DA1-related protein 6 [Arabidopsis thaliana]
Protein Classification
LIM_DA1 and DA1-like domain-containing protein( domain architecture ID 10175213)
LIM_DA1 and DA1-like domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| DA1-like | pfam12315 | Protein DA1; Proteins in this family include protein DA1 and its homologs. In Arabidopsis ... |
419-633 | 1.61e-127 | ||||
Protein DA1; Proteins in this family include protein DA1 and its homologs. In Arabidopsis thaliana, DA1 is an ubiquitin receptor that limits final seed and organ size by restricting the period of cell proliferation. It may act maternally to control seed mass. : Pssm-ID: 463530 Cd Length: 214 Bit Score: 374.36 E-value: 1.61e-127
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| LIM_DA1 | cd09396 | The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ... |
277-332 | 7.30e-20 | ||||
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain of unknown function. DA1 is predicted as an ubiquitin receptor, which sets final seed and organ size by restricting the period of cell proliferation. The LIM domain is 50-60 amino acids in size and shares 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. : Pssm-ID: 188782 [Multi-domain] Cd Length: 53 Bit Score: 83.07 E-value: 7.30e-20
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| Smc super family | cl34174 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-211 | 1.19e-03 | ||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; The actual alignment was detected with superfamily member COG1196: Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.19e-03
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| Name | Accession | Description | Interval | E-value | |||||
| DA1-like | pfam12315 | Protein DA1; Proteins in this family include protein DA1 and its homologs. In Arabidopsis ... |
419-633 | 1.61e-127 | |||||
Protein DA1; Proteins in this family include protein DA1 and its homologs. In Arabidopsis thaliana, DA1 is an ubiquitin receptor that limits final seed and organ size by restricting the period of cell proliferation. It may act maternally to control seed mass. Pssm-ID: 463530 Cd Length: 214 Bit Score: 374.36 E-value: 1.61e-127
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| LIM_DA1 | cd09396 | The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ... |
277-332 | 7.30e-20 | |||||
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain of unknown function. DA1 is predicted as an ubiquitin receptor, which sets final seed and organ size by restricting the period of cell proliferation. The LIM domain is 50-60 amino acids in size and shares 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. Pssm-ID: 188782 [Multi-domain] Cd Length: 53 Bit Score: 83.07 E-value: 7.30e-20
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| LIM | pfam00412 | LIM domain; This family represents two copies of the LIM structural domain. |
277-312 | 5.60e-05 | |||||
LIM domain; This family represents two copies of the LIM structural domain. Pssm-ID: 395333 [Multi-domain] Cd Length: 57 Bit Score: 41.16 E-value: 5.60e-05
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-211 | 1.19e-03 | |||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.19e-03
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| LIM | smart00132 | Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ... |
277-312 | 1.34e-03 | |||||
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways. Pssm-ID: 214528 [Multi-domain] Cd Length: 54 Bit Score: 36.98 E-value: 1.34e-03
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| PTZ00121 | PTZ00121 | MAEBL; Provisional |
13-262 | 2.25e-03 | |||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.25e-03
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| Name | Accession | Description | Interval | E-value | |||||
| DA1-like | pfam12315 | Protein DA1; Proteins in this family include protein DA1 and its homologs. In Arabidopsis ... |
419-633 | 1.61e-127 | |||||
Protein DA1; Proteins in this family include protein DA1 and its homologs. In Arabidopsis thaliana, DA1 is an ubiquitin receptor that limits final seed and organ size by restricting the period of cell proliferation. It may act maternally to control seed mass. Pssm-ID: 463530 Cd Length: 214 Bit Score: 374.36 E-value: 1.61e-127
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| LIM_DA1 | cd09396 | The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain ... |
277-332 | 7.30e-20 | |||||
The Lim domain of DA1; The Lim domain of DA1: DA1 contains one copy of LIM domain and a domain of unknown function. DA1 is predicted as an ubiquitin receptor, which sets final seed and organ size by restricting the period of cell proliferation. The LIM domain is 50-60 amino acids in size and shares 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. Pssm-ID: 188782 [Multi-domain] Cd Length: 53 Bit Score: 83.07 E-value: 7.30e-20
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| LIM | cd08368 | LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ... |
277-339 | 3.94e-06 | |||||
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid). Pssm-ID: 259829 [Multi-domain] Cd Length: 53 Bit Score: 44.23 E-value: 3.94e-06
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| LIM3_Paxillin_like | cd09338 | The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ... |
277-310 | 1.14e-05 | |||||
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. 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: 188724 [Multi-domain] Cd Length: 53 Bit Score: 43.09 E-value: 1.14e-05
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| LIM | pfam00412 | LIM domain; This family represents two copies of the LIM structural domain. |
277-312 | 5.60e-05 | |||||
LIM domain; This family represents two copies of the LIM structural domain. Pssm-ID: 395333 [Multi-domain] Cd Length: 57 Bit Score: 41.16 E-value: 5.60e-05
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| LIM3_abLIM | cd09329 | The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ... |
277-312 | 1.81e-04 | |||||
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved 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: 188715 [Multi-domain] Cd Length: 52 Bit Score: 39.61 E-value: 1.81e-04
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| LIM1_Lrg1p_like | cd09391 | The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ... |
277-312 | 2.84e-04 | |||||
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares 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. Pssm-ID: 188777 Cd Length: 57 Bit Score: 39.21 E-value: 2.84e-04
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| LIM3_Enigma_like | cd09363 | The third LIM domain of Enigma-like family; The third LIM domain of Enigma-like family: The ... |
277-308 | 6.56e-04 | |||||
The third LIM domain of Enigma-like family; The third LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. 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: 188749 [Multi-domain] Cd Length: 54 Bit Score: 38.19 E-value: 6.56e-04
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| LIM2_PINCH | cd09332 | The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a ... |
277-312 | 1.07e-03 | |||||
The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. 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: 188718 [Multi-domain] Cd Length: 52 Bit Score: 37.32 E-value: 1.07e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-211 | 1.19e-03 | |||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.19e-03
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| LIM1_LIMPETin | cd09414 | The first LIM domain of protein LIMPETin; The first LIM domain of protein LIMPETin: LIMPETin ... |
277-307 | 1.22e-03 | |||||
The first LIM domain of protein LIMPETin; The first LIM domain of protein LIMPETin: LIMPETin contains 6 LIM domains at the C-terminal and an N-terminal PET domain. Four of the six LIM domains are highly homologous to the four and half LIM domain protein family and two of them show sequence similarity to the LIM domains of the Testin family. Thus, LIMPETin may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Its differential expression indicates that it is a transcription regulator. 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: 188798 [Multi-domain] Cd Length: 58 Bit Score: 37.38 E-value: 1.22e-03
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| LIM | smart00132 | Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ... |
277-312 | 1.34e-03 | |||||
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways. Pssm-ID: 214528 [Multi-domain] Cd Length: 54 Bit Score: 36.98 E-value: 1.34e-03
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| LIM1_CRP2 | cd09480 | The first LIM domain of Cysteine Rich Protein 2 (CRP2); The first LIM domain of Cysteine Rich ... |
277-332 | 1.80e-03 | |||||
The first LIM domain of Cysteine Rich Protein 2 (CRP2); The first LIM domain of Cysteine Rich Protein 2 (CRP2): The CRP family members include CRP1, CRP2, CRP3/MLP and TLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP2 specifically binds to protein inhibitor of activated STAT-1 (PIAS1) and a novel human protein designed CRP2BP (for CRP2 binding partner). PIAS1 specifically inhibits the STAT-1 pathway and CRP2BP is homologous to members of the histone acetyltransferase family raising the possibility that CRP2 is a modulator of cytokine-controlled pathways or is functionally active in the transcriptional regulatory network. 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: 188864 Cd Length: 55 Bit Score: 36.89 E-value: 1.80e-03
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| LIM3_Paxillin | cd09409 | The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor ... |
277-310 | 2.19e-03 | |||||
The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. 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: 188793 [Multi-domain] Cd Length: 53 Bit Score: 36.74 E-value: 2.19e-03
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| PTZ00121 | PTZ00121 | MAEBL; Provisional |
13-262 | 2.25e-03 | |||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.25e-03
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| PTZ00108 | PTZ00108 | DNA topoisomerase 2-like protein; Provisional |
92-277 | 2.34e-03 | |||||
DNA topoisomerase 2-like protein; Provisional Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 2.34e-03
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| LIM2_FHL | cd09345 | The second LIM domain of Four and a half LIM domains protein (FHL); The second LIM domain of ... |
277-311 | 5.74e-03 | |||||
The second LIM domain of Four and a half LIM domains protein (FHL); The second 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: 188731 [Multi-domain] Cd Length: 54 Bit Score: 35.35 E-value: 5.74e-03
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| LIM2_ENH | cd09457 | The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma ... |
277-311 | 6.58e-03 | |||||
The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. 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: 188841 [Multi-domain] Cd Length: 52 Bit Score: 35.39 E-value: 6.58e-03
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| LIM2_abLIM | cd09328 | The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ... |
277-315 | 7.43e-03 | |||||
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved 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: 188714 Cd Length: 56 Bit Score: 35.01 E-value: 7.43e-03
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| PTZ00121 | PTZ00121 | MAEBL; Provisional |
26-260 | 8.26e-03 | |||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 8.26e-03
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