssm-ID: 428015  Cd Length: 53  Bit Score: 76.09  E-value: 1.99e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002239183  64 DAEVEEAHHFLDECTLCRKGLAG--DIFMYRGDTPFCSEECRREQIEMD 110
Cdd:pfam04570   3 DSAPVPTAHFLSACYLCKKKLGPgkDIYMYRGDKAFCSEECRQQQMLMD 51
 
Name Accession Description Interval E-value
zf-FLZ pfam04570
zinc-finger of the FCS-type, C2-C2; zf-FLZ is a FCS-like zinc-finger domain found in higher ...
64-110 1.99e-19

zinc-finger of the FCS-type, C2-C2; zf-FLZ is a FCS-like zinc-finger domain found in higher plants. It is bryophitic in origin. It carries a zf-FCS-like C2-C2 zinc finger, consisting of a consensus cysteine-signature sequence with conserved phenyl alanine and serine residue associated with a third cysteine. It acts as a protein-protein interaction module.


Pssm-ID: 428015  Cd Length: 53  Bit Score: 76.09  E-value: 1.99e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002239183  64 DAEVEEAHHFLDECTLCRKGLAG--DIFMYRGDTPFCSEECRREQIEMD 110
Cdd:pfam04570   3 DSAPVPTAHFLSACYLCKKKLGPgkDIYMYRGDKAFCSEECRQQQMLMD 51
LIM3_FHL cd09346
The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of ...
77-98 3.52e-03

The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 int eracts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188732  Cd Length: 52  Bit Score: 33.84  E-value: 3.52e-03
                          10        20
                  ....*....|....*....|..
gi 1002239183  77 CTLCRKGLAGDIFMYRGDTPFC 98
Cdd:cd09346    27 CTGCKKQLAGQRFTSRDEYPYC 48
 
Name Accession Description Interval E-value
zf-FLZ pfam04570
zinc-finger of the FCS-type, C2-C2; zf-FLZ is a FCS-like zinc-finger domain found in higher ...
64-110 1.99e-19

zinc-finger of the FCS-type, C2-C2; zf-FLZ is a FCS-like zinc-finger domain found in higher plants. It is bryophitic in origin. It carries a zf-FCS-like C2-C2 zinc finger, consisting of a consensus cysteine-signature sequence with conserved phenyl alanine and serine residue associated with a third cysteine. It acts as a protein-protein interaction module.


Pssm-ID: 428015  Cd Length: 53  Bit Score: 76.09  E-value: 1.99e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002239183  64 DAEVEEAHHFLDECTLCRKGLAG--DIFMYRGDTPFCSEECRREQIEMD 110
Cdd:pfam04570   3 DSAPVPTAHFLSACYLCKKKLGPgkDIYMYRGDKAFCSEECRQQQMLMD 51
LIM3_FHL cd09346
The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of ...
77-98 3.52e-03

The third LIM domain of Four and a half LIM domains protein (FHL); The third LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 int eracts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188732  Cd Length: 52  Bit Score: 33.84  E-value: 3.52e-03
                          10        20
                  ....*....|....*....|..
gi 1002239183  77 CTLCRKGLAGDIFMYRGDTPFC 98
Cdd:cd09346    27 CTGCKKQLAGQRFTSRDEYPYC 48
 
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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